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Conserved domains on  [gi|2183974163|ref|WP_236080986|]
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non-ribosomal peptide synthetase, partial [Pseudomonas aeruginosa]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1000107)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
1-3183 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 5314.68  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163    1 MSVALRVARRFITLPLDKRMLYLAKMQEEGVTPANLPIPEVASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRG 80
Cdd:PRK12467     3 NNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   81 ELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPVPVTLAGD---DDAQAQIRAFVESETQQPFDLRNG 157
Cdd:PRK12467    83 ELDVSALRRAFDALVARHESLRTRFVQDE--EGFRQVIDASLSLTIPLDDLANeqgRARESQIEAYINEEVARPFDLANG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  158 PLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQL 237
Cdd:PRK12467   161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  238 EYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVG 317
Cdd:PRK12467   241 AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  318 VPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYN 397
Cdd:PRK12467   321 VPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  398 HQNLGSAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:PRK12467   401 HQNTATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  478 RRRLGDLPLLDAEERATLLQRSRLPASEYpAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGV 557
Cdd:PRK12467   481 RRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGV 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  558 GSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLER 637
Cdd:PRK12467   560 GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAD 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  638 LVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPL 717
Cdd:PRK12467   640 LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGAL 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  718 ARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCT-LLCGGEALAEDLAARMR--GLSAS 794
Cdd:PRK12467   720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRaLVCGGEALQVDLLARVRalGPGAR 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  795 TWNLYGPTETTIWSARFRLGEEARPF----LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERF 870
Cdd:PRK12467   800 LINHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERF 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  871 LPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLV 950
Cdd:PRK12467   880 VPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  951 PTeaalVDAESARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAM 1030
Cdd:PRK12467   960 PA----AVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRL 1035
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1031 AAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDA 1110
Cdd:PRK12467  1036 AAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQ 1115
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1111 SPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE 1190
Cdd:PRK12467  1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 RRPPVAGED---LKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQP 1267
Cdd:PRK12467  1196 PLLLAADKDeaqLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1268 PALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQ 1347
Cdd:PRK12467  1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQG 1427
Cdd:PRK12467  1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1428 HQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSrfASLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLAELTY 1507
Cdd:PRK12467  1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQ--AQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTY 1513
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1508 ATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAV 1587
Cdd:PRK12467  1514 ATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVAL 1593
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1588 VYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIR 1667
Cdd:PRK12467  1594 VFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIE 1673
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1668 LLLTQRAARERLPLGEGLPCLLLDAEHEW-AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW 1746
Cdd:PRK12467  1674 LLLTQSHLQARLPLPDGLRSLVLDQEDDWlEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEA 1753
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 FGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcaGQEV 1826
Cdd:PRK12467  1754 YQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD--EQVE 1831
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1827 PPLALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAG 1906
Cdd:PRK12467  1832 HPLSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDAS 1909
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:PRK12467  1910 LNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 1989
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAP-----SDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:PRK12467  1990 GEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLT 2069
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2062 ANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPRD 2141
Cdd:PRK12467  2070 PNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKD 2149
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2142 LFLHQTIRGLAGVAVEGRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHH 2221
Cdd:PRK12467  2150 LFQHQTVQSLAAVAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHH 2229
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2222 DALRLGFRLEDGTWRAEHRA-VEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHL 2300
Cdd:PRK12467  2230 DALRLGFVQEDGGWSAMHRApEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHL 2309
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2301 VVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCDDREGAQS 2380
Cdd:PRK12467  2310 VVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQ 2389
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2381 VRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWFTSL 2460
Cdd:PRK12467  2390 RRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSL 2469
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2461 FPLRLSPVAELGASIKRIKEQLRAIPHKGLGFGALRYLGSAEDRAALAALPSPRITFNYLGQFDGSFSADSSALFRPSAD 2540
Cdd:PRK12467  2470 YPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEKQALFVPSGE 2549
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2541 AAGSERDSDAPLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLAGLD 2620
Cdd:PRK12467  2550 FSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLS 2629
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2621 QRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQGAL 2700
Cdd:PRK12467  2630 QEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGEL 2709
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2701 EKPLQLVRKRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQ 2780
Cdd:PRK12467  2710 EEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2781 LLGEVLQRYRGETPSRSDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAF-AHGVRGAEGHADRYRQLDVTTS 2859
Cdd:PRK12467  2790 LLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALyPAPAEAVAGHGAHYLHLDATQT 2869
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2860 QRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQA 2939
Cdd:PRK12467  2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2940 VQGENLALREFEHTPLYDIQRWAGQVGEALFDNILVFENYPVSAALAEETPADMRIDALSNQEQTHYPLTLLVSAGETLE 3019
Cdd:PRK12467  2950 VQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLE 3029
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3020 LHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTP 3099
Cdd:PRK12467  3030 LEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTP 3109
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3100 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3179
Cdd:PRK12467  3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189

                   ....
gi 2183974163 3180 DSGV 3183
Cdd:PRK12467  3190 DSGV 3193
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
1-3183 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 5314.68  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163    1 MSVALRVARRFITLPLDKRMLYLAKMQEEGVTPANLPIPEVASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRG 80
Cdd:PRK12467     3 NNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   81 ELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPVPVTLAGD---DDAQAQIRAFVESETQQPFDLRNG 157
Cdd:PRK12467    83 ELDVSALRRAFDALVARHESLRTRFVQDE--EGFRQVIDASLSLTIPLDDLANeqgRARESQIEAYINEEVARPFDLANG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  158 PLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQL 237
Cdd:PRK12467   161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  238 EYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVG 317
Cdd:PRK12467   241 AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  318 VPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYN 397
Cdd:PRK12467   321 VPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  398 HQNLGSAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:PRK12467   401 HQNTATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  478 RRRLGDLPLLDAEERATLLQRSRLPASEYpAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGV 557
Cdd:PRK12467   481 RRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGV 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  558 GSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLER 637
Cdd:PRK12467   560 GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAD 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  638 LVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPL 717
Cdd:PRK12467   640 LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGAL 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  718 ARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCT-LLCGGEALAEDLAARMR--GLSAS 794
Cdd:PRK12467   720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRaLVCGGEALQVDLLARVRalGPGAR 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  795 TWNLYGPTETTIWSARFRLGEEARPF----LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERF 870
Cdd:PRK12467   800 LINHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERF 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  871 LPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLV 950
Cdd:PRK12467   880 VPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  951 PTeaalVDAESARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAM 1030
Cdd:PRK12467   960 PA----AVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRL 1035
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1031 AAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDA 1110
Cdd:PRK12467  1036 AAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQ 1115
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1111 SPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE 1190
Cdd:PRK12467  1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 RRPPVAGED---LKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQP 1267
Cdd:PRK12467  1196 PLLLAADKDeaqLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1268 PALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQ 1347
Cdd:PRK12467  1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQG 1427
Cdd:PRK12467  1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1428 HQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSrfASLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLAELTY 1507
Cdd:PRK12467  1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQ--AQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTY 1513
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1508 ATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAV 1587
Cdd:PRK12467  1514 ATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVAL 1593
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1588 VYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIR 1667
Cdd:PRK12467  1594 VFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIE 1673
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1668 LLLTQRAARERLPLGEGLPCLLLDAEHEW-AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW 1746
Cdd:PRK12467  1674 LLLTQSHLQARLPLPDGLRSLVLDQEDDWlEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEA 1753
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 FGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcaGQEV 1826
Cdd:PRK12467  1754 YQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD--EQVE 1831
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1827 PPLALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAG 1906
Cdd:PRK12467  1832 HPLSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDAS 1909
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:PRK12467  1910 LNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 1989
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAP-----SDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:PRK12467  1990 GEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLT 2069
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2062 ANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPRD 2141
Cdd:PRK12467  2070 PNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKD 2149
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2142 LFLHQTIRGLAGVAVEGRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHH 2221
Cdd:PRK12467  2150 LFQHQTVQSLAAVAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHH 2229
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2222 DALRLGFRLEDGTWRAEHRA-VEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHL 2300
Cdd:PRK12467  2230 DALRLGFVQEDGGWSAMHRApEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHL 2309
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2301 VVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCDDREGAQS 2380
Cdd:PRK12467  2310 VVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQ 2389
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2381 VRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWFTSL 2460
Cdd:PRK12467  2390 RRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSL 2469
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2461 FPLRLSPVAELGASIKRIKEQLRAIPHKGLGFGALRYLGSAEDRAALAALPSPRITFNYLGQFDGSFSADSSALFRPSAD 2540
Cdd:PRK12467  2470 YPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEKQALFVPSGE 2549
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2541 AAGSERDSDAPLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLAGLD 2620
Cdd:PRK12467  2550 FSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLS 2629
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2621 QRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQGAL 2700
Cdd:PRK12467  2630 QEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGEL 2709
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2701 EKPLQLVRKRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQ 2780
Cdd:PRK12467  2710 EEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2781 LLGEVLQRYRGETPSRSDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAF-AHGVRGAEGHADRYRQLDVTTS 2859
Cdd:PRK12467  2790 LLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALyPAPAEAVAGHGAHYLHLDATQT 2869
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2860 QRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQA 2939
Cdd:PRK12467  2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2940 VQGENLALREFEHTPLYDIQRWAGQVGEALFDNILVFENYPVSAALAEETPADMRIDALSNQEQTHYPLTLLVSAGETLE 3019
Cdd:PRK12467  2950 VQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLE 3029
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3020 LHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTP 3099
Cdd:PRK12467  3030 LEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTP 3109
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3100 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3179
Cdd:PRK12467  3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189

                   ....
gi 2183974163 3180 DSGV 3183
Cdd:PRK12467  3190 DSGV 3193
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1107-2421 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1123.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1107 ARDASPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPI 1186
Cdd:COG1020     13 AAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1187 AIEERRPPVAGEDLKG-----LVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAA 1261
Cdd:COG1020     93 PLPVVVLLVDLEALAEaaaeaAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1262 LRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEA 1341
Cdd:COG1020    173 AYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1342 LRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQA 1421
Cdd:COG1020    253 LRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRET 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1422 VVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRfasLGELEVEDLAWDVQTAQFDLTLDTYESSNGL 1501
Cdd:COG1020    333 LLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELE---LPGLTLEPLELDSGTAKFDLTLTVVETGDGL 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1502 LAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAER 1581
Cdd:COG1020    410 RLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAART 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:COG1020    490 PDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYML 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAARERLPlGEGLPCLLLDAEhEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:COG1020    570 EDAGARLVLTQSALAARLP-ELGVPVLALDAL-ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:COG1020    648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP 727
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGqevpPLALRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGaASPIGEPIPDLSWY 1901
Cdd:COG1020    728 EA----LPSLRLVLVGGEALPPELVRRWRARLPGA--RLVNLYGPTETTVDSTYYEVTPPDADGG-SVPIGRPIANTRVY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:COG1020    801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAAPSDPAALRdtlRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:COG1020    881 FRIELGEIEAALLQHPGVREAVVVAREdAPGDKRLVAYVVPEAGAAAAAALL---RLALALLLPPYMVPAAVVLLLPLPL 957
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2061 TANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPR 2140
Cdd:COG1020    958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2141 DLFLHQTIRGLAGVAVEGRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAH 2220
Cdd:COG1020   1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2221 HDALRLGFRLEDGTWRAEHRAVEAGEVLLWQ-------QSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRL 2293
Cdd:COG1020   1118 LLALLAALRARRAVRQEGPRLRLLVALAAALalaallaLLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2294 LLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCD 2373
Cdd:COG1020   1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 2374 DREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALAR 2421
Cdd:COG1020   1278 LLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLL 1325
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1582-2071 0e+00

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 719.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQraarerlplgeglpcllldaehewagypesdpqsavgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17643     81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEvPPLALRHVVFGGEALEVQALRPWFERFGDRAPRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWY 1901
Cdd:cd17643    204 RDGR-DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRVY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd17643    283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHEG-PGATQLVGYVVTQAAPSDPAAlrdTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd17643    363 FRIELGEIEAALATHPSVRDAAVIVREDePGDTRLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPL 439
                          490
                   ....*....|.
gi 2183974163 2061 TANGKLDRRAL 2071
Cdd:cd17643    440 TVNGKLDRAAL 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1596-2004 9.09e-166

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 517.97  E-value: 9.09e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIEL-GVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRA 1674
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1675 ARERLPlGEGLPCLLLDAEHEWAGYPESD---PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSA 1751
Cdd:TIGR01733   82 LASRLA-GLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRER-VTVLNQTPSAFKQLMQVACAgqevPPLA 1830
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPP----ALAS 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 LRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAGLNPV 1910
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGPGA--RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPV 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1911 PRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTT-GGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEI 1989
Cdd:TIGR01733  315 PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
                          410
                   ....*....|....*
gi 2183974163 1990 EARLLAQPGVAEAVV 2004
Cdd:TIGR01733  395 EAALLRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
1574-1980 1.80e-116

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 376.65  E-value: 1.80e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGE-RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQ--------RAARERLPLG------EGLPCLLLDAEHEWAGYPESDPQSAVGV--DNLAYV 1716
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDdalkleelLEALGKLEVVklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPdpDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1717 IYTSGSTGKPKGTLLPHGNVLR----LFDATRHWFGFSADDAWSLFHSYAFDFSV-WEIFGALLHGGRLVIVPYETSRSP 1791
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1792 EDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPlALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTV 1871
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1872 HVTYRPlsLADLDGGAASPIGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfsttgg 1950
Cdd:pfam00501  317 VVTTPL--PLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------- 387
                          410       420       430
                   ....*....|....*....|....*....|
gi 2183974163 1951 RLYRTGDLARYRCDGVVEYVGRIDHQVKIR 1980
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2087-2153 9.28e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 46.09  E-value: 9.28e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  2087 RSELEQRLAAIWADVLKLG---RVGLDDNFFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIRGLAG 2153
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAE 80
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
1-3183 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 5314.68  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163    1 MSVALRVARRFITLPLDKRMLYLAKMQEEGVTPANLPIPEVASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRG 80
Cdd:PRK12467     3 NNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   81 ELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPVPVTLAGD---DDAQAQIRAFVESETQQPFDLRNG 157
Cdd:PRK12467    83 ELDVSALRRAFDALVARHESLRTRFVQDE--EGFRQVIDASLSLTIPLDDLANeqgRARESQIEAYINEEVARPFDLANG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  158 PLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQL 237
Cdd:PRK12467   161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  238 EYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVG 317
Cdd:PRK12467   241 AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  318 VPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYN 397
Cdd:PRK12467   321 VPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  398 HQNLGSAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:PRK12467   401 HQNTATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  478 RRRLGDLPLLDAEERATLLQRSRLPASEYpAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGV 557
Cdd:PRK12467   481 RRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGV 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  558 GSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLER 637
Cdd:PRK12467   560 GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAD 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  638 LVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPL 717
Cdd:PRK12467   640 LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGAL 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  718 ARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCT-LLCGGEALAEDLAARMR--GLSAS 794
Cdd:PRK12467   720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRaLVCGGEALQVDLLARVRalGPGAR 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  795 TWNLYGPTETTIWSARFRLGEEARPF----LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERF 870
Cdd:PRK12467   800 LINHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERF 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  871 LPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLV 950
Cdd:PRK12467   880 VPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  951 PTeaalVDAESARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAM 1030
Cdd:PRK12467   960 PA----AVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRL 1035
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1031 AAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDA 1110
Cdd:PRK12467  1036 AAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQ 1115
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1111 SPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE 1190
Cdd:PRK12467  1116 PLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEE 1195
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 RRPPVAGED---LKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQP 1267
Cdd:PRK12467  1196 PLLLAADKDeaqLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQS 1275
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1268 PALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQ 1347
Cdd:PRK12467  1276 LQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQG 1427
Cdd:PRK12467  1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1428 HQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSrfASLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLAELTY 1507
Cdd:PRK12467  1436 HQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQ--AQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTY 1513
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1508 ATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAV 1587
Cdd:PRK12467  1514 ATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVAL 1593
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1588 VYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIR 1667
Cdd:PRK12467  1594 VFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIE 1673
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1668 LLLTQRAARERLPLGEGLPCLLLDAEHEW-AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW 1746
Cdd:PRK12467  1674 LLLTQSHLQARLPLPDGLRSLVLDQEDDWlEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEA 1753
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 FGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcaGQEV 1826
Cdd:PRK12467  1754 YQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD--EQVE 1831
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1827 PPLALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAG 1906
Cdd:PRK12467  1832 HPLSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDAS 1909
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:PRK12467  1910 LNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 1989
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAP-----SDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:PRK12467  1990 GEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLT 2069
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2062 ANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPRD 2141
Cdd:PRK12467  2070 PNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKD 2149
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2142 LFLHQTIRGLAGVAVEGRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHH 2221
Cdd:PRK12467  2150 LFQHQTVQSLAAVAQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHH 2229
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2222 DALRLGFRLEDGTWRAEHRA-VEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHL 2300
Cdd:PRK12467  2230 DALRLGFVQEDGGWSAMHRApEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHL 2309
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2301 VVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCDDREGAQS 2380
Cdd:PRK12467  2310 VVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQ 2389
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2381 VRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWFTSL 2460
Cdd:PRK12467  2390 RRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSL 2469
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2461 FPLRLSPVAELGASIKRIKEQLRAIPHKGLGFGALRYLGSAEDRAALAALPSPRITFNYLGQFDGSFSADSSALFRPSAD 2540
Cdd:PRK12467  2470 YPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEKQALFVPSGE 2549
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2541 AAGSERDSDAPLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLAGLD 2620
Cdd:PRK12467  2550 FSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLS 2629
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2621 QRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQGAL 2700
Cdd:PRK12467  2630 QEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGEL 2709
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2701 EKPLQLVRKRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQ 2780
Cdd:PRK12467  2710 EEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQ 2789
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2781 LLGEVLQRYRGETPSRSDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAF-AHGVRGAEGHADRYRQLDVTTS 2859
Cdd:PRK12467  2790 LLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALyPAPAEAVAGHGAHYLHLDATQT 2869
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2860 QRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQA 2939
Cdd:PRK12467  2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2940 VQGENLALREFEHTPLYDIQRWAGQVGEALFDNILVFENYPVSAALAEETPADMRIDALSNQEQTHYPLTLLVSAGETLE 3019
Cdd:PRK12467  2950 VQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLE 3029
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3020 LHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTP 3099
Cdd:PRK12467  3030 LEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTP 3109
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3100 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3179
Cdd:PRK12467  3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189

                   ....
gi 2183974163 3180 DSGV 3183
Cdd:PRK12467  3190 DSGV 3193
PRK12316 PRK12316
peptide synthase; Provisional
23-3183 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 3384.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   23 LAKMQEEGVTPANLPIPEVASAFeriPLSYAQERQWFLWQMDPQSAAYniPSALRLRGE-LDVEALSASLGAIVERHQSL 101
Cdd:PRK12316  1535 LAGLSQAQLDALPLPAGEIADIY---PLSPMQQGMLFHSLYEQEAGDY--INQLRVDVQgLDPDRFRAAWQATVDRHEIL 1609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  102 RTVFVEDEQLDGFRQQVLASVDVPVPV-TLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHH 180
Cdd:PRK12316  1610 RSGFLWQDGLEQPLQVIHKQVELPFAElDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHH 1689
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  181 VAADGWSMRVLVEELIALYGARrqgieaTLPDLPIQYADYAIW-QRHWLEAGERerqleYWMARLGGgqsvLELPT---D 256
Cdd:PRK12316  1690 ILMDGWSNAQLLGEVLQRYAGQ------PVAAPGGRYRDYIAWlQRQDAAASEA-----FWKEQLAA----LEEPTrlaQ 1754
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  257 RQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANR--NRVETERLIGF 334
Cdd:PRK12316  1755 AARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRpaELPGIEQQIGL 1834
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  335 FVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLvealQPERSLSHSPLFQAMYNHQNLGSAgrQSLAAQLP 414
Cdd:PRK12316  1835 FINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI----QRWAGQGGEALFDSLLVFENYPVA--EALKQGAP 1908
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  415 -GLSVEDLSwGAHSAQFDLTLDTYESEQgVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERA 493
Cdd:PRK12316  1909 aGLVFGRVS-NHEQTNYPLTLAVTLGET-LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQ 1986
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  494 TLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPM 573
Cdd:PRK12316  1987 RILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFEL 2066
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  574 VVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERLvHGYPAENPDLPEAP 653
Cdd:PRK12316  2067 VVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAEW-ADYPDTAPAVQLAG 2145
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  654 DSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQaQD 733
Cdd:PRK12316  2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WD 2224
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  734 PEALLDLVERQGVTVLQATPATWRMLCDSERVDllrGCTL-----LCGGEAL-AEDLAARMRGLSASTW-NLYGPTETTI 806
Cdd:PRK12316  2225 PEQLYDEMERHGVTILDFPPVYLQQLAEHAERD---GRPPavrvyCFGGEAVpAASLRLAWEALRPVYLfNGYGPTEAVV 2301
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 ----WSARFRLGEEAR-PFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSR 881
Cdd:PRK12316  2302 tpllWKCRPQDPCGAAyVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGER 2381
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  882 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAalvdaes 961
Cdd:PRK12316  2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDA------- 2454
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  962 arQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAMAAIWSEVLKLG 1041
Cdd:PRK12316  2455 --AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVE 2532
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1042 HIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDASPQLSFAQERQ 1121
Cdd:PRK12316  2533 QVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQ 2612
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1122 WFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIE-ERRPPVAGEDL 1200
Cdd:PRK12316  2613 WFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVlEDCAGVADAAI 2692
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1201 KGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAELPIQYADF 1280
Cdd:PRK12316  2693 RQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADY 2772
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1281 AAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGTLFMLLLAS 1360
Cdd:PRK12316  2773 AAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLAS 2852
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1361 FQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLVDAL 1440
Cdd:PRK12316  2853 FQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEAL 2932
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1441 QPERSLSHAPLFQVMYNHQrDDHRGSrfASLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLAELTYATDLFDASSAERI 1520
Cdd:PRK12316  2933 QPERSLSHSPLFQVMYNHQ-SGERAA--AQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERL 3009
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1521 AGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAVVYGERALDYGELN 1600
Cdd:PRK12316  3010 ARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELN 3089
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1601 LRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQraARERLP 1680
Cdd:PRK12316  3090 RRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ--SHLRLP 3167
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1681 LGEGLPCLLLDAEHEwaGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHS 1760
Cdd:PRK12316  3168 LAQGVQVLDLDRGDE--NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT 3245
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1761 YAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVpplALRHVVFGGEA 1840
Cdd:PRK12316  3246 FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT---SLKRIVCGGEA 3322
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1841 LEVQALRPWFERFGdraprLVNMYGITETTVHVTYRPLSLadlDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYV 1920
Cdd:PRK12316  3323 LPADLQQQVFAGLP-----LYNLYGPTEATITVTHWQCVE---EGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYL 3394
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1921 GGAGLARGYLNRPELSCTRFVADPFSTtGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVA 2000
Cdd:PRK12316  3395 GGEGLARGYHNRPGLTAERFVPDPFVP-GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVR 3473
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2001 EAVVLPHEGpgaTQLVGYVVTQAAPSDpaaLRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQ 2080
Cdd:PRK12316  3474 EAVVLAVDG---RQLVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ 3547
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2081 RDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPRDLFLHQTIRGLAGVAVEGRG 2160
Cdd:PRK12316  3548 QDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGG 3627
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2161 LAcAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHR 2240
Cdd:PRK12316  3628 VA-VDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHL 3706
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2241 AVEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQ 2320
Cdd:PRK12316  3707 PVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQ 3786
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2321 LQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCDDREGAQSVRHVRSARTELTEEATRRLL 2400
Cdd:PRK12316  3787 LLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLL 3866
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2401 QEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWFTSLFPLRLSPVAELGASIKRIKE 2480
Cdd:PRK12316  3867 QQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKE 3946
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2481 QLRAIPHKGLGFGALRYLGSAEDRAALAALPSPRITFNYLGQFDGSFSADsSALFRPSADAAGSERDSDAPLDNWLSLNG 2560
Cdd:PRK12316  3947 QLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFDGSFDEE-MALFVPAGESAGAEQSPDAPLDNWLSLNG 4025
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2561 QVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLAGLDQRQLDALPLAAGEVEDLYPL 2640
Cdd:PRK12316  4026 RVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPL 4105
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2641 SPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQGALEKPLQLVRKRVEVPFSVHDW 2720
Cdd:PRK12316  4106 SPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDW 4185
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2721 RDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSRSDGR 2800
Cdd:PRK12316  4186 RGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGGR 4265
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2801 YRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAFAH-GVRGAEGHADRYRQLDVTTSQRLAEFAREQKVTLNTLVQA 2879
Cdd:PRK12316  4266 YRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARaDLRSANGYGEHVRELDATATARLREFARTQRVTLNTLVQA 4345
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2880 AWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLALREFEHTPLYDIQ 2959
Cdd:PRK12316  4346 AWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQ 4425
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2960 RWAGQVGEALFDNILVFENYPVSAALAEETPADMRIDALSNQEQTHYPLTLLVSAGETLELHYSYSRQAFDEAAIECLAE 3039
Cdd:PRK12316  4426 RWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQTNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLAR 4505
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3040 RLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRR 3119
Cdd:PRK12316  4506 HLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRR 4585
                         3130      3140      3150      3160      3170      3180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 3120 ANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:PRK12316  4586 ANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA 4649
PRK05691 PRK05691
peptide synthase; Validated
14-3183 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 3130.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   14 LPLDKRMLY-----------LAKMQEEGvTPANLPIPEVASAfERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGEL 82
Cdd:PRK05691   633 IDLNLRQLFeaptlaafsaaVARQLAGG-GAAQAAIARLPRG-QALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGEL 710
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   83 DVEALSASLGAIVERHQSLRTVFVEDeqlDGFR-QQVLASVDVPV-PVTLAG--DDDAQAQIRAFVESETQQPFDLRNGP 158
Cdd:PRK05691   711 DEAALRASFQRLVERHESLRTRFYER---DGVAlQRIDAQGEFALqRIDLSDlpEAEREARAAQIREEEARQPFDLEKGP 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  159 LLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQLE 238
Cdd:PRK05691   788 LLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLA 867
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  239 YWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGV 318
Cdd:PRK05691   868 YWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGV 947
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  319 PVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSlshSPLFQAMYNH 398
Cdd:PRK05691   948 PNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFNH 1024
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  399 Q--NLGSAGRqslaaqLPGLSVEDLSWGAHSAQFDLTLDTYESEQG-VHAEFTYATDLFEAATVERLARHWRNLLEAVVA 475
Cdd:PRK05691  1025 QqrDLSALRR------LPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCE 1098
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  476 EPRRRLGDLPLLDAEERATLLQRSRLPASeyPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREE 555
Cdd:PRK05691  1099 DPQRALGDVQLLDAAERAQLAQWGQAPCA--PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDK 1176
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  556 GVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDL 635
Cdd:PRK05691  1177 GVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL 1256
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  636 ErlVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYV 715
Cdd:PRK05691  1257 H--LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFW 1334
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  716 PLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSErvdLLRGCT----LLCGGEALAEDLAARMRGL 791
Cdd:PRK05691  1335 PLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP---LAAACTslrrLFSGGEALPAELRNRVLQR 1411
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  792 --SASTWNLYGPTETTI----WSARFRLGEeaRPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGL 865
Cdd:PRK05691  1412 lpQVQLHNRYGPTETAInvthWQCQAEDGE--RSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPAL 1489
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  866 TAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTL 945
Cdd:PRK05691  1490 TAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQL 1569
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  946 VAYLvpTEAALVDAESARqqelrsaLKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASavRDAHVAPEGE 1025
Cdd:PRK05691  1570 VGYY--TGEAGQEAEAER-------LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ--QREHVEPRTE 1638
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1026 LERAMAAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAA----QG 1101
Cdd:PRK05691  1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGernsQG 1718
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1102 GIVRCARDASPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIH 1181
Cdd:PRK05691  1719 AIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVA 1798
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1182 ------------PTLPIAIEERRppvagedLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQ 1249
Cdd:PRK05691  1799 edsglrmdwqdfSALPADARQQR-------LQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMD 1871
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1250 VLVDELIRVYAALRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRR 1329
Cdd:PRK05691  1872 IFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGEL 1951
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1330 IGIPLPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQL 1409
Cdd:PRK05691  1952 YRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQM 2031
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1410 PFRELLRQVRQAVVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRfaSLGELEVEDLAWDVQTAQFD 1489
Cdd:PRK05691  2032 SVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSR--QLAGMTVEYLVNDARATKFD 2109
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1490 LTLDTYESSNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASC 1569
Cdd:PRK05691  2110 LNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQT 2189
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:PRK05691  2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQRA---ARERLPLGEGLPCLLLDAEhEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKP 1726
Cdd:PRK05691  2270 PEYPLERLHYMIEDSGIGLLLSDRAlfeALGELPAGVARWCLEDDAA-ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKP 2348
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1727 KGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPyETSRSPEDFLRLLCRERVTVL 1806
Cdd:PRK05691  2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRA-QGQWGAEEICQLIREQQVSIL 2427
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1807 NQTPSAFKQLMQ-VACAGQEVPplaLRHVVFGGEAL---EVQALRPWFerfgdrAPRLV-NMYGITETTVhvtyRPL-SL 1880
Cdd:PRK05691  2428 GFTPSYGSQLAQwLAGQGEQLP---VRMCITGGEALtgeHLQRIRQAF------APQLFfNAYGPTETVV----MPLaCL 2494
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1881 A--DLDGGAAS-PIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGD 1957
Cdd:PRK05691  2495 ApeQLEEGAASvPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGD 2574
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1958 LARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDP---AALRDT 2034
Cdd:PRK05691  2575 LVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDeaqAALREA 2654
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2035 LRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFF 2114
Cdd:PRK05691  2655 LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFF 2734
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2115 ELGGDSIISIQVVSRARQAGIRLAPRDLFLHQTIRGLAGVAVEgRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWN 2194
Cdd:PRK05691  2735 ELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATH-SEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWN 2813
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2195 QSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEvLLWQQSVADGQALEALAEQVQRSLDLG 2274
Cdd:PRK05691  2814 QALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQE-LLWQVTVADFAECAALFADAQRSLDLQ 2892
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2275 SGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEG 2354
Cdd:PRK05691  2893 QGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLRE 2972
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2355 ERGYWLAQLEGVSTELPCDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLI 2434
Cdd:PRK05691  2973 ELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLV 3052
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2435 QLEGHGREELFEDIDLTRTVGWFTSLFPLRLSP----VAELGASIKRIKEQLRAIPHKGLGFGALRYLGSAEDRAALAAL 2510
Cdd:PRK05691  3053 QLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPapgdDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAAL 3132
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2511 PSPRITFNYLGQFDGSFSADssALFRPSADAAGSERDSDAPLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAY 2590
Cdd:PRK05691  3133 PQAPITFNYLGQFDQSFASD--ALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAY 3210
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2591 RDELLALIEHCCAADVEGVTPSDFPLAGLDQRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG 2670
Cdd:PRK05691  3211 LAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINS 3290
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2671 -LDPQRFREAWQAALDAHEVLRSGFLWQgALEKPLQLVRKRVEVPFSVHDWR--DRADLAEALDALAAGEAGLGFELAEA 2747
Cdd:PRK05691  3291 aLDPERFAQAWQAVVARHEALRASFSWN-AGETMLQVIHKPGRTPIDYLDWRglPEDGQEQRLQALHKQEREAGFDLLNQ 3369
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2748 PLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSR-----SDGRYRDYIAWLQRQDAGRTEAFWKQ 2822
Cdd:PRK05691  3370 PPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGReaqlpVPPRYRDYIGWLQRQDLAQARQWWQD 3449
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2823 RLQRLGEPTlLVPA---FAHGVRGAEGH---ADRYRQLDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAF 2896
Cdd:PRK05691  3450 NLRGFERPT-PIPSdrpFLREHAGDSGGmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLF 3528
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2897 GATVSGRPAELRGIEEQIGLFINTLPV-VASPCPEQP--IGDWLQAVQGENLALREFEHTPLYDIQRWAG-QVGEALFDN 2972
Cdd:PRK05691  3529 GVTVAGRPVSMPQMQRTVGLFINSIALrVQLPAAGQRcsVRQWLQGLLDSNMELREYEYLPLVAIQECSElPKGQPLFDS 3608
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2973 ILVFENYPVSAALAEETpadMRIDALSNQEQTH--YPLTLLVSAGETLELHYSYSRQAFDEAAIECLAERLERLLLGMCE 3050
Cdd:PRK05691  3609 LFVFENAPVEVSVLDRA---QSLNASSDSGRTHtnFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQ 3685
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3051 NPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER 3130
Cdd:PRK05691  3686 GFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAA 3765
                         3210      3220      3230      3240      3250
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 3131 GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:PRK05691  3766 GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRT 3818
PRK12316 PRK12316
peptide synthase; Provisional
1113-3183 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2713.61  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1113 QLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEErr 1192
Cdd:PRK12316    51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEF-- 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1193 ppvagEDLKGLVETE--------AHR----PFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYA 1260
Cdd:PRK12316   129 -----EDCSGLPEAEqearlrdeAQReslqPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1261 ALRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAE 1340
Cdd:PRK12316   204 AYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1341 ALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQ 1420
Cdd:PRK12316   284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1421 AVVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRFASLGELEVEDLAWDVQTAQFDLTLDTYESSNG 1500
Cdd:PRK12316   364 TVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGR 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1501 LLAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAE 1580
Cdd:PRK12316   444 LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVER 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1581 RPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYM 1660
Cdd:PRK12316   524 TPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM 603
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1661 IEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEW-AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRL 1739
Cdd:PRK12316   604 LEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWlEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNR 683
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1740 FDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQV 1819
Cdd:PRK12316   684 LCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 763
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1820 ACAGQEVPplaLRHVVFGGEALEVQALrpwfERFGDRAP--RLVNMYGITETTVHVTYrplSLADLDGGAASPIGEPIPD 1897
Cdd:PRK12316   764 EDVASCTS---LRRIVCSGEALPADAQ----EQVFAKLPqaGLYNLYGPTEAAIDVTH---WTCVEEGGDSVPIGRPIAN 833
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1898 LSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTtGGRLYRTGDLARYRCDGVVEYVGRIDHQV 1977
Cdd:PRK12316   834 LACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQV 912
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1978 KIRGFRIELGEIEARLLAQPGVAEAVVLPHEGpgaTQLVGYVVTQAAPSDpaaLRDTLRQALKASLPEHMVPAHLLFLER 2057
Cdd:PRK12316   913 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---KQLVGYVVLESEGGD---WREALKAHLAASLPEYMVPAQWLALER 986
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2058 LPLTANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRL 2137
Cdd:PRK12316   987 LPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2138 APRDLFLHQTIRGLAGVAVEGRGLAcAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQAL 2217
Cdd:PRK12316  1067 SPRDLFQHQTIRSLALVAKAGQATA-ADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERL 1145
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2218 LAHHDALRLGFRLEDGTWRAEHRAVEAGEVLlWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVI 2297
Cdd:PRK12316  1146 VAHHDALRLRFREEDGGWQQAYAAPQAGEVL-WQRQAASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVI 1224
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2298 HHLVVDGVSWRILLEDLQTAYRQLQAgqavALPAKTSAFKAWAERLQAHArdGGLEGERGYWLAQLEGVSTELPCDDREG 2377
Cdd:PRK12316  1225 HHLVVDGVSWRILLEDLQRAYADLDA----DLPARTSSYQAWARRLHEHA--GARAEELDYWQAQLEDAPHELPCENPDG 1298
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2378 AQSVRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWF 2457
Cdd:PRK12316  1299 ALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWF 1378
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2458 TSLFPLRLSPVAELGASIKRIKEQLRAIPHKGLGFGALRYLGSAEDRAALAALPSPRITFNYLGQFDGSFsaDSSALFRP 2537
Cdd:PRK12316  1379 TSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNYLGQFDRQF--DEAALFVP 1456
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2538 SADAAGSERDSDAPLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLA 2617
Cdd:PRK12316  1457 ATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLA 1536
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2618 GLDQRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQ 2697
Cdd:PRK12316  1537 GLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQ 1616
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2698 GALEKPLQLVRKRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWS 2777
Cdd:PRK12316  1617 DGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWS 1696
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2778 NSQLLGEVLQRYRGETPSRSDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAFAhGVRGAEGHADRYRQLDVT 2857
Cdd:PRK12316  1697 NAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAAR-TEDGQVGYGDHQQLLDPA 1775
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2858 TSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWL 2937
Cdd:PRK12316  1776 QTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWL 1855
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2938 QAVQGENLALREFEHTPLYDIQRWAGQVGEALFDNILVFENYPVSAALAEETPADMRIDALSNQEQTHYPLTLLVSAGET 3017
Cdd:PRK12316  1856 QEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQGAPAGLVFGRVSNHEQTNYPLTLAVTLGET 1935
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3018 LELHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYPLQRGVHRLFEEQVER 3097
Cdd:PRK12316  1936 LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAAR 2015
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3098 TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3177
Cdd:PRK12316  2016 APEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYM 2095

                   ....*.
gi 2183974163 3178 LEDSGV 3183
Cdd:PRK12316  2096 LEDSGA 2101
PRK12316 PRK12316
peptide synthase; Provisional
4-1371 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1403.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163    4 ALRVARRFITLPLDKRMLYLAKMQEEGVTPANLPIPEVASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELD 83
Cdd:PRK12316     6 SLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   84 VEALSASLGAIVERHQSLRTVFVEdeQLDGFRQQVLASVDVPVP-VTLAGDDDA--QAQIRAFVESETQQPFDLRNGPLL 160
Cdd:PRK12316    86 RQALERAFASLVQRHETLRTVFPR--GADDSLAQVPLDRPLEVEfEDCSGLPEAeqEARLRDEAQRESLQPFDLCEGPLL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  161 RARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYW 240
Cdd:PRK12316   164 RVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYW 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  241 MARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPV 320
Cdd:PRK12316   244 RAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPI 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  321 ANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQN 400
Cdd:PRK12316   324 ANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQP 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  401 LgsAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRR 480
Cdd:PRK12316   404 L--VADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQAR 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  481 LGDLPLLDAEERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSD 560
Cdd:PRK12316   482 VDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPD 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  561 VLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERLVH 640
Cdd:PRK12316   562 VLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLE 641
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  641 GYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARG 720
Cdd:PRK12316   642 GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 721
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  721 ASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLL-CGGEALAEDLAARMRGL--SASTWN 797
Cdd:PRK12316   722 ARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIvCSGEALPADAQEQVFAKlpQAGLYN 801
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  798 LYGPTETTI----WSARFRLGEEarPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPD 873
Cdd:PRK12316   802 LYGPTEAAIdvthWTCVEEGGDS--VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPS 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  874 PFaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQpgvAGPTLVAYLVPTE 953
Cdd:PRK12316   880 PF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLES 955
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  954 AALVdaesarqqeLRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAMAAI 1033
Cdd:PRK12316   956 EGGD---------WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAI 1026
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1034 WSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRlDLQVPLRTLFEHSTLRAYAQAV--AQLAPAAQGgivrcarDAS 1111
Cdd:PRK12316  1027 WQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLALVAkaGQATAADQG-------PAS 1098
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1112 PQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEER 1191
Cdd:PRK12316  1099 GEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQ 1178
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1192 RPPVAGEDLKGLVEtEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALrhdqppaLA 1271
Cdd:PRK12316  1179 RQAASEEELLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADL-------DA 1250
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1272 ELPIQYADFAAW-QRQWMDGGERERQLDYWVSRLGGEQPllELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQ 1350
Cdd:PRK12316  1251 DLPARTSSYQAWaRRLHEHAGARAEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAY 1328
                         1370      1380
                   ....*....|....*....|..
gi 2183974163 1351 GTLFM-LLLASFQALLHRYSGQ 1371
Cdd:PRK12316  1329 RTQVNdLLLTALARVTCRWSGQ 1350
PRK05691 PRK05691
peptide synthase; Validated
518-2434 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1196.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  518 AQAGLTPDAPALLF----GEER--LSYAELNALANRLAWRLREEGVGSDVLVgIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:PRK05691    17 RRAAQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAY 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 P-----QYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGL------QSLLLDDLERLvhgyPAENPDLPE-APDSLCYA 659
Cdd:PRK05691    96 PpesarRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELaaanapELLCVDTLDPA----LAEAWQEPAlQPDDIAFL 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 IYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR--DRLLSVTTFSFDIfGL--ELYVPLARGAS-MLLASREQAQDP 734
Cdd:PRK05691   172 QYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDM-GLigGLLQPIFSGVPcVLMSPAYFLERP 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  735 EALLDLVERQGVTVLQATPATWRmLCdSERV--------DLLRGCTLLCGGEALAEDLAARMR------GLSASTW-NLY 799
Cdd:PRK05691   251 LRWLEAISEYGGTISGGPDFAYR-LC-SERVsesalerlDLSRWRVAYSGSEPIRQDSLERFAekfaacGFDPDSFfASY 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  800 GPTETTIWSARFRLGE---------------EARPFLGGPLENT-------ALYILDSE-MNPCPPGVAGELLIGGDGLA 856
Cdd:PRK05691   329 GLAEATLFVSGGRRGQgipaleldaealarnRAEPGTGSVLMSCgrsqpghAVLIVDPQsLEVLGDNRVGEIWASGPSIA 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  857 RGYHRRPGLTAERFLpdpfAADGSRLYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIEtRLLEqdsvREAVVVA 936
Cdd:PRK05691   409 HGYWRNPEASAKTFV----EHDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVE----REVEVVR 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  937 QPGVAgptlvAYLVP---TEAALVDAESAR--QQELRS-ALKNSLLAVLPD--YMVPAHMLLLE--NLPLTPNGKINRKA 1006
Cdd:PRK05691   479 KGRVA-----AFAVNhqgEEGIGIAAEISRsvQKILPPqALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSA 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1007 --LPLPDAS------------AVRDAHVAPEGELERAMAAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDL 1072
Cdd:PRK05691   554 crLRLADGSldsyalfpalqaVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGI 633
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1073 QVPLRTLFEHSTLRAYAQAVAQL---APAAQGGIVRCARDASPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRD 1149
Cdd:PRK05691   634 DLNLRQLFEAPTLAAFSAAVARQlagGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEA 713
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1150 ALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIE----ERRPPVAGEDLKGLV-ETEAHRPFDLQRGPLLRVLL 1224
Cdd:PRK05691   714 ALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQridlSDLPEAEREARAAQIrEEEARQPFDLEKGPLLRVTL 793
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1225 LPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRL 1304
Cdd:PRK05691   794 VRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQL 873
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1305 GGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRN 1384
Cdd:PRK05691   874 GDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRP 953
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1385 REETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLVDALQPERSLShapLFQVMYNHQRDDHR 1464
Cdd:PRK05691   954 RLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQVMFNHQQRDLS 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1465 GSRfaSLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLA-ELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELK 1543
Cdd:PRK05691  1031 ALR--RLPGLLAEELPWHSREAKFDLQLHSEEDRNGRLTlSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQ 1108
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1544 LLDEAEaRADLLQWNPGPQdfTPAS-CLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVG 1622
Cdd:PRK05691  1109 LLDAAE-RAQLAQWGQAPC--APAQaWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVA 1185
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1623 LAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHeWAGYPES 1702
Cdd:PRK05691  1186 IAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLH-LDSWPSQ 1264
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1703 DPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVI 1782
Cdd:PRK05691  1265 APGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVL 1344
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1783 VPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQevpPLALRHVVFGGEALEVqALRpwfERFGDRAP--RL 1860
Cdd:PRK05691  1345 AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAA---CTSLRRLFSGGEALPA-ELR---NRVLQRLPqvQL 1417
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1861 VNMYGITETTVHVTYRPLSLADldgGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRF 1940
Cdd:PRK05691  1418 HNRYGPTETAINVTHWQCQAED---GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERF 1494
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1941 VADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVV 2020
Cdd:PRK05691  1495 VPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYT 1574
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2021 TQAAPSDPAalrDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDAsrLQRDYTAPRSELEQRLAAIWAD 2100
Cdd:PRK05691  1575 GEAGQEAEA---ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW--QQREHVEPRTELQQQIAAIWRE 1649
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2101 VLKLGRVGLDDNFFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIRGLAgvAVEGRGLACAE---QGPI-----SG 2171
Cdd:PRK05691  1650 VLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFA--EQVARIQAAGErnsQGAIarvdrSQ 1727
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2172 STPLLPIQQ-MFFELDI-PRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAvEAGEVLL 2249
Cdd:PRK05691  1728 PVPLSYSQQrMWFLWQMePDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAE-DSGLRMD 1806
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2250 WQQSVADG-----QALEALA-EQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQA 2323
Cdd:PRK05691  1807 WQDFSALPadarqQRLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLD 1886
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2324 GQA---VALPAKTSAFKAWaerlQAHARDGGlEGER--GYWLAQL--EGVSTELPCD-DREGAQSVRHvRSARTELTEEA 2395
Cdd:PRK05691  1887 DREsplEPLPVQYLDYSVW----QRQWLESG-ERQRqlDYWKAQLgnEHPLLELPADrPRPPVQSHRG-ELYRFDLSPEL 1960
                         2010      2020      2030      2040
                   ....*....|....*....|....*....|....*....|
gi 2183974163 2396 TRRLlqEAPAAYRTQVNDLLLTA-LARVIGRWTGQADTLI 2434
Cdd:PRK05691  1961 AARV--RAFNAQRGLTLFMTMTAtLAALLYRYSGQRDLRI 1998
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1107-2421 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1123.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1107 ARDASPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPI 1186
Cdd:COG1020     13 AAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1187 AIEERRPPVAGEDLKG-----LVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAA 1261
Cdd:COG1020     93 PLPVVVLLVDLEALAEaaaeaAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLA 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1262 LRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEA 1341
Cdd:COG1020    173 AYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1342 LRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQA 1421
Cdd:COG1020    253 LRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRET 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1422 VVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRfasLGELEVEDLAWDVQTAQFDLTLDTYESSNGL 1501
Cdd:COG1020    333 LLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELE---LPGLTLEPLELDSGTAKFDLTLTVVETGDGL 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1502 LAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAER 1581
Cdd:COG1020    410 RLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAART 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:COG1020    490 PDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYML 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAARERLPlGEGLPCLLLDAEhEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:COG1020    570 EDAGARLVLTQSALAARLP-ELGVPVLALDAL-ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:COG1020    648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP 727
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGqevpPLALRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGaASPIGEPIPDLSWY 1901
Cdd:COG1020    728 EA----LPSLRLVLVGGEALPPELVRRWRARLPGA--RLVNLYGPTETTVDSTYYEVTPPDADGG-SVPIGRPIANTRVY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:COG1020    801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAAPSDPAALRdtlRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:COG1020    881 FRIELGEIEAALLQHPGVREAVVVAREdAPGDKRLVAYVVPEAGAAAAAALL---RLALALLLPPYMVPAAVVLLLPLPL 957
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2061 TANGKLDRRALPAPDASRLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAPR 2140
Cdd:COG1020    958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2141 DLFLHQTIRGLAGVAVEGRGLACAEQGPISGSTPLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAH 2220
Cdd:COG1020   1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2221 HDALRLGFRLEDGTWRAEHRAVEAGEVLLWQ-------QSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRL 2293
Cdd:COG1020   1118 LLALLAALRARRAVRQEGPRLRLLVALAAALalaallaLLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2294 LLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCD 2373
Cdd:COG1020   1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 2374 DREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQVNDLLLTALAR 2421
Cdd:COG1020   1278 LLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLL 1325
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
36-1366 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1101.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   36 LPIPEVASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFV-EDEQLDGF 114
Cdd:COG1020      6 AAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRtRAGRPVQV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  115 RQQVLASVDVPVPVTLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEE 194
Cdd:COG1020     86 IQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  195 LIALYGARRQGIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQL 274
Cdd:COG1020    166 LLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRL 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  275 PQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDL 354
Cdd:COG1020    246 PAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAEL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  355 LQQTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAgrqslAAQLPGLSVEDLSWGAHSAQFDLTL 434
Cdd:COG1020    326 LARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPAD-----ELELPGLTLEPLELDSGTAKFDLTL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  435 DTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERATLLQRSRLPASEYPAGQGVHR 514
Cdd:COG1020    401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  515 LFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQY 594
Cdd:COG1020    481 LFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  595 PADRLQYMIDDSGLRLLLSQQSVLARLPQSdGLQSLLLDDLErlVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMV 674
Cdd:COG1020    561 PAERLAYMLEDAGARLVLTQSALAARLPEL-GVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMV 637
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  675 RHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPA 754
Cdd:COG1020    638 EHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPS 717
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  755 TWRMLCDSERVDLLRGCTLLCGGEALAEDLAARMRGLSAST--WNLYGPTETTIWSARFRLGEE----ARPFLGGPLENT 828
Cdd:COG1020    718 LLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGArlVNLYGPTETTVDSTYYEVTPPdadgGSVPIGRPIANT 797
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  829 ALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVK 908
Cdd:COG1020    798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  909 IRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPTEAALVDAESARQQelrsalknsLLAVLPDYMVPAH 987
Cdd:COG1020    878 IRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKrLVAYVVPEAGAAAAAALLRLA---------LALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  988 MLLLENLPLTPNGKINRKALPLPDASAVRDAhVAPEGELERAMAAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVR 1067
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAAAAAAAA-AAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAA 1027
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1068 RRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDASPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLR 1147
Cdd:COG1020   1028 RLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLL 1107
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1148 RDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE---RRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLL 1224
Cdd:COG1020   1108 LLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALaalLALLLAAAAAAAELLAAAALLLLLALLLLALLLL 1187
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1225 LPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRL 1304
Cdd:COG1020   1188 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALL 1267
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 1305 GGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGTLFMLLLASFQALLH 1366
Cdd:COG1020   1268 ALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
PRK12316 PRK12316
peptide synthase; Provisional
30-1100 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 969.43  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   30 GVTPANLPI-----------PEVASAFERI-PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGeLDVEALSASLGAIVER 97
Cdd:PRK12316  4073 GVTPSDFPLagldqarldalPLPLGEIEDIyPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDR 4151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   98 HQSLRTVFVEDEQLDGFRQQVLASVDVPVPV-TLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTL 176
Cdd:PRK12316  4152 HDVLRSGFVWQGELGRPLQVVHKQVSLPFAElDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIY 4231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  177 TIHHVAADGWSMRVLVEELIALYGARrqgieaTLPDLPIQYADYAIW-QRHWLEAGERerqleYWMARLGGGQSVLELPT 255
Cdd:PRK12316  4232 TNHHILMDGWSNSQLLGEVLERYSGR------PPAQPGGRYRDYIAWlQRQDAAASEA-----FWREQLAALDEPTRLAQ 4300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  256 DRQRPALPSYRG-ARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANR--NRVETERLI 332
Cdd:PRK12316  4301 AIARADLRSANGyGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQI 4380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  333 GFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLvealQPERSLSHSPLFQAMYNHQN--LGSAGRQSLA 410
Cdd:PRK12316  4381 GLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENypVSEALQQGAP 4456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  411 AQLPGLSVEdlSWGAHSAQFDLTLDTYESEQgvhAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAE 490
Cdd:PRK12316  4457 GGLRFGEVT--NHEQTNYPLTLAVGLGETLS---LQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKA 4531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  491 ERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERG 570
Cdd:PRK12316  4532 EQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERS 4611
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  571 VPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDlERLVHGYPAENPDLP 650
Cdd:PRK12316  4612 AEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDR-DEDWEGFPAHDPAVR 4690
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  651 EAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASrEQ 730
Cdd:PRK12316  4691 LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD-DS 4769
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  731 AQDPEALLDLVERQGVTVLQATPATWRMLC--DSERVDLLRGCTLLCGGEALAEDLAARMRGL--SASTWNLYGPTETTI 806
Cdd:PRK12316  4770 LWDPERLYAEIHEHRVTVLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRAlkPVYLFNGYGPTETTV 4849
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 WSARFRL------GEEARPfLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGS 880
Cdd:PRK12316  4850 TVLLWKArdgdacGAAYMP-IGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG 4928
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAALVDAE 960
Cdd:PRK12316  4929 RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADAD 5008
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  961 sARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAMAAIWSEVLKL 1040
Cdd:PRK12316  5009 -EAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQL 5087
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1041 GHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQ 1100
Cdd:PRK12316  5088 ERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
PRK12316 PRK12316
peptide synthase; Provisional
1148-2152 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 923.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1148 RDALQGALDllvqRHETLRTTFVEHD--GAPRQVIHP--TLPIAIEE-RRPPVAGEDLKGLVETEAHRPFDLQRGPLLRV 1222
Cdd:PRK12316  4142 RAAWQAALD----RHDVLRSGFVWQGelGRPLQVVHKqvSLPFAELDwRGRADLQAALDALAAAERERGFDLQRAPLLRL 4217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1223 LLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAAlrhdQPPALAELpiQYADFAAW-QRQwmDGGERERqldYWV 1301
Cdd:PRK12316  4218 VLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG----RPPAQPGG--RYRDYIAWlQRQ--DAAASEA---FWR 4286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1302 SRLGGEQPLLELPSDRPRPQQQSHRGRRIGIP-LPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPI 1380
Cdd:PRK12316  4287 EQLAALDEPTRLAQAIARADLRSANGYGEHVReLDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATV 4366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1381 ANR--NREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLvdalQPERSLSHAPLFQVMYNH 1458
Cdd:PRK12316  4367 AGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEI----QRWAGQGGEALFDSLLVF 4442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1459 QRD--DHRGSRFASLGELEVEDLAWDVQTAQFDLTLDTYESsngLLAELTYATDLFDASSAERIAGHWLNLLRSIVARPE 1536
Cdd:PRK12316  4443 ENYpvSEALQQGAPGGLRFGEVTNHEQTNYPLTLAVGLGET---LSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQ 4519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1537 ARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVG 1616
Cdd:PRK12316  4520 RRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVG 4599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1617 PDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEW 1696
Cdd:PRK12316  4600 PEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDW 4679
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1697 AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLH 1776
Cdd:PRK12316  4680 EGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLIN 4759
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1777 GGRLVIVPYETSrSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPlaLRHVVFGGEALEVQALRPWFERFgdR 1856
Cdd:PRK12316  4760 GASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPS--LRVYCFGGEAVAQASYDLAWRAL--K 4834
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1857 APRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELS 1936
Cdd:PRK12316  4835 PVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALT 4914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1937 CTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV 2016
Cdd:PRK12316  4915 AERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV 4994
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2017 GYVVTQA-----APSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQRDYTAPRSELE 2091
Cdd:PRK12316  4995 GYVVPQDpaladADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELE 5074
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2092 QRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRAR-QAGIRLAPRDLFLHQTIRGLA 2152
Cdd:PRK12316  5075 QQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFV 5136
PRK12467 PRK12467
peptide synthase; Provisional
29-1418 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 851.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   29 EGVTPANLPI-----------PEVASAFERI-PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGeLDVEALSASLGAIVE 96
Cdd:PRK12467  2616 RGVTPSDFPLaglsqeqldrlPVAVGDIEDIyPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVID 2694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   97 RHQSLRTVFVEDEQLDGFRQQVLASVDVPVPVTLAGDD-DAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLT 175
Cdd:PRK12467  2695 RHEILRSGFLWDGELEEPLQVVYKQARLPFSRLDWRDRaDLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLI 2774
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  176 LTIHHVAADGWSMRVLVEELIALYGARrqgieaTLPDLPIQYADYAiwqrHWLEAGERERQLEYWMARLGGGQSVLEL-P 254
Cdd:PRK12467  2775 YTNHHILMDGWSGSQLLGEVLQRYFGQ------PPPAREGRYRDYI----AWLQAQDAEASEAFWKEQLAALEEPTRLaR 2844
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  255 TDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANR--NRVETERLI 332
Cdd:PRK12467  2845 ALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQL 2924
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  333 GFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLP-FEQLVEALQPERSLSHSPLFQAMYnhqnlgsagrqSLAA 411
Cdd:PRK12467  2925 GLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPlADIQRWAGQGGEALFDSILVFENY-----------PISE 2993
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  412 QLPGLSVEDLSWGAHSAQ----FDLTLDTYESEQgVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLL 487
Cdd:PRK12467  2994 ALKQGAPSGLRFGAVSSReqtnYPLTLAVGLGDT-LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTL 3072
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  488 DAEERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIAL 567
Cdd:PRK12467  3073 AAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAV 3152
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  568 ERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLErlVHGYPAENP 647
Cdd:PRK12467  3153 ERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLD--LNGYSENNP 3230
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  648 DLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLAS 727
Cdd:PRK12467  3231 STRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD 3310
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  728 REQaQDPEALLDLVERQGVTVLQATPATWRMLC-DSERVDLLRGCTLLCGGEALAEDLAARMRGL--SASTWNLYGPTET 804
Cdd:PRK12467  3311 NDL-WDPEELWQAIHAHRISIACFPPAYLQQFAeDAGGADCASLDIYVFGGEAVPPAAFEQVKRKlkPRGLTNGYGPTEA 3389
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  805 TIWSARFRLGEEARPFL-----GGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADG 879
Cdd:PRK12467  3390 VVTVTLWKCGGDAVCEApyapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSG 3469
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  880 SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPteaalvda 959
Cdd:PRK12467  3470 GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVP-------- 3541
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  960 eSARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASaVRDAHVAPEGELERAMAAIWSEVLK 1039
Cdd:PRK12467  3542 -ADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK-GSREYVAPRSEVEQQLAAIWADVLG 3619
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1040 LGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEhstlrayAQAVAQLAPAAQGGIVRCARDASPQlsfaqe 1119
Cdd:PRK12467  3620 VEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS-------APTIAELAGYSPLGDVPVNLLLDLN------ 3686
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1120 rqwfiwrldphsaaynipvalrlkgplrrdALQGALDLLVQRHETLRTTFvehDGAPRQVIhptlpiaIEERRPpvaged 1199
Cdd:PRK12467  3687 ------------------------------RLETGFPALFCRHEGLGTVF---DYEPLAVI-------LEGDRH------ 3720
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1200 lkglveteahrpfdlqrgpllrvlllplatdecVLVLTLHHIIADGWsmqvlvdelirvyaalrhdQPPALAELPIQYAD 1279
Cdd:PRK12467  3721 ---------------------------------VLGLTCRHLLDDGW-------------------QDTSLQAMAVQYAD 3748
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1280 FAAWQRQWMDGGERerqldywvsrlggeqpllelpsdrprpqqqshrgrriGIPLPAELAEALRRLAQAEQgtlfmllla 1359
Cdd:PRK12467  3749 YILWQQAKGPYGLL-------------------------------------GWSLGGTLARLVAELLEREG--------- 3782
                         1370      1380      1390      1400      1410
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 1360 sfqallhrysgqndirvgvpianrnreETEGLIGFFVNTQVLRAELDGQLPFRELLRQV 1418
Cdd:PRK12467  3783 ---------------------------ESEAFLGLFDNTLPLPDEFVPQAEFLELLRQL 3814
PRK12467 PRK12467
peptide synthase; Provisional
1142-2269 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 816.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1142 LKGPLRRDALQGALDllvqRHETLRTTFVEHDGA--PRQVIHP--TLPIA-IEERRPPVAGEDLKGLVETEAHRPFDLQR 1216
Cdd:PRK12467  2680 LDVERFRTAWQAVID----RHEILRSGFLWDGELeePLQVVYKqaRLPFSrLDWRDRADLEQALDALAAADRQQGFDLLS 2755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1217 GPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAAlrhdQPPALAELpiQYADFAAW-QRQwmDGGERER 1295
Cdd:PRK12467  2756 APLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG----QPPPAREG--RYRDYIAWlQAQ--DAEASEA 2827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1296 qldYWVSRLGG-EQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDI 1374
Cdd:PRK12467  2828 ---FWKEQLAAlEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTV 2904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1375 RVGVPIANRNRE--ETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQdlpfeqlvdalqperslsHAPLF 1452
Cdd:PRK12467  2905 CFGATVAGRPAQlrGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFE------------------HTPLA 2966
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1453 QVmynhQRDDHRGSR--FASL-----------------GELEVEDLAWDVQTaQFDLTL-----DTyessngLLAELTYA 1508
Cdd:PRK12467  2967 DI----QRWAGQGGEalFDSIlvfenypisealkqgapSGLRFGAVSSREQT-NYPLTLavglgDT------LELEFSYD 3035
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1509 TDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAVV 1588
Cdd:PRK12467  3036 RQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALV 3115
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1589 YGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRL 1668
Cdd:PRK12467  3116 FGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL 3195
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1669 LLTQRAARERLPLGEGLPCLLLDAEHEWaGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFG 1748
Cdd:PRK12467  3196 LLTQAHLLEQLPAPAGDTALTLDRLDLN-GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE 3274
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1749 FSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETsRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPP 1828
Cdd:PRK12467  3275 LDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDA-GGADCAS 3352
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1829 LalRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAGLN 1908
Cdd:PRK12467  3353 L--DIYVFGGEAVPPAAFEQVKRKLKPRG--LTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLN 3428
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 PVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGE 1988
Cdd:PRK12467  3429 PVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 3508
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1989 IEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAapsDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:PRK12467  3509 IEARLLQHPSVREAVVLARDGAGGKQLVAYVVPAD---PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2069 RALPAPDASrLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQT 2147
Cdd:PRK12467  3586 KALPDPDAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPT 3664
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2148 IRGLAGVAvegrglacaeQGPISGSTPLLPIQqmffeldiprRQHWNQSVLLEPGQALDGTLLETALQALLAHHDA---L 2224
Cdd:PRK12467  3665 IAELAGYS----------PLGDVPVNLLLDLN----------RLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHvlgL 3724
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2225 RLGFRLEDGtW---RAEHRAVEAGEVLLWQQSVA---------DGQALEALAEQVQR 2269
Cdd:PRK12467  3725 TCRHLLDDG-WqdtSLQAMAVQYADYILWQQAKGpygllgwslGGTLARLVAELLER 3780
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1582-2071 0e+00

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 719.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQraarerlplgeglpcllldaehewagypesdpqsavgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17643     81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEvPPLALRHVVFGGEALEVQALRPWFERFGDRAPRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWY 1901
Cdd:cd17643    204 RDGR-DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRVY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd17643    283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHEG-PGATQLVGYVVTQAAPSDPAAlrdTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd17643    363 FRIELGEIEAALATHPSVRDAAVIVREDePGDTRLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPL 439
                          490
                   ....*....|.
gi 2183974163 2061 TANGKLDRRAL 2071
Cdd:cd17643    440 TVNGKLDRAAL 450
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1114-1535 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 645.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIE---- 1189
Cdd:cd19531      4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPvvdl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1190 -ERRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPP 1268
Cdd:cd19531     84 sGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1269 ALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQA 1348
Cdd:cd19531    164 PLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALARR 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1349 EQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGH 1428
Cdd:cd19531    244 EGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAH 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1429 QDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGsrfASLGELEVEDLAWDVQTAQFDLTLDTYESSNGLLAELTYA 1508
Cdd:cd19531    324 QDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAA---LELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                          410       420
                   ....*....|....*....|....*..
gi 2183974163 1509 TDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19531    401 TDLFDAATIERMAGHFQTLLEAIVADP 427
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
47-477 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 641.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPV 126
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVD--GEPVQVILPPLPLPL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PV---TLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARR 203
Cdd:cd19531     79 PVvdlSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  204 QGIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQ 283
Cdd:cd19531    159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  284 ALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAAL 363
Cdd:cd19531    239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  364 GAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAgrqslAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGV 443
Cdd:cd19531    319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAA-----ALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGL 393
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2183974163  444 HAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19531    394 RGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
41-1167 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 607.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   41 VASAFERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLA 120
Cdd:PRK10252     1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDN--GEVWQWVDP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  121 SVDVPVP--VTLAGDDDAQAQIRAFVESETQQPFDLRNG-PLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIA 197
Cdd:PRK10252    79 ALTFPLPeiIDLRTQPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  198 LYGARRQGI---EATLPDLPIQYADYAIWQRHwlEAGERERQleYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQL 274
Cdd:PRK10252   159 IYCAWLRGEptpASPFTPFADVVEEYQRYRAS--EAWQRDAA--FWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  275 PQALGRQLqaLAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDL 354
Cdd:PRK10252   235 TDGAFRQL--AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  355 LQQTRVAALGAQSHQDLPFEQLVEAL---QPERSLsHSPLFQAMYNHQNLGSAGRQSLAAQLPGLSVEDLswgahsaqfd 431
Cdd:PRK10252   313 ATRLAAQLKKMRRHQRYDAEQIVRDSgraAGDEPL-FGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDL---------- 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  432 lTLDTYESEQG-VHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERAtllQRSRLPASEYP-AG 509
Cdd:PRK10252   382 -ELALFPDEHGgLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYA---QLAQVNATAVEiPE 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  510 QGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVP 589
Cdd:PRK10252   458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  590 LDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLErlvhGYPAENPDLPEAPDSLCYAIYTSGSTGQP 669
Cdd:PRK10252   538 LDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPL----APQGAAPLQLSQPHHTAYIIFTSGSTGRP 613
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  670 KGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVL 749
Cdd:PRK10252   614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTT 693
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLCDSERVDLLRGCTL-----LCGGEALAEDLAARMRGL-SASTWNLYGPTET----TIWSArfrLGEEARP 819
Cdd:PRK10252   694 HFVPSMLAAFVASLTPEGARQSCAslrqvFCSGEALPADLCREWQQLtGAPLHNLYGPTEAavdvSWYPA---FGEELAA 770
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 F------LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaADGSRLYRTGDLARYRA 893
Cdd:PRK10252   771 VrgssvpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLD 849
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  894 DGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-------LVAYLVPTEAALVDAEsarqqe 966
Cdd:PRK10252   850 DGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAAtggdarqLVGYLVSQSGLPLDTS------ 923
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  967 lrsALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDaSAVRDAHVAPEGELERAMAAIWSEVLKLGHIGRD 1046
Cdd:PRK10252   924 ---ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPE-LKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDAD 999
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1047 DNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVA---QLAPAAQGGIVRCARDAS-PQLSFAQERQW 1122
Cdd:PRK10252  1000 ADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDaeeDESRRLGFGTILPLREGDgPTLFCFHPASG 1079
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 1123 FIW-------RLDPHSAAYNIPvALRLKGPLrrdALQGALDLLVQRH-ETLRT 1167
Cdd:PRK10252  1080 FAWqfsvlsrYLDPQWSIYGIQ-SPRPDGPM---QTATSLDEVCEAHlATLLE 1128
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
524-1007 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 600.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLerlvhGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA-----AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE 763
Cdd:cd12116    156 HSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLlRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSARFRLGEEARPF-LGGPLENTALYILDSEMNPCPP 842
Cdd:cd12116    236 WQGR-AGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIpIGRPLANTQVYVLDAALRPVPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  843 GVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETR 922
Cdd:cd12116    315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  923 LLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:cd12116    395 LAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA-----ALRAHLRAT----LPAYMVPSAFVRLDALPLTANGKL 465

                   ....*
gi 2183974163 1003 NRKAL 1007
Cdd:cd12116    466 DRKAL 470
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1582-2071 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 589.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRaarerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd05930     81 EDSGAKLVLTDP-------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvac 1821
Cdd:cd05930    124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ--- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPLALRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGaASPIGEPIPDLSWY 1901
Cdd:cd05930    201 ELELAALPSLRLVLVGGEALPPDLVRRWRELLPGA--RLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVY 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd05930    278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAAPSDPAAlrdTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd05930    357 YRIELGEIEAALLAHPGVREAAVVAREdGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPL 433
                          490
                   ....*....|.
gi 2183974163 2061 TANGKLDRRAL 2071
Cdd:cd05930    434 TPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
524-1007 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 583.72  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd05930     81 EDSGAKLVLTD--------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRML---C 760
Cdd:cd05930    123 LWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLlqeL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  761 DSERVDLLRgcTLLCGGEALAEDLAARMRGLSAST--WNLYGPTETTIWSARFRLGEEARPF----LGGPLENTALYILD 834
Cdd:cd05930    203 ELAALPSLR--LVLVGGEALPPDLVRRWRELLPGArlVNLYGPTEATVDATYYRVPPDDEEDgrvpIGRPIPNTRVYVLD 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  835 SEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 914
Cdd:cd05930    281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF-GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  915 ELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLEN 993
Cdd:cd05930    360 ELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEE-----ELRAHLAER----LPDYMVPSAFVVLDA 430
                          490
                   ....*....|....
gi 2183974163  994 LPLTPNGKINRKAL 1007
Cdd:cd05930    431 LPLTPNGKVDRKAL 444
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1572-2071 1.26e-177

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 555.27  E-value: 1.26e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLTQRAARERLPlgeGLPCLLLDAEHeWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLL 1731
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAG---GLEVAVVIDEA-LDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1732 PHGNVLRLFDATRhWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPS 1811
Cdd:cd12117    157 THRGVVRLVKNTN-YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1812 AFKQLmqvacAGQEVPPLA-LRHVVFGGEALEVQALRPWFERFGDraPRLVNMYGITETTVHVTYRPLSLADLDGGAAsP 1890
Cdd:cd12117    236 LFNQL-----ADEDPECFAgLRELLTGGEVVSPPHVRRVLAACPG--LRLVNGYGPTENTTFTTSHVVTELDEVAGSI-P 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1891 IGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsTTGGRLYRTGDLARYRCDGVVEYV 1970
Cdd:cd12117    308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFL 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1971 GRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEG-PGATQLVGYVVTQAAPSDpaalrDTLRQALKASLPEHMVP 2049
Cdd:cd12117    387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLVAYVVAEGALDA-----AELRAFLRERLPAYMVP 461
                          490       500
                   ....*....|....*....|..
gi 2183974163 2050 AHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd12117    462 AAFVVLDELPLTANGKVDRRAL 483
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1114-2152 1.65e-177

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 585.47  E-value: 1.65e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE--- 1190
Cdd:PRK10252    10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEiid 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 -RRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLL-LPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPP 1268
Cdd:PRK10252    90 lRTQPDPHAAAQALMQADLQQDLRVDSGKPLVFHQlIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1269 ALAELPiQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALrrLAQA 1348
Cdd:PRK10252   170 PASPFT-PFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQL--AAQA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1349 EQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGH 1428
Cdd:PRK10252   247 SGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRH 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1429 QDLPFEQLVDAL---QPERSLsHAPLFQVMYNHQRDDHRG--SRFASLGELEVEDLAwdvqtaqFDLTLDtyeSSNGLLA 1503
Cdd:PRK10252   327 QRYDAEQIVRDSgraAGDEPL-FGPVLNIKVFDYQLDFPGvqAQTHTLATGPVNDLE-------LALFPD---EHGGLSI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1504 ELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEArADLLQWNPGPQDFtPASCLHRLIERQAAERPR 1583
Cdd:PRK10252   396 EILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEI-PETTLSALVAQQAAKTPD 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1584 ATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIED 1663
Cdd:PRK10252   474 APALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1664 SGIRLLLTQRAARERLPLGEGLPCLLLDAehEWAGyPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDAT 1743
Cdd:PRK10252   554 ARPSLLITTADQLPRFADVPDLTSLCYNA--PLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1744 RHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPS---AFkqLMQVA 1820
Cdd:PRK10252   631 QNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSmlaAF--VASLT 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1821 CAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdrAPrLVNMYGITETTVHVTYRPLSLADLDG--GAASPIGEPIPDL 1898
Cdd:PRK10252   709 PEGARQSCASLRQVFCSGEALPADLCREWQQLTG--AP-LHNLYGPTEAAVDVSWYPAFGEELAAvrGSSVPIGYPVWNT 785
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYVGRIDHQVK 1978
Cdd:PRK10252   786 GLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLK 864
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1979 IRGFRIELGEIEARLLAQPGVAEAVVL-------PHEGPGATQLVGYVVTQaapSDPAALRDTLRQALKASLPEHMVPAH 2051
Cdd:PRK10252   865 IRGQRIELGEIDRAMQALPDVEQAVTHacvinqaAATGGDARQLVGYLVSQ---SGLPLDTSALQAQLRERLPPHMVPVV 941
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2052 LLFLERLPLTANGKLDRRALPAPDASRlQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRAR 2131
Cdd:PRK10252   942 LLQLDQLPLSANGKLDRKALPLPELKA-QVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLS 1020
                         1050      1060
                   ....*....|....*....|..
gi 2183974163 2132 QA-GIRLAPRDLFLHQTIRGLA 2152
Cdd:PRK10252  1021 RQfARQVTPGQVMVASTVAKLA 1042
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
524-1008 1.39e-172

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 539.65  E-value: 1.39e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd17649     81 EDSGAGLLLTH-------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE 763
Cdd:cd17649    124 QATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEA 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDL------LRGCTLlcGGEALAEDLAARMRGLSASTWNLYGPTETTI----WSARFRLGEE-ARPFLGGPLENTALYI 832
Cdd:cd17649    204 DRTGdgrppsLRLYIF--GGEALSPELLRRWLKAPVRLFNAYGPTEATVtplvWKCEAGAARAgASMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  833 LDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 912
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  913 RIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPteaalvdAESARQQELRSALKNSLLAVLPDYMVPAHMLLLE 992
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVL-------RAAAAQPELRAQLRTALRASLPDYMVPAHLVFLA 434
                          490
                   ....*....|....*.
gi 2183974163  993 NLPLTPNGKINRKALP 1008
Cdd:cd17649    435 RLPLTPNGKLDRKALP 450
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1582-2072 1.17e-171

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 536.95  E-value: 1.17e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAarerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17649     81 EDSGAGLLLTHHP------------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPLALRHVVFGGEALEVQALRPWFERfgdrAPRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWY 1901
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWLKA----PVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAY 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd17649    281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPaALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:cd17649    361 FRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQP-ELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
                          490
                   ....*....|.
gi 2183974163 2062 ANGKLDRRALP 2072
Cdd:cd17649    440 PNGKLDRKALP 450
PRK05691 PRK05691
peptide synthase; Validated
1127-2156 2.02e-168

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 587.91  E-value: 2.02e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1127 LDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDG-APRQVIHPTLPIAIEE---RRPPVAGED--L 1200
Cdd:PRK05691  3273 LEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGeTMLQVIHKPGRTPIDYldwRGLPEDGQEqrL 3352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1201 KGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAELPiQYADF 1280
Cdd:PRK05691  3353 QALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPP-RYRDY 3431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1281 AAW-QRQwmdGGERERQldYWVSRLGGEQPLLELPSDRP--RPQQQSHRGRRIG---IPLPAELAEALRRLAQAEQGTLF 1354
Cdd:PRK05691  3432 IGWlQRQ---DLAQARQ--WWQDNLRGFERPTPIPSDRPflREHAGDSGGMVVGdcyTRLDAADGARLRELAQAHQLTVN 3506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1355 MLLLASFQALLHRYSGQNDIRVGVPIANRNRE--ETEGLIGFFVNTQVLRAEL--DGQ-LPFRELLRQVRQAVVEAQGHQ 1429
Cdd:PRK05691  3507 TFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVQLpaAGQrCSVRQWLQGLLDSNMELREYE 3586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1430 DLPfeqLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRFASLGELEVEDLAWDVQTaQFDLTLDTYESSNgLLAELTYAT 1509
Cdd:PRK05691  3587 YLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHT-NFPLTAVCYPGDD-LGLHLSYDQ 3661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1510 DLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQWNPGPQDFTPASCLHRLIERQAAERPRATAVVY 1589
Cdd:PRK05691  3662 RYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASC 3741
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1590 GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLL 1669
Cdd:PRK05691  3742 LDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVL 3821
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1670 LTQRAARER-LPLGEGLPC-----LLLDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDAT 1743
Cdd:PRK05691  3822 VCSAACREQaRALLDELGCanrprLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSK 3901
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1744 RHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSafkqLMQVACAG 1823
Cdd:PRK05691  3902 VPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPS----LIQGMLAE 3977
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1824 QEVPPLALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGgAASPIGEPIPDLSWYLL 1903
Cdd:PRK05691  3978 DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIG--LVNAYGPAECSDDVAFFRVDLASTRG-SYLPIGSPTDNNRLYLL 4054
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1904 DAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFR 1983
Cdd:PRK05691  4055 DEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYR 4134
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1984 IELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTAN 2063
Cdd:PRK05691  4135 IELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNAN 4214
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2064 GKLDRRALPAPDASRLQ-RDYTAPRSELEQRLAAIWADVLKLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAP-RD 2141
Cdd:PRK05691  4215 GKLDRKALPALDIGQLQsQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPlRA 4294
                         1050      1060
                   ....*....|....*....|..
gi 2183974163 2142 LF-------LHQTIRGLAGVAV 2156
Cdd:PRK05691  4295 MFecstveeLAEYIEGLAGSAI 4316
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1571-2071 4.16e-168

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 528.38  E-value: 4.16e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1571 HRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDP 1650
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1651 RYPSDRLGYMIEDSGIRLLLTQRAARERLPlgeGLPCLLLDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTL 1730
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1731 LPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTP 1810
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1811 SAFKQLMQVACAGQEVpplALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVTYRPLSLADLDGGAasP 1890
Cdd:cd17646    238 SMLRVFLAEPAAGSCA---SLRRVFCSGEALPPELAARFLALPG---AELHNLYGPTEAAIDVTHWPVRGPAETPSV--P 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1891 IGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYV 1970
Cdd:cd17646    310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1971 GRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGP-GATQLVGYVVTQAAPSDPAAlrDTLRQALKASLPEHMVP 2049
Cdd:cd17646    389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPaGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVP 466
                          490       500
                   ....*....|....*....|..
gi 2183974163 2050 AHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd17646    467 AAFVVLDALPLTANGKLDRAAL 488
PRK05691 PRK05691
peptide synthase; Validated
36-1099 1.19e-167

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 585.21  E-value: 1.19e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   36 LPIPevASAFERI-PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQldgf 114
Cdd:PRK05691  3247 LPVP--AAEIEDVyPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAG---- 3320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  115 rQQVLASVDVPVPVTL------AGDDDAQAQ-IRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWS 187
Cdd:PRK05691  3321 -ETMLQVIHKPGRTPIdyldwrGLPEDGQEQrLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWC 3399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  188 MRVLVEELIALYGARRQGIEATLPDLPiQYADYAIW-QRHWLEAGERerqleYWMARLGGGQSVLELPTDRqrPALPSYR 266
Cdd:PRK05691  3400 RSLLMNDFFEIYTALGEGREAQLPVPP-RYRDYIGWlQRQDLAQARQ-----WWQDNLRGFERPTPIPSDR--PFLREHA 3471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  267 GARHELQ-------LPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANR--NRVETERLIGFFVN 337
Cdd:PRK05691  3472 GDSGGMVvgdcytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFIN 3551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  338 TQVLRADL---DAQMPFLDLLQQTRVAALGAQSHQDLPfeqLVeALQPERSLSH-SPLFQAMYNHQNlgSAGRQSLAAQL 413
Cdd:PRK05691  3552 SIALRVQLpaaGQRCSVRQWLQGLLDSNMELREYEYLP---LV-AIQECSELPKgQPLFDSLFVFEN--APVEVSVLDRA 3625
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  414 PGLSVEDLSWGAHSaQFDLTLDTYESEQ-GVHaeFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEER 492
Cdd:PRK05691  3626 QSLNASSDSGRTHT-NFPLTAVCYPGDDlGLH--LSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQER 3702
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  493 ATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVP 572
Cdd:PRK05691  3703 DFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLD 3782
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  573 MVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQS-------VLARLPQSDGLQSLLLDDLERlvHGYPAE 645
Cdd:PRK05691  3783 LLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcreqaraLLDELGCANRPRLLVWEEVQA--GEVASH 3860
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  646 NPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLE-LYVPLArGASML 724
Cdd:PRK05691  3861 NPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQfLAAPLF-GARVE 3939
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  725 LASREQAQDPEALLDLVERQGVTVLQATPA-TWRMLC-DSERVDLLRgcTLLCGGEALAEDLAAR--MRGLSASTWNLYG 800
Cdd:PRK05691  3940 IVPNAIAHDPQGLLAHVQAQGITVLESVPSlIQGMLAeDRQALDGLR--WMLPTGEAMPPELARQwlQRYPQIGLVNAYG 4017
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  801 PTETTIWSARFRLGEEAR-----PfLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPF 875
Cdd:PRK05691  4018 PAECSDDVAFFRVDLASTrgsylP-IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPF 4096
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  876 AADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAA 955
Cdd:PRK05691  4097 GAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTV 4176
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  956 LVDAesarqqELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASAVRD-AHVAPEGELERAMAAIW 1034
Cdd:PRK05691  4177 LAQG------ALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSqAYLAPRNELEQTLATIW 4250
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 1035 SEVLKLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAA 1099
Cdd:PRK05691  4251 ADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGSA 4315
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1574-2072 1.27e-166

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 524.22  E-value: 1.27e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP 1653
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1654 SDRLGYMIEDSGIRLLLTQRAARERLPlGEGLPCLLLDAEhEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPH 1733
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELA-VELVAVTLLDQP-GAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1734 GNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAF 1813
Cdd:cd17651    159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLMQVAcAGQEVPPLALRHVVFGGEALEV-QALRPWFERFgdRAPRLVNMYGITETTVhVTYRPLSLADLDGGAASPIG 1892
Cdd:cd17651    239 RALAEHG-RPLGVRLAALRYLLTGGEQLVLtEDLREFCAGL--PGLRLHNHYGPTETHV-VTALSLPGDPAAWPAPPPIG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1893 EPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYVGR 1972
Cdd:cd17651    315 RPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGR 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1973 IDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAAPSDPAAlrdTLRQALKASLPEHMVPAH 2051
Cdd:cd17651    394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSA 470
                          490       500
                   ....*....|....*....|.
gi 2183974163 2052 LLFLERLPLTANGKLDRRALP 2072
Cdd:cd17651    471 FVLLDALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1596-2004 9.09e-166

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 517.97  E-value: 9.09e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIEL-GVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRA 1674
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1675 ARERLPlGEGLPCLLLDAEHEWAGYPESD---PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSA 1751
Cdd:TIGR01733   82 LASRLA-GLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRER-VTVLNQTPSAFKQLMQVACAgqevPPLA 1830
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPP----ALAS 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 LRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSWYLLDAGLNPV 1910
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGPGA--RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPV 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1911 PRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTT-GGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEI 1989
Cdd:TIGR01733  315 PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
                          410
                   ....*....|....*
gi 2183974163 1990 EARLLAQPGVAEAVV 2004
Cdd:TIGR01733  395 EAALLRHPGVREAVV 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1572-2075 1.91e-165

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 520.73  E-value: 1.91e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLTQRAARERLpLGEGLpCLLLDaEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLL 1731
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPPI-AFIGL-IDLLD-EDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1732 PHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPS 1811
Cdd:cd17655    158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1812 AFKQLMQVacagQEVPPLALRHVVFGGEALEVQALRPWFERFGDrAPRLVNMYGITETTVHVTYRPLSLADlDGGAASPI 1891
Cdd:cd17655    238 HLKLLDAA----DDSEGLSLKHLIVGGEALSTELAKKIIELFGT-NPTITNAYGPTETTVDASIYQYEPET-DQQVSVPI 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1892 GEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsTTGGRLYRTGDLARYRCDGVVEYVG 1971
Cdd:cd17655    312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEG-PGATQLVGYVVtqaapSDPAALRDTLRQALKASLPEHMVPA 2050
Cdd:cd17655    391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDeQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPS 465
                          490       500
                   ....*....|....*....|....*
gi 2183974163 2051 HLLFLERLPLTANGKLDRRALPAPD 2075
Cdd:cd17655    466 YFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
514-1011 5.51e-165

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 519.58  E-value: 5.51e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQ 593
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSQQSVLARLpqsDGLQSLLLDDLERLVHGyPAENPDLPEAPDSLCYAIYTSGSTGQPKGVM 673
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPPI---AFIGLIDLLDEDTIYHE-ESENLEPVSKSDDLAYVIYTSGSTGKPKGVM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  674 VRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATP 753
Cdd:cd17655    157 IEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  754 ATWRMLcdsERVDLLRGC---TLLCGGEALAEDLAAR---MRGLSASTWNLYGPTETTIWSARFRLGEEAR----PFLGG 823
Cdd:cd17655    237 AHLKLL---DAADDSEGLslkHLIVGGEALSTELAKKiieLFGTNPTITNAYGPTETTVDASIYQYEPETDqqvsVPIGK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  824 PLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRI 903
Cdd:cd17655    314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVP-GERMYRTGDLARWLPDGNIEFLGRI 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  904 DHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTeaalvdaESARQQELRSALKNSllavLPDY 982
Cdd:cd17655    393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGqNYLCAYIVSE-------KELPVAQLREFLARE----LPDY 461
                          490       500
                   ....*....|....*....|....*....
gi 2183974163  983 MVPAHMLLLENLPLTPNGKINRKALPLPD 1011
Cdd:cd17655    462 MIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1582-2071 1.37e-163

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 514.53  E-value: 1.37e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAARERLPLGEGLPCLLLDAehewAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAA----AAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvac 1821
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD--- 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEvpPLALRHVVFGGEALEVQALrpwfERFGDRAPRLVNMYGITETTVHVTYRPLSLADldggAASPIGEPIPDLSWY 1901
Cdd:cd12116    234 AGWQ--GRAGLTALCGGEALPPDLA----ARLLSRVGSLWNLYGPTETTIWSTAARVTAAA----GPIPIGRPLANTQVY 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd12116    304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVtqaAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:cd12116    384 HRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVV---LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLT 460
                          490
                   ....*....|
gi 2183974163 2062 ANGKLDRRAL 2071
Cdd:cd12116    461 ANGKLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1582-2072 3.44e-163

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 511.80  E-value: 3.44e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQraarerlplgeglpcllldaehewagypesdpqsavgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17652     81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLmqvac 1821
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL----- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPLalRHVVFGGEALEVQALRPWferfgdrAP--RLVNMYGITETTVHVTYRPLsladLDGGAASPIGEPIPDLS 1899
Cdd:cd17652    199 PPDDLPDL--RTLVVAGEACPAELVDRW-------APgrRMINAYGPTETTVCATMAGP----LPGGGVPPIGRPVPGTR 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1900 WYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKI 1979
Cdd:cd17652    266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1980 RGFRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAAPSDPAAlrdTLRQALKASLPEHMVPAHLLFLERL 2058
Cdd:cd17652    346 RGFRIELGEVEAALTEHPGVAEAVVVVRDdRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYMVPAAFVVLDAL 422
                          490
                   ....*....|....
gi 2183974163 2059 PLTANGKLDRRALP 2072
Cdd:cd17652    423 PLTPNGKLDRRALP 436
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
513-1007 2.84e-162

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 511.44  E-value: 2.84e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  513 HRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDP 592
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  593 QYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERlvhgYPAENPDLPEAPDSLCYAIYTSGSTGQPKGV 672
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAA----PPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  673 MVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQAT 752
Cdd:cd17646    157 MVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  753 PATWRMLCDSERVDLLRGCTL-LCGGEALAEDLAARMRGLS-ASTWNLYGPTETTIWSARFRL-GEEARPFL--GGPLEN 827
Cdd:cd17646    237 PSMLRVFLAEPAAGSCASLRRvFCSGEALPPELAARFLALPgAELHNLYGPTEAAIDVTHWPVrGPAETPSVpiGRPVPN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  828 TALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRIDHQV 907
Cdd:cd17646    317 TRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGP-GSRMYRTGDLARWRPDGALEFLGRSDDQV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  908 KIRGFRIELGEIETRLLEQDSVREAVVVAQ-PGVAGPTLVAYLVPTEaalvDAESARQQELRSALKnsllAVLPDYMVPA 986
Cdd:cd17646    396 KIRGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAA----GAAGPDTAALRAHLA----ERLPEYMVPA 467
                          490       500
                   ....*....|....*....|.
gi 2183974163  987 HMLLLENLPLTPNGKINRKAL 1007
Cdd:cd17646    468 AFVVLDALPLTANGKLDRAAL 488
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
514-1007 4.84e-162

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 510.59  E-value: 4.84e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQ 593
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSQQSVLARLpqsDGLQSLLLDDLERLvhGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVM 673
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRA---GGLEVAVVIDEALD--AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  674 VRHRALTNFVCSiARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATP 753
Cdd:cd12117    156 VTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  754 ATWRMLCDsERVDLLRGC-TLLCGGEALAEDLAARMRGLSAST--WNLYGPTETTIWSARFRLGEEA----RPFLGGPLE 826
Cdd:cd12117    235 ALFNQLAD-EDPECFAGLrELLTGGEVVSPPHVRRVLAACPGLrlVNGYGPTENTTFTTSHVVTELDevagSIPIGRPIA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaADGSRLYRTGDLARYRADGVIEYLGRIDHQ 906
Cdd:cd12117    314 NTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFLGRIDDQ 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPTEAalVDAEsarqqELRSALKnsllAVLPDYMVP 985
Cdd:cd12117    393 VKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKrLVAYVVAEGA--LDAA-----ELRAFLR----ERLPAYMVP 461
                          490       500
                   ....*....|....*....|..
gi 2183974163  986 AHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd12117    462 AAFVVLDELPLTANGKVDRRAL 483
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2174-2601 2.59e-161

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 506.02  E-value: 2.59e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEVLLWQQS 2253
Cdd:cd19534      3 PLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEVVD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2254 V---ADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALP 2330
Cdd:cd19534     83 LsslAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2331 AKTSaFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELPCDDregAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQ 2410
Cdd:cd19534    163 SKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDP---EQTYGDARTVSFTLDEEETEALLQEANAAYRTE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2411 VNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLTRTVGWFTSLFPLRLSPVA--ELGASIKRIKEQLRAIPHK 2488
Cdd:cd19534    239 INDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLRRIPNK 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2489 GLGFGALRYLgSAEDRAALAALPSPRITFNYLGQFDGSFSADssALFRPSADAAGSERDSDAPLDNWLSLNGQVYAGRLG 2568
Cdd:cd19534    319 GIGYGILRYL-TPEGTKRLAFHPQPEISFNYLGQFDQGERDD--ALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLV 395
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163 2569 IDWSFSAARFSEASILRLADAYRDELLALIEHC 2601
Cdd:cd19534    396 ITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1569-2072 1.78e-157

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 496.96  E-value: 1.78e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1569 CLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPL 1648
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1649 DPRYPSDRLGYMIEDSGIRLLLTQraarerlplgeglpcllldaehewagyPEsdpqsavgvdNLAYVIYTSGSTGKPKG 1728
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ---------------------------PE----------NLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1729 TLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQ 1808
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1809 TPSAFKQLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDRaPRLVNMYGITETTVHVTYRPLSLADLDGGAA 1888
Cdd:cd17644    204 PPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNF-IQLINVYGPTEATIAATVCRLTQLTERNITS 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1889 SPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPF-STTGGRLYRTGDLARYRCDGVV 1967
Cdd:cd17644    283 VPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNI 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1968 EYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEG-PGATQLVGYVVtqaAPSDPAALRDTLRQALKASLPEH 2046
Cdd:cd17644    363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDY 439
                          490       500
                   ....*....|....*....|....*.
gi 2183974163 2047 MVPAHLLFLERLPLTANGKLDRRALP 2072
Cdd:cd17644    440 MIPSAFVVLEELPLTPNGKIDRRALP 465
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
516-1008 4.36e-156

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 493.78  E-value: 4.36e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  516 FEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYP 595
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  596 ADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQslLLDDLERLVHGYPAEnPDLPEAPDSLCYAIYTSGSTGQPKGVMVR 675
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVAV--TLLDQPGAAAGADAE-PDPALDADDLAYVIYTSGSTGRPKGVVMP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 HRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPAT 755
Cdd:cd17651    158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  756 WRMLCDSERVDLLRGCTL---LCGGEAL--AEDLAARMRGLSASTW-NLYGPTETTIWSARFRLGE----EARPFLGGPL 825
Cdd:cd17651    238 LRALAEHGRPLGVRLAALrylLTGGEQLvlTEDLREFCAGLPGLRLhNHYGPTETHVVTALSLPGDpaawPAPPPIGRPI 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  826 ENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRIDH 905
Cdd:cd17651    318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADD 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  906 QVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTEAALVDAEsarqqELRSALKnsllAVLPDYMV 984
Cdd:cd17651    397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGDPEAPVDAA-----ELRAALA----THLPEYMV 467
                          490       500
                   ....*....|....*....|....
gi 2183974163  985 PAHMLLLENLPLTPNGKINRKALP 1008
Cdd:cd17651    468 PSAFVLLDALPLTPNGKLDRRALP 491
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2638-3052 1.52e-155

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 489.41  E-value: 1.52e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGaLEKPLQLVRKRVEVPFS 2716
Cdd:cd19543      2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEG-LGEPLQVVLKDRKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2717 VHDWRDRADLAEALDALAAGEAGL--GFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYR---- 2790
Cdd:cd19543     81 ELDLSHLSEAEQEAELEALAEEDRerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalge 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2791 GETPSR-SDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQRLAEFAREQ 2869
Cdd:cd19543    161 GQPPSLpPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQH 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2870 KVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLALRE 2949
Cdd:cd19543    241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2950 FEHTPLYDIQRWAGQvGEALFDNILVFENYPVSAALAEETPAD-MRIDALSNQEQTHYPLTLLVSAGETLELHYSYSRQA 3028
Cdd:cd19543    321 HEYVPLYEIQAWSEG-KQALFDHLLVFENYPVDESLEEEQDEDgLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAEV 399
                          410       420
                   ....*....|....*....|....
gi 2183974163 3029 FDEAAIECLAERLERLLLGMCENP 3052
Cdd:cd19543    400 FDEATIERLLGHLRRVLEQVAANP 423
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
537-934 1.24e-153

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 483.31  E-value: 1.24e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  537 SYAELNALANRLAWRLREE-GVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ 615
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SVLARLPQSDGLQSLLLDDLERLVHGYPAEN-PDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLA 694
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPpPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  695 RDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQG-VTVLQATPATWRMLCDSERVDLLRGCTL 773
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  774 LCGGEALAEDLAARMRGLSAST--WNLYGPTETTIWSARFRL------GEEARPfLGGPLENTALYILDSEMNPCPPGVA 845
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGArlINLYGPTETTVWSTATLVdpddapRESPVP-IGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  846 GELLIGGDGLARGYHRRPGLTAERFLPDPFAA-DGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLL 924
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 2183974163  925 EQDSVREAVV 934
Cdd:TIGR01733  400 RHPGVREAVV 409
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
47-477 6.43e-151

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 476.53  E-value: 6.43e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVL--ASVDV 124
Cdd:cd19540      1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDD--GGPYQVVLpaAEARP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  125 PVPVTLAGDDDAQAQIRAFVEsetqQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQ 204
Cdd:cd19540     79 DLTVVDVTEDELAARLAEAAR----RGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  205 GIEATLPDLPIQYADYAIWQRHWLEAGER-----ERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALG 279
Cdd:cd19540    155 GRAPDWAPLPVQYADYALWQRELLGDEDDpdslaARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELH 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  280 RQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTR 359
Cdd:cd19540    235 ARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVR 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  360 VAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAgrqslAAQLPGLSVEDLSWGAHSAQFDLTL----- 434
Cdd:cd19540    315 ETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAA-----TLELPGLTVEPVPVDTGVAKFDLSFtlter 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2183974163  435 -DTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19540    390 rDADGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
524-1008 8.05e-151

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 476.36  E-value: 8.05e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd17652     81 ADARPALLLTT--------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLcdsE 763
Cdd:cd17652    123 AAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL---P 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLLRGCTLLCGGEALAEDLAARmrglsastW-------NLYGPTETTIWSARFR-LGEEARPFLGGPLENTALYILDS 835
Cdd:cd17652    200 PDDLPDLRTLVVAGEACPAELVDR--------WapgrrmiNAYGPTETTVCATMAGpLPGGGVPPIGRPVPGTRVYVLDA 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  836 EMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 915
Cdd:cd17652    272 RLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  916 LGEIETRLLEQDSVREAVVVAQ-PGVAGPTLVAYLVPTEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLENL 994
Cdd:cd17652    352 LGEVEAALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPTAA-----ELRAHLAER----LPGYMVPAAFVVLDAL 422
                          490
                   ....*....|....
gi 2183974163  995 PLTPNGKINRKALP 1008
Cdd:cd17652    423 PLTPNGKLDRRALP 436
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1114-1535 8.91e-148

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 467.28  E-value: 8.91e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEERRP 1193
Cdd:cd19540      4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLTVV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1194 PVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAEL 1273
Cdd:cd19540     84 DVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1274 PIQYADFAAWQRQWMdGGERE------RQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQ 1347
Cdd:cd19540    164 PVQYADYALWQRELL-GDEDDpdslaaRQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAR 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQG 1427
Cdd:cd19540    243 EHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1428 HQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGsrfASLGELEVEDLAWDVQTAQFDLTL------DTYESSNGL 1501
Cdd:cd19540    323 HQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAT---LELPGLTVEPVPVDTGVAKFDLSFtlterrDADGAPAGL 399
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2183974163 1502 LAELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19540    400 TGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
512-1008 1.98e-147

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 468.07  E-value: 1.98e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKG 671
Cdd:cd17644     82 PNYPQERLTYILEDAQISVLLTQ--------------------------------------PENLAYVIYTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQA 751
Cdd:cd17644    124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDS---ERVDLLRGCTL-LCGGEALAEDLA---ARMRGLSASTWNLYGPTETTIWSARFRL-----GEEARP 819
Cdd:cd17644    204 PPAYWHLLVLElllSTIDLPSSLRLvIVGGEAVQPELVrqwQKNVGNFIQLINVYGPTEATIAATVCRLtqlteRNITSV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 FLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFA-ADGSRLYRTGDLARYRADGVIE 898
Cdd:cd17644    284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsSESERLYKTGDLARYLPDGNIE 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  899 YLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTEAALVDAEsarqqELRSALKNSlla 977
Cdd:cd17644    364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGnKRLVAYIVPHYEESPSTV-----ELRQFLKAK--- 435
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2183974163  978 vLPDYMVPAHMLLLENLPLTPNGKINRKALP 1008
Cdd:cd17644    436 -LPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
524-1007 8.31e-146

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 462.55  E-value: 8.31e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd17643     81 ADSGPSLLLTD--------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE 763
Cdd:cd17643    123 AATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAA 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLLRGCTL---LCGGEALA----EDLAARMRGLSASTWNLYGPTETTIWSARFRLGEE-----ARPFLGGPLENTALY 831
Cdd:cd17643    203 DRDGRDPLALryvIFGGEALEaamlRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAAdlpaaAASPIGRPLPGLRVY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  832 ILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRG 911
Cdd:cd17643    283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  912 FRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPTEAalvdaesarQQELRSALKNSLLAVLPDYMVPAHMLL 990
Cdd:cd17643    363 FRIELGEIEAALATHPSVRDAAVIVREDEPGDTrLVAYVVADDG---------AAADIAELRALLKELLPDYMVPARYVP 433
                          490
                   ....*....|....*..
gi 2183974163  991 LENLPLTPNGKINRKAL 1007
Cdd:cd17643    434 LDALPLTVNGKLDRAAL 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1570-2071 4.01e-142

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 451.77  E-value: 4.01e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQRaarerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGT 1729
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTDP-------------------------------------DDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1730 LLPHGNVLRLFDATRHwfGFSADDAWSLFH--SYAFDFSVWEIFGALLHGGRLVIVpyETSRSPEDFLRllcRERVTVLN 1807
Cdd:cd12115    124 AIEHRNAAAFLQWAAA--AFSAEELAGVLAstSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLPA---AAEVTLIN 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1808 QTPSAFKQLMQvacagQEVPPLALRHVVFGGEALEVQALRPWFERfgDRAPRLVNMYGITETTVHVTYRPLSLADLDgga 1887
Cdd:cd12115    197 TVPSAAAELLR-----HDALPASVRVVNLAGEPLPRDLVQRLYAR--LQVERVVNLYGPSEDTTYSTVAPVPPGASG--- 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1888 ASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTtGGRLYRTGDLARYRCDGVV 1967
Cdd:cd12115    267 EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPDGLL 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1968 EYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQAApsdPAALRDTLRQALKASLPEH 2046
Cdd:cd12115    346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAY 422
                          490       500
                   ....*....|....*....|....*
gi 2183974163 2047 MVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd12115    423 MVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1570-2071 3.82e-139

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 444.68  E-value: 3.82e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTqraarerlplgeglpcllldaehewagypeSDPqsavgvDNLAYVIYTSGSTGKPKGT 1729
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLT------------------------------SSP------SDAAYVIFTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1730 LLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGrLVIVPYETSRsPEDFLRLLCRERVTVLNQT 1809
Cdd:cd05918    125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG-CLCIPSEEDR-LNDLAGFINRLRVTWAFLT 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1810 PSAFKQLMQvacagQEVPPLalRHVVFGGEALEVQALRPWferfGDRApRLVNMYGITETTVHVTYRPlslaDLDGGAAS 1889
Cdd:cd05918    203 PSVARLLDP-----EDVPSL--RTLVLGGEALTQSDVDTW----ADRV-RLINAYGPAECTIAATVSP----VVPSTDPR 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1890 PIGEPIPDLSWyLLDAGLN--PVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPF------STTGGRLYRTGDLARY 1961
Cdd:cd05918    267 NIGRPLGATCW-VVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRY 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1962 RCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE----AVVLPHEGPGATQLVGYVV-----TQAAPSDPAALR 2032
Cdd:cd05918    346 NPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvvEVVKPKDGSSSPQLVAFVVldgssSGSGDGDSLFLE 425
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 2033 DT---------LRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05918    426 PSdefralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
512-1007 1.34e-138

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 441.76  E-value: 1.34e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKG 671
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTD--------------------------------------PDDLAYVIYTSGSTGRPKG 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLAsreqaQDPEALLDLVERQGVTVLQA 751
Cdd:cd12115    123 VAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINT 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDSErvDLLRGCTLLC-GGEALAEDLAARMRGLS--ASTWNLYGPTETTIWS--ARFRLGEEARPFLGGPLE 826
Cdd:cd12115    198 VPSAAAELLRHD--ALPASVRVVNlAGEPLPRDLVQRLYARLqvERVVNLYGPSEDTTYStvAPVPPGASGEVSIGRPLA 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRIDHQ 906
Cdd:cd12115    276 NTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPteaalvdaeSARQQELRSALKNSLLAVLPDYMVP 985
Cdd:cd12115    355 VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGeRRLVAYIVA---------EPGAAGLVEDLRRHLGTRLPAYMVP 425
                          490       500
                   ....*....|....*....|..
gi 2183974163  986 AHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd12115    426 SRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1582-2071 2.59e-135

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 432.28  E-value: 2.59e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQraarerlplgeglpcllldaehewagyPEsdpqsavgvdNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17650     81 EDSGAKLLLTQ---------------------------PE----------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSL-FHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVa 1820
Cdd:cd17650    124 AWRREYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1821 CAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDRApRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSW 1900
Cdd:cd17650    203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGM-RIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAM 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1901 YLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIR 1980
Cdd:cd17650    282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1981 GFRIELGEIEARLLAQPGVAEAVV-LPHEGPGATQLVGYVVTQAAPsDPAALRDTLRQalkaSLPEHMVPAHLLFLERLP 2059
Cdd:cd17650    361 GFRIELGEIESQLARHPAIDEAVVaVREDKGGEARLCAYVVAAATL-NTAELRAFLAK----ELPSYMIPSYYVQLDALP 435
                          490
                   ....*....|..
gi 2183974163 2060 LTANGKLDRRAL 2071
Cdd:cd17650    436 LTPNGKVDRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
524-1007 3.85e-135

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 431.89  E-value: 3.85e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd17650     81 EDSGAKLLLTQ--------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARD-RLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRML--- 759
Cdd:cd17650    123 HAWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVmay 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  760 CDSERVDLLRGCTLLCGGEA--------LAEDLAARMRglsasTWNLYGPTETTIWSARF-----RLGEEARPFLGGPLE 826
Cdd:cd17650    203 VYRNGLDLSAMRLLIVGSDGckaqdfktLAARFGQGMR-----IINSYGVTEATIDSTYYeegrdPLGDSANVPIGRPLP 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRIDHQ 906
Cdd:cd17650    278 NTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP-GERMYRTGDLARWRADGNVELLGRVDHQ 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPteaalvdAESARQQELRSALKNSllavLPDYMVP 985
Cdd:cd17650    357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEArLCAYVVA-------AATLNTAELRAFLAKE----LPSYMIP 425
                          490       500
                   ....*....|....*....|..
gi 2183974163  986 AHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd17650    426 SYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
524-1007 1.15e-134

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 431.69  E-value: 1.15e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERlvhgyPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAA-----PAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE 763
Cdd:cd12114    156 LDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLLRGCTL---LCGGEALAEDLAARMRGLSAST--WNLYGPTETTIWSARFRLGEEAR-----PFlGGPLENTALYIL 833
Cdd:cd12114    236 EAAQALLPSLrlvLLSGDWIPLDLPARLRALAPDArlISLGGATEASIWSIYHPIDEVPPdwrsiPY-GRPLANQRYRVL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  834 DSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPfaaDGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFR 913
Cdd:cd12114    315 DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYR 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  914 IELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEaalvDAESARQQELRSALKnsllAVLPDYMVPAHMLLLEN 993
Cdd:cd12114    392 IELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDN----DGTPIAPDALRAFLA----QTLPAYMIPSRVIALEA 463
                          490
                   ....*....|....
gi 2183974163  994 LPLTPNGKINRKAL 1007
Cdd:cd12114    464 LPLTANGKVDRAAL 477
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1582-2071 4.38e-132

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 424.38  E-value: 4.38e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEWAGYPESDPQSavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP----DDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAC 1821
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPlALRHVVFGGEALEVQALRPWFERFGDraPRLVNMYGITETTVHVTYRPLslADLDGGAAS-PIGEPIPDLSW 1900
Cdd:cd12114    237 AAQALLP-SLRLVLLSGDWIPLDLPARLRALAPD--ARLISLGGATEASIWSIYHPI--DEVPPDWRSiPYGRPLANQRY 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1901 YLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPfstTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIR 1980
Cdd:cd12114    312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1981 GFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAAlrDTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd12114    389 GYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAP--DALRAFLAQTLPAYMIPSRVIALEALPL 466
                          490
                   ....*....|.
gi 2183974163 2061 TANGKLDRRAL 2071
Cdd:cd12114    467 TANGKVDRAAL 477
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1582-2072 7.76e-128

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 411.02  E-value: 7.76e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVG-PDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYM 1660
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1661 IEDSGIRLLLTqraarerlplgeglpcllldaehewagypesdpqsavGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLF 1740
Cdd:cd17648     81 LEDTGARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1741 DATRHWFGFSA--DDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQ 1818
Cdd:cd17648    124 TSLSERYFGRDngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1819 VACAgqevpplALRHVVFGGEALEVQALRPWFERFgdrAPRLVNMYGITETTVHVTYRPLSLadlDGGAASPIGEPIPDL 1898
Cdd:cd17648    204 ARLP-------HLKRVDAAGEEFTAPVFEKLRSRF---AGLIINAYGPTETTVTNHKRFFPG---DQRFDKSLGRPVRNT 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFST-------TGGRLYRTGDLARYRCDGVVEYVG 1971
Cdd:cd17648    271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargRNARLYKTGDLVRWLPSGELEYLG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQ------LVGYVVTQAAPSDPAALRDtlrqALKASLPE 2045
Cdd:cd17648    351 RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHVPESDLLS----FLRAKLPR 426
                          490       500
                   ....*....|....*....|....*..
gi 2183974163 2046 HMVPAHLLFLERLPLTANGKLDRRALP 2072
Cdd:cd17648    427 YMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
512-1007 4.01e-126

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 407.31  E-value: 4.01e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSqqsvlarlpqsdglqslllddlerlvhgypaenpdlpEAPDSLCYAIYTSGSTGQPKG 671
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLT-------------------------------------SSPSDAAYVIFTSGSTGKPKG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDpeALLDLVERQGVTVLQA 751
Cdd:cd05918    124 VVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLcDSERVDLLRgcTLLCGGEALAEDLAArmrglsasTW-------NLYGPTETTIWSARFRLGEEARP-FLGG 823
Cdd:cd05918    202 TPSVARLL-DPEDVPSLR--TLVLGGEALTQSDVD--------TWadrvrliNAYGPAECTIAATVSPVVPSTDPrNIGR 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  824 PLeNTALYILDSE-MN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPF------AADGSRLYRTGDLARYRADG 895
Cdd:cd05918    271 PL-GATCWVVDPDnHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDG 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  896 VIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVA----QPGVAGPTLVAYLVPTEAALVDAESARQ------- 964
Cdd:cd05918    350 SLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLDGSSSGSGDGDSLflepsde 429
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2183974163  965 -QELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05918    430 fRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1582-2072 4.73e-126

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 406.86  E-value: 4.73e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1582 PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMI 1661
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1662 EDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEWAGypeSDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFD 1741
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDT---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1742 ATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNqTPSAFkqLMQVAC 1821
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LPVAF--LKFIFS 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPLA--LRHVVFGGEALEVQalRPWFERFGDRAPRLVNMYGITETTVHVTYRplsladLDGGAA----SPIGEPI 1895
Cdd:cd17656    236 EREFINRFPtcVKHIITAGEQLVIT--NEFKEMLHEHNVHLHNHYGPSETHVVTTYT------INPEAEipelPPIGKPI 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1896 PDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTgGRLYRTGDLARYRCDGVVEYVGRIDH 1975
Cdd:cd17656    308 SNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN-ERMYRTGDLARYLPDGNIEFLGRADH 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1976 QVKIRGFRIELGEIEARLLAQPGVAEAVVLPH-EGPGATQLVGYVVTQAAPSDpaalrDTLRQALKASLPEHMVPAHLLF 2054
Cdd:cd17656    387 QVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELNI-----SQLREYLAKQLPEYMIPSFFVP 461
                          490
                   ....*....|....*...
gi 2183974163 2055 LERLPLTANGKLDRRALP 2072
Cdd:cd17656    462 LDQLPLTPNGKVDRKALP 479
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
523-1008 5.13e-124

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 401.08  E-value: 5.13e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSQQSvLARLPQSDGLQSLLLDDLERLVHGypaENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNF 682
Cdd:cd17656     81 MLDSGVRVVLTQRH-LKSKLSFNKSTILLEDPSISQEDT---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  683 VCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCdS 762
Cdd:cd17656    157 LHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF-S 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  763 ER--VDLLRGCT--LLCGGEAL--AEDLAARMRGLSASTWNLYGPTETTIWSArFRLGEEAR----PFLGGPLENTALYI 832
Cdd:cd17656    236 ERefINRFPTCVkhIITAGEQLviTNEFKEMLHEHNVHLHNHYGPSETHVVTT-YTINPEAEipelPPIGKPISNTWIYI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  833 LDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADgSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 912
Cdd:cd17656    315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN-ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  913 RIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPtEAALVDAEsarqqelrsaLKNSLLAVLPDYMVPAHMLLL 991
Cdd:cd17656    394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVM-EQELNISQ----------LREYLAKQLPEYMIPSFFVPL 462
                          490
                   ....*....|....*..
gi 2183974163  992 ENLPLTPNGKINRKALP 1008
Cdd:cd17656    463 DQLPLTPNGKVDRKALP 479
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1578-2071 1.38e-122

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 395.85  E-value: 1.38e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGirllltqraarerlplgeglPCLLLDAEHEwagypesdpqsavgvdnLAYVIYTSGSTGKPKGTLLPHGNVL 1737
Cdd:cd05945     81 REILDAAK--------------------PALLIADGDD-----------------NAYIIFTSGSTGRPKGVQISHDNLV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1738 RLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLM 1817
Cdd:cd05945    124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1818 QVACAGQEVPPlALRHVVFGGEALEVQALRPWFERFGDRapRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPD 1897
Cdd:cd05945    204 LSPTFTPESLP-SLRHFLFCGEVLPHKTARALQQRFPDA--RIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPG 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1898 LSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPfsttGGRLYRTGDLARYRCDGVVEYVGRIDHQV 1977
Cdd:cd05945    281 AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQV 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1978 KIRGFRIELGEIEARLLAQPGVAEAVVLP-HEGPGATQLVGYVVTQaaPSDPAALRDTLRQALKASLPEHMVPAHLLFLE 2056
Cdd:cd05945    357 KLNGYRIELEEIEAALRQVPGVKEAVVVPkYKGEKVTELIAFVVPK--PGAEAGLTKAIKAELAERLPPYMIPRRFVYLD 434
                          490
                   ....*....|....*
gi 2183974163 2057 RLPLTANGKLDRRAL 2071
Cdd:cd05945    435 ELPLNANGKIDRKAL 449
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1114-1535 3.52e-121

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 390.86  E-value: 3.52e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIhptlpIAIEERRP 1193
Cdd:cd19538      4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLI-----LEEDEATP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1194 P-----VAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPP 1268
Cdd:cd19538     79 KleikeVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1269 ALAELPIQYADFAAWQRQWMDGGER-----ERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALR 1343
Cdd:cd19538    159 ELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1344 RLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVV 1423
Cdd:cd19538    239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1424 EAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQrddhrGSRFASlgeLEVEDLAWDVQ-----TAQFDLTLD----- 1493
Cdd:cd19538    319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQ-----NTPQPS---LDLPGLEAKLElrtvgSAKFDLTFElreqy 390
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2183974163 1494 TYESSNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19538    391 NDGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1572-2071 4.71e-121

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 390.52  E-value: 4.71e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLTQRAArerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLL 1731
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTDSP-----------------------------------DDLAYIIFTSGSTGIPKGVMV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1732 PHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIvpyetsRSPEDFLRLLCRErVTVLNQTPS 1811
Cdd:cd17653    126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPS 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1812 AFkqlmqVACAGQEVPplALRHVVFGGEALEVQALRPWFERfgdraPRLVNMYGITETTVHVTYRPLSLadldgGAASPI 1891
Cdd:cd17653    199 IL-----STLSPQDFP--NLKTIFLGGEAVPPSLLDRWSPG-----RRLYNAYGPTECTISSTMTELLP-----GQPVTI 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1892 GEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFStTGGRLYRTGDLARYRCDGVVEYVG 1971
Cdd:cd17653    262 GKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLEFLG 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RIDHQVKIRGFRIELGEIEARLLA-QPGVAEAVVLPHEGpgatQLVGYVVTQAApsDPAALRDTLRQalkaSLPEHMVPA 2050
Cdd:cd17653    341 REDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNG----RLVAFVTPETV--DVDGLRSELAK----HLPSYAVPD 410
                          490       500
                   ....*....|....*....|.
gi 2183974163 2051 HLLFLERLPLTANGKLDRRAL 2071
Cdd:cd17653    411 RIIALDSFPLTANGKVDRKAL 431
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
513-1008 1.03e-120

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 389.99  E-value: 1.03e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  513 HRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDP 592
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  593 QYPADRLQYMIDDSGLRLLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGV 672
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN--------------------------------------PDDLAYVIYTSGSTGLPKGV 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  673 MVRHRALTNFvCSIARQP-GMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTV--L 749
Cdd:cd17645    123 MIEHHNLVNL-CEWHRPYfGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsfL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLCDSERvdlLRgcTLLCGGEALAedlaaRMRGLSASTWNLYGPTETTIWSARFRLG-EEARPFLGGPLENT 828
Cdd:cd17645    202 PTGAAEQFMQLDNQS---LR--VLLTGGDKLK-----KIERKGYKLVNNYGPTENTVVATSFEIDkPYANIPIGKPIDNT 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  829 ALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdGSRLYRTGDLARYRADGVIEYLGRIDHQVK 908
Cdd:cd17645    272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP-GERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  909 IRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPteaalvdAESARQQELRSALKNSllavLPDYMVPAH 987
Cdd:cd17645    351 IRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYLVAYVTA-------PEEIPHEELREWLKND----LPDYMIPTY 419
                          490       500
                   ....*....|....*....|.
gi 2183974163  988 MLLLENLPLTPNGKINRKALP 1008
Cdd:cd17645    420 FVHLKALPLTANGKVDRKALP 440
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1571-2072 2.95e-120

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 388.84  E-value: 2.95e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1571 HRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDP 1650
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1651 RYPSDRLGYMIEDSGIRLLLTQraarerlplgeglpcllldaehewagypesdpqsavgVDNLAYVIYTSGSTGKPKGTL 1730
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN-------------------------------------PDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1731 LPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTP 1810
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPT 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1811 SAFKQLMQVACAgqevpplALRHVVFGGEALEVQALRPWferfgdrapRLVNMYGITETTVHVTyrplsLADLDGGAAS- 1889
Cdd:cd17645    204 GAAEQFMQLDNQ-------SLRVLLTGGDKLKKIERKGY---------KLVNNYGPTENTVVAT-----SFEIDKPYANi 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1890 PIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsTTGGRLYRTGDLARYRCDGVVEY 1969
Cdd:cd17645    263 PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEF 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1970 VGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHE-GPGATQLVGYVVTQaAPSDPAALRDTlrqaLKASLPEHMV 2048
Cdd:cd17645    342 LGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEdADGRKYLVAYVTAP-EEIPHEELREW----LKNDLPDYMI 416
                          490       500
                   ....*....|....*....|....
gi 2183974163 2049 PAHLLFLERLPLTANGKLDRRALP 2072
Cdd:cd17645    417 PTYFVHLKALPLTANGKVDRKALP 440
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
47-477 3.48e-120

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 388.16  E-value: 3.48e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDeqlDGFRQQVLASVDVPV 126
Cdd:cd19538      1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE---DGVPYQLILEEDEAT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PVTLAGDDDaQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGI 206
Cdd:cd19538     78 PKLEIKEVD-EEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  207 EATLPDLPIQYADYAIWQRHWLEAGER-----ERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQ 281
Cdd:cd19538    157 APELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  282 LQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVA 361
Cdd:cd19538    237 LLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKET 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  362 ALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNlgsagrqslaAQLPGLSVEDLSWGAH-----SAQFDLTLD- 435
Cdd:cd19538    317 NLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQN----------TPQPSLDLPGLEAKLElrtvgSAKFDLTFEl 386
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163  436 ----TYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19538    387 reqyNDGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
524-1008 1.03e-119

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 387.53  E-value: 1.03e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVG-SDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSQQSVLArlpqsdglqslllddlerlvhgypaenpdlpeapdslcYAIYTSGSTGQPKGVMVRHRALTNF 682
Cdd:cd17648     81 LEDTGARVVITNSTDLA--------------------------------------YAIYTSGTTGKPKGVLVEHGSVVNL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  683 VCSIARQPGMLARD--RLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLc 760
Cdd:cd17648    123 RTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  761 DSERVDLLRgcTLLCGGEALAEDLAARMRG-LSASTWNLYGPTETTIWS--ARFRLGEEARPFLGGPLENTALYILDSEM 837
Cdd:cd17648    202 DLARLPHLK--RVDAAGEEFTAPVFEKLRSrFAGLIINAYGPTETTVTNhkRFFPGDQRFDKSLGRPVRNTKCYVLNDAM 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  838 NPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADG-------SRLYRTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:cd17648    280 KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  911 GFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT------LVAYLVPteaalvDAESARQQELRSALKnsllAVLPDYMV 984
Cdd:cd17648    360 GQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLP------EPGHVPESDLLSFLR----AKLPRYMV 429
                          490       500
                   ....*....|....*....|....
gi 2183974163  985 PAHMLLLENLPLTPNGKINRKALP 1008
Cdd:cd17648    430 PARLVRLEGIPVTINGKLDVRALP 453
AMP-binding pfam00501
AMP-binding enzyme;
1574-1980 1.80e-116

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 376.65  E-value: 1.80e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGE-RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQ--------RAARERLPLG------EGLPCLLLDAEHEWAGYPESDPQSAVGV--DNLAYV 1716
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDdalkleelLEALGKLEVVklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPdpDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1717 IYTSGSTGKPKGTLLPHGNVLR----LFDATRHWFGFSADDAWSLFHSYAFDFSV-WEIFGALLHGGRLVIVPYETSRSP 1791
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1792 EDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPlALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTV 1871
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1872 HVTYRPlsLADLDGGAASPIGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfsttgg 1950
Cdd:pfam00501  317 VVTTPL--PLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------- 387
                          410       420       430
                   ....*....|....*....|....*....|
gi 2183974163 1951 RLYRTGDLARYRCDGVVEYVGRIDHQVKIR 1980
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1570-2073 3.91e-115

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 374.53  E-value: 3.91e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTqraarerlplgeglpcllldaehewagypesdpqsavgvdnlAYVIYTSGSTGKPKGT 1729
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1730 LLPHGNVLRLFDATRHWFGFSADDAW----SLFHSYAFdfsVWEIFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTV 1805
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTV 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1806 LNQTPSAFKQLMQVACAGQEVPPlALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVTYRPlslADLDG 1885
Cdd:COG0318    193 LFGVPTMLARLLRHPEFARYDLS-SLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNP---EDPGE 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFvADPFsttggrlYRTGDLARYRCDG 1965
Cdd:COG0318    266 RRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDG 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1966 VVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQAlkasL 2043
Cdd:COG0318    338 YLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVvgVPDEKWGERVVAFVVLRPGAELDAEELRAFLRER----L 413
                          490       500       510
                   ....*....|....*....|....*....|
gi 2183974163 2044 PEHMVPAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:COG0318    414 ARYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
514-1007 6.06e-114

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 370.10  E-value: 6.06e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQ 593
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSqqsvlarlpqsdglqslllddlerlvhgypaenpdlPEAPDSLCYAIYTSGSTGQPKGVM 673
Cdd:cd17653     81 LPSARIQAILRTSGATLLLT------------------------------------TDSPDDLAYIIFTSGSTGIPKGVM 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  674 VRHRALTNFVC-SIAR---QPGmlarDRLLSVTTFSFDIFGLELYVPLARGASMLLAsreqaqDPEALLDLVERQgVTVL 749
Cdd:cd17653    125 VPHRGVLNYVSqPPARldvGPG----SRVAQVLSIAFDACIGEIFSTLCNGGTLVLA------DPSDPFAHVART-VDAL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLcDSERVDLLRGCTLlcGGEALAEDLAARMRGlSASTWNLYGPTETTIWSARFRLGEEARPFLGGPLENTA 829
Cdd:cd17653    194 MSTPSILSTL-SPQDFPNLKTIFL--GGEAVPPSLLDRWSP-GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNST 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  830 LYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKI 909
Cdd:cd17653    270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  910 RGFRIELGEIE-TRLLEQDSVREAVVVaqpgVAGPTLVAYLVPteaalvdaESARQQELRSALKNSllavLPDYMVPAHM 988
Cdd:cd17653    349 RGFRINLEEIEeVVLQSQPEVTQAAAI----VVNGRLVAFVTP--------ETVDVDGLRSELAKH----LPSYAVPDRI 412
                          490
                   ....*....|....*....
gi 2183974163  989 LLLENLPLTPNGKINRKAL 1007
Cdd:cd17653    413 IALDSFPLTANGKVDRKAL 431
AMP-binding pfam00501
AMP-binding enzyme;
516-910 1.28e-110

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 360.09  E-value: 1.28e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  516 FEAQAGLTPDAPALLFGE-ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQY 594
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  595 PADRLQYMIDDSGLRLLLSQQSVLA-----------------RLPQSDGLQSLLLDDLERLVHGYPAENPdlPEAPDSLC 657
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLeellealgklevvklvlVLDRDPVLKEEPLPEEAKPADVPPPPPP--PPDPDDLA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  658 YAIYTSGSTGQPKGVMVRHRALTNFVCSIARQP----GMLARDRLLSVTTFSFDI-FGLELYVPLARGASMLLASREQAQ 732
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPAL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  733 DPEALLDLVERQGVTVLQATPATWRMLCDSERVDL-----LRgcTLLCGGEALAEDLAARMRGLSAST-WNLYGPTETTI 806
Cdd:pfam00501  239 DPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRallssLR--LVLSGGAPLPPELARRFRELFGGAlVNGYGLTETTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 WSARFRLGEEARPFL---GGPLENTALYILD-SEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDpfaadgsRL 882
Cdd:pfam00501  317 VVTTPLPLDEDLRSLgsvGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GW 389
                          410       420
                   ....*....|....*....|....*...
gi 2183974163  883 YRTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
48-496 2.94e-110

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 360.50  E-value: 2.94e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   48 IPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDgFRQQVLASVDVPVP 127
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGE-PVQVILEERPFELE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  128 VTLAGDDDAQAQ---IRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQ 204
Cdd:pfam00668   84 IIDISDLSESEEeeaIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  205 GieATLPDLPIQ-YADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQ 283
Cdd:pfam00668  164 G--EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  284 ALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAAL 363
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  364 GAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGV 443
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163  444 HAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERATLL 496
Cdd:pfam00668  402 TIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2619-3183 1.45e-108

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 381.13  E-value: 1.45e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2619 LDQRQLDALPLAAGEVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEGLDPQRFREAWQAALDAHEVLRSGFLWQG 2698
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2699 ALEKPLQLVRkRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSN 2778
Cdd:COG1020     81 RPVQVIQPVV-AAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2779 SQLLGEVLQRY----------RGETPSRSDGRYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPTLLVPAFAHGVRGAEGHA 2848
Cdd:COG1020    160 GLLLAELLRLYlaayagaplpLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2849 DRYRQLDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPC 2928
Cdd:COG1020    240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2929 PEQPIGDWLQAVQGENLALREFEHTPLYDIQRWAGQVGEA----LFDNILVFENYPVSA-ALAEETPADMRIDalsnQEQ 3003
Cdd:COG1020    318 GDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLsrnpLFQVMFVLQNAPADElELPGLTLEPLELD----SGT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3004 THYPLTLLVS-AGETLELHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLEGWNATAAEYP 3082
Cdd:COG1020    394 AKFDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYP 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3083 LQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAY 3162
Cdd:COG1020    474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
                          570       580
                   ....*....|....*....|.
gi 2183974163 3163 VPVDPEYPEERQAYMLEDSGV 3183
Cdd:COG1020    554 VPLDPAYPAERLAYMLEDAGA 574
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1114-1555 1.49e-108

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 355.49  E-value: 1.49e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEH-DGAPRQVIHPTLPIAIEErr 1192
Cdd:pfam00668    7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQeNGEPVQVILEERPFELEI-- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1193 ppvagEDLKGLVETEAHR------------PFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYA 1260
Cdd:pfam00668   85 -----IDISDLSESEEEEaieafiqrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1261 ALRHDQPPALAELPiQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAE 1340
Cdd:pfam00668  160 QLLKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1341 ALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQ 1420
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1421 AVVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSrFASLGELEVEDLAWDV---QTAQFDLTLDTYES 1497
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDS-QEEEFQLSELDLSVSSvieEEAKYDLSLTASER 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 1498 SNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEaRADLL 1555
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE-KQKLL 454
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
523-1007 1.65e-108

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 355.02  E-value: 1.65e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:cd05945      4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSqqsvlarlpqsdglqslllddlerlvhgypaenpdlpeAPDSLCYAIYTSGSTGQPKGVMVRHRALTNF 682
Cdd:cd05945     84 LDAAKPALLIA--------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  683 VCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLC-- 760
Cdd:cd05945    126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLls 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  761 ---DSERVDLLRGcTLLCGgEALAEDLAARMRGL--SASTWNLYGPTETTIWSARFRLGEEA-----RPFLGGPLENTAL 830
Cdd:cd05945    206 ptfTPESLPSLRH-FLFCG-EVLPHKTARALQQRfpDARIYNTYGPTEATVAVTYIEVTPEVldgydRLPIGYAKPGAKL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  831 YILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDpfaaDGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:cd05945    284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD----EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  911 GFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALvdaesarqQELRSALKNSLLAVLPDYMVPAHML 989
Cdd:cd05945    360 GYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVPKPGAE--------AGLTKAIKAELAERLPPYMIPRRFV 431
                          490
                   ....*....|....*...
gi 2183974163  990 LLENLPLTPNGKINRKAL 1007
Cdd:cd05945    432 YLDELPLNANGKIDRKAL 449
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
47-477 6.13e-107

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 349.76  E-value: 6.13e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQlDGFRQQVLASVDVPV 126
Cdd:cd19539      1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDG-GVPRQEILPPGPAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PVTL--AGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQ 204
Cdd:cd19539     80 EVRDlsDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  205 GIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQsVLELPTDRQRPALPSYRGARHELQLPQALGRQLQA 284
Cdd:cd19539    160 GPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAE-PTALPTDRPRPAGFPYPGADLRFELDAELVAALRE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  285 LAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALG 364
Cdd:cd19539    239 LAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  365 AQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAGRqslaAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVH 444
Cdd:cd19539    319 AQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGEL----ELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLR 394
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163  445 AEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19539    395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
512-1007 3.97e-106

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 348.34  E-value: 3.97e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSqqsvlarlpqsdglqslllddlerlvhgypaenpdlpeapdslCYAIYTSGSTGQPKG 671
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTSGTTGRPKG 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDiFGL--ELYVPLARGASMLLASReqaQDPEALLDLVERQGVTVL 749
Cdd:COG0318    118 VMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHV-FGLtvGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLC---DSERVDL--LRgcTLLCGGEALAEDLAARMRGLSAST-WNLYGPTETT--IWSARFRLGEEARPFL 821
Cdd:COG0318    194 FGVPTMLARLLrhpEFARYDLssLR--LVVSGGAPLPPELLERFEERFGVRiVEGYGLTETSpvVTVNPEDPGERRPGSV 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  822 GGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLG 901
Cdd:COG0318    272 GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RDG--WLRTGDLGRLDEDGYLYIVG 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  902 RIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVDAEsarqqELRSALKnsllAVLP 980
Cdd:COG0318    344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDeKWGERVVAFVVLRPGAELDAE-----ELRAFLR----ERLA 414
                          490       500
                   ....*....|....*....|....*..
gi 2183974163  981 DYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:COG0318    415 RYKVPRRVEFVDELPRTASGKIDRRAL 441
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1112-1535 7.77e-106

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 346.67  E-value: 7.77e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1112 PQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHD-GAPRQVIHPTLPIAIEE 1190
Cdd:cd19539      2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 RRPPVAGEDLKGLVET----EAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQ 1266
Cdd:cd19539     82 RDLSDPDSDRERRLEEllreRESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1267 PPALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLlELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLA 1346
Cdd:cd19539    162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPT-ALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1347 QAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQ 1426
Cdd:cd19539    241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1427 GHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRFASLGELEVEDLAWDvqTAQFDLTLDTYESSNGLLAELT 1506
Cdd:cd19539    321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPD--GAKFDLNLTVTEEGTGLRGSLG 398
                          410       420
                   ....*....|....*....|....*....
gi 2183974163 1507 YATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19539    399 YATSLFDEETIQGFLADYLQVLRQLLANP 427
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
240-1095 9.91e-100

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 355.14  E-value: 9.91e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  240 WMARLGGgQSVLELPTDRQRPALPSYRGARHELQLPQALGrqlqalAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVP 319
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  320 VANRNRVeterligffvntQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSL-SHSPLFQAMYNH 398
Cdd:TIGR03443   75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQD 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  399 QNlgsagrqslAAQLPGLSVEDLSwgahsaqfDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPR 478
Cdd:TIGR03443  143 AP---------DNQQTTYSTGSTT--------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  479 RRLGDLPLLdaeeraTLLQRSRLPA-------SEYPAGqgVHRLFEAQAGLTPD------APALLFGEER---LSYAELN 542
Cdd:TIGR03443  206 EPIGKVSLI------TPSQKSLLPDptkdldwSGFRGA--IHDIFADNAEKHPDrtcvveTPSFLDPSSKtrsFTYKQIN 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  543 ALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS-------QQ 615
Cdd:TIGR03443  278 EASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekagtlDQ 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SV----------LARLP----QSDG------LQSLLLDDLERLVHgYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVR 675
Cdd:TIGR03443  358 LVrdyidkelelRTEIPalalQDDGslvggsLEGGETDVLAPYQA-LKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGR 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 HRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPAT 755
Cdd:TIGR03443  437 HFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  756 WRMLCDSERV------------DLL--RGCTLLcggEALAEDLaarmrglsaSTWNLYGPTETTIWSARFRLGEEAR--P 819
Cdd:TIGR03443  517 GQLLSAQATTpipslhhaffvgDILtkRDCLRL---QTLAENV---------CIVNMYGTTETQRAVSYFEIPSRSSdsT 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 FL---------GGPLENTALYILD--SEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGS-------- 880
Cdd:TIGR03443  585 FLknlkdvmpaGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldken 664
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 -------------RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAV-VVAQPGVAGPTLV 946
Cdd:TIGR03443  665 nkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtLVRRDKDEEPTLV 744
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  947 AYLVPTE--------AALVDAESA---------RQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPL 1009
Cdd:TIGR03443  745 SYIVPQDksdeleefKSEVDDEESsdpvvkgliKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPF 824
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1010 PDASAV------RDAHVAPE--GELERAMAAIWSEVL--KLGHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTL 1079
Cdd:TIGR03443  825 PDTAQLaavaknRSASAADEefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLI 904
                          970
                   ....*....|....*.
gi 2183974163 1080 FEHSTLRAYAQAVAQL 1095
Cdd:TIGR03443  905 FKSPTIKGFAKEVDRL 920
PRK12316 PRK12316
peptide synthase; Provisional
2627-3183 3.65e-92

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 337.70  E-value: 3.65e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2627 LPLAAG-EVEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLwQGALEKPL 2704
Cdd:PRK12316    38 FPIPAGvSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGpLDRQALERAFASLVQRHETLRTVFP-RGADDSLA 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2705 QLVRKR-VEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLG 2783
Cdd:PRK12316   117 QVPLDRpLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIE 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2784 EVLQRYRGETPSRSDG------RYRDYI----AWLQRQDAGRTEAFWKqrlQRLGE--PTLLVPA-----FAHGVRGaeg 2846
Cdd:PRK12316   197 EFSRFYSAYATGAEPGlpalpiQYADYAlwqrSWLEAGEQERQLEYWR---AQLGEehPVLELPTdhprpAVPSYRG--- 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2847 haDRYR-QLDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRP-AELRGIeeqIGLFINTLPVV 2924
Cdd:PRK12316   271 --SRYEfSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNrAEVEGL---IGFFVNTQVLR 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2925 ASPCPEQPIGDWLQAVQGENL---------------AL---REFEHTPLYDIqrwagqvgealfdnilVFENYPVSAALA 2986
Cdd:PRK12316   346 SVFDGRTRVATLLAGVKDTVLgaqahqdlpferlveALkveRSLSHSPLFQV----------------MYNHQPLVADIE 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2987 E-ETPADMRIDALSNQEQT-HYPLTL-LVSAGETLELHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLA 3063
Cdd:PRK12316   410 AlDTVAGLEFGQLEWKSRTtQFDLTLdTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLD 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3064 VAERYQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAME 3143
Cdd:PRK12316   490 AEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAME 569
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 2183974163 3144 RSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:PRK12316   570 RSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGV 609
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1300-2153 1.25e-86

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 314.31  E-value: 1.25e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1300 WVSRLGgEQPLLELPSDRPRPQQQSHrgrrigipLPAELAEALRRLAQAEQG--TLFMLLLASFQALLHRYSGQNDIRVG 1377
Cdd:TIGR03443    2 WSERLD-NPTLSVLPHDYLRPANNRL--------VEATYSLQLPSAEVTAGGgsTPFIILLAAFAALVYRLTGDEDIVLG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1378 VpianrnREETEGligffvNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLVDALQPERSL-SHAPLFQVMY 1456
Cdd:TIGR03443   73 T------SSNKSG------RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAF 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1457 NHQRDDhrgsrfaSLGELEVEDLAwdvqtaqfDLTLDTYESSNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVARPE 1536
Cdd:TIGR03443  141 QDAPDN-------QQTTYSTGSTT--------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1537 ARIAELKLLDEAEaRADL------LQWNpgpqDFTpaSCLHRLIERQAAERPRATAVV---------YGERALDYGELNL 1601
Cdd:TIGR03443  206 EPIGKVSLITPSQ-KSLLpdptkdLDWS----GFR--GAIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1602 RANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAA------ 1675
Cdd:TIGR03443  279 ASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAgtldql 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 -----RERLPLGEGLPCL-LLDAEHEWAGYPESD------PQSA---------VGVDNLAYVIYTSGSTGKPKGTLLPHG 1734
Cdd:TIGR03443  359 vrdyiDKELELRTEIPALaLQDDGSLVGGSLEGGetdvlaPYQAlkdtptgvvVGPDSNPTLSFTSGSEGIPKGVLGRHF 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1735 NVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPsAFK 1814
Cdd:TIGR03443  439 SLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTP-AMG 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1815 QLMqVACAGQEVPplALRHVVFGGEAL------EVQALrpwferfgdrAP--RLVNMYGITETTVHVTY--------RPL 1878
Cdd:TIGR03443  518 QLL-SAQATTPIP--SLHHAFFVGDILtkrdclRLQTL----------AEnvCIVNMYGTTETQRAVSYfeipsrssDST 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1879 SLADLDGgaASPIGEPIPDLSwyLLDAGLNPVPRGC----IGELYVGGAGLARGYLNRPELSCTRFVADPFSTTG----- 1949
Cdd:TIGR03443  585 FLKNLKD--VMPAGKGMKNVQ--LLVVNRNDRTQTCgvgeVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidl 660
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1950 ----------------GRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL-PHEGPGA 2012
Cdd:TIGR03443  661 dkennkperefwlgprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLvRRDKDEE 740
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2013 TQLVGYVVTQ---------------AAPSDPA--------ALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRR 2069
Cdd:TIGR03443  741 PTLVSYIVPQdksdeleefksevddEESSDPVvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP 820
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2070 ALPAPD------ASRLQRDYTAPR--SELEQRLAAIWADVL--KLGRVGLDDNFFELGGDSIISIQVVSRARQAGIRLAP 2139
Cdd:TIGR03443  821 ALPFPDtaqlaaVAKNRSASAADEefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELP 900
                          970
                   ....*....|....*
gi 2183974163 2140 RDL-FLHQTIRGLAG 2153
Cdd:TIGR03443  901 LGLiFKSPTIKGFAK 915
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1111-1535 8.24e-85

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 286.13  E-value: 8.24e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1111 SPQLSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAI-E 1189
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFqE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1190 ERRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPA 1269
Cdd:cd20484     81 EDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1270 LAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAE 1349
Cdd:cd20484    161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1350 QGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQ 1429
Cdd:cd20484    241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1430 DLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGS------RFASLGELE-VEDLAwdvQTAQFDLTLDTYESSNGLL 1502
Cdd:cd20484    321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSlqqflaEYQDVLSIEfVEGIH---QEGEYELVLEVYEQEDRFT 397
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163 1503 AELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd20484    398 LNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1574-2071 1.60e-84

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 287.95  E-value: 1.60e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP 1653
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1654 SDRLGYMIEDSGIRLLLtqraARERLPLG-EGLPCLLLDA-EHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLL 1731
Cdd:PRK04813    88 AERIEMIIEVAKPSLII----ATEELPLEiLGIPVITLDElKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1732 PHGNVLRLFDatrhW----FGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLN 1807
Cdd:PRK04813   164 SHDNLVSFTN----WmledFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1808 QTPSaFKQ--LMQVACAGQEVPplALRHVVFGGEALEVQALRPWFERFGDraPRLVNMYGITETTVHVTYRPLSLADLDG 1885
Cdd:PRK04813   240 STPS-FADmcLLDPSFNEEHLP--NLTHFLFCGEELPHKTAKKLLERFPS--ATIYNTYGPTEATVAVTSIEITDEMLDQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFvadpFSTTGGRLYRTGDLARYRcDG 1965
Cdd:PRK04813   315 YKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYLE-DG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1966 VVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPG-ATQLVGYVVTQAAP-SDPAALRDTLRQALKASL 2043
Cdd:PRK04813   390 LLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkVQYLIAYVVPKEEDfEREFELTKAIKKELKERL 469
                          490       500
                   ....*....|....*....|....*...
gi 2183974163 2044 PEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK04813   470 MEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
47-477 3.47e-81

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 275.73  E-value: 3.47e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLdGFRQQVLASvdvpv 126
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV-PFQKIEPSK----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PVTLAGDDDA---QAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARR 203
Cdd:cd20484     75 PLSFQEEDISslkESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  204 QGIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQ 283
Cdd:cd20484    155 QGKQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIK 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  284 ALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAAL 363
Cdd:cd20484    235 SFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  364 GAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQN-LGSAGRQSLAAQL-PGLSVEDLSWGAHSAQFDLTLDTYESEQ 441
Cdd:cd20484    315 DGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNfLQSTSLQQFLAEYqDVLSIEFVEGIHQEGEYELVLEVYEQED 394
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2183974163  442 GVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd20484    395 RFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
47-474 8.88e-81

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 274.52  E-value: 8.88e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPV 126
Cdd:cd20483      1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGD--DFGEQQVLDDPSFHL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PVT-LAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGA-RRQ 204
Cdd:cd20483     79 IVIdLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlRAG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  205 GIEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGG-QSVLELP-TDRQRPALPSYRGARHELQLPQALGRQL 282
Cdd:cd20483    159 RDLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIpDASKLLPfAKAERPPVKDYERSTVEATLDKELLARM 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  283 QALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAA 362
Cdd:cd20483    239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  363 LGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSagrqslaaqLPGLSVED---LSWGAHSA--QFDLTLDTY 437
Cdd:cd20483    319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGK---------FPEYDTGDfkfTDYDHYDIptACDIALEAE 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2183974163  438 ESEQ-GVHAEFTYATDLFEAATVERLARHWRNLLEAVV 474
Cdd:cd20483    390 EDPDgGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVI 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
512-1007 2.59e-80

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 275.62  E-value: 2.59e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFE-AQAglTPDAPALLFGEERLSYAELNALANRLAWRLREEGV--GSDVLV--GIALErgvpMVVALLAVLKAGGA 586
Cdd:PRK04813     5 IETIEEfAQT--QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLpdKSPIIVfgHMSPE----MLATFLGAVKAGHA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  587 YVPLDPQYPADRLQYMIDDSGLRLLLSqqsvLARLPQS-DGLQSLLLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGS 665
Cdd:PRK04813    79 YIPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEiLGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  666 TGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQG 745
Cdd:PRK04813   155 TGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  746 VTVLQATPATWRM------LCDSERVDLLRgcTLLCGgEAL----AEDLaaRMRGLSASTWNLYGPTETTIWSARFRLGE 815
Cdd:PRK04813   235 INVWVSTPSFADMclldpsFNEEHLPNLTH--FLFCG-EELphktAKKL--LERFPSATIYNTYGPTEATVAVTSIEITD 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 EA-----RPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpFAADGSRLYRTGDLAr 890
Cdd:PRK04813   310 EMldqykRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAG- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  891 YRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpgvagPT--------LVAYLVPTEAalvdaESA 962
Cdd:PRK04813   385 YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-------PYnkdhkvqyLIAYVVPKEE-----DFE 452
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2183974163  963 RQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK04813   453 REFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1114-1535 2.60e-79

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 270.05  E-value: 2.60e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPiaieerRP 1193
Cdd:cd19066      4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTV------RF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1194 PVAGEDLKGLVETEA----------HRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALR 1263
Cdd:cd19066     78 RIEIIDLRNLADPEArllelidqiqQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1264 HDQPpALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALR 1343
Cdd:cd19066    158 RQKP-TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1344 RLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVV 1423
Cdd:cd19066    237 EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1424 EAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQrddhrgSRFASLGELEV-----EDLAWDvQTAQFDLTLDTYESS 1498
Cdd:cd19066    317 EAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFK------NNQQQLGKTGGfifttPVYTSS-EGTVFDLDLEASEDP 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2183974163 1499 NG-LLAELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19066    390 DGdLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1114-1354 7.47e-79

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 261.51  E-value: 7.47e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFiwrLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIE---- 1189
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEvvdl 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1190 -ERRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPP 1268
Cdd:COG4908     78 sALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1269 ALAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQA 1348
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                   ....*.
gi 2183974163 1349 EQGTLF 1354
Cdd:COG4908    238 HGATVN 243
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1114-1535 8.09e-77

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 262.78  E-value: 8.09e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFV--EHDGAPRQVIHPTLPIAIEER 1191
Cdd:cd19532      4 MSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFtdPEDGEPMQGVLASSPLRLEHV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1192 rpPVAGEDLkglVETEAHR----PFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAalrhDQP 1267
Cdd:cd19532     84 --QISDEAE---VEEEFERlknhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN----GQP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1268 paLAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGGEQ---PLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRR 1344
Cdd:cd19532    155 --LLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPeplPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1345 LAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVE 1424
Cdd:cd19532    233 ASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1425 AQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHqRDDHRGSRfaSLGELEVEDLAW-DVQTAqFDLTLDTYESSNG--L 1501
Cdd:cd19532    313 ALAHSRVPFDVLLDELGVPRSATHSPLFQVFINY-RQGVAESR--PFGDCELEGEEFeDARTP-YDLSLDIIDNPDGdcL 388
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2183974163 1502 LaELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19532    389 L-TLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
49-477 9.15e-76

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 259.70  E-value: 9.15e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   49 PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDGFRQQVLA-SVDVPVP 127
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLAsSPLRLEH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  128 VTLAGDDDAQAQIRAFVesetQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARrqgie 207
Cdd:cd19532     83 VQISDEAEVEEEFERLK----NHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQ----- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  208 aTLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLEL---PTDRQRPALPSYRGARHELQLPQALGRQLQA 284
Cdd:cd19532    154 -PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAARIKE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  285 LAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALG 364
Cdd:cd19532    233 ASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  365 AQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQnLGSAGRQSLA-AQLPGLSVEDlswgAHSAqFDLTLDTYESEQG- 442
Cdd:cd19532    313 ALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYR-QGVAESRPFGdCELEGEEFED----ARTP-YDLSLDIIDNPDGd 386
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2183974163  443 VHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19532    387 CLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
48-477 1.07e-75

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 259.65  E-value: 1.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   48 IPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVED----EQ--LDGFRQQVLAS 121
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEagryEQvvLDKTVRFRIEI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  122 VDvpvpvtLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGA 201
Cdd:cd19066     82 ID------LRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  202 RRQGiEATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQ 281
Cdd:cd19066    156 AERQ-KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  282 LQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVA 361
Cdd:cd19066    235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  362 ALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYN-HQNLGSAGRQSLAAqlpgLSVEDLSWgAHSAQFDLTLDTYE-S 439
Cdd:cd19066    315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTfKNNQQQLGKTGGFI----FTTPVYTS-SEGTVFDLDLEASEdP 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2183974163  440 EQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19066    390 DGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
46-477 1.74e-74

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 256.64  E-value: 1.74e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   46 ERIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQldGFRQQVL--ASVD 123
Cdd:cd19546      3 DEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGG--DVHQRILdaDAAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  124 VPVPVTLAGDDDAQAQIRAfvesETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARR 203
Cdd:cd19546     81 PELPVVPATEEELPALLAD----RAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  204 QGIEATLPDLPIQYADYAIWQRHWLeAGERER------QLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQA 277
Cdd:cd19546    157 EGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  278 LGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRN-RVETERLIGFFVNTQVLRADLDAQMPFLDLLQ 356
Cdd:cd19546    236 VHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  357 QTRVAALGAQSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAGRQSlaAQLPGLSVEDLSWGAHSAQFDLTLDT 436
Cdd:cd19546    316 RVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDA--PELPGLRTSPVPLGTEAMELDLSLAL 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2183974163  437 YE------SEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19546    394 TErrnddgDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2174-2614 2.24e-74

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 256.88  E-value: 2.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQ--MFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGT----WRAEHRAVE-AGE 2246
Cdd:pfam00668    6 PLSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGepvqVILEERPFElEII 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2247 VLLWQQSVADGQALEALAEQ-VQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQ 2325
Cdd:pfam00668   86 DISDLSESEEEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2326 AVALPAKTSaFKAWAERLQAHARDGGLEGERGYWLAQLEG--VSTELPCDDREGAQsvRHVRSARTELT-EEATRRLLQE 2402
Cdd:pfam00668  166 PLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGelPVLQLPKDYARPAD--RSFKGDRLSFTlDEDTEELLRK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2403 APAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREElfEDIDltRTVGWFTSLFPLRL--SPVAELGASIKRIKE 2480
Cdd:pfam00668  243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIE--RMVGMFVNTLPLRIdpKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2481 QLR-AIPHKGLGFGALRYLgSAEDRAAL-AALPSPRITF-NYLGQFdgsfsaDSSALFRPSADAAGSERDSDAPLDNWLS 2557
Cdd:pfam00668  319 DLLsAEPHQGYPFGDLVND-LRLPRDLSrHPLFDPMFSFqNYLGQD------SQEEEFQLSELDLSVSSVIEEEAKYDLS 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2558 LNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDF 2614
Cdd:pfam00668  392 LTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2634-3071 1.16e-73

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 254.57  E-value: 1.16e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2634 VEDLYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQgALEKPLQLVRKRVE 2712
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIRQ-ENGEPVQVILEERP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2713 VPFSVHDWRDRADLAEALDALAAGEAGL--GFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYR 2790
Cdd:pfam00668   80 FELEIIDISDLSESEEEEAIEAFIQRDLqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2791 G-----ETPSRSDGRYRDYIAWLQR----QDAGRTEAFWKQRLQRLGEPTLLVPAFAH-GVRGAEGHADRYRqLDVTTSQ 2860
Cdd:pfam00668  160 QllkgePLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARpADRSFKGDRLSFT-LDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2861 RLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPCPEQPIGDWLQAV 2940
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2941 QGENLALREFEHTPLYDIQR----WAGQVGEALFDNILVFENYPVSAALAEE---TPADMRIDaLSNQEQTHYPLTLLVS 3013
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLGQDSQEEEfqlSELDLSVS-SVIEEEAKYDLSLTAS 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 3014 -AGETLELHYSYSRQAFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLL 3071
Cdd:pfam00668  396 eRGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
50-294 2.21e-73

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 245.72  E-value: 2.21e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   50 LSYAQERQWFlwqMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPVPVT 129
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED--GEPVQRIDPDADLPLEVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  130 LAGD---DDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQGI 206
Cdd:COG4908     76 DLSAlpePEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  207 EATLPDLPIQYADYAIWQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQALA 286
Cdd:COG4908    156 PPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235

                   ....*...
gi 2183974163  287 QREGTTLF 294
Cdd:COG4908    236 KAHGATVN 243
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1571-2071 3.38e-73

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 256.96  E-value: 3.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1571 HRLIERQAAERPRATAVVY-----GERALDYGELNLRANRLAHRLIELGVGP-DVlVGLAAERSLEMIVGLLAILKAGGA 1644
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1645 YVPLDPRYPSDRLGYMIEDSGIRLLLTQ----------------RAARERLP-------LGEGLPCLLLDAEHEWAGYPE 1701
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPslehvivVGRTGADVPMEGDLDWDELLA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1702 SDPQSA----VGVDNLAYVIYTSGSTGKPKGTLLPHGNVLrLFDAT--RHWFGFSADD--------AWSLFHSYAfdfsv 1767
Cdd:COG0365    171 AASAEFepepTDADDPLFILYTSGTTGKPKGVVHTHGGYL-VHAATtaKYVLDLKPGDvfwctadiGWATGHSYI----- 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1768 weIFGALLHGGRLVIvpYE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvacAGQEVPP----LALRHVVFGGEA 1840
Cdd:COG0365    245 --VYGPLLNGATVVL--YEgrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMK---AGDEPLKkydlSSLRLLGSAGEP 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1841 LEVQALRPWFERFGdrAPrLVNMYGITETTVHVtyrplsLADLDGGAASP--IGEPIPDLSWYLLDAGLNPVPRGCIGEL 1918
Cdd:COG0365    318 LNPEVWEWWYEAVG--VP-IVDGWGQTETGGIF------ISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGEL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1919 YVGGA--GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQ 1996
Cdd:COG0365    389 VIKGPwpGMFRGYWNDPE----RYRETYFGRFPG-WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 1997 PGVAEAVV--LPHEGPGaTQLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:COG0365    464 PAVAEAAVvgVPDEIRG-QVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1114-1532 5.37e-73

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 251.80  E-value: 5.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQ--VIHPTLPIAIEER 1191
Cdd:cd20483      4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQqvLDDPSFHLIVIDL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1192 RPPVAGE-DLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPA- 1269
Cdd:cd20483     84 SEAADPEaALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLAt 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1270 LAELPIQYADFAAWQRQWMDGGERERQLDYWVSRLGG--EQPLLeLP---SDRPrPQQQSHRGRRIGIpLPAELAEALRR 1344
Cdd:cd20483    164 VPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipDASKL-LPfakAERP-PVKDYERSTVEAT-LDKELLARMKR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1345 LAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVE 1424
Cdd:cd20483    241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1425 AQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRddHRGSRFASLGELEVEDL-AWDVQTaQFDLTLDTYE-SSNGLL 1502
Cdd:cd20483    321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQV--HGKFPEYDTGDFKFTDYdHYDIPT-ACDIALEAEEdPDGGLD 397
                          410       420       430
                   ....*....|....*....|....*....|
gi 2183974163 1503 AELTYATDLFDASSAERIAGHWLNLLRSIV 1532
Cdd:cd20483    398 LRLEFSTTLYDSADMERFLDNFVTFLTSVI 427
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2637-3052 7.75e-73

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 251.08  E-value: 7.75e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2637 LYPLSPMQQGMLFHSLYQQNSGDYINQMRLD-VEGLDPQRFREAWQAALDAHEVLRSGFLWQgALEKPLQLVRKRVEVPF 2715
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWR-DRAEPLQYVRDDLAPPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2716 SVHDWR----DRADLAEALDALAAGEAGLGfeLAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRY-- 2789
Cdd:cd19547     80 ALLDWSgedpDRRAELLERLLADDRAAGLS--LADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYee 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2790 --RGETPSRSDGR-YRDYIAWLQRQDA--GRTEAFWKQRLQRLgEPTllvpAFAHGVRGAEGHADR-YRQLDVTTSQRLA 2863
Cdd:cd19547    158 laHGREPQLSPCRpYRDYVRWIRARTAqsEESERFWREYLRDL-TPS----PFSTAPADREGEFDTvVHEFPEQLTRLVN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2864 EFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGE 2943
Cdd:cd19547    233 EAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRD 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2944 NLALREFEHTPLYDIQRWAGQV---GEALFDNILVFENYPvsaalAEETPAD---MRIDALSNQEQTHYPLTLLVSAGET 3017
Cdd:cd19547    313 LATTAAHGHVPLAQIKSWASGErlsGGRVFDNLVAFENYP-----EDNLPGDdlsIQIIDLHAQEKTEYPIGLIVLPLQK 387
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2183974163 3018 LELHYSYSRQAFDEAAIECLAERLERLLLGMCENP 3052
Cdd:cd19547    388 LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1713-2067 8.17e-73

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 247.97  E-value: 8.17e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1713 LAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPyetSRSPE 1792
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1793 DFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPlALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVH 1872
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLS-SLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTETGGT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1873 VTyrpLSLADLDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELscTRFVadpfstTGGRL 1952
Cdd:cd04433    155 VA---TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEA--TAAV------DEDGW 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1953 YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAAlr 2032
Cdd:cd04433    224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA-- 301
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2183974163 2033 DTLRQALKASLPEHMVPAHLLFLERLPLTANGKLD 2067
Cdd:cd04433    302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1114-1535 1.84e-72

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 250.86  E-value: 1.84e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEERRP 1193
Cdd:cd19546      7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPVV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1194 PVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAEL 1273
Cdd:cd19546     87 PATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPERAPL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1274 PIQYADFAAWQRQWMDgGERER------QLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQ 1347
Cdd:cd19546    167 PLQFADYALWERELLA-GEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNRE-ETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQ 1426
Cdd:cd19546    246 SAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREAR 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1427 GHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRFASLGELEVEDLAWDVQTAQFDLTLDTYE------SSNG 1500
Cdd:cd19546    326 RHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLALTErrnddgDPDG 405
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2183974163 1501 LLAELTYATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19546    406 LDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1570-2071 1.14e-69

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 243.62  E-value: 1.14e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPcllldaehewaGYPESDPqsavgvDNLAYVIYTSGSTGKPKGT 1729
Cdd:cd05936     81 PLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLG-----------ERVALTP------EDVAVLQYTSGTTGVPKGA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1730 LLPHGNVLRLFDATRHWFGFS--ADD----AWSLFHSYAFDFSVweiFGALLHGGRLVIVPyetSRSPEDFLRLLCRERV 1803
Cdd:cd05936    144 MLTHRNLVANALQIKAWLEDLleGDDvvlaALPLFHVFGLTVAL---LLPLALGATIVLIP---RFRPIGVLKEIRKHRV 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1804 TVLNQTPSAFKQLMQVAcAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDrapRLVNMYGITETTVHVTYRPLSLADL 1883
Cdd:cd05936    218 TIFPGVPTMYIALLNAP-EFKKRDFSSLRLCISGGAPLPVEVAERFEELTGV---PIVEGYGLTETSPVVAVNPLDGPRK 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1884 DGGaaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpfsttGGRLyRTGDLARYRC 1963
Cdd:cd05936    294 PGS----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-------DGWL-RTGDIGYMDE 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1964 DGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATqLVGYVVTQaapSDPAALRDTLRQALKA 2041
Cdd:cd05936    362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVvgVPDPYSGEA-VKAFVVLK---EGASLTEEEIIAFCRE 437
                          490       500       510
                   ....*....|....*....|....*....|
gi 2183974163 2042 SLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05936    438 QLAGYKVPRQVEFRDELPKSAVGKILRREL 467
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
656-1002 1.11e-66

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 230.25  E-value: 1.11e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  656 LCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASReqaQDPE 735
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  736 ALLDLVERQGVTVLQATPATWRMLCD---SERVDL--LRgcTLLCGGEALAEDLAAR-MRGLSASTWNLYGPTETTIWSA 809
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKapeSAGYDLssLR--ALVSGGAPLPPELLERfEEAPGIKLVNGYGLTETGGTVA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  810 RFRLGEEARPF--LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGD 887
Cdd:cd04433    157 TGPPDDDARKPgsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDG--WYRTGD 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVDAEsarqqE 966
Cdd:cd04433    229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdPEWGERVVAVVVLRPGADLDAE-----E 303
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2183974163  967 LRSALKnsllAVLPDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:cd04433    304 LRAHVR----ERLAPYKVPRRVVFVDALPRTASGKI 335
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2637-3035 5.53e-66

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 231.18  E-value: 5.53e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2637 LYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGaLEKPLQLVRKRVEVPF 2715
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIEDG-LGQPVQVVHRQAQVPV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2716 SVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHH-LIYTNHHILMDGWSNSQLLGEVLQRYRGET- 2793
Cdd:cd19536     80 TELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLe 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2794 ------PSRSDgrYRDYIAWLQRQ-DAGRTEAFWKQRLQrlgEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQRLAEFA 2866
Cdd:cd19536    160 ykplslPPAQP--YRDFVAHERASiQQAASERYWREYLA---GATLATLPALSEAVGGGPEQDSELLVSVPLPVRSRSLA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2867 REQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASpCPEQPIGDWLQAVQGENLA 2946
Cdd:cd19536    235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVT-LSEETVEDLLKRAQEQELE 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2947 LREFEHTPLYDIQRWAGqvGEALFDNILVFENYPVSAALAEET-PADMRIDALSNQEQTHYPLTLLVS-AGETLELHYSY 3024
Cdd:cd19536    314 SLSHEQVPLADIQRCSE--GEPLFDSIVNFRHFDLDFGLPEWGsDEGMRRGLLFSEFKSNYDVNLSVLpKQDRLELKLAY 391
                          410
                   ....*....|.
gi 2183974163 3025 SRQAFDEAAIE 3035
Cdd:cd19536    392 NSQVLDEEQAQ 402
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
520-1002 1.68e-65

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 230.19  E-value: 1.68e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLsqqsvlarlpqsdglqslllddlerlvhgypaenpdlpeapDSLCYAIYTSGSTGQPKGVMVRHRAL 679
Cdd:cd17631     85 AYILADSGAKVLF-----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  680 TNFVCSIARQPGMLARDRLLSVTTFsFDIFGLELYVP--LARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWR 757
Cdd:cd17631    124 LWNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQ 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  758 MLCDSER---VDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTETTIwSARFRLGEEARPFLGG---PLENTALY 831
Cdd:cd17631    200 ALLQHPRfatTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP-GVTFLSPEDHRRKLGSagrPVFFVEVR 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  832 ILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRG 911
Cdd:cd17631    279 IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF------RDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  912 FRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqelrsALKNSLLAVLPDYMVPAHMLL 990
Cdd:cd17631    351 ENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVAVVVPRPGAELDED---------ELIAHCRERLARYKIPKSVEF 421
                          490
                   ....*....|..
gi 2183974163  991 LENLPLTPNGKI 1002
Cdd:cd17631    422 VDALPRNATGKI 433
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1570-2073 1.04e-64

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 230.82  E-value: 1.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTqraARERL-----------------------PLGEGLPCLLLDAEHEWAGYPESDPQS 1706
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVT---SSERLdllhpalpgchdlrtliivgdpaHASEGHPGEEPASWPKLLALGDADPPH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1707 AVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYE 1786
Cdd:TIGR03098  159 PVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 TsrsPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcagqeVPPLA---LRHVVFGGEALEVQALRPWFERFGDRAPRLvnM 1863
Cdd:TIGR03098  239 L---PRDVLKALEKHGITGLAAVPPLWAQLAQLD-----WPESAapsLRYLTNSGGAMPRATLSRLRSFLPNARLFL--M 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1864 YGITEtTVHVTYRPLSLADLDGGAaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVAD 1943
Cdd:TIGR03098  309 YGLTE-AFRSTYLPPEEVDRRPDS---IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPL 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1944 P----FSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYV 2019
Cdd:TIGR03098  385 PpfpgELHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLV 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2020 VTqaAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:TIGR03098  465 VT--PPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
49-477 3.65e-64

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 225.93  E-value: 3.65e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   49 PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEdEQLDGFRQQVLASVDVPVPV 128
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVW-EGLGEPLQVVLKDRKLPWRE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  129 T-LAGDDDAQ--AQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQG 205
Cdd:cd19543     82 LdLSHLSEAEqeAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  206 IEATLPDLPiQYADYAiwqrHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQAL 285
Cdd:cd19543    162 QPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQEL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  286 AQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNR--VETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAAL 363
Cdd:cd19543    237 ARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  364 GAQSHQDLPfeqLVEaLQpERSLSHSPLFQAMYNHQN--LGSAGRQSLAAQlpGLSVEDLSwGAHSAQFDLTLDTYESEQ 441
Cdd:cd19543    317 ELREHEYVP---LYE-IQ-AWSEGKQALFDHLLVFENypVDESLEEEQDED--GLRITDVS-AEEQTNYPLTVVAIPGEE 388
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2183974163  442 gVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19543    389 -LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
514-1007 3.91e-64

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 227.45  E-value: 3.91e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQ 593
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSqqsvlarlpqsdglqsllLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVM 673
Cdd:cd05936     83 YTPRELEHILNDSGAKALIV------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  674 VRHRALTNFVCSIAR--QPGMLARDRLLSVTTFsFDIFGLE--LYVPLARGASMLLASReqaQDPEALLDLVERQGVTVL 749
Cdd:cd05936    145 LTHRNLVANALQIKAwlEDLLEGDDVVLAALPL-FHVFGLTvaLLLPLALGATIVLIPR---FRPIGVLKEIRKHRVTIF 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLC---DSERVDL--LRGCtlLCGGEALAEDLAARMRGLSAStwNL---YGPTETTIWSARFRLGEEARP-F 820
Cdd:cd05936    221 PGVPTMYIALLnapEFKKRDFssLRLC--ISGGAPLPVEVAERFEELTGV--PIvegYGLTETSPVVAVNPLDGPRKPgS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  821 LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLpdpfaaDGsrLYRTGDLARYRADGVIEYL 900
Cdd:cd05936    297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DG--WLRTGDIGYMDEDGYFFIV 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  901 GRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVDAEsarqqELRSALKnsllAVL 979
Cdd:cd05936    369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPdPYSGEAVKAFVVLKEGASLTEE-----EIIAFCR----EQL 439
                          490       500
                   ....*....|....*....|....*...
gi 2183974163  980 PDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05936    440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1127-1535 5.00e-64

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 225.55  E-value: 5.00e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1127 LDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFV-EHDGAPRQVIHptlpiaiEERRPPVAGEDLKGLVE 1205
Cdd:cd19543     17 LDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVL-------KDRKLPWRELDLSHLSE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1206 TEA------------HRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAEL 1273
Cdd:cd19543     90 AEQeaelealaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1274 PiQYADFAAW-QRQwmdggERERQLDYWVSRLGGEQPLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGT 1352
Cdd:cd19543    170 R-PYRDYIAWlQRQ-----DKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVT 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1353 LFMLLLASFQALLHRYSGQNDIRVGVPIANRNRE--ETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQD 1430
Cdd:cd19543    244 LNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAElpGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEY 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1431 LPfeqLVDaLQpERSLSHAPLFQ---VMYNHQRDDHRGSRFASLGeLEVEDLAWDVQTaQFDLTLDTYEsSNGLLAELTY 1507
Cdd:cd19543    324 VP---LYE-IQ-AWSEGKQALFDhllVFENYPVDESLEEEQDEDG-LRITDVSAEEQT-NYPLTVVAIP-GEELTIKLSY 395
                          410       420
                   ....*....|....*....|....*...
gi 2183974163 1508 ATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19543    396 DAEVFDEATIERLLGHLRRVLEQVAANP 423
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
524-1007 1.40e-63

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 225.43  E-value: 1.40e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEER----LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:cd17654      1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLSQQsvlarlpqsdglqsllLDDLERLVHGYPAENPDLPeAPDSLCYAIYTSGSTGQPKGVMVRHRAL 679
Cdd:cd17654     81 LTVMKKCHVSYLLQNK----------------ELDNAPLSFTPEHRHFNIR-TDECLAYVIHTSGTTGTPKIVAVPHKCI 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  680 TNFVCSiARQPGMLARDRLLSVTTF-SFDIFGLELYVPLARGASMLLASREQAQDPEALLD-LVERQGVTVLQATPATWR 757
Cdd:cd17654    144 LPNIQH-FRSLFNITSEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFR 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  758 MLCDSERVDL-------LRgcTLLCGGEA---LAEDLAARMRGLSASTWNLYGPTETTIWSARFRLGEEARPF-LGGPLE 826
Cdd:cd17654    223 RFGSQSIKSTvlsatssLR--VLALGGEPfpsLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVqLGSPLL 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMNPcppgVAGELLIGgdGLARGYhrrpgltaerFLPDPFAADGSRLYRTGDLARyRADGVIEYLGRIDHQ 906
Cdd:cd17654    301 GTVIEVRDQNGSE----GTGQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQ 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVrEAVVVA----QpgvagpTLVAYLVPTEAalvdaeSAR-QQELRSALKNSllAVLPD 981
Cdd:cd17654    364 IKRRGKRINLDLIQQVIESCLGV-ESCAVTlsdqQ------RLIAFIVGESS------SSRiHKELQLTLLSS--HAIPD 428
                          490       500
                   ....*....|....*....|....*.
gi 2183974163  982 YMVpahmlLLENLPLTPNGKINRKAL 1007
Cdd:cd17654    429 TFV-----QIDKLPLTSHGKVDKSEL 449
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
511-1007 1.16e-62

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 224.66  E-value: 1.16e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  511 GVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPL 590
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  591 DPQYPADRLQYMIDDSGLRLLLSQQSVLARL----PQSDGLQSLLL-DDLERLVHGYPAEN--------------PDLPE 651
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLhpalPGCHDLRTLIIvGDPAHASEGHPGEEpaswpkllalgdadPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  652 APDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDiFGL-ELYVPLARGASMLLASREQ 730
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFD-YGFnQLTTAFYVGATVVLHDYLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  731 AQDpeaLLDLVERQGVTVLQATPATWRMLCD----SERVDLLRgcTLLCGGEALAEDLAARMRGL--SASTWNLYGPTET 804
Cdd:TIGR03098  240 PRD---VLKALEKHGITGLAAVPPLWAQLAQldwpESAAPSLR--YLTNSGGAMPRATLSRLRSFlpNARLFLMYGLTEA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  805 tiWSARFRLGEEA--RP-FLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSR 881
Cdd:TIGR03098  315 --FRSTYLPPEEVdrRPdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELH 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  882 LYRT----GDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTLVAYLVPTEAALV 957
Cdd:TIGR03098  393 LPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF---GVPDPTLGQAIVLVVTPPG 469
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2183974163  958 DAESARqQELRSALKnsllAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:TIGR03098  470 GEELDR-AALLAECR----ARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1574-2068 2.58e-62

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 220.94  E-value: 2.58e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP 1653
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1654 SDRLGYMIEDSGIRLLLtqraarerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPH 1733
Cdd:cd17631     81 PPEVAYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTH 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1734 GNVLRLFDATRHWFGFSADD----AWSLFHSYAFDFSVweiFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTVLNQT 1809
Cdd:cd17631    121 RNLLWNAVNALAALDLGPDDvllvVAPLFHIGGLGVFT---LPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLV 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1810 PSAFKQLMQVACAgQEVPPLALRHVVFGGEALEVQALRPWFErfgdRAPRLVNMYGITETTVHVTYrpLSLADLDGGAAS 1889
Cdd:cd17631    195 PTMIQALLQHPRF-ATTDLSSLRAVIYGGAPMPERLLRALQA----RGVKFVQGYGMTETSPGVTF--LSPEDHRRKLGS 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1890 pIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELscTRfvadpfSTTGGRLYRTGDLARYRCDGVVEY 1969
Cdd:cd17631    268 -AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEA--TA------AAFRDGWFHTGDLGRLDEDGYLYI 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1970 VGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQAlkasLPEHM 2047
Cdd:cd17631    339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVigVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRER----LARYK 414
                          490       500
                   ....*....|....*....|.
gi 2183974163 2048 VPAHLLFLERLPLTANGKLDR 2068
Cdd:cd17631    415 IPKSVEFVDALPRNATGKILK 435
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
513-1020 4.25e-62

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 224.61  E-value: 4.25e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  513 HRLFEAQAGLTPDAPALLF----GEER-LSYAELNALANRLAWRLREEGVG-SDVlVGIALERGVPMVVALLAVLKAGGA 586
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKkGDR-VAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  587 YVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLAR-------------LPQSDGLQSLLL-------------DDLERLVH 640
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEAKVLITADGGLRGgkvidlkekvdeaLEELPSLEHVIVvgrtgadvpmegdLDWDELLA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  641 GYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHR-----ALTNFVCSIARQPGmlarDRLLSVTTFSFdIFGL--EL 713
Cdd:COG0365    171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGgylvhAATTAKYVLDLKPG----DVFWCTADIGW-ATGHsyIV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  714 YVPLARGASMLLA-SREQAQDPEALLDLVERQGVTVLQATPATWRML-----CDSERVDL--LRgcTLLCGGEALAEDLA 785
Cdd:COG0365    246 YGPLLNGATVVLYeGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALmkagdEPLKKYDLssLR--LLGSAGEPLNPEVW 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  786 ARMR---GLS-ASTWnlyGPTETT-IWSArFRLGEEARP-FLGGPLENTALYILDSEMNPCPPGVAGELLIGGD--GLAR 857
Cdd:COG0365    324 EWWYeavGVPiVDGW---GQTETGgIFIS-NLPGLPVKPgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  858 GYHRRPGLTAERFLpDPFaaDGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQ 937
Cdd:COG0365    400 GYWNDPERYRETYF-GRF--PG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  938 P-GVAGPTLVAYLVPTEAALVDAesarqqELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL-------PL 1009
Cdd:COG0365    475 PdEIRGQVVKAFVVLKPGVEPSD------ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLrkiaegrPL 548
                          570
                   ....*....|.
gi 2183974163 1010 PDASAVRDAHV 1020
Cdd:COG0365    549 GDTSTLEDPEA 559
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2638-3036 4.47e-62

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 219.10  E-value: 4.47e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLyqQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGALEKPLQLVRKRVEVPFS 2716
Cdd:cd19542      2 YPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSsVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPIE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2717 VHDWRDRADLAEALDALAAGEaglgfeLAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSR 2796
Cdd:cd19542     80 EVETDEDSLDALTRDLLDDPT------LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2797 SdGRYRDYIAWLQRQDAGRTEAFWKQRLQrlGEPTLLVPAfahgvrgAEGHADRYRQLDVT--TSQRLAEFAREQKVTLN 2874
Cdd:cd19542    154 A-PPFSDYISYLQSQSQEESLQYWRKYLQ--GASPCAFPS-------LSPKRPAERSLSSTrrSLAKLEAFCASLGVTLA 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2875 TLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLALREFEHTP 2954
Cdd:cd19542    224 SLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLS 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2955 LYDIQRWAGQ-VGEALFDNILVFENYPvsAALAEETPADMRIDALSNQEQTHYPLTLLV-SAGETLELHYSYSRQAFDEA 3032
Cdd:cd19542    304 LREIQRALGLwPSGTLFNTLVSYQNFE--ASPESELSGSSVFELSAAEDPTEYPVAVEVePSGDSLKVSLAYSTSVLSEE 381

                   ....
gi 2183974163 3033 AIEC 3036
Cdd:cd19542    382 QAEE 385
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1573-2071 4.75e-60

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 217.08  E-value: 4.75e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK07656    10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQ-------RAARERLPLGE-------GLPCLLLDAEHEWAGY--PESDPQSAVGV--DNLA 1714
Cdd:PRK07656    90 TADEAAYILARGDAKALFVLglflgvdYSATTRLPALEhvvicetEEDDPHTEKMKTFTDFlaAGDPAERAPEVdpDDVA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 YVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHsyAFDFSVwEIFGALLHGGRLVIVPyetSRS 1790
Cdd:PRK07656   170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylaANPFFH--VFGYKA-GVNAPLMRGATILPLP---VFD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1791 PEDFLRLLCRERVTVLNQTPSAFKQLMQVacAGQEVPPLA-LRHVVFGGEALEVQALRPWFERFGdrAPRLVNMYGITET 1869
Cdd:PRK07656   244 PDEVFRLIETERITVLPGPPTMYNSLLQH--PDRSAEDLSsLRLAVTGAASMPVALLERFESELG--VDIVLTGYGLSEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1870 TVHVTYRPlsladLDGGA---ASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfs 1946
Cdd:PRK07656   320 SGVTTFNR-----LDDDRktvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD--- 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1947 ttgGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGAtqlVG--YVVTQ 2022
Cdd:PRK07656   392 ---GWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgvPDERLGE---VGkaYVVLK 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2023 -AAPSDPAALRDTLRqalkaslpEHM----VPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK07656   465 pGAELTEEELIAYCR--------EHLakykVPRSIEFLDELPKNATGKVLKRAL 510
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2638-3036 9.49e-60

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 212.16  E-value: 9.49e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLyqQNSGDYINQMRLDV-EGLDPQRFREAWQAALDAHEVLRSGFLwQGALEKPLQLVRKRVEVPfs 2716
Cdd:cd19545      2 YPCTPLQEGLMALTA--RQPGAYVGQRVFELpPDIDLARLQAAWEQVVQANPILRTRIV-QSDSGGLLQVVVKESPIS-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2717 vhdWRDRADLAEALDALAAGEAGLGfelaeAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSR 2796
Cdd:cd19545     77 ---WTESTSLDEYLEEDRAAPMGLG-----GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2797 SDGrYRDYIAWLQRQDAGRTEAFWKQRLQRLGEPtllvPAFAHGVRGAEGHADRYRQLDVTTSQRlaefaREQKVTLNTL 2876
Cdd:cd19545    149 PPP-FSRFVKYLRQLDDEAAAEFWRSYLAGLDPA----VFPPLPSSRYQPRPDATLEHSISLPSS-----ASSGVTLATV 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2877 VQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLALREFEHTPLY 2956
Cdd:cd19545    219 LRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQ 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2957 DIQRWAGQVGEAL-FDNILV----FENYPVSAALAEETPADMRIDALSNqeqthYPLTLLVS-AGETLELHYSYSRQAFD 3030
Cdd:cd19545    299 NIRRLGPDARAACnFQTLLVvqpaLPSSTSESLELGIEEESEDLEDFSS-----YGLTLECQlSGSGLRVRARYDSSVIS 373

                   ....*.
gi 2183974163 3031 EAAIEC 3036
Cdd:cd19545    374 EEQVER 379
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
512-1007 1.48e-59

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 215.82  E-value: 1.48e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSQQSVLARL----PQSDGLQS-LLLDDLER-----LVHGYP---AENPDLPEAPD---- 654
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDSEFVPLLaailPQLPTVRTvIVEGDGPAaplapEVGEYEellAAASDTFDFPDiden 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLEL-YVPLARGASMLLASReqaQD 733
Cdd:PRK06187   168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIPRR---FD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  734 PEALLDLVERQGVTVLQATPATWRMLCDSER---VDL--LRgcTLLCGGEALAEDLAARMRG-LSASTWNLYGPTET--T 805
Cdd:PRK06187   244 PENLLDLIETERVTFFFAVPTIWQMLLKAPRayfVDFssLR--LVIYGGAALPPALLREFKEkFGIDLVQGYGMTETspV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWSARFRLGEEARPFL----GGPLENTALYILDSEMNPCPP--GVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADG 879
Cdd:PRK06187   322 VSVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI------DGG 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  880 srLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVD 958
Cdd:PRK06187   396 --WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPVAVVVLKPGATLD 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2183974163  959 AEsarqqelrsALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06187   474 AK---------ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1570-2071 3.63e-59

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 214.67  E-value: 3.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQ-------RAARERLP-------LGEGLPCLLLDAEHEW----AGYPESDPQSAVGVD 1711
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDsefvpllAAILPQLPtvrtvivEGDGPAAPLAPEVGEYeellAAASDTFDFPDIDEN 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1712 NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFDFSVweifGALLHGGRLVIVP-YE 1786
Cdd:PRK06187   168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDvylvIVPMFHVHAWGLPY----LALMAGAKQVIPRrFD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 tsrsPEDFLRLLCRERVTVLNQTPSAFKQLMQ-VACAGQEVPPlaLRHVVFGGEALEVQALRPWFERFGdraPRLVNMYG 1865
Cdd:PRK06187   244 ----PENLLDLIETERVTFFFAVPTIWQMLLKaPRAYFVDFSS--LRLVIYGGAALPPALLREFKEKFG---IDLVQGYG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1866 ITETTVHVTYRPLSlADLDGGAASPI--GEPIPDLSWYLLDAGLNPVPR--GCIGELYVGGAGLARGYLNRPELSCTRFV 1941
Cdd:PRK06187   315 MTETSPVVSVLPPE-DQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETID 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1942 ADpfsttggrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGATQLVGYV 2019
Cdd:PRK06187   394 GG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvPDEKWGERPVAVVV 465
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2020 VTQAAPSDPAALRDTLRQalkaSLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06187   466 LKPGATLDAKELRAFLRG----RLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
PRK05691 PRK05691
peptide synthase; Validated
1566-2623 5.11e-59

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 228.13  E-value: 5.11e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1566 PASCLHRLiERQAAERPRATAVVY------GERALDYGELNLRANRLAHRLIELGVGPDVLVgLAAERSLEMIVGLLAIL 1639
Cdd:PRK05691     8 PLTLVQAL-QRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1640 KAGGAYVPLDP-----RYPSDRLGYMIEDSGIRLLLTQRAARERLplgEGLPCLLLDAEHEWAGYPESDPQSA------- 1707
Cdd:PRK05691    86 YAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDTLDPALAeawqepa 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1708 VGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD-----AW-SLFHSYAfdfsvweIFGALLHG---- 1777
Cdd:PRK05691   163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddvivSWlPLYHDMG-------LIGGLLQPifsg 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1778 ------------GRLV-----IVPYE-TSRSPEDFLRLLCRERVTvlnqtPSAFKQLmqvacagqevpPLALRHVVF-GG 1838
Cdd:PRK05691   236 vpcvlmspayflERPLrwleaISEYGgTISGGPDFAYRLCSERVS-----ESALERL-----------DLSRWRVAYsGS 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1839 EALEVQALRPWFERF---GDRAPRLVNMYGITETTVHVTY----RPLSLADLDG----------GAASPI---GEPIPDL 1898
Cdd:PRK05691   300 EPIRQDSLERFAEKFaacGFDPDSFFASYGLAEATLFVSGgrrgQGIPALELDAealarnraepGTGSVLmscGRSQPGH 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpfSTTGGRLYRTGDLARYRcDGVVEYVGRIDHQV 1977
Cdd:PRK05691   380 AVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV----EHDGRTWLRTGDLGFLR-DGELFVTGRLKDML 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1978 KIRGFRIELGEIEARL-----LAQPGVAEAVVLPH---EGPGATQLVGYVVTQAAPsdPAALRDTLRQALKASLPEhmVP 2049
Cdd:PRK05691   455 IVRGHNLYPQDIEKTVereveVVRKGRVAAFAVNHqgeEGIGIAAEISRSVQKILP--PQALIKSIRQAVAEACQE--AP 530
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2050 AHLLFLE--RLPLTANGKLDRRA---------------LPAPDASrLQRDYTAPRSELEQRLAAIWADVLKLGRVGLDDN 2112
Cdd:PRK05691   531 SVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAV-EAAQTAASGDELQARIAAIWCEQLKVEQVAADDH 609
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2113 FFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIRGLAgvAVEGRGLacAEQGPISGSTPLLPIQQMF--------- 2182
Cdd:PRK05691   610 FFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFS--AAVARQL--AGGGAAQAAIARLPRGQALpqslaqnrl 685
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2183 ---FELDiPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTwrAEHRAVEAGEVLLWQQSVAD--- 2256
Cdd:PRK05691   686 wllWQLD-PQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGV--ALQRIDAQGEFALQRIDLSDlpe 762
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2257 ----GQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAK 2332
Cdd:PRK05691   763 aereARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPL 842
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2333 TSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTELP-CDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQV 2411
Cdd:PRK05691   843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLElATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2412 NDLLLTALARVIGRWTGQADTLIQLEGHGREELfediDLTRTVGWFTSLFPLRLS-----PVAELGASIKRIKEQLRAip 2486
Cdd:PRK05691   923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRL----ETQGLVGFFINTQVLRAQldgrlPFTALLAQVRQATLGAQA-- 996
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2487 HKGLGFGALrylgsaedraaLAALPSPRITfnylGQFDGSFS---ADSSALFRPSADAAGS--ERDSDAPLDnwLSLNGQ 2561
Cdd:PRK05691   997 HQDLPFEQL-----------VEALPQAREQ----GLFQVMFNhqqRDLSALRRLPGLLAEElpWHSREAKFD--LQLHSE 1059
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2562 V-YAGRLGIDWSFSAARFSEASILRLADAYrdelLALIEHCCAADVEGVtpSDFPLAGLDQRQ 2623
Cdd:PRK05691  1060 EdRNGRLTLSFDYAAELFDAATIERLAEHF----LALLEQVCEDPQRAL--GDVQLLDAAERA 1116
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
537-1010 5.39e-57

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 208.14  E-value: 5.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  537 SYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRlqymiddsglrlllsqQS 616
Cdd:cd17647     22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------------QN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  617 VLARLPQSDGLQSLllddlerlvhgypaENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARD 696
Cdd:cd17647     86 IYLGVAKPRGLIVI--------------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEND 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  697 RLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRML---CDSERVDLLRGCTL 773
Cdd:cd17647    152 KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLtaqATTPFPKLHHAFFV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  774 lcgGEALAEDLAARMRGLS--ASTWNLYGPTETTIWSARFRLGEEAR--PFL---------GGPLENTALYILD--SEMN 838
Cdd:cd17647    232 ---GDILTKRDCLRLQTLAenVRIVNMYGTTETQRAVSYFEVPSRSSdpTFLknlkdvmpaGRGMLNVQLLVVNrnDRTQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  839 PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADG---------------------SRLYRTGDLARYRADGVI 897
Cdd:cd17647    309 ICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGDC 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  898 EYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTEAALVDAESA-------------- 962
Cdd:cd17647    389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEePTLVSYIVPRFDKPDDESFAqedvpkevstdpiv 468
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  963 ----RQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALPLP 1010
Cdd:cd17647    469 kgliGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1601-2071 3.48e-56

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 203.83  E-value: 3.48e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1601 LRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGA----YVPLDPRYPSDRLGYMIEDSGIRLLLTQRAAR 1676
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1677 ERLPLGE---GLPCLLLDAEhEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD 1753
Cdd:cd05922     81 DRLRDALpasPDPGTVLDAD-GIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 AWSLFHSYAFDFSVWEIFGALLHGGRLVIVPyeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPplALRH 1833
Cdd:cd05922    160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLP--SLRY 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1834 VVFGGEALEVQALRpwfeRFGDRAP--RLVNMYGITETTVHVTYRPlslADLDGGAASPIGEPIPDLSWYLLDAGLNPVP 1911
Cdd:cd05922    236 LTQAGGRLPQETIA----RLRELLPgaQVYVMYGQTEATRRMTYLP---PERILEKPGSIGLAIPGGEFEILDDDGTPTP 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1912 RGCIGELYVGGAGLARGYLNRPElsctrFVADPfSTTGGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEA 1991
Cdd:cd05922    309 PGEPGEIVHRGPNVMKGYWNDPP-----YRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1992 RLLAQPGVAEAVVLPHEGPgATQLVGYVVTQAAPSDPAALRDTLRqalkASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05922    382 AARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDPKDVLRSLA----ERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1596-2072 1.01e-55

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 201.37  E-value: 1.01e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTqraa 1675
Cdd:cd05934      6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 rerlplgeglpcllldaehewagypesdpqsavgvdNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD-- 1753
Cdd:cd05934     82 ------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDvy 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 --AWSLFHSYAfdfSVWEIFGALLHGGRLVIVP-YETSRspedFLRLLCRERVTVLNQTPSAFKQLMQvacagQEVPPLA 1830
Cdd:cd05934    126 ltVLPLFHINA---QAVSVLAALSVGATLVLLPrFSASR----FWSDVRRYGATVTNYLGAMLSYLLA-----QPPSPDD 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 LRH---VVFGGEALEvQALRPWFERFGdraPRLVNMYGITETTVHVtyrplsLADLDG-GAASPIGEPIPDLSWYLLDAG 1906
Cdd:cd05934    194 RAHrlrAAYGAPNPP-ELHEEFEERFG---VRLLEGYGMTETIVGV------IGPRDEpRRPGSIGRPAPGYEVRIVDDD 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYV---GGAGLARGYLNRPELSCTRFvadpfstTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFR 1983
Cdd:cd05934    264 GQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1984 IELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQalkaSLPEHMVPAHLLFLERLPLT 2061
Cdd:cd05934    336 ISSAEVERAILRHPAVREAAVvaVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEG----QLAYFKVPRYIRFVDDLPKT 411
                          490
                   ....*....|.
gi 2183974163 2062 ANGKLDRRALP 2072
Cdd:cd05934    412 PTEKVAKAQLR 422
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1592-2074 1.19e-55

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 204.29  E-value: 1.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1592 RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSdrlgymiedsgirlllt 1671
Cdd:cd17647     19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP----------------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1672 qraARERLPLGEGLPCLLLDAEHewAGYpesdpqsAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSA 1751
Cdd:cd17647     82 ---ARQNIYLGVAKPRGLIVIRA--AGV-------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSafkqLMQVACAGQEVPPLAL 1831
Cdd:cd17647    150 NDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPA----MGQLLTAQATTPFPKL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1832 RHVVFGGEAL------EVQALRPWFerfgdrapRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPD----LSWY 1901
Cdd:cd17647    226 HHAFFVGDILtkrdclRLQTLAENV--------RIVNMYGTTETQRAVSYFEVPSRSSDPTFLKNLKDVMPAgrgmLNVQ 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPVPRGC----IGELYVGGAGLARGYLNRPELSCTRFVADPFSTTG---------------------GRLYRTG 1956
Cdd:cd17647    298 LLVVNRNDRTQICgigeVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTG 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1957 DLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL-PHEGPGATQLVGYVVTQAAP---------- 2025
Cdd:cd17647    378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvRRDKDEEPTLVSYIVPRFDKpddesfaqed 457
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2026 ------SDPAA--------LRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAP 2074
Cdd:cd17647    458 vpkevsTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1584-2071 1.80e-55

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 201.36  E-value: 1.80e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1584 ATAVVYGERALDYGELNLRANRLAHRLIELG-VGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIE 1662
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1663 DSGIRLLLtqraarerlplgeglpcllldaehewagypesdpqsavgvdNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDA 1742
Cdd:cd05941     82 DSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1743 TRHWFGFSADD----AWSLFHSYAFdfsVWEIFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTV----------LNQ 1808
Cdd:cd05941    121 LVDAWRWTEDDvllhVLPLHHVHGL---VNALLCPLFAGASVEFLP---KFDPKEVAISRLMPSITVfmgvptiytrLLQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1809 TPSAFKQLMQVACAgqeVPPLALRHVVFGGEALEVQALRPWFERFGDrapRLVNMYGITETTVHVTyRPLSLADLDGGaa 1888
Cdd:cd05941    195 YYEAHFTDPQFARA---AAAERLRLMVSGSAALPVPTLEEWEAITGH---TLLERYGMTEIGMALS-NPLDGERRPGT-- 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1889 spIGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVV 1967
Cdd:cd05941    266 --VGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYY 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1968 EYVGRI-DHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGatQLVGYVVTQAAPSDPAALRDtLRQALKASLP 2044
Cdd:cd05941    337 WILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVigVPDPDWG--ERVVAVVVLRAGAAALSLEE-LKEWAKQRLA 413
                          490       500
                   ....*....|....*....|....*..
gi 2183974163 2045 EHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05941    414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1596-2071 5.11e-55

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 200.39  E-value: 5.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQraa 1675
Cdd:cd17654     19 YADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN--- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 rerlplgeglpCLLLDAehewagyPESDPQSAVGVD-----NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFS 1750
Cdd:cd17654     96 -----------KELDNA-------PLSFTPEHRHFNirtdeCLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1751 ADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLL-CRERVTVLNQTPSAFKQLMQVACAGQEVPPL 1829
Cdd:cd17654    158 SEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTVLSAT 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1830 -ALRHVVFGGEAL----EVQALRPWFERFgdrapRLVNMYGITETTVHVTYRPLSladlDGGAASPIGEPIPDLSWYLLD 1904
Cdd:cd17654    238 sSLRVLALGGEPFpslvILSSWRGKGNRT-----RIFNIYGITEVSCWALAYKVP----EEDSPVQLGSPLLGTVIEVRD 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1905 AGLNPVPrgciGELYVGgaGLARGYlnrpelsctrFVADPFSTTGGRLYRTGDLARyRCDGVVEYVGRIDHQVKIRGFRI 1984
Cdd:cd17654    309 QNGSEGT----GQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRI 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1985 ELGEIEARLLAQPGVAEAVVLPHEgpgATQLVGYVVTQaaPSDpAALRDTLRqalKASLPEHMVPAHLLFLERLPLTANG 2064
Cdd:cd17654    372 NLDLIQQVIESCLGVESCAVTLSD---QQRLIAFIVGE--SSS-SRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHG 442

                   ....*..
gi 2183974163 2065 KLDRRAL 2071
Cdd:cd17654    443 KVDKSEL 449
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2174-2601 5.72e-54

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 196.48  E-value: 5.72e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQMFFELDI--PRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGT---WRAEHRAVEAGEVL 2248
Cdd:cd19066      3 PLSPMQRGMWFLKKlaTDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRyeqVVLDKTVRFRIEII 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2249 -LWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAV 2327
Cdd:cd19066     83 dLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2328 ALPAKTSaFKAWAERLQAHARDGGLEGERGYWLAQLEGVSTE--LPCDDREGAQSVRHVRSARTELTEEATRRLLQEApA 2405
Cdd:cd19066    163 LPPPVGS-YADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPlpLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA-R 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2406 AYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGReelfEDIDLTRTVGWFTSLFPLRL--SPVAELGASIKRIKEQLR 2483
Cdd:cd19066    241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQSR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2484 AIPHKGLGFGALRYLGSAEDRAAlAALPSPRITFNYLGQFDGSFSADSSALFRPsaDAAGSERdsdAPLDNWLSLNGQVy 2563
Cdd:cd19066    317 EAIEHQRVPFIELVRHLGVVPEA-PKHPLFEPVFTFKNNQQQLGKTGGFIFTTP--VYTSSEG---TVFDLDLEASEDP- 389
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2183974163 2564 AGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHC 2601
Cdd:cd19066    390 DGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
2470-2627 6.64e-54

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 186.33  E-value: 6.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2470 ELGASIKRIKEQLRAIPHKGLGFGALRYLgsAEDRAALAALPSPRITFNYLGQFDGSfsaDSSALFRPSADAAGSERDSD 2549
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYL--TEPEEKLAASPQPEISFNYLGQFDAD---SNDELFQPSSYSPGEAISPE 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2550 APLDNWLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEHCCAADVEGVTPSDFPLAGLDQRQLDAL 2627
Cdd:TIGR01720   76 SPRPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1572-2071 1.27e-53

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 197.98  E-value: 1.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAE-RPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDP 1650
Cdd:cd05959      7 TLVDLNLNEgRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1651 RYPSDRLGYMIEDSGIRLLLT--------QRAARERLPL--------GEGLPCLLLDAEHEWAGYPESDPQSAVGVDNLA 1714
Cdd:cd05959     87 LLTPDDYAYYLEDSRARVVVVsgelapvlAAALTKSEHTlvvlivsgGAGPEAGALLLAELVAAEAEQLKPAATHADDPA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 YVIYTSGSTGKPKGTLLPHGN---VLRLFdaTRHWFGFSADD----AWSLFHSYAFDFSVWEIFGAllhGGRLVIVPyet 1787
Cdd:cd05959    167 FWLYSSGSTGRPKGVVHLHADiywTAELY--ARNVLGIREDDvcfsAAKLFFAYGLGNSLTFPLSV---GATTVLMP--- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1788 SR-SPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEvPPLALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGI 1866
Cdd:cd05959    239 ERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSR-DLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGS 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1867 TETT-VHVTYRPlslADLDGGAAspiGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpf 1945
Cdd:cd05959    315 TEMLhIFLSNRP---GRVRYGTT---GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 sttgGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGP-GATQLVGYVVTQAA 2024
Cdd:cd05959    385 ----GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdGLTKPKAFVVLRPG 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2183974163 2025 PSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05959    461 YEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2175-2412 1.40e-53

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 189.09  E-value: 1.40e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2175 LLPIQQMFFELDiPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAE-HRAVEAG-EVLLWQQ 2252
Cdd:COG4908      1 LSPAQKRFLFLE-PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRiDPDADLPlEVVDLSA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2253 SVADGQ---ALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVAL 2329
Cdd:COG4908     80 LPEPEReaeLEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2330 PAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEGVS--TELPCDDREGAQSVRHVRSARTELTEEATRRLLQEApAAY 2407
Cdd:COG4908    160 PELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPpvLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238

                   ....*
gi 2183974163 2408 RTQVN 2412
Cdd:COG4908    239 GATVN 243
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
525-1007 2.35e-53

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 195.20  E-value: 2.35e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  525 DAPALLFGEERLSYAELNALANRLAWRLREEG-VGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGlrlllsqqsvlarlpqsdglQSLLLDDlerlvhgypaenpdlpeapdslCYAIYTSGSTGQPKGVMVRHRALTNFV 683
Cdd:cd05941     81 TDSE--------------------PSLVLDP----------------------ALILYTSGTTGRPKGVVLTHANLAANV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  684 CSIARQPGMLARDRLLSVTTFsFDIFGL--ELYVPLARGASMLLASREqaqDPEALLDLVERQGVTVLQATPATWRMLCD 761
Cdd:cd05941    119 RALVDAWRWTEDDVLLHVLPL-HHVHGLvnALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLLQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  762 S------ERVDLLRGCT-----LLCGGEALAEDLAARMRGLSAST-WNLYGPTETTIwSARFRLGEEARP-FLGGPLENT 828
Cdd:cd05941    195 YyeahftDPQFARAAAAerlrlMVSGSAALPVPTLEEWEAITGHTlLERYGMTEIGM-ALSNPLDGERRPgTVGMPLPGV 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  829 ALYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRI-DHQ 906
Cdd:cd05941    274 QARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRSsVDI 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTL----VAYLVPTE-AALVDAEsarqqelrsALKNSLLAVLPD 981
Cdd:cd05941    347 IKSGGYKVSALEIERVLLAHPGVSECAVI---GVPDPDWgervVAVVVLRAgAAALSLE---------ELKEWAKQRLAP 414
                          490       500
                   ....*....|....*....|....*.
gi 2183974163  982 YMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05941    415 YKRPRRLILVDELPRNAMGKVNKKEL 440
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1585-2071 2.64e-52

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 191.91  E-value: 2.64e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1585 TAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDS 1664
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1665 GIRLLLTQRaarerlplgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDA-T 1743
Cdd:cd05919     82 EARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAmA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1744 RHWFGFSADD----AWSLFHSYAFDFSVWeifGALLHGGRLVIVPyeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLMqV 1819
Cdd:cd05919    125 REALGLTPGDrvfsSAKMFFGYGLGNSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLL-D 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1820 ACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETT-VHVTYRPlsladldgGAASP--IGEPIP 1896
Cdd:cd05919    199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGhIFLSNRP--------GAWRLgsTGRPVP 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1897 DLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpfsttgGRLYRTGDLARYRCDGVVEYVGRIDHQ 1976
Cdd:cd05919    268 GYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDM 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1977 VKIRGFRIELGEIEARLLAQPGVAEAVVLP-HEGPGATQLVGYVVTqAAPSDPA-ALRDTLRQALKASLPEHMVPAHLLF 2054
Cdd:cd05919    340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVAvPESTGLSRLTAFVVL-KSPAAPQeSLARDIHRHLLERLSAHKVPRRIAF 418
                          490
                   ....*....|....*..
gi 2183974163 2055 LERLPLTANGKLDRRAL 2071
Cdd:cd05919    419 VDELPRTATGKLQRFKL 435
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1114-1535 7.79e-52

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 190.27  E-value: 7.79e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPIAIEE--- 1190
Cdd:cd19533      4 LTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHidl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 RRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPAL 1270
Cdd:cd19533     84 SGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1271 AELPiQYADFAAWQRQWMDGGERERQLDYWVSRLGGeqpLLELPSDRPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQ 1350
Cdd:cd19533    164 APFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFED---LPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAAEAHG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1351 GTLFMLLLASFQALLHRYSGQNDIRVGVPIANR-NREETEGLiGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQ 1429
Cdd:cd19533    240 ASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1430 DLPFEQLVDALQPERSLshAPLFQVMYNHQRDDhRGSRFAsLGELEVEDLAWDVQTaqfDLTLDTYE--SSNGLLAELTY 1507
Cdd:cd19533    319 RYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFD-YGLDFG-GVVGLTHNLSSGPTN---DLSIFVYDrdDESGLRIDFDA 391
                          410       420
                   ....*....|....*....|....*...
gi 2183974163 1508 ATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19533    392 NPALYSGEDLARHQERLLRLLEEAAADP 419
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
543-1007 8.35e-52

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 191.11  E-value: 8.35e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  543 ALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGA----YVPLDPQYPADRLQYMIDDSGLRLLLSQQSVL 618
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  619 AR----LPQS-DGLQSLLLDDLERLVHGYPAenpdLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGML 693
Cdd:cd05922     81 DRlrdaLPASpDPGTVLDADGIRAARASAPA----HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  694 ARDRLLSVTTFSFDiFGL-ELYVPLARGASMLLASREQAqdPEALLDLVERQGVTVLQATPATWRMLC----DSERVDLL 768
Cdd:cd05922    157 ADDRALTVLPLSYD-YGLsVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTrlgfDPAKLPSL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  769 RgcTLLCGGEALAEDLAARMRGL--SASTWNLYGPTETTIWSARF---RLGEeaRP-FLGGPLENTALYILDSEMNPCPP 842
Cdd:cd05922    234 R--YLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTYLppeRILE--KPgSIGLAIPGGEFEILDDDGTPTPP 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  843 GVAGELLIGGDGLARGYHRRPgltaerflpdPFAADGSR---LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 919
Cdd:cd05922    310 GEPGEIVHRGPNVMKGYWNDP----------PYRRKEGRgggVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  920 ETRLLEQDSVREAVVVAQPGVAGPTLVayLVPTEAALVDAESARQqelrsalknSLLAVLPDYMVPAHMLLLENLPLTPN 999
Cdd:cd05922    380 EAAARSIGLIIEAAAVGLPDPLGEKLA--LFVTAPDKIDPKDVLR---------SLAERLPPYKVPATVRVVDELPLTAS 448

                   ....*...
gi 2183974163 1000 GKINRKAL 1007
Cdd:cd05922    449 GKVDYAAL 456
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2638-3012 1.01e-51

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 189.57  E-value: 1.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLYQQNSGDYINQMRL---DVEGLDpqRFREAWQAALDAHEVLRSGFLWQGaLEKPLQLVRKRVEVP 2714
Cdd:cd19544      2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLafdSRARLD--AFLAALQQVIDRHDILRTAILWEG-LSEPVQVVWRQAELP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2715 fsVHDWR-DRADLAEALDALAAGEAGLGFELAEAPLLRLVLVR-TGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGE 2792
Cdd:cd19544     79 --VEELTlDPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2793 T----PSRSdgrYRDYIAWLQRQ-DAGRTEAFWKQRLQRLGEPTLlvPAFAHGVRGAEGHADRYRQ-LDVTTSQRLAEFA 2866
Cdd:cd19544    157 AaalpPPVP---YRNFVAQARLGaSQAEHEAFFREMLGDVDEPTA--PFGLLDVQGDGSDITEARLaLDAELAQRLRAQA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2867 REQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASpCPEQPIGDWLQAVQGENLA 2946
Cdd:cd19544    232 RRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVR-LGGRSVREAVRQTHARLAE 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 2947 LREFEHTPLYDIQRWAG-QVGEALFDNILvfeNY--PVSAALAEETPADMRIDALSNQEQTHYPLTLLV 3012
Cdd:cd19544    311 LLRHEHASLALAQRCSGvPAPTPLFSALL---NYrhSAAAAAAAALAAWEGIELLGGEERTNYPLTLSV 376
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
512-1007 1.20e-51

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 192.43  E-value: 1.20e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAqAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:PRK07656     8 PELLARA-ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSQQSVLArlpqSDGLQSLLLDDLERLVHGYPAENPDLPE-------------------- 651
Cdd:PRK07656    87 TRYTADEAAYILARGDAKALFVLGLFLG----VDYSATTRLPALEHVVICETEEDDPHTEkmktftdflaagdpaerape 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  652 -APDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLE--LYVPLARGASMLLASR 728
Cdd:PRK07656   163 vDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPF-FHVFGYKagVNAPLMRGATILPLPV 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  729 eqaQDPEALLDLVERQGVTVLQATPATWRMLCDSER---VDL--LRGCtlLCGGEALAEDLAARMRglsaSTWNL----- 798
Cdd:PRK07656   242 ---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDrsaEDLssLRLA--VTGAASMPVALLERFE----SELGVdivlt 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  799 -YGPTE----TTIwsarFRLGEEARPF---LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAErf 870
Cdd:PRK07656   313 gYGLSEasgvTTF----NRLDDDRKTVagtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA-- 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  871 lpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP----GVAGptlV 946
Cdd:PRK07656   387 -----AIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPderlGEVG---K 458
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  947 AYLVPTEAALVDAES----ARQQelrsalknsllavLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07656   459 AYVVLKPGAELTEEEliayCREH-------------LAKYKVPRSIEFLDELPKNATGKVLKRAL 510
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
536-1003 3.30e-50

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 187.42  E-value: 3.30e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ 615
Cdd:cd05911     11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SVLARL-----------------PQSDGLQSLLLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRa 678
Cdd:cd05911     91 DGLEKVkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  679 ltNFVCSI-----ARQPGMLARDRLLSVTTFsFDIFGLELYV-PLARGASMLLASReqaQDPEALLDLVERQGVTVLQAT 752
Cdd:cd05911    170 --NLIANLsqvqtFLYGNDGSNDVILGFLPL-YHIYGLFTTLaSLLNGATVIIMPK---FDSELFLDLIEKYKITFLYLV 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  753 PATWRMLCDSERVDL-----LRgcTLLCGGEALAEDLAARMRGLSASTW--NLYGPTETTIWSARFRLGEEARPFLGGPL 825
Cdd:cd05911    244 PPIAAALAKSPLLDKydlssLR--VILSGGAPLSKELQELLAKRFPNATikQGYGMTETGGILTVNPDGDDKPGSVGRLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  826 ENTALYILDSE-MNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRID 904
Cdd:cd05911    322 PNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYLYIVDRKK 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  905 HQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVpteaaLVDAESARQQELRsalknsllavlpDYM 983
Cdd:cd05911    395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPdEVSGELPRAYVV-----RKPGEKLTEKEVK------------DYV 457
                          490       500
                   ....*....|....*....|....*....
gi 2183974163  984 ---VPAHMLL------LENLPLTPNGKIN 1003
Cdd:cd05911    458 akkVASYKQLrggvvfVDEIPKSASGKIL 486
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
47-477 1.28e-49

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 183.72  E-value: 1.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqlDGFRQQVLASVDVPV 126
Cdd:cd19533      1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE--GEPYQWIDPYTPVPI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  127 PVT-LAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQG 205
Cdd:cd19533     79 RHIdLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  206 IEATLPDLPiQYADYAIWQRHWLEAGERERQLEYWMARLGGgqsVLELPTDRQRPALPSYRGARHELQLPQALGRQLQAL 285
Cdd:cd19533    159 RPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFED---LPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  286 AQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGA 365
Cdd:cd19533    235 AEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  366 QSHQDLPFEQLVEALQPERSLshSPLFQAMYNHQ----NLGSAGRQSLAAQLPGLSVEDLSwgahsaqfdLTLDTYESEQ 441
Cdd:cd19533    315 LRHQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMpfdyGLDFGGVVGLTHNLSSGPTNDLS---------IFVYDRDDES 383
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2183974163  442 GVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19533    384 GLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
527-1007 1.35e-49

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 184.20  E-value: 1.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  527 PALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDS 606
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  607 GLRLLLSQQsvlarlpqsdglqslllddlerlvhgypaenpdlpeapDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSI 686
Cdd:cd05919     82 EARLVVTSA--------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  687 ARQP-GMLARDRLLSVTTFSFDiFGL--ELYVPLARGASMLLASreQAQDPEALLDLVERQGVTVLQATPATWRML---C 760
Cdd:cd05919    124 AREAlGLTPGDRVFSSAKMFFG-YGLgnSLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLldsC 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  761 DSERVDL--LRGCTllCGGEALAEDLAAR-MRGLSASTWNLYGPTET--TIWSAR---FRLGEearpfLGGPLENTALYI 832
Cdd:cd05919    201 AGSPDALrsLRLCV--SAGEALPRGLGERwMEHFGGPILDGIGATEVghIFLSNRpgaWRLGS-----TGRPVPGYEIRL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  833 LDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 912
Cdd:cd05919    274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQ 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  913 RIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEaalvdaESARQQELRSALKNSLLAVLPDYMVPAHMLLL 991
Cdd:cd05919    346 WVSPVEVESLIIQHPAVAEAAVVAVPeSTGLSRLTAFVVLKS------PAAPQESLARDIHRHLLERLSAHKVPRRIAFV 419
                          490
                   ....*....|....*.
gi 2183974163  992 ENLPLTPNGKINRKAL 1007
Cdd:cd05919    420 DELPRTATGKLQRFKL 435
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
524-1007 6.56e-49

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 183.67  E-value: 6.56e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEER--LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQY 601
Cdd:cd05926      1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  602 MIDDSGLRLLLSQQSVL---ARLPQSDGL--QSLLLDDLERLVHG----YPAENPDLPEA-------PDSLCYAIYTSGS 665
Cdd:cd05926     81 YLADLGSKLVLTPKGELgpaSRAASKLGLaiLELALDVGVLIRAPsaesLSNLLADKKNAksegvplPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  666 TGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGL--ELYVPLARGASMLLASReqaQDPEALLDLVER 743
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGGSVVLPPR---FSASTFWPDVRD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  744 QGVTVLQATPATWRMLCDSE---------RVDLLRGCtllcgGEALAEDLAARM-RGLSASTWNLYGPTETT--IWSARF 811
Cdd:cd05926    237 YNATWYTAVPTIHQILLNRPepnpespppKLRFIRSC-----SASLPPAVLEALeATFGAPVLEAYGMTEAAhqMTSNPL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  812 RLGEEaRPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARY 891
Cdd:cd05926    312 PPGPR-KPGSVGKPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVDAEsarqqelrsA 970
Cdd:cd05926    384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDeKYGEEVAAAVVLREGASVTEE---------E 454
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2183974163  971 LKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05926    455 LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1578-2074 2.03e-48

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 181.73  E-value: 2.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLieLGVGPdvlVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:PRK07787    10 AAAADIADAVRIGGRVLSRSDLAGAATAVAERV--AGARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGIRLLLTqraarERLPLGEGLPCLLLDAEHE-WAGYPESDPQSAvgvdnlAYVIYTSGSTGKPKGTLLPHGNV 1736
Cdd:PRK07787    85 RHILADSGAQAWLG-----PAPDDPAGLPHVPVRLHARsWHRYPEPDPDAP------ALIVYTSGTTGPPKGVVLSRRAI 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1737 LRLFDATRHWFGFSADD----AWSLFHSYAFdfsVWEIFGALLHGGRLVivpyETSR-SPEDFLRLLcRERVTVLNQTPS 1811
Cdd:PRK07787   154 AADLDALAEAWQWTADDvlvhGLPLFHVHGL---VLGVLGPLRIGNRFV----HTGRpTPEAYAQAL-SEGGTLYFGVPT 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1812 AFKQLmqvacAGQEVPPLAL---RHVVFGGEALEVqalrPWFERFGDRA-PRLVNMYGITETTVHVTYRplslADldgGA 1887
Cdd:PRK07787   226 VWSRI-----AADPEAARALrgaRLLVSGSAALPV----PVFDRLAALTgHRPVERYGMTETLITLSTR----AD---GE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1888 ASP--IGEPIPDLSWYLLDAGLNPVPRG--CIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRC 1963
Cdd:PRK07787   290 RRPgwVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDP 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1964 DGVVEYVGR--IDhQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTqAAPSDPAALRDTLRQAL 2039
Cdd:PRK07787   363 DGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVvgVPDDDLG-QRIVAYVVG-ADDVAADELIDFVAQQL 439
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2183974163 2040 KAslpeHMVPAHLLFLERLPLTANGKLDRRALPAP 2074
Cdd:PRK07787   440 SV----HKRPREVRFVDALPRNAMGKVLKKQLLSE 470
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1596-2071 2.71e-48

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 179.84  E-value: 2.71e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQraa 1675
Cdd:cd05972      3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD--- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 rerlplgeglpcllldaehewagypESDPqsavgvdnlAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD-- 1753
Cdd:cd05972     80 -------------------------AEDP---------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDih 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 ------AWSLFHSYAFdfsvweiFGALLHGGRlVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEvp 1827
Cdd:cd05972    126 wniadpGWAKGAWSSF-------FGPWLLGAT-VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYK-- 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1828 PLALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTvhvtyrpLSLADLDGGAASP--IGEPIPDLSWYLLDA 1905
Cdd:cd05972    196 FSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-------LTVGNFPDMPVKPgsMGRPTPGYDVAIIDD 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1906 GLNPVPRGCIGELYV--GGAGLARGYLNRPELSCTRFVADpfsttggrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFR 1983
Cdd:cd05972    266 DGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1984 IELGEIEARLLAQPGVAEAVVLPHEGPGATQLV-GYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTA 2062
Cdd:cd05972    338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTI 417

                   ....*....
gi 2183974163 2063 NGKLDRRAL 2071
Cdd:cd05972    418 SGKIRRVEL 426
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1596-2075 1.27e-47

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 178.46  E-value: 1.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAA 1675
Cdd:cd05969      3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 RERLPlgeglpcllldaehewagyPEsDPqsavgvdnlAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD-- 1753
Cdd:cd05969     83 YERTD-------------------PE-DP---------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDiy 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 ------AWSLFHSYAfdfsvweIFGALLHGGRLVIvpYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVP 1827
Cdd:cd05969    134 wctadpGWVTGTVYG-------IWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKY 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1828 PL-ALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVtyrplsLADLDGGAASP--IGEPIPDLSWYLLD 1904
Cdd:cd05969    205 DLsSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIM------IANYPCMPIKPgsMGKPLPGVKAAVVD 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1905 AGLNPVPRGCIGELYV--GGAGLARGYLNRPELSCTRFVadpfsttgGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGF 1982
Cdd:cd05969    276 ENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGH 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1983 RIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV-GYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLT 2061
Cdd:cd05969    348 RVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIkAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKT 427
                          490
                   ....*....|....
gi 2183974163 2062 ANGKLDRRALPAPD 2075
Cdd:cd05969    428 RSGKIMRRVLKAKE 441
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
533-1008 6.26e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 175.94  E-value: 6.26e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  533 EERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL 612
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 SqqsvlarlpqsdglqslllddlerlvhgypaenpdlpeapdSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGM 692
Cdd:cd05934     81 V-----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  693 LARDRLLSVT-TFSFDIFGLELYVPLARGASMLLASREQAQdpeALLDLVERQGVTVLQATPATWRMLC-----DSERVD 766
Cdd:cd05934    120 GEDDVYLTVLpLFHINAQAVSVLAALSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYLLaqppsPDDRAH 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  767 LLRGCtllCGGEALAEDLAARMRGLSASTWNLYGPTETT--IWSARfrlGEEARPF---LGGPLENTAlyILDSEMNPCP 841
Cdd:cd05934    197 RLRAA---YGAPNPPELHEEFEERFGVRLLEGYGMTETIvgVIGPR---DEPRRPGsigRPAPGYEVR--IVDDDGQELP 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  842 PGVAGELLI---GGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 918
Cdd:cd05934    269 AGEPGELVIrglRGWGFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  919 IETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLENLPLT 997
Cdd:cd05934    341 VERAILRHPAVREAAVVAVPDeVGEDEVKAVVVLRPGETLDPE-----ELFAFCEGQ----LAYFKVPRYIRFVDDLPKT 411
                          490
                   ....*....|.
gi 2183974163  998 PNGKINRKALP 1008
Cdd:cd05934    412 PTEKVAKAQLR 422
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1592-2066 1.16e-46

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 177.02  E-value: 1.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1592 RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT 1671
Cdd:cd05911      9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1672 --------QRAARErlpLGEGLPCLLLDAEHEWAGYPESDPQSAVGV-------------DNLAYVIYTSGSTGKPKGTL 1730
Cdd:cd05911     89 dpdglekvKEAAKE---LGPKDKIIVLDDKPDGVLSIEDLLSPTLGEededlppplkdgkDDTAAILYSSGTTGLPKGVC 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1731 LPHGNVL-RLFDATRHWFG-FSADDAW----SLFHSYAFdfsvWEIFGALLHGGRLVIvpyeTSR-SPEDFLRLLCRERV 1803
Cdd:cd05911    166 LSHRNLIaNLSQVQTFLYGnDGSNDVIlgflPLYHIYGL----FTTLASLLNGATVII----MPKfDSELFLDLIEKYKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1804 TVLNQTPSafkqlmqVACAGQEVPPLA------LRHVVFGGEAL--EVQalrpwfERFGDRAP--RLVNMYGITETTVHV 1873
Cdd:cd05911    238 TFLYLVPP-------IAAALAKSPLLDkydlssLRVILSGGAPLskELQ------ELLAKRFPnaTIKQGYGMTETGGIL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSlaDLDGGAAspiGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrl 1952
Cdd:cd05911    305 TVNPDG--DDKPGSV---GRLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------- 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1953 YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPH----EGPGAtqlvgYVVTQAAPS 2026
Cdd:cd05911    373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigIPDevsgELPRA-----YVVRKPGEK 447
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163 2027 DPAA-LRDTLRQalkaslpeHMVPAHLL-----FLERLPLTANGKL 2066
Cdd:cd05911    448 LTEKeVKDYVAK--------KVASYKQLrggvvFVDEIPKSASGKI 485
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1596-2071 4.18e-46

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 173.77  E-value: 4.18e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQraa 1675
Cdd:cd05971      9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD--- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 rerlplgeglpcllldaehewagypesdpqsavGVDNLAYVIYTSGSTGKPKGTLLPH----GNV------LRLFDATRH 1745
Cdd:cd05971     86 ---------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLpgvqfpFNLFPRDGD 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1746 WFGFSADDAW--SLFHSyafdfsvweIFGALLHGgrLVIVPYETSR-SPEDFLRLLCRERVTVLNQTPSAFKqLMQVACA 1822
Cdd:cd05971    133 LYWTPADWAWigGLLDV---------LLPSLYFG--VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTALK-MMRQQGE 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1823 GQEVPPLALRHVVFGGEALEVQALRPWFERFGDRAPRLvnmYGITETTVhVTYRPLSLADLDGGAaspIGEPIPDLSWYL 1902
Cdd:cd05971    201 QLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEF---YGQTECNL-VIGNCSALFPIKPGS---MGKPIPGHRVAI 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1903 LDAGLNPVPRGCIGELYV--GGAGLARGYLNRPELSCTRFVADPFsttggrlyRTGDLARYRCDGVVEYVGRIDHQVKIR 1980
Cdd:cd05971    274 VDDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSS 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1981 GFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV-GYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLP 2059
Cdd:cd05971    346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVkAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELP 425
                          490
                   ....*....|..
gi 2183974163 2060 LTANGKLDRRAL 2071
Cdd:cd05971    426 RTATGKIRRREL 437
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1570-2071 7.17e-46

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 175.72  E-value: 7.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPD--VLVGLAaeRSLEMIVGLLAILKAGGAYVP 1647
Cdd:COG1021     27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGdrVVVQLP--NVAEFVIVFFALFRAGAIPVF 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LdprYPSDR---LGYMIEDSGIRLLLTQRAA------------RERLP-------LGEGLPCLLLDAeheWAGYPESDPQ 1705
Cdd:COG1021    105 A---LPAHRraeISHFAEQSEAVAYIIPDRHrgfdyralarelQAEVPslrhvlvVGDAGEFTSLDA---LLAAPADLSE 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1706 SAVGVDNLAYVIYTSGSTGKPKgtLLP--HG----NVLRLFDATrhwfGFSADDAW--SLFHSYAFDFSVWEIFGALLHG 1777
Cdd:COG1021    179 PRPDPDDVAFFQLSGGTTGLPK--LIPrtHDdylySVRASAEIC----GLDADTVYlaALPAAHNFPLSSPGVLGVLYAG 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1778 GRLVIVPyetSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdra 1857
Cdd:COG1021    253 GTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLD-AAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG--- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1858 PRLVNMYGITETTVHVTyrplSLADLDGGAASPIGEPI-PDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELS 1936
Cdd:COG1021    326 CTLQQVFGMAEGLVNYT----RLDDPEEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHN 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1937 CTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVkIR-GFRIELGEIEARLLAQPGVAEAVV--LPHEgpgat 2013
Cdd:COG1021    402 ARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVvaMPDE----- 468
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2014 qLVG-----YVVTQAAPSDPAALRDTLRQalkASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:COG1021    469 -YLGerscaFVVPRGEPLTLAELRRFLRE---RGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1570-2071 1.83e-45

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 173.28  E-value: 1.83e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGP--DVLVGLAaeRSLEMIVGLLAILKAGGAYVP 1647
Cdd:cd05920     17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPgdRVVVQLP--NVAEFVVLFFALLRLGAVPVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRLGYMIEDSGIRLLLTQRaarerlplgeglpcllldaEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPK 1727
Cdd:cd05920     95 ALPSHRRSELSAFCAHAEAVAYIVPD-------------------RHAGFDHRALARELAESIPEVALFLLSGGTTGTPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1728 gtLLP--HGNVLRLFDATRHWFGFSADDAW----SLFHSYAFdfSVWEIFGALLHGGRLVIVPyetSRSPEDFLRLLCRE 1801
Cdd:cd05920    156 --LIPrtHNDYAYNVRASAEVCGLDQDTVYlavlPAAHNFPL--ACPGVLGTLLAGGRVVLAP---DPSPDAAFPLIERE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1802 RVTVLNQTPSAFKQLMQvACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVTyrplSLA 1881
Cdd:cd05920    229 GVTVTALVPALVSLWLD-AAASRRADLSSLRLLQVGGARLSPALARRVPPVLG---CTLQQVFGMAEGLLNYT----RLD 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1882 DLDGGAASPIGEPI-PDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLAR 1960
Cdd:cd05920    301 DPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVR 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1961 YRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGV--AEAVVLPHEGPGATQLVGYVVTQAAPSdPAALRDTLRQa 2038
Cdd:cd05920    374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVhdAAVVAMPDELLGERSCAFVVLRDPPPS-AAQLRRFLRE- 451
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2183974163 2039 lkASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05920    452 --RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
536-1007 6.00e-45

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 170.21  E-value: 6.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ 615
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 svlarlpqsdglqslllddlerlvhgypaenpdlpeapDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05972     81 --------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPD 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLSV------TTFSFDIFGlelyvPLARGASMLLASREQAqDPEALLDLVERQGVTVLQATPATWRMLC--DSERVDL 767
Cdd:cd05972    123 DIHWNIadpgwaKGAWSSFFG-----PWLLGATVFVYEGPRF-DAERILELLERYGVTSFCGPPTAYRMLIkqDLSSYKF 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  768 LRGCTLLCGGEALAEDLAARMRG-LSASTWNLYGPTETTIWSARFRlGEEARP-FLGGPLENTALYILDSEMNPCPPGVA 845
Cdd:cd05972    197 SHLRLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTETGLTVGNFP-DMPVKPgSMGRPTPGYDVAIIDDDGRELPPGEE 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  846 GEL--LIGGDGLARGYHRRPGLTAERFLPDpfaadgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRL 923
Cdd:cd05972    276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  924 LEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALvdaesaRQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:cd05972    348 LEHPAVAEAAVVGSPDpVRGEVVKAFVVLTSGYE------PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421

                   ....*
gi 2183974163 1003 NRKAL 1007
Cdd:cd05972    422 RRVEL 426
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2638-3035 7.93e-45

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 169.84  E-value: 7.93e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGalEKPLQLVRKRVEVPFS 2716
Cdd:cd19531      2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGpLDVAALERALNELVARHEALRTTFVEVD--GEPVQVILPPLPLPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2717 VHDWRDRADLAEALDALA--AGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETP 2794
Cdd:cd19531     80 VVDLSGLPEAEREAEAQRlaREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2795 SRSDG------RYRDYIAWlQRQ--DAGRTE---AFWKQRLQrlGEPTLLV-------PAfahgVRGAEGhaDRYR-QLD 2855
Cdd:cd19531    160 GRPSPlpplpiQYADYAVW-QREwlQGEVLErqlAYWREQLA--GAPPVLElptdrprPA----VQSFRG--ARVRfTLP 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2856 VTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRP-AELrgiEEQIGLFINTLPVVASPCPEQPIG 2934
Cdd:cd19531    231 AELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAEL---EGLIGFFVNTLVLRTDLSGDPTFR 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2935 DWLQAVQGENL---------------AL---REFEHTPLYdiqrwagQVgealfdnILVFENYPVSAALAeetpADMRID 2996
Cdd:cd19531    308 ELLARVRETALeayahqdlpfeklveALqpeRDLSRSPLF-------QV-------MFVLQNAPAAALEL----PGLTVE 369
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2183974163 2997 ALSNQEQT-HYPLTLLVS-AGETLELHYSYSRQAFDEAAIE 3035
Cdd:cd19531    370 PLEVDSGTaKFDLTLSLTeTDGGLRGSLEYNTDLFDAATIE 410
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2748-3181 8.22e-45

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 179.85  E-value: 8.22e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2748 PLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRG-----ETPSRSDGRYRDYIAWLQRQDAG----RTEA 2818
Cdd:PRK10252   119 PLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgePTPASPFTPFADVVEEYQRYRASeawqRDAA 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2819 FWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQRLAEFAREQKVT--LNTLVqAAWLillQRFTGQDTVAF 2896
Cdd:PRK10252   199 FWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRPdlALALV-ALWL---GRLCGRMDYAA 274
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2897 GATVSGR--PAELRGIeeqiGLFINTLPVVASPCPEQPIGDWLQAVQGEnlaLREFEHTPLYD---IQRWAGQVG--EAL 2969
Cdd:PRK10252   275 GFIFMRRlgSAALTAT----GPVLNVLPLRVHIAAQETLPELATRLAAQ---LKKMRRHQRYDaeqIVRDSGRAAgdEPL 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2970 FD---NILVFEnYPVsaalaeetpadmRIDALsnQEQTHY---------PLTLLVSAGETLELHYSYSRQAFDEAAIECL 3037
Cdd:PRK10252   348 FGpvlNIKVFD-YQL------------DFPGV--QAQTHTlatgpvndlELALFPDEHGGLSIEILANPQRYDEATLIAH 412
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3038 AERLERLLLGMCENPGASLGELDSLAVAErYQLLEGWNATAAEYPLQRgVHRLFEEQVERTPTAPALAFGEERLDYAELN 3117
Cdd:PRK10252   413 AERLKALIAQFAADPALLCGDVDILLPGE-YAQLAQVNATAVEIPETT-LSALVAQQAAKTPDAPALADARYQFSYREMR 490
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 3118 RRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3181
Cdd:PRK10252   491 EQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 554
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1593-2071 1.49e-44

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 170.96  E-value: 1.49e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1593 ALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQ 1672
Cdd:cd05926     14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1673 RAarERLPLGEGLP---CLLLDAEHEWAGYPESDPQSAVGV----------------DNLAYVIYTSGSTGKPKGTLLPH 1733
Cdd:cd05926     94 KG--ELGPASRAASklgLAILELALDVGVLIRAPSAESLSNlladkknaksegvplpDDLALILHTSGTTGRPKGVPLTH 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1734 GNVLRlfdATRH---WFGFSADDA----WSLFHSYAfdfsvweIFGALL----HGGRLVIVPyetSRSPEDFLRLLCRER 1802
Cdd:cd05926    172 RNLAA---SATNitnTYKLTPDDRtlvvMPLFHVHG-------LVASLLstlaAGGSVVLPP---RFSASTFWPDVRDYN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1803 VTVLNQTPSAFKQLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdrAPrLVNMYGITETTVHVTYRPlslad 1882
Cdd:cd05926    239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG--AP-VLEAYGMTEAAHQMTSNP----- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1883 LDGGAASP--IGEPI-PDLSwyLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLA 1959
Cdd:cd05926    311 LPPGPRKPgsVGKPVgVEVR--ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1960 RYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGatQLVGYVVTQAApsDPAALRDTLRQ 2037
Cdd:cd05926    382 YLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgVPDEKYG--EEVAAAVVLRE--GASVTEEELRA 457
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2183974163 2038 ALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05926    458 FCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2637-3035 2.46e-44

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 168.36  E-value: 2.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2637 LYPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLwQGAlEKPLQLVRKRVEVP- 2714
Cdd:cd19066      1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGsLDLARLKQALDAVMERHDVLRTRFC-EEA-GRYEQVVLDKTVRFr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2715 FSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRG--- 2791
Cdd:cd19066     79 IEIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2792 --ETPSRSDGRYRDYIAWLQRQ----DAGRTEAFWKQRLQRLGEPTLLVPAFAHG-VRGAEGHADRYRqLDVTTSQRLAE 2864
Cdd:cd19066    159 qkPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSqVASYEVLTLEFF-LRSEETKRLRE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2865 FAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGEN 2944
Cdd:cd19066    238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2945 LALREFEHTPLYDIQRWAGQVGEA----LFDNILVFENYPVSAALAEETPADMRIDALSnqEQTHYPLTLLVSAGET--L 3018
Cdd:cd19066    316 REAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSS--EGTVFDLDLEASEDPDgdL 393
                          410
                   ....*....|....*..
gi 2183974163 3019 ELHYSYSRQAFDEAAIE 3035
Cdd:cd19066    394 LLRLEYSRGVYDERTID 410
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
520-1007 2.73e-44

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 170.24  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:cd05959     14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLL---------------DDLERLVhgyPAENPDLPEA---PDSLCYAIY 661
Cdd:cd05959     94 AYYLEDSRARVVVVSGELAPVLAAALTKSEHTLvvlivsggagpeagaLLLAELV---AAEAEQLKPAathADDPAFWLY 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  662 TSGSTGQPKGVMVRHRALTnFVCSIARQP--GMLARDRLLSVTTFSFDI-FGLELYVPLARGASMLLASREQAqdPEALL 738
Cdd:cd05959    171 SSGSTGRPKGVVHLHADIY-WTAELYARNvlGIREDDVCFSAAKLFFAYgLGNSLTFPLSVGATTVLMPERPT--PAAVF 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  739 DLVERQGVTVLQATPATWRMLCDSERV-----DLLRGCTllCGGEALAEDLAARMRGLSAST-WNLYGPTET-----TIW 807
Cdd:cd05959    248 KRIRRYRPTVFFGVPTLYAAMLAAPNLpsrdlSSLRLCV--SAGEALPAEVGERWKARFGLDiLDGIGSTEMlhiflSNR 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  808 SARFRLGEEARPFLGGPLEntalyILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLpdpfaadGSrLYRTGD 887
Cdd:cd05959    326 PGRVRYGTTGKPVPGYEVE-----LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGD 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPTEAALVDAESARqqE 966
Cdd:cd05959    393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkPKAFVVLRPGYEDSEALEE--E 470
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2183974163  967 LRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05959    471 LKEFVKDRLAP----YKYPRWIVFVDELPKTATGKIQRFKL 507
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
535-1007 1.42e-43

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 166.12  E-value: 1.42e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL--L 612
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAvvG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 SQQSVLARLPqsdglqslllddlerlvhgypaenpdlpeapdslcyaiYTSGSTGQPKGVMVRHRALTNFVCSIARQPGM 692
Cdd:cd05935     81 SELDDLALIP--------------------------------------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  693 LARDRLLSVTTFsFDIFGLE--LYVPLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDSERV---DL 767
Cdd:cd05935    123 TPSDVILACLPL-FHVTGFVgsLNTAVYVGGTYVLMAR---WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFktrDL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  768 LRGCTLLCGGEALAEDLAARMRGLSASTWN-LYGPTETTIWSARFRLGEEARPFLGGPLENTALYILDSE-MNPCPPGVA 845
Cdd:cd05935    199 SSLKVLTGGGAPMPPAVAEKLLKLTGLRFVeGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIEtGRELPPNEV 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  846 GELLIGGDGLARGYHRRPGLTAERFLPDpfaaDGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLE 925
Cdd:cd05935    279 GEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  926 QDSVREAVVVAQPG-VAGPTLVAYLV--PTEAALVDAES----ARQQelrsalknsllavLPDYMVPAHMLLLENLPLTP 998
Cdd:cd05935    355 HPAI*EVCVISVPDeRVGEEVKAFIVlrPEYRGKVTEEDiiewAREQ-------------MAAYKYPREVEFVDELPRSA 421

                   ....*....
gi 2183974163  999 NGKINRKAL 1007
Cdd:cd05935    422 SGKILWRLL 430
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
534-1007 8.14e-43

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 164.14  E-value: 8.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  534 ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS 613
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 qqsvlarlpqsdglqslllddlerlvhgypaenpdlpEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGML 693
Cdd:cd05971     85 -------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLF 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  694 ARDRLLSVTTFSFDIFG--LELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRML------CDSERV 765
Cdd:cd05971    128 PRDGDLYWTPADWAWIGglLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrqqgeqLKHAQV 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  766 DLLrgcTLLCGGEALAEDLAARMR-GLSASTWNLYGPTEttiwsARFRLGEEARPF------LGGPLENTALYILDSEMN 838
Cdd:cd05971    208 KLR---AIATGGESLGEELLGWAReQFGVEVNEFYGQTE-----CNLVIGNCSALFpikpgsMGKPIPGHRVAIVDDNGT 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  839 PCPPGVAGELLIG-GDGLAR-GYHRRPGLTAERFLPDPFaadgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 916
Cdd:cd05971    280 PLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  917 GEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVDaesarqQELRSALKNSLLAVLPDYMVPAHMLLLENLP 995
Cdd:cd05971    352 AEIEECLLKHPAVLMAAVVGIPDpIRGEIVKAFVVLNPGETPS------DALAREIQELVKTRLAAHEYPREIEFVNELP 425
                          490
                   ....*....|..
gi 2183974163  996 LTPNGKINRKAL 1007
Cdd:cd05971    426 RTATGKIRRREL 437
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3089-3183 8.69e-43

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 165.58  E-value: 8.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3089 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3168
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90
                   ....*....|....*
gi 2183974163 3169 YPEERQAYMLEDSGV 3183
Cdd:cd17655     81 YPEERIQYILEDSGA 95
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1576-2070 1.42e-42

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 166.26  E-value: 1.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAERPRATAVVY------GERALDYGELNLRANRLAHRLIELGVGPDVlVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:cd05931      1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPS---DRLGYMIEDSGIRLLLTQRAARERL-------PLGEGLPCLLLDAEHewAGYPESDPQSAVGVDNLAYVIYT 1719
Cdd:cd05931     80 PPTPGrhaERLAAILADAGPRVVLTTAAALAAVrafaasrPAAGTPRLLVVDLLP--DTSAADWPPPSPDPDDIAYLQYT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1720 SGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDA---W-SLFHSYAFDFSvweIFGALLHGGRLVIV-PYETSRSPEDF 1794
Cdd:cd05931    158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVvvsWlPLYHDMGLIGG---LLTPLYSGGPSVLMsPAAFLRRPLRW 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1795 LRLLCRERVTVlnqTPS---AFkQLMQVACAGQEVPPLAL---RHVVFGGEALEVQALRPWFERFGD---RAPRLVNMYG 1865
Cdd:cd05931    235 LRLISRYRATI---SAApnfAY-DLCVRRVRDEDLEGLDLsswRVALNGAEPVRPATLRRFAEAFAPfgfRPEAFRPSYG 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1866 ITETTVHVT------------YRPLSLADLDGGAASPI---------GEPIPDLSWYLLDA-GLNPVPRGCIGELYVGGA 1923
Cdd:cd05931    311 LAEATLFVSggppgtgpvvlrVDRDALAGRAVAVAADDpaarelvscGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGP 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1924 GLARGYLNRPELSCTRFVADPfSTTGGRLYRTGDLARYRcDGVVEYVGRIDHQVKIRGFRIELGEIEARLLA-----QPG 1998
Cdd:cd05931    391 SVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEahpalRPG 468
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 1999 VAEAVVLPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALKAslpEHMVPAH-LLFLER--LPLTANGKLDRRA 2070
Cdd:cd05931    469 CVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAR---EHGVAPAdVVLVRPgsIPRTSSGKIQRRA 540
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1584-2071 8.07e-42

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 161.49  E-value: 8.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1584 ATAVVYGERALDYGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYmie 1662
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY--- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1663 dsgirllltqraarerlPLGEGLPCLLLDAEHEWAgypesdpqsavgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDA 1742
Cdd:cd05958     78 -----------------ILDKARITVALCAHALTA------------SDDICILAFTSGTTGAPKATMHFHRDPLASADR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1743 -TRHWFGFSADDAW----SLFHSYAFDFSVWEIFGAllhGGRLVIVPyetSRSPEDFLRLLCRERVTVLNQTPSAFKQLM 1817
Cdd:cd05958    129 yAVNVLRLREDDRFvgspPLAFTFGLGGVLLFPFGV---GASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYRAML 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1818 QVACAGQevPPLA-LRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETtVHVtyrplsLADLDGGAASP--IGEP 1894
Cdd:cd05958    203 AHPDAAG--PDLSsLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEM-FHI------FISARPGDARPgaTGKP 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1895 IPDLSWYLLDAGLNPVPRGCIGELYVGGaglargylnrpELSCtRFVADPFSTT---GGRLYrTGDLARYRCDGVVEYVG 1971
Cdd:cd05958    271 VPGYEAKVVDDEGNPVPDGTIGRLAVRG-----------PTGC-RYLADKRQRTyvqGGWNI-TGDTYSRDPDGYFRHQG 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV-GYVVTQAAPSDPAALRDTLRQALKASLPEHMVPA 2050
Cdd:cd05958    338 RSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVkAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPR 417
                          490       500
                   ....*....|....*....|.
gi 2183974163 2051 HLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05958    418 AIEFVTELPRTATGKLQRFAL 438
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2640-2874 8.18e-42

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 155.20  E-value: 8.18e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2640 LSPMQQGMLFHslyQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGalEKPLQLVRKRVEVPFSVH 2718
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGpLDVEALERALRELVRRHPALRTRFVEED--GEPVQRIDPDADLPLEVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2719 DWRD--RADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSR 2796
Cdd:COG4908     76 DLSAlpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2797 S------DGRYRDYIAWLQRQ----DAGRTEAFWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQRLAEFA 2866
Cdd:COG4908    156 PpplpelPIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235

                   ....*...
gi 2183974163 2867 REQKVTLN 2874
Cdd:COG4908    236 KAHGATVN 243
PRK06178 PRK06178
acyl-CoA synthetase; Validated
496-1007 1.35e-41

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 163.67  E-value: 1.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  496 LQRSRLPAS-----EYPAGQ-GVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALER 569
Cdd:PRK06178    13 LQQAAWPAGiprepEYPHGErPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  570 GVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQ-------QSVLARLPQSDGLQSLLLD--------- 633
Cdd:PRK06178    93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALdqlapvvEQVRAETSLRHVIVTSLADvlpaeptlp 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  634 ----------------DLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHR-----ALTNFVCSIARQPGm 692
Cdd:PRK06178   173 lpdslraprlaaagaiDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGED- 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  693 lardrllSVTTFSFDIF-----GLELYVPLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDSERV-- 765
Cdd:PRK06178   252 -------SVFLSFLPEFwiageNFGLLFPLFSGATLVLLAR---WDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFae 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  766 -DL--LRGCTLLCGGEALAEDLAARMRGLSASTW--NLYGPTET----TIwSARFRLGEE---ARP-FLGGPLENTALYI 832
Cdd:PRK06178   322 yDLssLRQVRVVSFVKKLNPDYRQRWRALTGSVLaeAAWGMTEThtcdTF-TAGFQDDDFdllSQPvFVGLPVPGTEFKI 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  833 LDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRG 911
Cdd:PRK06178   401 CDFETGeLLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL------RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  912 FRIELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAvlpdYMVPaHMLL 990
Cdd:PRK06178   473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPdKGQVPVAFVQLKPGADLTAA-----ALQAWCRENMAV----YKVP-EIRI 542
                          570
                   ....*....|....*..
gi 2183974163  991 LENLPLTPNGKINRKAL 1007
Cdd:PRK06178   543 VDALPMTATGKVRKQDL 559
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
70-477 1.73e-41

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 159.39  E-value: 1.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   70 YNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDGFRQQVLASVDVPVPVTlagdDDAQAQIRAFVESETQ 149
Cdd:cd19542     22 YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPIEEV----ETDEDSLDALTRDLLD 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  150 QPFdLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYgarrqgiEATLPDLPIQYADYAiwqRHwLE 229
Cdd:cd19542     98 DPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY-------NGQLLPPAPPFSDYI---SY-LQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  230 AGERERQLEYWMARLGGGQSVLElptdrqrPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYS 309
Cdd:cd19542    166 SQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQAAWALVLARYT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  310 GQDEIRVGVPVANRN--RVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALqpeRSLS 387
Cdd:cd19542    239 GSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRAL---GLWP 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  388 HSPLFQAMYNHQNLGSAGrqslAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWR 467
Cdd:cd19542    316 SGTLFNTLVSYQNFEASP----ESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFD 391
                          410
                   ....*....|
gi 2183974163  468 NLLEAVVAEP 477
Cdd:cd19542    392 DILEALLANP 401
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1531-2073 2.01e-41

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 163.14  E-value: 2.01e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1531 IVARPEARIAELKLLDEAEARADLlQWNPGPQDFT--PASCL---HRLIERQAA-ERPRATAVVY----GERALDYGELN 1600
Cdd:PRK04319     2 KVETLPVIKGEPNLKDYEETYATF-SWEEVEKEFSwlETGKVniaYEAIDRHADgGRKDKVALRYldasRKEKYTYKELK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1601 LRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPL----DPRYPSDRLgymiEDSGIRLLLTQRAAR 1676
Cdd:PRK04319    81 ELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRL----EDSEAKVLITTPALL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1677 ERLPLGEgLPCL---------------LLDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGN------ 1735
Cdd:PRK04319   157 ERKPADD-LPSLkhvllvgedveegpgTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAmlqhyq 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1736 ----VLRLFDATRHWfgFSADDAWSLFHSYAfdfsvweIFGALLHGGRLVIvpYETSRSPEDFLRLLCRERVTVLNQTPS 1811
Cdd:PRK04319   236 tgkyVLDLHEDDVYW--CTADPGWVTGTSYG-------IFAPWLNGATNVI--DGGRFSPERWYRILEDYKVTVWYTAPT 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1812 AFKQLMQvacAGQEVPP----LALRHVVFGGEALEVQALRpWFER-FGDrapRLVNMYGITETTVH--VTY-----RPLS 1879
Cdd:PRK04319   305 AIRMLMG---AGDDLVKkydlSSLRHILSVGEPLNPEVVR-WGMKvFGL---PIHDNWWMTETGGImiANYpamdiKPGS 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1880 LadldggaaspiGEPIPDLSWYLLDAGLNPVPRGCIGELYV--GGAGLARGYLNRPE--LSCtrFVADpfsttggrLYRT 1955
Cdd:PRK04319   378 M-----------GKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEkyESY--FAGD--------WYVS 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1956 GDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV--------GYvvtqaAPSD 2027
Cdd:PRK04319   437 GDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIkafvalrpGY-----EPSE 511
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163 2028 paALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:PRK04319   512 --ELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1574-2071 3.42e-41

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 160.80  E-value: 3.42e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK06839     8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQR---AARERLPLGEGL--------PCLLLDAEHEWAGYP-ESDPqsavgvdnlaYVI-YT 1719
Cdd:PRK06839    88 TENELIFQLKDSGTTVLFVEKtfqNMALSMQKVSYVqrvisitsLKEIEDRKIDNFVEKnESAS----------FIIcYT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1720 SGSTGKPKGTLLPHGNVlrLFDATRHWFG--FSADDA----WSLFHSYAFDFSVweiFGALLHGGRlVIVPYETsrSPED 1793
Cdd:PRK06839   158 SGTTGKPKGAVLTQENM--FWNALNNTFAidLTMHDRsivlLPLFHIGGIGLFA---FPTLFAGGV-IIVPRKF--EPTK 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1794 FLRLLCRERVTVLNQTPSAFKQLMQvaCAGQEVPPL-ALRHVVFGGEALEVQALRpwfeRFGDRAPRLVNMYGITETTVH 1872
Cdd:PRK06839   230 ALSMIEKHKVTVVMGVPTIHQALIN--CSKFETTNLqSVRWFYNGGAPCPEELMR----EFIDRGFLFGQGFGMTETSPT 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1873 VTYrpLSLADLDGGAASpIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPElsctrfvADPFSTTGGRL 1952
Cdd:PRK06839   304 VFM--LSEEDARRKVGS-IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPD-------ATEETIQDGWL 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1953 YrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGATQLVGYVVTQAAPSDPAA 2030
Cdd:PRK06839   374 C-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVgrQHVKWGEIPIAFIVKKSSSVLIEKD 452
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2183974163 2031 LRDTLRQalkaSLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06839   453 VIEHCRL----FLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK08316 PRK08316
acyl-CoA synthetase; Validated
520-1002 5.74e-41

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 160.87  E-value: 5.74e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLSQ-------QSVLARLPQSDGLQSLLLD---------DLERLVHGYPAENPDLPEAPDSLCYAIYTS 663
Cdd:PRK08316   101 AYILDHSGARAFLVDpalaptaEAALALLPVDTLILSLVLGgreapggwlDFADWAEAGSVAEPDVELADDDLAQILYTS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  664 GSTGQPKGVMVRHRALT-NFVCSIArQPGMLARDRLLSVT----TFSFDIF-GLELYVplarGASMLLAsreQAQDPEAL 737
Cdd:PRK08316   181 GTESLPKGAMLTHRALIaEYVSCIV-AGDMSADDIPLHALplyhCAQLDVFlGPYLYV----GATNVIL---DAPDPELI 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  738 LDLVERQGVTVLQATPATWRMLC---DSERVDL--LRGCtllCGG------EALAEdLAARMRGLsaSTWNLYGPTE--- 803
Cdd:PRK08316   253 LRTIEAERITSFFAPPTVWISLLrhpDFDTRDLssLRKG---YYGasimpvEVLKE-LRERLPGL--RFYNCYGQTEiap 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  804 -TTIWSAR---FRLGEEARPFLggpleNTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADG 879
Cdd:PRK08316   327 lATVLGPEehlRRPGSAGRPVL-----NVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF------RGG 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  880 srLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVD 958
Cdd:PRK08316   396 --WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDpKWIEAVTAVVVPKAGATVT 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163  959 AES----ARQQelrsalknsllavLPDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:PRK08316   474 EDEliahCRAR-------------LAGFKVPKRVIFVDELPRNPSGKI 508
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1573-2069 7.78e-41

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 160.82  E-value: 7.78e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQR-------AARERLP-------LGEGLPCLLLDAEHEW-----AGYPESD--PQSAvgvD 1711
Cdd:PRK07798    88 VEDELRYLLDDSDAVALVYERefaprvaEVLPRLPklrtlvvVEDGSGNDLLPGAVDYedalaAGSPERDfgERSP---D 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1712 NLaYVIYTSGSTGKPKGTLLPHGNVLR-LFDATRHWFGFSADDAWSLFHSYAFDF--------------SVWEIFGALLH 1776
Cdd:PRK07798   165 DL-YLLYTGGTTGMPKGVMWRQEDIFRvLLGGRDFATGEPIEDEEELAKRAAAGPgmrrfpapplmhgaGQWAAFAALFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1777 GGRLVIVPyETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPL-ALRHVVFGGEALEVQALRPWFERFGD 1855
Cdd:PRK07798   244 GQTVVLLP-DVRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLsSLFAIASGGALFSPSVKEALLELLPN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1856 RAprLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEpipdlSWYLLDAGLNPVPRGcigelyVGGAG-LAR------G 1928
Cdd:PRK07798   323 VV--LTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPG------SGEIGwIARrghiplG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1929 YLNRPELSctrfvADPFSTTGGRLYR-TGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--L 2005
Cdd:PRK07798   390 YYKDPEKT-----AETFPTIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVvgV 464
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2006 PHEGPGatQLVGYVVTQAAPSDPAAlrDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRR 2069
Cdd:PRK07798   465 PDERWG--QEVVAVVQLREGARPDL--AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
506-1007 2.31e-40

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 158.26  E-value: 2.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  506 YPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGG 585
Cdd:cd05920     11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  586 AYVPLDPQYPADRLQYMIDDSGLRLLlsqqsVLARLPQSDGLQSLLLDDLErlvhgypaenpdlpEAPDSLCYAIyTSGS 665
Cdd:cd05920     91 VPVLALPSHRRSELSAFCAHAEAVAY-----IVPDRHAGFDHRALARELAE--------------SIPEVALFLL-SGGT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  666 TGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFD-------IFGLelyvpLARGASMLLASREqaqDPEALL 738
Cdd:cd05920    151 TGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfplacpgVLGT-----LLAGGRVVLAPDP---SPDAAF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  739 DLVERQGVTVLQATPAT---WRMLCDSERVDLLRGCTLLCGGEALAEDLAARMRG-LSASTWNLYGPTETTIWSARFR-- 812
Cdd:cd05920    223 PLIEREGVTVTALVPALvslWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvLGCTLQQVFGMAEGLLNYTRLDdp 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  813 ----LGEEARPFlgGPLENtaLYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDL 888
Cdd:cd05920    303 deviIHTQGRPM--SPDDE--IRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDL 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  889 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALvdaesaRQQEL 967
Cdd:cd05920    372 VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDeLLGERSCAFVVLRDPPP------SAAQL 445
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2183974163  968 RSALKNSLLAvlpDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05920    446 RRFLRERGLA---AYKLPDRIEFVDSLPLTAVGKIDKKAL 482
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1550-2066 2.49e-40

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 160.44  E-value: 2.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1550 ARADLLQWNPGPQDFTPASCLhrliERQAAERPRATAVVY------GERALDYGELNLRANRLAHRLIELGVGPDVLVGL 1623
Cdd:cd17634     39 PGAPSIKWFEDATLNLAANAL----DRHLRENGDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAI 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1624 AAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT-----------------QRAA----------- 1675
Cdd:cd17634    115 YMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvplkknvDDALnpnvtsvehvi 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 ---RERLPLGeGLPCLLLDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGN-VLRLFDATRHWFGFSA 1751
Cdd:cd17634    195 vlkRTGSDID-WQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DD--------AWSLFHSyafdfsvWEIFGALLHGGRLVIvpYE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVA 1820
Cdd:cd17634    274 GDiywctadvGWVTGHS-------YLLYGPLACGATTLL--YEgvpNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAG 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1821 CAGQEVPPLALRHVVFG-GEALEVQALRPWFERFGDRAPRLVNMYGITETT-VHVTYRPLsLADLDGGAASpigEPIPDL 1898
Cdd:cd17634    345 DDAIEGTDRSSLRILGSvGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGgFMITPLPG-AIELKAGSAT---RPVFGV 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLDAGLNPVPRGCIGELYVGGA--GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQ 1976
Cdd:cd17634    421 QPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRSDDV 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1977 VKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLF 2054
Cdd:cd17634    496 INVAGHRLGTAEIESVLVAHPKVAEAAVvgIPHAIKG-QAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHW 574
                          570
                   ....*....|..
gi 2183974163 2055 LERLPLTANGKL 2066
Cdd:cd17634    575 VDSLPKTRSGKI 586
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
49-477 9.13e-40

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 154.91  E-value: 9.13e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   49 PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEqLDGFRQQVLASVDVPVP- 127
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDG-LGQPVQVVHRQAQVPVTe 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  128 VTLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDH-VLTLTIHHVAADGWSMRVLVEELIALYGARRQGI 206
Cdd:cd19536     82 LDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  207 EATLPdlPIQ-YADYAIWQRhwlEAGERERQLEYWMARLGGgqsvLELPTdrqRPALPSYRGARHELQLPQALGRQLQA- 284
Cdd:cd19536    162 PLSLP--PAQpYRDFVAHER---ASIQQAASERYWREYLAG----ATLAT---LPALSEAVGGGPEQDSELLVSVPLPVr 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  285 ---LAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVET--ERLIGFFVNTQVLRADLdAQMPFLDLLQQTR 359
Cdd:cd19536    230 srsLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaERLLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  360 VAALGAQSHQDLPfeqlVEALQpeRSLSHSPLFQAMYNHQNlgsaGRQSLAAQLPGLSVEDLSWGAHSAQ---FDLTLDT 436
Cdd:cd19536    309 EQELESLSHEQVP----LADIQ--RCSEGEPLFDSIVNFRH----FDLDFGLPEWGSDEGMRRGLLFSEFksnYDVNLSV 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2183974163  437 YESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19536    379 LPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1119-1534 9.15e-40

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 153.88  E-value: 9.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1119 ERQWFIW-RLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPTLPiaieeRRPPVAG 1197
Cdd:cd19537      8 EREWWHKyQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPP-----RVQRVDT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1198 EDlkglVETEAHRPFDLqrgpllrvlllplATDECV--------LVLTLHHIIADGWSMQVLVDELIRVYAALRhdqppa 1269
Cdd:cd19537     83 LD----VWKEINRPFDL-------------EREDPIrvfispdtLLVVMSHIICDLTTLQLLLREVSAAYNGKL------ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1270 LAELPIQYADFAAWQRQwmdggERERQLDYWVSRLGGeQPLLELPsdrPRPQQQSHRGRRIGIPLPAELAEALRRLAQAE 1349
Cdd:cd19537    140 LPPVRREYLDSTAWSRP-----ASPEDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSS 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1350 QGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFvntqvlraeLDgQLPFR------------ELLRQ 1417
Cdd:cd19537    211 GITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLF---------LE-PLPIRirfpsssdasaaDFLRA 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1418 VRQAVVEAQGHQdLPFEQLVDALQPERSLSHAPLFQVM--YNhqrdDHRGSRfaslGELEVEDLawDVQT-----AQFDL 1490
Cdd:cd19537    281 VRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFH----DDRGVS----LALPIPGV--EPLYtwaegAKFPL 349
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2183974163 1491 TLD-TYESSNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVAR 1534
Cdd:cd19537    350 MFEfTALSDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
535-1002 1.29e-39

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 154.85  E-value: 1.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQ 614
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  615 QSVLARLPQSDglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLA 694
Cdd:cd05903     81 ERFRQFDPAAM---------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  695 RDRLLSVTTFSFDI-FGLELYVPLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDS-----ERVDLL 768
Cdd:cd05903    134 GDVFLVASPMAHQTgFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMGATPFLTDLLNAveeagEPLSRL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  769 RgcTLLCGG----EALAEDLAARMRGLSASTWnlyGPTETTIWSARFRLGEEARPFL--GGPLENTALYILDSEMNPCPP 842
Cdd:cd05903    211 R--TFVCGGatvpRSLARRAAELLGAKVCSAY---GSTECPGAVTSITPAPEDRRLYtdGRPLPGVEIKVVDDTGATLAP 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  843 GVAGELLIGGDGLARGYHRRPGLTAeRFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRiDHQVKIR-GFRIELGEIET 921
Cdd:cd05903    286 GVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGW-------FRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVED 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  922 RLLEQDSVREAVVVAQPGV-AGPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAvlpDYMVPAHMLLLENLPLTPNG 1000
Cdd:cd05903    357 LLLGHPGVIEAAVVALPDErLGERACAVVVTKSGALLTFD-----ELVAYLDRQGVA---KQYWPERLVHVDDLPRTPSG 428

                   ..
gi 2183974163 1001 KI 1002
Cdd:cd05903    429 KV 430
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1576-2065 2.42e-39

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 155.42  E-value: 2.42e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAERPRATAV-VYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPS 1654
Cdd:PRK07514    10 RAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1655 DRLGYMIEDSGIRLLLTQRAARERL-PLGE--GLPCLL-LDAEHEW------AGYPESDPQSAVGVDNLAYVIYTSGSTG 1724
Cdd:PRK07514    90 AELDYFIGDAEPALVVCDPANFAWLsKIAAaaGAPHVEtLDADGTGslleaaAAAPDDFETVPRGADDLAAILYTSGTTG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1725 KPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAfdfsvweIF----GALLHGGRLVIVPyetSRSPEDFLR 1796
Cdd:PRK07514   170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDvlihALPIFHTHG-------LFvatnVALLAGASMIFLP---KFDPDAVLA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1797 LLcrERVTVLNQTPSAFKQLMQVACAGQEvpplALRHV---VFGGEALEVQALRPWFERFGDrapRLVNMYGITETTVhV 1873
Cdd:PRK07514   240 LM--PRATVMMGVPTFYTRLLQEPRLTRE----AAAHMrlfISGSAPLLAETHREFQERTGH---AILERYGMTETNM-N 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSlADLDGGAaspIGEPIPDLSWYLLDAGLN-PVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrl 1952
Cdd:PRK07514   310 TSNPYD-GERRAGT---VGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1953 YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE-AVV-LPHE--GPGATQLVgyVVTQAAPSDP 2028
Cdd:PRK07514   379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsAVIgVPHPdfGEGVTAVV--VPKPGAALDE 456
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2183974163 2029 AAlrdtLRQALKASLPEHMVPAHLLFLERLPLTANGK 2065
Cdd:PRK07514   457 AA----ILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
485-1007 4.04e-39

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 155.98  E-value: 4.04e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  485 PLLDAEERAtllqRSRlpaseyPAGQGVHRL----FEAQAGLTPDAPALL------FGEERLSYAELNALANRLAWRLRE 554
Cdd:PRK13295     5 AVLLPPRRA----ASI------AAGHWHDRTinddLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLAR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  555 EGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ--------SVLARL-PQSD 625
Cdd:PRK13295    75 LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKtfrgfdhaAMARRLrPELP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  626 GLQSLLL------DDLERLVHGYPAEN-PDLPE-------APDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPG 691
Cdd:PRK13295   155 ALRHVVVvggdgaDSFEALLITPAWEQePDAPAilarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  692 MLARDRLLSVTTFSFDI-FGLELYVPLARGASMLLasrEQAQDPEALLDLVERQGVT-VLQATPatwrMLCDSERVDLLR 769
Cdd:PRK13295   235 LGADDVILMASPMAHQTgFMYGLMMPVMLGATAVL---QDIWDPARAAELIRTEGVTfTMASTP----FLTDLTRAVKES 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  770 GC------TLLCGGEALAEDLAARMR-GLSASTWNLYGPTETTIWSArFRLG---EEARPFLGGPLENTALYILDSEMNP 839
Cdd:PRK13295   308 GRpvsslrTFLCAGAPIPGALVERARaALGAKIVSAWGMTENGAVTL-TKLDdpdERASTTDGCPLPGVEVRVVDADGAP 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  840 CPPGVAGELLIGGDGLARGYHRRPGLTAErflpdpfAADGsrLYRTGDLARYRADGVIEYLGRiDHQVKIRGFR-IELGE 918
Cdd:PRK13295   387 LPAGQIGRLQVRGCSNFGGYLKRPQLNGT-------DADG--WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVE 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  919 IETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAVlpDYMvPAHMLLLENLPLT 997
Cdd:PRK13295   457 IEALLYRHPAIAQVAIVAYPDERlGERACAFVVPRPGQSLDFE-----EMVEFLKAQKVAK--QYI-PERLVVRDALPRT 528
                          570
                   ....*....|
gi 2183974163  998 PNGKINRKAL 1007
Cdd:PRK13295   529 PSGKIQKFRL 538
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
501-1007 4.40e-39

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 155.89  E-value: 4.40e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  501 LPAS-EYPAGQGVHRLfEAQAGLTPDAPALLFGEERLSYAELNALANRLA-WRLREEGVGSDVLVGIALERGVPMVVALL 578
Cdd:PRK08314     1 LPKSlTLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAgYLQQECGVRKGDRVLLYMQNSPQFVIAYY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  579 AVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQ---SDGLQSLLL--------DDLERLVHGYPAENP 647
Cdd:PRK08314    80 AILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPavgNLRLRHVIVaqysdylpAEPEIAVPAWLRAEP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  648 DLPEA------------------------PDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTT 703
Cdd:PRK08314   160 PLQALapggvvawkealaaglappphtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  704 FsFDIFGLE--LYVPLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPAtwrMLCD------SERVDLlrgCTLLC 775
Cdd:PRK08314   240 L-FHVTGMVhsMNAPIYAGATVVLMPR---WDREAAARLIERYRVTHWTNIPT---MVVDflaspgLAERDL---SSLRY 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  776 ---GGEALAEDLAARMRGLSASTW-NLYGPTETTiwsARFRLGEEARP---FLGGPLENTALYILDSEM-NPCPPGVAGE 847
Cdd:PRK08314   310 iggGGAAMPEAVAERLKELTGLDYvEGYGLTETM---AQTHSNPPDRPklqCLGIPTFGVDARVIDPETlEELPPGEVGE 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  848 LLIGGDGLARGYHRRPGLTAERFlpdpFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQD 927
Cdd:PRK08314   387 IVVHGPQVFKGYWNRPEATAEAF----IEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  928 SVREAVVVAQPGV-AGPTLVAYLV--PTEAALVDAES----ARQQelrsalknslLAVlpdYMVPAHMLLLENLPLTPNG 1000
Cdd:PRK08314   463 AIQEACVIATPDPrRGETVKAVVVlrPEARGKTTEEEiiawAREH----------MAA---YKYPRIVEFVDSLPKSGSG 529

                   ....*..
gi 2183974163 1001 KINRKAL 1007
Cdd:PRK08314   530 KILWRQL 536
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
509-1007 9.38e-39

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 154.53  E-value: 9.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  509 GQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGV--GSDVLVgiALERGVPMVVALLAVLKAGGA 586
Cdd:COG1021     24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLrpGDRVVV--QLPNVAEFVIVFFALFRAGAI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  587 YVPLdpqYPADR---LQYMIDDSGLRLLLSQ------------QSVLARLPqsdGLQSLLLD-------DLERLVHGyPA 644
Cdd:COG1021    102 PVFA---LPAHRraeISHFAEQSEAVAYIIPdrhrgfdyralaRELQAEVP---SLRHVLVVgdageftSLDALLAA-PA 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  645 ENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRAltnFVCSI---ARQPGMLARDRLLSV-------TTFSFDIFGlely 714
Cdd:COG1021    175 DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDD---YLYSVrasAEICGLDADTVYLAAlpaahnfPLSSPGVLG---- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  715 vPLARGASMLLASREqaqDPEALLDLVERQGVTVLQATPA---TWRMLCDSERVDL--LRgcTLLCGGEALAEDLAARMR 789
Cdd:COG1021    248 -VLYAGGTVVLAPDP---SPDTAFPLIERERVTVTALVPPlalLWLDAAERSRYDLssLR--VLQVGGAKLSPELARRVR 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  790 -GLSASTWNLYGPTETTIWSARFRLGEEARpflggplENTA---------LYILDSEMNPCPPGVAGELLIGGDGLARGY 859
Cdd:COG1021    322 pALGCTLQQVFGMAEGLVNYTRLDDPEEVI-------LTTQgrpispddeVRIVDEDGNPVPPGEVGELLTRGPYTIRGY 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  860 HRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHQVkIR-GFRIELGEIETRLLEQDSVREAVVVAQP 938
Cdd:COG1021    395 YRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMP 466
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  939 GVA-GPTLVAYLVPTEAALvdaesaRQQELRSALKNSLLAvlpDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:COG1021    467 DEYlGERSCAFVVPRGEPL------TLAELRRFLRERGLA---AFKLPDRLEFVDALPLTAVGKIDKKAL 527
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
536-1007 9.48e-39

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 152.27  E-value: 9.48e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ 615
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SVLARLPQSDGLqslllddlerLVHgypaenpdlpeapdslcyaiYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05969     81 ELYERTDPEDPT----------LLH--------------------YTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPD 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLS------VTTFSFDIFGlelyvPLARGASMLlaSREQAQDPEALLDLVERQGVTVLQATPATWRMLCDS-----ER 764
Cdd:cd05969    131 DIYWCtadpgwVTGTVYGIWA-----PWLNGVTNV--VYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdelaRK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  765 VDL--LRgcTLLCGGEAL-AEDLAARMRGLSASTWNLYGPTET-TIWSARFrLGEEARP-FLGGPLENTALYILDSEMNP 839
Cdd:cd05969    204 YDLssLR--FIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETgSIMIANY-PCMPIKPgSMGKPLPGVKAAVVDENGNE 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  840 CPPGVAGELLIGGD--GLARGYHRRPGLTAERFLpdpfaaDGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 917
Cdd:cd05969    281 LPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI------DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  918 EIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAalVDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPL 996
Cdd:cd05969    353 EVESALMEHPAVAEAGVIGKPDpLRGEIIKAFISLKEG--FEPSDELKEEIINFVRQKLGA----HVAPREIEFVDNLPK 426
                          490
                   ....*....|.
gi 2183974163  997 TPNGKINRKAL 1007
Cdd:cd05969    427 TRSGKIMRRVL 437
PRK07798 PRK07798
acyl-CoA synthetase; Validated
515-1001 1.13e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 154.27  E-value: 1.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  515 LFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQY 594
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  595 PADRLQYMIDDSGLRLLLSQQS-------VLARLPQ-------SDGLQSLLLD---DLERLVHGYPAENPDLPEAPDSLc 657
Cdd:PRK07798    88 VEDELRYLLDDSDAVALVYEREfaprvaeVLPRLPKlrtlvvvEDGSGNDLLPgavDYEDALAAGSPERDFGERSPDDL- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  658 YAIYTSGSTGQPKGVMVRHraltnfvcSIARQPGMLARDRLLS--------VTTFSFDIFGLELYV--PLARGASMLLA- 726
Cdd:PRK07798   167 YLLYTGGTTGMPKGVMWRQ--------EDIFRVLLGGRDFATGepiedeeeLAKRAAAGPGMRRFPapPLMHGAGQWAAf 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  727 -----------SREQAQDPEALLDLVERQGVTVLQAT-PATWRMLCDS----ERVDLLRGCTLLCGGEALAEDLAARMRG 790
Cdd:PRK07798   239 aalfsgqtvvlLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDAlearGPYDLSSLFAIASGGALFSPSVKEALLE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  791 L--SASTWNLYGPTET----TIWSARFRLGEEARPFLGGPleNTALyiLDSEMNPCPPGvagellIGGDG-LAR------ 857
Cdd:PRK07798   319 LlpNVVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIGP--RTVV--LDEDGNPVEPG------SGEIGwIARrghipl 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  858 GYHRRPGLTAERFlpdpFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQ 937
Cdd:PRK07798   389 GYYKDPEKTAETF----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGV 464
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  938 PGVA-GPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGK 1001
Cdd:PRK07798   465 PDERwGQEVVAVVQLREGARPDLA-----ELRAHCRSSLAG----YKVPRAIWFVDEVQRSPAGK 520
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
502-1005 2.02e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 154.39  E-value: 2.02e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  502 PAS-EYPAGQGVHrLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAV 580
Cdd:PRK05605    24 PHDlDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  581 LKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL---SQQSVLARLPQSDGLQSLLLDDL---------------------- 635
Cdd:PRK05605   103 LRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTPLETIVSVNMiaampllqrlalrlpipalrka 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  636 --------------ERLVH---GYPAENPDLPE-APDSLCYAIYTSGSTGQPKGVMVRHRAL-TNFVCSIARQPGMLARD 696
Cdd:PRK05605   183 raaltgpapgtvpwETLVDaaiGGDGSDVSHPRpTPDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGP 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  697 -RLLSVTTFsFDIFGLELYVPLAR--GASMLLASREqaqDPEALLDLVERQGVTVLQATPATWRMLCDS---ERVDLLRG 770
Cdd:PRK05605   263 eRVLAALPM-FHAYGLTLCLTLAVsiGGELVLLPAP---DIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeeRGVDLSGV 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  771 CTLLCGGEALAEDLAARMRGLSAStwNL---YGPTETTIWSARFRLGEEARP-FLGGPLENTALYILDSEmNPC---PPG 843
Cdd:PRK05605   339 RNAFSGAMALPVSTVELWEKLTGG--LLvegYGLTETSPIIVGNPMSDDRRPgYVGVPFPDTEVRIVDPE-DPDetmPDG 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  844 VAGELLIGGDGLARGYHRRPGLTAERFLPDpfaadgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRL 923
Cdd:PRK05605   416 EEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  924 LEQDSVREAVVVAQPGVAGP-TLVAYLVPTEAALVDAESarqqeLRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKI 1002
Cdd:PRK05605   488 REHPGVEDAAVVGLPREDGSeEVVAAVVLEPGAALDPEG-----LRAYCREHLTR----YKVPRRFYHVDELPRDQLGKV 558

                   ...
gi 2183974163 1003 NRK 1005
Cdd:PRK05605   559 RRR 561
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1573-2071 2.56e-38

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 152.78  E-value: 2.56e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPRATaVVY-----GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAA---ERSLEMivgLLAILKAGGA 1644
Cdd:cd12119      1 LLEHAARLHGDRE-IVSrthegEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLEL---YYAVPGMGAV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1645 YVPLDPRYPSDRLGYMIEDSGIRLLLTQR-------AARERLPLGEGLPCL-------------------LLDAEHEWAG 1698
Cdd:cd12119     77 LHTINPRLFPEQIAYIINHAEDRVVFVDRdflplleAIAPRLPTVEHVVVMtddaampepagvgvlayeeLLAAESPEYD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1699 YPESDpqsavgvDNLAYVI-YTSGSTGKPKGTLLPH-GNVL-----RLFDAtrhwFGFSADDAW----SLFHSYAfdfsv 1767
Cdd:cd12119    157 WPDFD-------ENTAAAIcYTSGTTGNPKGVVYSHrSLVLhamaaLLTDG----LGLSESDVVlpvvPMFHVNA----- 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1768 WEI-FGALLHGGRLVIV-PYEtsrSPEDFLRLLCRERVTVLNQTPSAFKQLMQ-VACAGQEVPPLalRHVVFGGEALEvQ 1844
Cdd:cd12119    221 WGLpYAAAMVGAKLVLPgPYL---DPASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSL--RRVVIGGSAVP-R 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1845 ALRPWFErfgDRAPRLVNMYGITETT--VHVTYRPLSLADLDGGAA----SPIGEPIPDLSWYLLDAGLNPVPR--GCIG 1916
Cdd:cd12119    295 SLIEAFE---ERGVRVIHAWGMTETSplGTVARPPSEHSNLSEDEQlalrAKQGRPVPGVELRIVDDDGRELPWdgKAVG 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1917 ELYVGGAGLARGYLNRPElsctrfvADPFSTTGGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQ 1996
Cdd:cd12119    372 ELQVRGPWVTKSYYKNDE-------ESEALTEDGWL-RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAH 443
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 1997 PGVAEAVVL--PHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALkaslPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd12119    444 PAVAEAAVIgvPHPKWGERPLAVVVLKEGATVTAEELLEFLADKV----AKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3089-3183 2.76e-38

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 151.97  E-value: 2.76e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3089 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3168
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90
                   ....*....|....*
gi 2183974163 3169 YPEERQAYMLEDSGV 3183
Cdd:cd12117     81 LPAERLAFMLADAGA 95
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
536-1007 4.67e-38

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 150.44  E-value: 4.67e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSqq 615
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 svlarlpqsdglqslllddlerlvhgypaenpdlpEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05907     84 -----------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLSVTTFSFdIFGLE--LYVPLARGASMLLASreqaqDPEALLDLVERQGVTVLQATPATWRMLCDSERVDL---LRG 770
Cdd:cd05907    129 DRHLSFLPLAH-VFERRagLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAvpgLKR 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  771 CTLL-----------CGGEALAEDLAARMRGLSASTWNLYGPTET----TIWSA-RFRLGEearpfLGGPLENTALYIld 834
Cdd:cd05907    203 KLFDlavggrlrfaaSGGAPLPAELLHFFRALGIPVYEGYGLTETsavvTLNPPgDNRIGT-----VGKPLPGVEVRI-- 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  835 semnpcppGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRI-DHQVKIRGFR 913
Cdd:cd05907    276 --------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKN 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  914 IELGEIETRLLEQDSVREAVVVAQpgvAGPTLVAYLVPTEAALVD------------AESARQQELRSALK---NSLLAV 978
Cdd:cd05907    341 ISPEPIENALKASPLISQAVVIGD---GRPFLVALIVPDPEALEAwaeehgiaytdvAELAANPAVRAEIEaavEAANAR 417
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2183974163  979 LPDYMVPAHMLLL------ENLPLTPNGKINRKAL 1007
Cdd:cd05907    418 LSRYEQIKKFLLLpepftiENGELTPTLKLKRPVI 452
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1565-2074 6.26e-38

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 151.68  E-value: 6.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1565 TPASCLHR------LIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAI 1638
Cdd:PRK06188     3 TMADLLHSgatyghLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1639 LKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAA-RER-LPLGEGLPCLLL--------DAEHEWAGYPESDPQSAV 1708
Cdd:PRK06188    83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPfVERaLALLARVPSLKHvltlgpvpDGVDLLAAAAKFGPAPLV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1709 GVD---NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFDFSVweifgALLHGGRLV 1781
Cdd:PRK06188   163 AAAlppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPrflmCTPLSHAGGAFFLP-----TLLRGGTVI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1782 IVPyetSRSPEDFLRLLCRERVTVLNQTPSAFKQLMqvacagqEVPPLA------LRHVVFGGEALEVQALRPWFERFGd 1855
Cdd:PRK06188   238 VLA---KFDPAEVLRAIEEQRITATFLVPTMIYALL-------DHPDLRtrdlssLETVYYGASPMSPVRLAEAIERFG- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1856 raPRLVNMYGITETTVHVTYrpLSLADLDGGAA---SPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNR 1932
Cdd:PRK06188   307 --PIFAQYYGQTEAPMVITY--LRKRDHDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1933 PELSCTRFvadpfstTGGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHE-- 2008
Cdd:PRK06188   383 PEETAEAF-------RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgvPDEkw 454
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2009 GPGATQLVgyVVTQAAPSDPAALRDTLRQAlKASlpeHMVPAHLLFLERLPLTANGKLDRRALPAP 2074
Cdd:PRK06188   455 GEAVTAVV--VLRPGAAVDAAELQAHVKER-KGS---VHAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK09088 PRK09088
acyl-CoA synthetase; Validated
519-1007 7.35e-38

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 150.73  E-value: 7.35e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  519 QAGLTPDAPAL--LFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPA 596
Cdd:PRK09088     4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  597 DRLQYMIDDSGLRLLLSQQSvlarlPQSDGLQSLLLDDLERLVHGY-PAENPDLPeaPDSLCYAIYTSGSTGQPKGVMVR 675
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDA-----VAAGRTDVEDLAAFIASADALePADTPSIP--PERVSLILFTSGTSGQPKGVMLS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 HRALTNFVCSIARQPGMLARDRLLsVTTFSFDIFGLELYV--PLARGASMLLASreqAQDPEALLDLVERQ--GVTVLQA 751
Cdd:PRK09088   157 ERNLQQTAHNFGVLGRVDAHSSFL-CDAPMFHIIGLITSVrpVLAVGGSILVSN---GFEPKRTLGRLGDPalGITHYFC 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDSERVD--LLRGCTLLCGGEA--LAEDLAARMR---------GLSASTWNLYGPTETTIWSARfrLGEEar 818
Cdd:PRK09088   233 VPQMAQAFRAQPGFDaaALRHLTALFTGGAphAAEDILGWLDdgipmvdgfGMSEAGTVFGMSVDCDVIRAK--AGAA-- 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  819 pflGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaaDGSRLYRTGDLARYRADGVIE 898
Cdd:PRK09088   309 ---GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-------TGDGWFRTGDIARRDADGFFW 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  899 YLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqELRSALKnsllA 977
Cdd:PRK09088   379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGAPLDLE-----RIRSHLS----T 449
                          490       500       510
                   ....*....|....*....|....*....|
gi 2183974163  978 VLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK09088   450 RLAKYKVPKHLRLVDALPRTASGKLQKARL 479
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
526-1007 1.46e-37

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 148.78  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  526 APALLFGEERLSYAELNALANRLAWRLREEGV---GSDVLvgIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGivpGNRVL--LRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSQQSVLARlpqsdglqslllddlerlvhgypaenpdlpeapDSLCYAIYTSGSTGQPKGVMVRHRALTNF 682
Cdd:cd05958     79 LDKARITVALCAHALTAS---------------------------------DDICILAFTSGTTGAPKATMHFHRDPLAS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  683 VCSIARQP-GMLARDRLLSVTTFSFDI-FGLELYVPLARGASMLLASREQAQDpeaLLDLVERQGVTVLQATPATWR-ML 759
Cdd:cd05958    126 ADRYAVNVlRLREDDRFVGSPPLAFTFgLGGVLLFPFGVGASGVLLEEATPDL---LLSAIARYKPTVLFTAPTAYRaML 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  760 CDSERVDLLRGCTLLC--GGEALAEDLAARMRGLSAS-TWNLYGPTET--TIWSARfrlGEEARP-FLGGPLENTALYIL 833
Cdd:cd05958    203 AHPDAAGPDLSSLRKCvsAGEALPAALHRAWKEATGIpIIDGIGSTEMfhIFISAR---PGDARPgATGKPVPGYEAKVV 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  834 DSEMNPCPPGVAGELLIGGDglargyhrrpglTAERFLPDPFAA---DGSRLYrTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:cd05958    280 DDEGNPVPDGTIGRLAVRGP------------TGCRYLADKRQRtyvQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  911 GFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLV-AYLVPTEAALVDAESARQqelrsaLKNSLLAVLPDYMVPAHML 989
Cdd:cd05958    347 GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVkAFVVLRPGVIPGPVLARE------LQDHAKAHIAPYKYPRAIE 420
                          490
                   ....*....|....*...
gi 2183974163  990 LLENLPLTPNGKINRKAL 1007
Cdd:cd05958    421 FVTELPRTATGKLQRFAL 438
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3099-3183 2.18e-37

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 148.44  E-value: 2.18e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd05930     81 EDSGA 85
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1594-2071 2.67e-37

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 148.05  E-value: 2.67e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1594 LDYGELNLRANRLAHRLIELGVGP-DVLVGLAAeRSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQ 1672
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPgDVVAGLLP-RTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1673 RAARERLPlgeglpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLP------HGNVLR----LFDA 1742
Cdd:cd05973     80 AANRHKLD------------------------------SDPFVMMFTSGTTGLPKGVPVPlralaaFGAYLRdavdLRPE 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1743 TRHWFgfSADDAWSLFHSYAfdfsvweIFGALLHGGRLVIvpYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACA 1822
Cdd:cd05973    130 DSFWN--AADPGWAYGLYYA-------ITGPLALGHPTIL--LEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAE 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1823 GQEVPPLALRHVVFGGEALEVQALRpWFerfGDRAPRLV-NMYGITETTV-----HVTYRPLSladldggaASPIGEPIP 1896
Cdd:cd05973    199 VPARPKGRLRRVSSAGEPLTPEVIR-WF---DAALGVPIhDHYGQTELGMvlanhHALEHPVH--------AGSAGRAMP 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1897 DLSWYLLDAGLNPVPRGCIGELYVGGAglargylNRPELSCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQ 1976
Cdd:cd05973    267 GWRVAVLDDDGDELGPGEPGRLAIDIA-------NSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDV 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1977 VKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLV-GYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFL 2055
Cdd:cd05973    340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVkAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFV 419
                          490
                   ....*....|....*.
gi 2183974163 2056 ERLPLTANGKLDRRAL 2071
Cdd:cd05973    420 DELPKTPSGKIQRFLL 435
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1573-2071 1.67e-36

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 147.39  E-value: 1.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK08316    16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQRAARERLP--------LGEGLPCLLLDAEHE--------WA-GYPESDPQSAVGVDNLAY 1715
Cdd:PRK08316    96 TGEELAYILDHSGARAFLVDPALAPTAEaalallpvDTLILSLVLGGREAPggwldfadWAeAGSVAEPDVELADDDLAQ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1716 VIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFDfsvweIF--GALLHGGRLVIVPyetSR 1789
Cdd:PRK08316   176 ILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDiplhALPLYHCAQLD-----VFlgPYLYVGATNVILD---AP 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1790 SPEDFLRLLCRERVTVLNQTPSAFKQLmqvacagqevpplaLRHVVFggEALEVQALR-----------PWFERFGDRAP 1858
Cdd:PRK08316   248 DPELILRTIEAERITSFFAPPTVWISL--------------LRHPDF--DTRDLSSLRkgyygasimpvEVLKELRERLP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1859 --RLVNMYGITE----TTVhvtyrpLSLADLDGGAASPiGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNR 1932
Cdd:PRK08316   312 glRFYNCYGQTEiaplATV------LGPEEHLRRPGSA-GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDD 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1933 PELSctrfvADPFSttGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHE-- 2008
Cdd:PRK08316   385 PEKT-----AEAFR--GG-WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVigLPDPkw 456
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2009 GPGATQLVgyVVTQAAPSDPAALRDTLRQALKAslpeHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08316   457 IEAVTAVV--VPKAGATVTEDELIAHCRARLAG----FKVPKRVIFVDELPRNPSGKILKREL 513
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1594-2071 1.88e-36

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 145.31  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1594 LDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQR 1673
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1674 AarerlplgeglpcllldaehewagypesdpqsavgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD 1753
Cdd:cd05935     82 E-----------------------------------LDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 ----AWSLFHSYAFDFSVweiFGALLHGGRLVIVpyetSRSPEDFLR-LLCRERVTVLNQTPSAFKQLMqvACAGQEVPP 1828
Cdd:cd05935    127 vilaCLPLFHVTGFVGSL---NTAVYVGGTYVLM----ARWDRETALeLIEKYKVTFWTNIPTMLVDLL--ATPEFKTRD 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1829 LALRHVVFGGEALEVQALRpwfERFGDRAP-RLVNMYGITETTVHVTYRPLSLADLdggaaSPIGEPIPDLSWYLLDA-G 1906
Cdd:cd05935    198 LSSLKVLTGGGAPMPPAVA---EKLLKLTGlRFVEGYGLTETMSQTHTNPPLRPKL-----QCLGIP*FGVDARVIDIeT 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfstTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:cd05935    270 GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWP 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVVL--PHEGPGATqLVGYVVTQAAPSDPAALRDTLRQAlKASLPEHMVPAHLLFLERLPLTANG 2064
Cdd:cd05935    346 AEVEAKLYKHPAI*EVCVIsvPDERVGEE-VKAFIVLRPEYRGKVTEEDIIEWA-REQMAAYKYPREVEFVDELPRSASG 423

                   ....*..
gi 2183974163 2065 KLDRRAL 2071
Cdd:cd05935    424 KILWRLL 430
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1570-2071 2.04e-36

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 146.50  E-value: 2.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALD--YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVP 1647
Cdd:cd05923      3 VFEMLRRAASRAPDACAIADPARGLRltYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLL------DAEHEWAGYPESDPQSAVGVDnlAYVIYTSG 1721
Cdd:cd05923     83 INPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLAlsdlvgLGEPESAGPLIEDPPREPEQP--AFVFYTSG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1722 STGKPKGTLLPHGNVLR--LFDAT----RHWFGFSADDAWSLFHSYAFdFSVweIFGALLHGGRLVIVPYEtsrSPEDFL 1795
Cdd:cd05923    161 TTGLPKGAVIPQRAAESrvLFMSTqaglRHGRHNVVLGLMPLYHVIGF-FAV--LVAALALDGTYVVVEEF---DPADAL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1796 RLLCRERVTVLNQTPSAFKQLM-QVACAGQEVPplALRHVVFGGEALEVQALrpwfERFGDRAP-RLVNMYGITEttvhv 1873
Cdd:cd05923    235 KLIEQERVTSLFATPTHLDALAaAAEFAGLKLS--SLRHVTFAGATMPDAVL----ERVNQHLPgEKVNIYGTTE----- 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSLADLDGGAA-----------SPIGEPIPDLswylldaglnpVPRGCIGELYVGGAGLA--RGYLNRPELSCTRF 1940
Cdd:cd05923    304 AMNSLYMRDARTGTEmrpgffsevriVRIGGSPDEA-----------LANGEEGELIVAAAADAafTGYLNQPEATAKKL 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1941 VAdpfsttggRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGY 2018
Cdd:cd05923    373 QD--------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVigVADERWGQSVTACV 444
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2019 VVTQAAPSDpaalrDTLRQALKAS-LPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05923    445 VPREGTLSA-----DELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
517-1007 2.94e-36

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 146.87  E-value: 2.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  517 EAQAGLTPDAPALLF----GEER-LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:cd05970     24 DAMAKEYPDKLALVWcddaGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLS------QQSVLARLPQSDGLQSLLL---------DDLERLVHGYPaenPDL--PEAPD 654
Cdd:cd05970    104 HQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPECPSKPKLVWvgdpvpegwIDFRKLIKNAS---PDFerPTANS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLC-----YAIYTSGSTGQPKgvMVRHR---ALTNFVCSIARQpGMLARDRLLSV--TTFSFDIFGlELYVPLARGASML 724
Cdd:cd05970    181 YPCgedilLVYFSSGTTGMPK--MVEHDftyPLGHIVTAKYWQ-NVREGGLHLTVadTGWGKAVWG-KIYGQWIAGAAVF 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  725 LASREQAqDPEALLDLVERQGVTVLQATPATWRMLC--DSERVDL--LRGCTLlcGGEALAEDLAARMRGLSA-STWNLY 799
Cdd:cd05970    257 VYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIreDLSRYDLssLRYCTT--AGEALNPEVFNTFKEKTGiKLMEGF 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  800 GPTETTIWSARFRlGEEARP-FLGGPLENTALYILDSEMNPCPPGVAGELLIGGD-----GLARGYHRRPGLTAERFlpd 873
Cdd:cd05970    334 GQTETTLTIATFP-WMEPKPgSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW--- 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  874 pfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPT 952
Cdd:cd05970    410 ---HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDpIRGQVVKATIVLA 484
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  953 EaalvDAESArqQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05970    485 K----GYEPS--EELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3091-3183 3.06e-36

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 145.95  E-value: 3.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3091 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3170
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90
                   ....*....|...
gi 2183974163 3171 EERQAYMLEDSGV 3183
Cdd:cd17651     81 AERLAFMLADAGP 93
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3087-3183 3.31e-36

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 145.27  E-value: 3.31e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3166
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90
                   ....*....|....*..
gi 2183974163 3167 PEYPEERQAYMLEDSGV 3183
Cdd:cd17644     82 PNYPQERLTYILEDAQI 98
PRK07787 PRK07787
acyl-CoA synthetase; Validated
514-1007 7.75e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 144.36  E-value: 7.75e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPD-APALLFGEERLSYAELNALANRLAWRLREEGvgsdvLVGIALERGVPMVVALLAVLKAGGAYVPLDP 592
Cdd:PRK07787     3 SLNPAAVAAAADiADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  593 QYPADRLQYMIDDSGLRLLLSqqsvlARLPQSDGLQSLLLDDLERLVHGYPaeNPDlpeaPDSLCYAIYTSGSTGQPKGV 672
Cdd:PRK07787    78 DSGVAERRHILADSGAQAWLG-----PAPDDPAGLPHVPVRLHARSWHRYP--EPD----PDAPALIVYTSGTTGPPKGV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  673 MVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLELYV--PLARGASMLLASREqaqDPEALLDLVERQGvTVLQ 750
Cdd:PRK07787   147 VLSRRAIAADLDALAEAWQWTADDVLVHGLPL-FHVHGLVLGVlgPLRIGNRFVHTGRP---TPEAYAQALSEGG-TLYF 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  751 ATPATW-RMLCDSERVDLLRGCTLLCGGEA-LAEDLAARMRGLSA-STWNLYGPTETTI-WSARFrlGEEARP-FLGGPL 825
Cdd:PRK07787   222 GVPTVWsRIAADPEAARALRGARLLVSGSAaLPVPVFDRLAALTGhRPVERYGMTETLItLSTRA--DGERRPgWVGLPL 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  826 ENTALYILDSEMNPCPPGVA--GELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGR- 902
Cdd:PRK07787   300 AGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRIVGRe 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  903 -IDhQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTL----VAYLV----PTEAALVDaESARQqelrsalkn 973
Cdd:PRK07787   373 sTD-LIKSGGYRIGAGEIETALLGHPGVREAAVV---GVPDDDLgqriVAYVVgaddVAADELID-FVAQQ--------- 438
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2183974163  974 slLAVlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07787   439 --LSV---HKRPREVRFVDALPRNAMGKVLKKQL 467
PRK06188 PRK06188
acyl-CoA synthetase; Validated
524-1007 9.49e-36

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 145.13  E-value: 9.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLS-----QQSVLARLPQSDGLQSLL-------LDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKG 671
Cdd:PRK06188   106 EDAGISTLIVdpapfVERALALLARVPSLKHVLtlgpvpdGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSfDIFGLELYVPLARGASMLLAsreQAQDPEALLDLVERQGVTVLQA 751
Cdd:PRK06188   186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVL---AKFDPAEVLRAIEEQRITATFL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDSERV---DLLRGCTLLCGGEALAED-LAARMRGLSASTWNLYGPTET----TIWSARFRLGEEARPFL-- 821
Cdd:PRK06188   262 VPTMIYALLDHPDLrtrDLSSLETVYYGASPMSPVrLAEAIERFGPIFAQYYGQTEApmviTYLRKRDHDPDDPKRLTsc 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  822 GGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLG 901
Cdd:PRK06188   342 GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG--WLHTGDVAREDEDGFYYIVD 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  902 RIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAVlp 980
Cdd:PRK06188   414 RKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVVLRPGAAVDAA-----ELQAHVKERKGSV-- 486
                          490       500
                   ....*....|....*....|....*..
gi 2183974163  981 dyMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06188   487 --HAPKQVDFVDSLPLTALGKPDKKAL 511
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1114-1535 1.13e-35

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 142.59  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1114 LSFAQERQWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHD-GAPRQVIHPTLPIAIEE-- 1190
Cdd:cd19536      4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTEld 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1191 -RRPPVAGEDLKGLVETEAHRPFDLQRGPLLRVLLLPLATDE-CVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPP 1268
Cdd:cd19536     84 lTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERErFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYKPL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1269 ALAElPIQYADFAAWQRQWMDGGERERqldYWVSRLGGEQpLLELPSdrPRPQQQSHRGRRIGIPLPAELAEALRRLAQA 1348
Cdd:cd19536    164 SLPP-AQPYRDFVAHERASIQQAASER---YWREYLAGAT-LATLPA--LSEAVGGGPEQDSELLVSVPLPVRSRSLAKR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1349 EQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREET--EGLIGFFVNTQVLRAELDGQlPFRELLRQVRQAVVEAQ 1426
Cdd:cd19536    237 SGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQELESL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1427 GHQDLPfeqLVDAlqpERSLSHAPLFQVMYNHqRDDHRGSRFASLGELEVEDLawDVQTAQFDLTLDTYESSNGLLAELT 1506
Cdd:cd19536    316 SHEQVP---LADI---QRCSEGEPLFDSIVNF-RHFDLDFGLPEWGSDEGMRR--GLLFSEFKSNYDVNLSVLPKQDRLE 386
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163 1507 ----YATDLFDASSAERIAGHWLNLLRSIVARP 1535
Cdd:cd19536    387 lklaYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1593-2066 1.29e-35

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 142.90  E-value: 1.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1593 ALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQ 1672
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1673 RAARERLPLGEGlpcllldaehewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSAD 1752
Cdd:cd05903     81 ERFRQFDPAAMP--------------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1753 D----AWSLFHSYAFdfsVWEIFGALLHGGRLVIvpyETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPP 1828
Cdd:cd05903    135 DvflvASPMAHQTGF---VYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLS 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1829 lALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVTYRPLslaDLDGGAASPIGEPIPDLSWYLLDAGLN 1908
Cdd:cd05903    209 -RLRTFVCGGATVPRSLARRAAELLG---AKVCSAYGSTECPGAVTSITP---APEDRRLYTDGRPLPGVEIKVVDDTGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 PVPRGCIGELYVGGAGLARGYLNRPELSctrFVADPfsttgGRLYRTGDLARYRCDGVVEYVGRiDHQVKIR-GFRIELG 1987
Cdd:cd05903    282 TLAPGVEGELLSRGPSVFLGYLDRPDLT---ADAAP-----EGWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1988 EIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQAAPS-DPAALRDTLrqaLKASLPEHMVPAHLLFLERLPLTANG 2064
Cdd:cd05903    353 EVEDLLLGHPGVIEAAVvaLPDERLG-ERACAVVVTKSGALlTFDELVAYL---DRQGVAKQYWPERLVHVDDLPRTPSG 428

                   ..
gi 2183974163 2065 KL 2066
Cdd:cd05903    429 KV 430
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1134-1535 1.56e-35

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 141.67  E-value: 1.56e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1134 YNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPR--QVIHPTLPIAIEE-----------RRPPVAGEDL 1200
Cdd:cd19542     22 YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTflQVVLKSLDPPIEEvetdedsldalTRDLLDDPTL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1201 KGlveTEAHRpFDLQRGpllrvlllplATDECVLVLTLHHIIADGWSMQVLVDELIRVYaalrHDQPPALAElpiQYADF 1280
Cdd:cd19542    102 FG---QPPHR-LTLLET----------SSGEVYLVLRISHALYDGVSLPIILRDLAAAY----NGQLLPPAP---PFSDY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1281 AAWQRQwmdgGERERQLDYWVSRLGGEQPLLELPSDRPRPQQQShrgrrigIPLPAELAEALRRLAQAEQGTLFMLLLAS 1360
Cdd:cd19542    161 ISYLQS----QSQEESLQYWRKYLQGASPCAFPSLSPKRPAERS-------LSSTRRSLAKLEAFCASLGVTLASLFQAA 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1361 FQALLHRYSGQNDIRVGVPIANRN--REETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLVD 1438
Cdd:cd19542    230 WALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQR 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1439 ALqpeRSLSHAPLFQVMYNHQRDDHRGSrFASLGELEVEDLAWDVQTaQFDLTLDTYESSNGLLAELTYATDLFDASSAE 1518
Cdd:cd19542    310 AL---GLWPSGTLFNTLVSYQNFEASPE-SELSGSSVFELSAAEDPT-EYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
                          410
                   ....*....|....*..
gi 2183974163 1519 RIAGHWLNLLRSIVARP 1535
Cdd:cd19542    385 ELLEQFDDILEALLANP 401
PRK07514 PRK07514
malonyl-CoA synthase; Validated
514-1007 1.92e-35

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 143.86  E-value: 1.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGltPDAPALLFGE-ERLSYAELNALANRLAWRLREEGV--GSDVLVGIalERGVPMVVALLAVLKAGGAYVPL 590
Cdd:PRK07514     8 ALRAAFAD--RDAPFIETPDgLRYTYGDLDAASARLANLLVALGVkpGDRVAVQV--EKSPEALALYLATLRAGAVFLPL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  591 DPQYPADRLQYMIDDSGLRLLL---SQQSVLARLPQSDGLQSLL-LDD-----LERLVHGYPAENPDLPEAPDSLCYAIY 661
Cdd:PRK07514    84 NTAYTLAELDYFIGDAEPALVVcdpANFAWLSKIAAAAGAPHVEtLDAdgtgsLLEAAAAAPDDFETVPRGADDLAAILY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  662 TSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSvttfSFDIF---GL--ELYVPLARGASMLLASReqaQDPEA 736
Cdd:PRK07514   164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH----ALPIFhthGLfvATNVALLAGASMIFLPK---FDPDA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  737 LLDLVERqgVTVLQATPATW-RMLCDservdllrgctllcggEALAEDLAARMR----G---LSASTWN----------- 797
Cdd:PRK07514   237 VLALMPR--ATVMMGVPTFYtRLLQE----------------PRLTREAAAHMRlfisGsapLLAETHRefqertghail 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  798 -LYGPTETTIWSARFRLGEEARPFLGGPLENTALYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPF 875
Cdd:PRK07514   299 eRYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  876 aadgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVP 951
Cdd:PRK07514   379 -------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI---GVPhpdfGEGVTAVVVP 448
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163  952 TEAALVDaESARQQELRSALKNsllavlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07514   449 KPGAALD-EAAILAALKGRLAR--------FKQPKRVFFVDELPRNTMGKVQKNLL 495
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1596-2071 2.12e-35

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 141.72  E-value: 2.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGirllltqraa 1675
Cdd:cd05912      4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD---------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 rerlplgeglpcllldaehewagypesdpqsaVGVDNLAYVIYTSGSTGKPKGTLLPHGNvlrlfdatrHWF-------- 1747
Cdd:cd05912     74 --------------------------------VKLDDIATIMYTSGTTGKPKGVQQTFGN---------HWWsaigsaln 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1748 -GFSADDAW----SLFHSYAfdFSVweIFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVacA 1822
Cdd:cd05912    113 lGLTEDDNWlcalPLFHISG--LSI--LMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEI--L 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1823 GQEVPPlALRHVVFGGEalevQALRPWFERFGDRAPRLVNMYGITETTVH-VTYRPLSLADLDGGAaspiGEPIPDLSWY 1901
Cdd:cd05912    184 GEGYPN-NLRCILLGGG----PAPKPLLEQCKEKGIPVYQSYGMTETCSQiVTLSPEDALNKIGSA----GKPLFPVELK 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 LLDAGLNPvprGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlyRTGDLARYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:cd05912    255 IEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGG 323
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1982 FRIELGEIEARLLAQPGVAEAVVLPHEGPGATQL-VGYVVTQAAPSdpaalRDTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd05912    324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVpVAFVVSERPIS-----EEELIAYCSEKLAKYKVPKKIYFVDELPR 398
                          490
                   ....*....|.
gi 2183974163 2061 TANGKLDRRAL 2071
Cdd:cd05912    399 TASGKLLRHEL 409
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1576-2086 2.39e-35

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 144.51  E-value: 2.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAERPRATAVVYGERA-LDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPS 1654
Cdd:PRK06087    31 QTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1655 DRLGYMIEDSGIRLLLTQRAARERLPLGEGLPC----------LLLDAE----------HEWAGY-PESDPQSAVGvDNL 1713
Cdd:PRK06087   111 AELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLqnqlpqlqqiVGVDKLapatsslslsQIIADYePLTTAITTHG-DEL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1714 AYVIYTSGSTGKPKGTLLPHGNVL---RLFDATrhwFGFSADD----AWSLFHSYAFDFSVWEIFgalLHGGRLVIvpyE 1786
Cdd:PRK06087   190 AAVLFTSGTEGLPKGVMLTHNNILaseRAYCAR---LNLTWQDvfmmPAPLGHATGFLHGVTAPF---LIGARSVL---L 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 TSRSPEDFLRLLCRERVT-VLNQTPSAFKQLMQVACAGQEVPplALRHVVFGGEALEVQALRPWFErfgdRAPRLVNMYG 1865
Cdd:PRK06087   261 DIFTPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTIPKKVARECQQ----RGIKLLSVYG 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1866 ITETTVHVTYRPLSLADLDGGAAspiGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPF 1945
Cdd:PRK06087   335 STESSPHAVVNLDDPLSRFMHTD---GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 sttggrlYRTGDLARYRCDGVVEYVGRiDHQVKIRGFR-IELGEIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQ 2022
Cdd:PRK06087   412 -------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVvaMPDERLG-ERSCAYVVLK 482
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2023 AAPSDPaALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQRDYTAP 2086
Cdd:PRK06087   483 APHHSL-TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEE 545
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
532-1007 3.41e-35

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 143.54  E-value: 3.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  532 GEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL 611
Cdd:cd12119     22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  612 LSQQS-------VLARLPQ-------SDGLQSLLLDDL-----ERLVHGYPAE--NPDLPE-APDSLCYaiyTSGSTGQP 669
Cdd:cd12119    102 FVDRDflplleaIAPRLPTvehvvvmTDDAAMPEPAGVgvlayEELLAAESPEydWPDFDEnTAAAICY---TSGTTGNP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  670 KGVMVRHRALTNFVCSIARQPGML--ARDRLLSVT-TFSFDIFGLElYVPLARGASMLLASReqAQDPEALLDLVERQGV 746
Cdd:cd12119    179 KGVVYSHRSLVLHAMAALLTDGLGlsESDVVLPVVpMFHVNAWGLP-YAAAMVGAKLVLPGP--YLDPASLAELIEREGV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  747 TVLQATPATWRML---CDSERVDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTET----TI----WSARFRLGE 815
Cdd:cd12119    256 TFAAGVPTVWQGLldhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsplgTVarppSEHSNLSED 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 EARPFL---GGPLENTALYILDSEMNPCP--PGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLAR 890
Cdd:cd12119    336 EQLALRakqGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALT------EDG--WLRTGDVAT 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  891 YRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG---VAGPtlVAYLVPTEAALVDAEsarqqel 967
Cdd:cd12119    408 IDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHpkwGERP--LAVVVLKEGATVTAE------- 478
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2183974163  968 rsALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd12119    479 --ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1578-2022 3.55e-35

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 143.14  E-value: 3.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGE--RALDYGELNLRANRLAHRLIELGVGP-DVlVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPS 1654
Cdd:cd05904     15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKgDV-VLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1655 DRLGYMIEDSGIRLLLTQRAARERLPlGEGLPCLLLDAEHEWAGYPESD---------PQSAVGVDNLAYVIYTSGSTGK 1725
Cdd:cd05904     94 AEIAKQVKDSGAKLAFTTAELAEKLA-SLALPVVLLDSAEFDSLSFSDLlfeadeaepPVVVIKQDDVAALLYSSGTTGR 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1726 PKGTLLPHGN-------VLRLFDATRHwfgfsADDAW----SLFHSYAFDFsvweIFGALLH-GGRLVIVP-YETsrspE 1792
Cdd:cd05904    173 SKGVMLTHRNliamvaqFVAGEGSNSD-----SEDVFlcvlPMFHIYGLSS----FALGLLRlGATVVVMPrFDL----E 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1793 DFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEvPPLALRHVVFGGEAL--EVQalrpwfERFGDRAP--RLVNMYGITE 1868
Cdd:cd05904    240 ELLAAIERYKVTHLPVVPPIVLALVKSPIVDKY-DLSSLRQIMSGAAPLgkELI------EAFRAKFPnvDLGQGYGMTE 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1869 TT--VHVTYRPLSLAdldgGAASPIGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpf 1945
Cdd:cd05904    313 STgvVAMCFAPEKDR----AKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-- 386
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 1946 sttgGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQL-VGYVVTQ 2022
Cdd:cd05904    387 ----GWL-HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVpMAFVVRK 459
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1576-2093 3.64e-35

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 143.64  E-value: 3.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAER-PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPS 1654
Cdd:PRK07470    14 RQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1655 DRLGYMIEDSGIRLLLTQ-------RAARE-----RLPLGEGLPCLLLDAEHEWAGYPESDPQSA-VGVDNLAYVIYTSG 1721
Cdd:PRK07470    94 DEVAYLAEASGARAMICHadfpehaAAVRAaspdlTHVVAIGGARAGLDYEALVARHLGARVANAaVDHDDPCWFFFTSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1722 STGKPKGTLLPHGNVLrlFDATRHWF----GFSADDA----WSLFHsyafdfsvweifGALLH-------GGRLVIVPYE 1786
Cdd:PRK07470   174 TTGRPKAAVLTHGQMA--FVITNHLAdlmpGTTEQDAslvvAPLSH------------GAGIHqlcqvarGAATVLLPSE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 tSRSPEDFLRLLCRERVTVLNQTPSAFKQLMqvacagqEVPPLA------LRHVVFGG----EALEVQALRpwfeRFGdr 1856
Cdd:PRK07470   240 -RFDPAEVWALVERHRVTNLFTVPTILKMLV-------EHPAVDrydhssLRYVIYAGapmyRADQKRALA----KLG-- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1857 aPRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGE---PIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRP 1933
Cdd:PRK07470   306 -KVLVQYFGLGEVTGNITVLPPALHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNP 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1934 ELSCTRFVADPFsttggrlyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPG 2011
Cdd:PRK07470   385 EANAKAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLgvPDPVWG 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2012 AtqlVGYVVTQAapSDPAAL-RDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALpapdasrlqrdytapRSEL 2090
Cdd:PRK07470   457 E---VGVAVCVA--RDGAPVdEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV---------------REEL 516

                   ...
gi 2183974163 2091 EQR 2093
Cdd:PRK07470   517 EER 519
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1553-2073 4.45e-35

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 144.56  E-value: 4.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1553 DLLQWNPGPQDFTPASC--LHRLIERQAAERPRATAVVY-GE----RALDYGELNLRANRLAHRLIELGVGPDVLVGLAA 1625
Cdd:cd05968     44 DLSGGKPWAAWFVGGRMniVEQLLDKWLADTRTRPALRWeGEdgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYL 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1626 ERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQ----RAARERLPLGE------------------ 1683
Cdd:cd05968    124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftRRGREVNLKEEadkacaqcptvekvvvvr 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1684 --GLPCLLLDAEHEWagYPE----SDPQSA-VGVDNLAYVIYTSGSTGKPKGTLLPHGN--VLRLFDATrHWFGFSADDA 1754
Cdd:cd05968    204 hlGNDFTPAKGRDLS--YDEeketAGDGAErTESEDPLMIIYTSGTTGKPKGTVHVHAGfpLKAAQDMY-FQFDLKPGDL 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1755 WSLFHSYAFDFSVWEIFGALLHGGRLVIvpYETS---RSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPL-A 1830
Cdd:cd05968    281 LTWFTDLGWMMGPWLIFGGLILGATMVL--YDGApdhPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLsS 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 LRhvVFG--GEALEVQALRPWFERFGDRAPRLVNMYGITETT----VHVTYRPLSLADLDGgaaspigePIPDLSWYLLD 1904
Cdd:cd05968    359 LR--VLGstGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISggilGNVLIKPIKPSSFNG--------PVPGMKADVLD 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1905 AGLNPVpRGCIGELYVGGA--GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGF 1982
Cdd:cd05968    429 ESGKPA-RPEVGELVLLAPwpGMTRGFWRDED----RYLETYWSRFDN-VWVHGDFAYYDEEGYFYILGRSDDTINVAGK 502
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1983 RIELGEIEARLLAQPGVAE--AVVLPHEGPGaTQLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPL 2060
Cdd:cd05968    503 RVGPAEIESVLNAHPAVLEsaAIGVPHPVKG-EAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPK 581
                          570
                   ....*....|...
gi 2183974163 2061 TANGKLDRRALPA 2073
Cdd:cd05968    582 TRNAKVMRRVIRA 594
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3099-3182 5.50e-35

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 141.24  E-value: 5.50e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                   ....
gi 2183974163 3179 EDSG 3182
Cdd:cd17652     81 ADAR 84
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3087-3183 5.64e-35

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 141.30  E-value: 5.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3166
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90
                   ....*....|....*..
gi 2183974163 3167 PEYPEERQAYMLEDSGV 3183
Cdd:cd12115     81 PAYPPERLRFILEDAQA 97
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
49-476 6.76e-35

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 139.63  E-value: 6.76e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   49 PLSYAqERQWFLW-QMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDeqlDGF----------RQQ 117
Cdd:cd19537      3 ALSPI-EREWWHKyQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPR---DGGlrrsysssppRVQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  118 VLASVDVPVPVTLAGDDDAQAQIRAFVESETqqpfdlrngpllrarllrlaaddhvLTLTIHHVAADGWSMRVLVEELIA 197
Cdd:cd19537     79 RVDTLDVWKEINRPFDLEREDPIRVFISPDT-------------------------LLVVMSHIICDLTTLQLLLREVSA 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  198 LYGARrqgieaTLPDLPIQYADYAIWQRHwleagERERQLEYWMARLGGGQsVLELPTdrqRPALPSYRGARHELQLPQA 277
Cdd:cd19537    134 AYNGK------LLPPVRREYLDSTAWSRP-----ASPEDLDFWSEYLSGLP-LLNLPR---RTSSKSYRGTSRVFQLPGS 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  278 LGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVntQVL----RADLDAQMPFLD 353
Cdd:cd19537    199 LYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFL--EPLpiriRFPSSSDASAAD 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  354 LLQQTRVAALGAQSHQdLPFEQLVEALQ-PERSLSHsPLFQAM--YNHqnlgsAGRQSLAAQLPGLSVEdLSWgAHSAQF 430
Cdd:cd19537    277 FLRAVRRSSQAALAHA-IPWHQLLEHLGlPPDSPNH-PLFDVMvtFHD-----DRGVSLALPIPGVEPL-YTW-AEGAKF 347
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2183974163  431 DLTLD-TYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAE 476
Cdd:cd19537    348 PLMFEfTALSDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1561-2081 7.32e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 142.79  E-value: 7.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1561 PQDFT-PASCLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAI 1638
Cdd:PRK08314     2 PKSLTlPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1639 LKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT-QRAARERLPL--GEGLPCLL-------------------LDAEHEW 1696
Cdd:PRK08314    82 LRANAVVVPVNPMNREEELAHYVTDSGARVAIVgSELAPKVAPAvgNLRLRHVIvaqysdylpaepeiavpawLRAEPPL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1697 AGYPESD--------------PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLF 1758
Cdd:PRK08314   162 QALAPGGvvawkealaaglapPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESvvlaVLPLF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1759 HSYAFDFSVweiFGALLHGGRLVIVPY---ETSRspedflRLLCRERVTVLNQTPSafkqlMQVACAGQevPPLA----- 1830
Cdd:PRK08314   242 HVTGMVHSM---NAPIYAGATVVLMPRwdrEAAA------RLIERYRVTHWTNIPT-----MVVDFLAS--PGLAerdls 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 -LRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVTYRPLSLADLDGgaaspIGEPIPDLSWYLLD-AGLN 1908
Cdd:PRK08314   306 sLRYIGGGGAAMPEAVAERLKELTG---LDYVEGYGLTETMAQTHSNPPDRPKLQC-----LGIPTFGVDARVIDpETLE 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 PVPRGCIGELYVGGAGLARGYLNRPELSctrfvADPFSTTGG-RLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELG 1987
Cdd:PRK08314   378 ELPPGEVGEIVVHGPQVFKGYWNRPEAT-----AEAFIEIDGkRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPA 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1988 EIEARLLAQPGVAEAVVL----PHEGPGATQLVgyVVTQAAPSDPAAlrdtlrQALKASLPEHM----VPAHLLFLERLP 2059
Cdd:PRK08314   453 EVENLLYKHPAIQEACVIatpdPRRGETVKAVV--VLRPEARGKTTE------EEIIAWAREHMaaykYPRIVEFVDSLP 524
                          570       580
                   ....*....|....*....|..
gi 2183974163 2060 LTANGKLDRRALPAPDASRLQR 2081
Cdd:PRK08314   525 KSGSGKILWRQLQEQEKARAAK 546
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
520-1021 8.52e-35

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 142.76  E-value: 8.52e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLF------GEERLSYAELNALANRLAWRLREEGVGSDVlVGIALERGVPMVVALLAVLKAGGAYVPL--- 590
Cdd:cd05931      3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  591 DPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQ------SDGLQSLLLDDLERLVHGYPAENPDLpeAPDSLCYAIYTSG 664
Cdd:cd05931     82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAfaasrpAAGTPRLLVVDLLPDTSAADWPPPSP--DPDDIAYLQYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  665 STGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDiFGLE--LYVPLARGA-SMLLASREQAQDPEALLDLV 741
Cdd:cd05931    160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHD-MGLIggLLTPLYSGGpSVLMSPAAFLRRPLRWLRLI 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  742 ERQGVTVLQATPATWRmLC-------DSERVDLLRGCTLLCGGE----ALAEDLAARMR--GLSASTwnL---YGPTETT 805
Cdd:cd05931    239 SRYRATISAAPNFAYD-LCvrrvrdeDLEGLDLSSWRVALNGAEpvrpATLRRFAEAFApfGFRPEA--FrpsYGLAEAT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 --------------IWSARFRL----------GEEARPFL--GGPLENTALYILDSEMN-PCPPGVAGELLIGGDGLARG 858
Cdd:cd05931    316 lfvsggppgtgpvvLRVDRDALagravavaadDPAARELVscGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASG 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  859 YHRRPGLTAERFLPDPfAADGSRLYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIETrlleqdSVREAVVVAQP 938
Cdd:cd05931    396 YWGRPEATAETFGALA-ATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEA------TAEEAHPALRP 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  939 GVAgptlVAYLVP---TEAALVDAESARQQ---ELRSALKNSLLAVLPDYMVPAHMLLLEN---LPLTPNGKINRkalpl 1009
Cdd:cd05931    468 GCV----AAFSVPddgEERLVVVAEVERGAdpaDLAAIAAAIRAAVAREHGVAPADVVLVRpgsIPRTSSGKIQR----- 538
                          570
                   ....*....|..
gi 2183974163 1010 pdaSAVRDAHVA 1021
Cdd:cd05931    539 ---RACRAAYLD 547
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1570-2070 1.17e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 142.19  E-value: 1.17e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:PRK06164    12 LASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQRAAR--------------ERLPL---------GEGLPCLLLDAEHEWAGYPESDPQS 1706
Cdd:PRK06164    92 TRYRSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdALPPLraiavvddaADATPAPAPGARVQLFALPDPAPPA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1707 AVGV-----DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW--SLFHSYAFDFSVweIFGALLHGGR 1779
Cdd:PRK06164   172 AAGEraadpDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLlaALPFCGVFGFST--LLGALAGGAP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1780 LVIVP-YETSRSpedfLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPplALRHVVFGGEALEVQALRPWFErfgDRAP 1858
Cdd:PRK06164   250 LVCEPvFDAART----ARALRRHRVTHTFGNDEMLRRILDTAGERADFP--SARLFGFASFAPALGELAALAR---ARGV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1859 RLVNMYGITETTVHVTYRPLSLAD----LDGGA-ASPIGE-PIPDlswyLLDAGLnpVPRGCIGELYVGGAGLARGYLNR 1932
Cdd:PRK06164   321 PLTGLYGSSEVQALVALQPATDPVsvriEGGGRpASPEARvRARD----PQDGAL--LPDGESGEIEIRAPSLMRGYLDN 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1933 PELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGA 2012
Cdd:PRK06164   395 PDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK 467
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 2013 TQLVGYVVTQA-APSDPAALRDTLRQALKAslpeHMVPAHLLFLERLPLT--ANGKLDRRA 2070
Cdd:PRK06164   468 TVPVAFVIPTDgASPDEAGLMAACREALAG----FKVPARVQVVEAFPVTesANGAKIQKH 524
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
524-950 1.33e-34

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 141.22  E-value: 1.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGE--ERLSYAELNALANRLAWRLREEGVGS-DVlVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQ 600
Cdd:cd05904     19 PSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKgDV-VLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  601 YMIDDSGLRLLLSQQSVLARLPQSdGLQSLLLDDLERLVHGY-----PAENPDLPEA---PDSLCYAIYTSGSTGQPKGV 672
Cdd:cd05904     98 KQVKDSGAKLAFTTAELAEKLASL-ALPVVLLDSAEFDSLSFsdllfEADEAEPPVVvikQDDVAALLYSSGTTGRSKGV 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  673 MVRHRALTNFVCSI-ARQPGMLAR-DRLLSVTTFsFDIFGLELYV--PLARGASMLLASReqaQDPEALLDLVERQGVTV 748
Cdd:cd05904    177 MLTHRNLIAMVAQFvAGEGSNSDSeDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVVMPR---FDLEELLAAIERYKVTH 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  749 LQATPATWRMLCDSERV---DLLRGCTLLCGGEALAEDLAARMR----------GlsastwnlYGPTETTIWSARFRLGE 815
Cdd:cd05904    253 LPVVPPIVLALVKSPIVdkyDLSSLRQIMSGAAPLGKELIEAFRakfpnvdlgqG--------YGMTESTGVVAMCFAPE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 EARPFLG--GPL-ENTALYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARY 891
Cdd:cd05904    325 KDRAKYGsvGRLvPNVEAKIVDPETGeSLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYI 397
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLV 950
Cdd:cd05904    398 DEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDeEAGEVPMAFVV 457
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3088-3183 1.38e-34

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 140.87  E-value: 1.38e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3088 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3167
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90
                   ....*....|....*.
gi 2183974163 3168 EYPEERQAYMLEDSGV 3183
Cdd:cd17646     81 GYPADRLAYMLADAGP 96
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3099-3183 1.42e-34

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 140.20  E-value: 1.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd17649     81 EDSGA 85
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1581-2071 5.68e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 138.94  E-value: 5.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1581 RPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYM 1660
Cdd:PRK03640    15 TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1661 IEDSGIRLLLTQRAARERlpLGEGLPCLLLDAEHEwaGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNvlrlf 1740
Cdd:PRK03640    95 LDDAEVKCLITDDDFEAK--LIPGISVKFAELMNG--PKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN----- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1741 datrHWF---------GFSADDAW----SLFHSYAfdFSVweIFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTVLN 1807
Cdd:PRK03640   166 ----HWWsavgsalnlGLTEDDCWlaavPIFHISG--LSI--LMRSVIYGMRVVLVE---KFDAEKINKLLQTGGVTIIS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1808 QTPSAFKQLMQVacAGQEVPPLALRHVVFGGEAlevqALRPWFERFGDRAPRLVNMYGITETTVH-VTYRPLSLADLDGG 1886
Cdd:PRK03640   235 VVSTMLQRLLER--LGEGTYPSSFRCMLLGGGP----APKPLLEQCKEKGIPVYQSYGMTETASQiVTLSPEDALTKLGS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1887 AaspiGEPIPDLSWYLLDAGlNPVPRGCIGELYVGGAGLARGYLNRPElsctrfvADPFSTTGGRLYrTGDLARYRCDGV 1966
Cdd:PRK03640   309 A----GKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYLNRED-------ATRETFQDGWFK-TGDIGYLDEEGF 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1967 VEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQlVGYVVTQAAPSDpaalrDTLRQALKASLP 2044
Cdd:PRK03640   376 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVvgVPDDKWGQVP-VAFVVKSGEVTE-----EELRHFCEEKLA 449
                          490       500
                   ....*....|....*....|....*..
gi 2183974163 2045 EHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK03640   450 KYKVPKRFYFVEELPRNASGKLLRHEL 476
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1562-2005 2.66e-33

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 139.08  E-value: 2.66e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1562 QDFTPASCLHRLIERQAAERPRATAVVY----GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLA 1637
Cdd:COG1022      5 SDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1638 ILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARER--LPLGEGLPCL----LLDAEHEW-------------AG 1698
Cdd:COG1022     85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDklLEVRDELPSLrhivVLDPRGLRddprllsldellaLG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1699 YPESDPQ------SAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLF----HSYAFdfsVW 1768
Cdd:COG1022    165 REVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplaHVFER---TV 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1769 EIFgALLHGGRLVIVPyetsrSPEDFLRLLcRE-RVTVLNQTP-----------------SAFKQLM---------QVAC 1821
Cdd:COG1022    242 SYY-ALAAGATVAFAE-----SPDTLAEDL-REvKPTFMLAVPrvwekvyagiqakaeeaGGLKRKLfrwalavgrRYAR 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 A---GQEVPP-LALRHVVFggEALevqALRPWFERFGDR-----------APRL--------VNM---YGITETTVHVTY 1875
Cdd:COG1022    315 ArlaGKSPSLlLRLKHALA--DKL---VFSKLREALGGRlrfavsggaalGPELarffralgIPVlegYGLTETSPVITV 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1876 RPLSLADLDGgaaspIGEPIPDLSWYLLDAglnpvprgciGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRT 1955
Cdd:COG1022    390 NRPGDNRIGT-----VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHT 447
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 1956 GDLARYRCDGVVEYVGRIDHQVKIR-GFRIELGEIEARLLAQPGVAEAVVL 2005
Cdd:COG1022    448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
PRK06164 PRK06164
acyl-CoA synthetase; Validated
515-1007 2.94e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 137.95  E-value: 2.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  515 LFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQY 594
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  595 PADRLQYMIDDSGLRLLL----------------SQQSVLARLPQ--------SDGLQSLLLDDLERLVHGYPAENPDL- 649
Cdd:PRK06164    95 RSHEVAHILGRGRARWLVvwpgfkgidfaailaaVPPDALPPLRAiavvddaaDATPAPAPGARVQLFALPDPAPPAAAg 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  650 -PEAPDSLCYAIYT-SGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSfDIFGLE-LYVPLARGASMLLa 726
Cdd:PRK06164   175 eRAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFC-GVFGFStLLGALAGGAPLVC- 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  727 srEQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLLCGGEALA---EDLAARMRGLSASTWNLYGPTE 803
Cdd:PRK06164   253 --EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFApalGELAALARARGVPLTGLYGSSE 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  804 ----------TTIWSARFRLGeearpflGGPLENTA-LYILDSEMNP-CPPGVAGELLIGGDGLARGYHRRPGLTAERFL 871
Cdd:PRK06164   331 vqalvalqpaTDPVSVRIEGG-------GRPASPEArVRARDPQDGAlLPDGESGEIEIRAPSLMRGYLDNPDATARALT 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  872 PDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVP 951
Cdd:PRK06164   404 DDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIP 476
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163  952 TeaalvDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNG---KINRKAL 1007
Cdd:PRK06164   477 T-----DGASPDEAGLMAACREALAG----FKVPARVQVVEAFPVTESAngaKIQKHRL 526
PRK07470 PRK07470
acyl-CoA synthetase; Validated
524-1007 2.95e-33

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 137.87  E-value: 2.95e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGV--GSDVLVGIAleRGVPMVVALLAVLKAGGAYVPLDPQYPADRLQY 601
Cdd:PRK07470    21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVrkGDRILVHSR--NCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAY 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  602 MIDDSGLRLLLSQ----QSVLARLPQSDGLQSLLLDDLERLVHGYPA---ENPDLPEAP-----DSLCYAIYTSGSTGQP 669
Cdd:PRK07470    99 LAEASGARAMICHadfpEHAAAVRAASPDLTHVVAIGGARAGLDYEAlvaRHLGARVANaavdhDDPCWFFFTSGTTGRP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  670 KGVMVRHRAL----TNFVCSIArqPGMLARDRLLSVTTFSFDIfGLELYVPLARGA-SMLLASREqaQDPEALLDLVERQ 744
Cdd:PRK07470   179 KAAVLTHGQMafviTNHLADLM--PGTTEQDASLVVAPLSHGA-GIHQLCQVARGAaTVLLPSER--FDPAEVWALVERH 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  745 GVTVLQATPATWRMLCDSERVDLLRGCTL----LCGGEALAEDLAARMRGLSASTWNLYGPTETT----IWSARF----- 811
Cdd:PRK07470   254 RVTNLFTVPTILKMLVEHPAVDRYDHSSLryviYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTgnitVLPPALhdaed 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  812 ----RLGEEARPFLGgplenTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGD 887
Cdd:PRK07470   334 gpdaRIGTCGFERTG-----MEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF------RDG--WFRTGD 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVDAEsarqqe 966
Cdd:PRK07470   401 LGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdPVWGEVGVAVCVARDGAPVDEA------ 474
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2183974163  967 lrsALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07470   475 ---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
655-1007 5.14e-33

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 132.45  E-value: 5.14e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLsVTTFSFDIFGLE-LYVPLARGASMLLASREQAqd 733
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAiLVRSLLAGAELVLLERNQA-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  734 peALLDLvERQGVTVLQATPATWRMLCDS----ERVDLLRGctLLCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSA 809
Cdd:cd17630     78 --LAEDL-APPGVTHVSLVPTQLQRLLDSgqgpAALKSLRA--VLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  810 RFRLGEEARPFLGGPLENTALYILDsemnpcppgvAGELLIGGDGLARGYHRRPgltaerfLPDPFAADGsrLYRTGDLA 889
Cdd:cd17630    153 TKRPDGFGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQ-------LVPEFNEDG--WFTTKDLG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  890 RYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTLVAYLVpteAALVDAESARQQELRS 969
Cdd:cd17630    214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPDEELGQRPV---AVIVGRGPADPAELRA 287
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2183974163  970 ALKNSllavLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd17630    288 WLKDK----LARFKLPKRIYPVPELPRTGGGKVDRRAL 321
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
524-1002 5.46e-33

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 138.09  E-value: 5.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLF-GEE-----RLSYAELNALANRLAWRLREEGVGSDVLVGIALergvPMV----VALLAVLKAGGAYVPLDPQ 593
Cdd:cd17634     67 GDRTAIIYeGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYM----PMIpeaaVAMLACARIGAVHSVIFGG 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSQQSVL--------------ARLPQSDGLQSLLLDDLER---------------LVHGYPA 644
Cdd:cd17634    143 FAPEAVAGRIIDSSSRLLITADGGVragrsvplkknvddALNPNVTSVEHVIVLKRTGsdidwqegrdlwwrdLIAKASP 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  645 ENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRH-----RALTNFVCSIARQPG---MLARDrLLSVTTFSFDIFGlelyvP 716
Cdd:cd17634    223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggylvYAATTMKYVFDYGPGdiyWCTAD-VGWVTGHSYLLYG-----P 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  717 LARGASMLL-ASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDS-----ERVDLLRGCTLLCGGEALAEDLAA---- 786
Cdd:cd17634    297 LACGATTLLyEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaiEGTDRSSLRILGSVGEPINPEAYEwywk 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  787 RMRGLSASTWNLYGPTETT--IWSAR-----FRLGEEARPFLGgplenTALYILDSEMNPCPPGVAGELLIGGD--GLAR 857
Cdd:cd17634    377 KIGKEKCPVVDTWWQTETGgfMITPLpgaieLKAGSATRPVFG-----VQPAVVDNEGHPQPGGTEGNLVITDPwpGQTR 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  858 GYHRRPgltaERFLPDPFAA-DGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVA 936
Cdd:cd17634    452 TLFGDH----ERFEQTYFSTfKG--MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVG 525
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  937 QP-GVAGPTLVAYLVpTEAALVDAESARqQELRSALKNSLLAVLpdymVPAHMLLLENLPLTPNGKI 1002
Cdd:cd17634    526 IPhAIKGQAPYAYVV-LNHGVEPSPELY-AELRNWVRKEIGPLA----TPDVVHWVDSLPKTRSGKI 586
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3088-3183 6.10e-33

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 134.99  E-value: 6.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3088 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3167
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90
                   ....*....|....*.
gi 2183974163 3168 EYPEERQAYMLEDSGV 3183
Cdd:cd17645     81 DYPGERIAYMLADSSA 96
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1713-2071 7.23e-33

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 132.07  E-value: 7.23e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1713 LAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFH--SYAFdfsvweIFGALLHGGRLVIVPYE 1786
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWllslPLYHvgGLAI------LVRSLLAGAELVLLERN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 tsrspEDFLRLLCRERVTVLNQTPSAFKQLMQvacAGQEVPPLA-LRHVVFGGEALEVQALrpwfERFGDRAPRLVNMYG 1865
Cdd:cd17630     76 -----QALAEDLAPPGVTHVSLVPTQLQRLLD---SGQGPAALKsLRAVLLGGAPIPPELL----ERAADRGIPLYTTYG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1866 ITETTVHVTyrplsLADLDGGAASPIGEPIPDlswylldAGLNPVPRGCIGelyVGGAGLARGYLNRPELsctrfvaDPF 1945
Cdd:cd17630    144 MTETASQVA-----TKRPDGFGRGGVGVLLPG-------RELRIVEDGEIW---VGGASLAMGYLRGQLV-------PEF 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 STTGgrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAP 2025
Cdd:cd17630    202 NEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP 279
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163 2026 SDPAAlrdtLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd17630    280 ADPAE----LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
537-1007 8.97e-33

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 136.80  E-value: 8.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  537 SYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ- 615
Cdd:PRK06087    51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTl 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 -----------SVLARLPQsdgLQSLLLDD----------LERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMV 674
Cdd:PRK06087   131 fkqtrpvdlilPLQNQLPQ---LQQIVGVDklapatsslsLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVML 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  675 RHRALtnfvcsIARQPGMLARdrlLSVTtfSFDIFGLElyVPL--ARG------ASMLLASREQAQD---PEALLDLVER 743
Cdd:PRK06087   208 THNNI------LASERAYCAR---LNLT--WQDVFMMP--APLghATGflhgvtAPFLIGARSVLLDiftPDACLALLEQ 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  744 QGVT-VLQATPATWRMLC--DSERVDL--LRgcTLLCGGEALAEDLAARMRGLSASTWNLYGPTETtIWSARFRLGEEAR 818
Cdd:PRK06087   275 QRCTcMLGATPFIYDLLNllEKQPADLsaLR--FFLCGGTTIPKKVARECQQRGIKLLSVYGSTES-SPHAVVNLDDPLS 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  819 PFL---GGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAeRFLPDpfaaDGsrLYRTGDLARYRADG 895
Cdd:PRK06087   352 RFMhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE----EG--WYYSGDLCRMDEAG 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  896 VIEYLGRiDHQVKIRGFR-IELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAYLVPTEaalvdaesarqQELRSALKN 973
Cdd:PRK06087   425 YIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErLGERSCAYVVLKA-----------PHHSLTLEE 492
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2183974163  974 sLLAVL-----PDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06087   493 -VVAFFsrkrvAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK06145 PRK06145
acyl-CoA synthetase; Validated
523-1007 9.33e-33

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 135.78  E-value: 9.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:PRK06145    15 TPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSQQSVLArlPQSDGLQSLLLD-----DLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHr 677
Cdd:PRK06145    95 LGDAGAKLLLVDEEFDA--IVALETPKIVIDaaaqaDSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSY- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  678 alTNFVCSIARQP---GMLARDRLLSVTTF----SFDIFGLELyvpLARGAsMLLASREqaQDPEALLDLVERQGVTVLQ 750
Cdd:PRK06145   172 --GNLHWKSIDHVialGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGG-TLRIHRE--FDPEAVLAAIERHRLTCAW 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  751 ATPA-TWRMLC--DSERVDLLRGCTLLCGGEALAEdlaARMRGLS-----ASTWNLYGPTETTIWSARFRLGEEARPF-- 820
Cdd:PRK06145   244 MAPVmLSRVLTvpDRDRFDLDSLAWCIGGGEKTPE---SRIRDFTrvftrARYIDAYGLTETCSGDTLMEAGREIEKIgs 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  821 LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlyRTGDLARYRADGVIEYL 900
Cdd:PRK06145   321 TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGFLYLT 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  901 GRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqelrsALKNSLLAVL 979
Cdd:PRK06145   393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPGATLTLE---------ALDRHCRQRL 463
                          490       500
                   ....*....|....*....|....*...
gi 2183974163  980 PDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06145   464 ASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1557-2069 1.30e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 136.67  E-value: 1.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1557 WNPGPQDFTPASCLHrLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLL 1636
Cdd:PRK05605    22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1637 AILKAGGAYVPLDPRYPSDRLGYMIEDSGIRL---------------------------------LLTQ----------R 1673
Cdd:PRK05605   101 AVLRLGAVVVEHNPLYTAHELEHPFEDHGARVaivwdkvaptverlrrttpletivsvnmiaampLLQRlalrlpipalR 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1674 AARERL--PLGEGLPC-LLLDAEHEWAGYPESDPqsAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFS 1750
Cdd:PRK05605   181 KARAALtgPAPGTVPWeTLVDAAIGGDGSDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGL 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1751 ADD------AWSLFHSY------AFDFSVweifgallhGGRLVIVPyeTSRSPEdFLRLLCRERVTVLNQTPSAFKQLMQ 1818
Cdd:PRK05605   259 GDGpervlaALPMFHAYgltlclTLAVSI---------GGELVLLP--APDIDL-ILDAMKKHPPTWLPGVPPLYEKIAE 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1819 VAcAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDrapRLVNMYGITETTVHVTYRPLSladlDGGAASPIGEPIPDL 1898
Cdd:PRK05605   327 AA-EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGG---LLVEGYGLTETSPIIVGNPMS----DDRRPGYVGVPFPDT 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLDAGlNP---VPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfsttggrLYRTGDLARYRCDGVVEYVGRIDH 1975
Cdd:PRK05605   399 EVRIVDPE-DPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKE 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1976 QVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALKAslpeHMVPAHLL 2053
Cdd:PRK05605   470 LIITGGFNVYPAEVEEVLREHPGVEDAAVvgLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTR----YKVPRRFY 545
                          570
                   ....*....|....*.
gi 2183974163 2054 FLERLPLTANGKLDRR 2069
Cdd:PRK05605   546 HVDELPRDQLGKVRRR 561
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3099-3183 3.51e-32

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 133.20  E-value: 3.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd17643     81 ADSGP 85
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
653-1004 1.39e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 128.93  E-value: 1.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  653 PDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLELYV--PLARGASMLLASReq 730
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPL-FHCFGSVLGVlaCLTHGATMVFPSP-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  731 AQDPEALLDLVERQGVTVLQATPAtwrMLCDS------ERVDLLRGCTLLCGGEALAEDLAARMR---GLSASTwNLYGP 801
Cdd:cd05917     78 SFDPLAVLEAIEKEKCTALHGVPT---MFIAElehpdfDKFDLSSLRTGIMAGAPCPPELMKRVIevmNMKDVT-IAYGM 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  802 TETTIWSARFRLGEEARPFL---GGPLENTALYILDSEMNP-CPPGVAGELLIGGDGLARGYHRRPGLTAErflpdpfAA 877
Cdd:cd05917    154 TETSPVSTQTRTDDSIEKRVntvGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVMKGYWNDPEKTAE-------AI 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  878 DGSRLYRTGDLARYRADGVIEYLGRIDHQVkIRGFR-IELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPT 952
Cdd:cd05917    227 DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVV---GVPderyGEEVCAWIRLK 302
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  953 EAALVDAEsarqqELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd05917    303 EGAELTEE-----DIKAYCKGKIAH----YKVPRYVFFVDEFPLTVSGKIQK 345
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1573-2180 1.58e-31

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 134.77  E-value: 1.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAE-----RPrataVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVP 1647
Cdd:PRK06060     9 LLAEQASEagwydRP----AFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEWAGYPESDPqsaVGVDNLAYVIYTSGSTGKPK 1727
Cdd:PRK06060    85 ANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1728 GTLLPHGNVLRLFDAT-RHWFGFSADD----AWSLFHSYAFDFSVWeifGALLHGGRLVIVPYETSrsPEDFLRLLCRER 1802
Cdd:PRK06060   162 AAIHRHADPLTFVDAMcRKALRLTPEDtglcSARMYFAYGLGNSVW---FPLATGGSAVINSAPVT--PEAAAILSARFG 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1803 VTVLNQTPSAFKQLMQvACAGQEVPplALRHVVFGGEALEVQALRPWFERFGDraprLVNMYGITETTVHVTYRPLSLAD 1882
Cdd:PRK06060   237 PSVLYGVPNFFARVID-SCSPDSFR--SLRCVVSAGEALELGLAERLMEFFGG----IPILDGIGSTEVGQTFVSNRVDE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1883 LDGGAaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPelsctrfvaDPFSTTGGRLyRTGDLARYR 1962
Cdd:PRK06060   310 WRLGT---LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCID 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1963 CDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE-AVVLPHEGPGATQLVGYVV-TQAAPSDPAALRDTLRQALk 2040
Cdd:PRK06060   377 SDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEaAVVAVRESTGASTLQAFLVaTSGATIDGSVMRDLHRGLL- 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2041 ASLPEHMVPAHLLFLERLPLTANGKLDRRALPA--------------------------PDASRLQRDYTAPRSELEQRL 2094
Cdd:PRK06060   456 NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKqsptkpiwelsltepgsgvraqrddlSASNMTIAGGNDGGATLRERL 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2095 A------------AIWADVLKL------GRVGLDDNFFELGGDSIISIQVVSR-ARQAGIRLAPRDLFLHQTIRGLAG-V 2154
Cdd:PRK06060   536 ValrqerqrlvvdAVCAEAAKMlgepdpWSVDQDLAFSELGFDSQMTVTLCKRlAAVTGLRLPETVGWDYGSISGLAQyL 615
                          650       660
                   ....*....|....*....|....*....
gi 2183974163 2155 AVEGRGLACAEQGPI---SGSTPLLPIQQ 2180
Cdd:PRK06060   616 EAELAGGHGRLKSAGpvnSGATGLWAIEE 644
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1711-2071 2.66e-31

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 131.30  E-value: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFDFSVWEifgALLHGGRLVIVPYE 1786
Cdd:cd05909    147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDvvfgALPFFHSFGLTGCLWL---PLLSGIKVVFHPNP 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 TsrSPEDFLRLLCRERVTVLNQTPSaFkqLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGI 1866
Cdd:cd05909    224 L--DYKKIPELIYDKKATILLGTPT-F--LRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG---IRILEGYGT 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1867 TETTVHVTyrpLSLADLDGGAASpIGEPIPDLSWYLLD-AGLNPVPRGCIGELYVGGAGLARGYLNRPELscTRFVAdpf 1945
Cdd:cd05909    296 TECSPVIS---VNTPQSPNKEGT-VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPEL--TSFAF--- 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 sttGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIE---ARLLAQPGVAEAVVLPHEGPGATQLVGYVvtq 2022
Cdd:cd05909    367 ---GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEdilSEILPEDNEVAVVSVPDGRKGEKIVLLTT--- 440
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2023 aapsDPAALRDTLRQALKAS-LPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05909    441 ----TTDTDPSSLNDILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1577-2071 3.26e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 130.70  E-value: 3.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1577 QAAERPRATAVV--YGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPS 1654
Cdd:PRK09088     4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1655 DRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEwagypESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHG 1734
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAL-----EPADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1735 NVlrlfDATRHWFGFSAD-DAWSLFHSYAFDFS----VWEIFGALLHGGRLVIVP-YETSRSpedfLRLLCRERVTVLNQ 1808
Cdd:PRK09088   159 NL----QQTAHNFGVLGRvDAHSSFLCDAPMFHiiglITSVRPVLAVGGSILVSNgFEPKRT----LGRLGDPALGITHY 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1809 TpsAFKQLMQVACAGQEVPPLALRH---VVFGGEALEVQALRPWFerfgDRAPRLVNMYGITETTVhVTYRPLSLADLDG 1885
Cdd:PRK09088   231 F--CVPQMAQAFRAQPGFDAAALRHltaLFTGGAPHAAEDILGWL----DDGIPMVDGFGMSEAGT-VFGMSVDCDVIRA 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GAASPiGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDG 1965
Cdd:PRK09088   304 KAGAA-GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADG 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1966 VVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQlVGYVVTQAAPSDPAALRDtLRQALKASLPE 2045
Cdd:PRK09088   376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE-VGYLAIVPADGAPLDLER-IRSHLSTRLAK 453
                          490       500
                   ....*....|....*....|....*.
gi 2183974163 2046 HMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK09088   454 YKVPKHLRLVDALPRTASGKLQKARL 479
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
518-1090 3.27e-31

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 133.62  E-value: 3.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  518 AQAGLTpDAPALlFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPAD 597
Cdd:PRK06060    15 SEAGWY-DRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  598 RLQYMIDDSGLRLLLSQQSVLARLPQSDglqslLLDDLERLVHGYPAENPDL-PEAPDSLCYAIYTSGSTGQPKGVMVRH 676
Cdd:PRK06060    93 DHALAARNTEPALVVTSDALRDRFQPSR-----VAEAAELMSEAARVAPGGYePMGGDALAYATYTSGTTGPPKAAIHRH 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  677 RALTNFVCSIARQPGMLA-RDRLLSVTTFSFdIFGL--ELYVPLARGASMLLASREQAQDPEALLDlvERQGVTVLQATP 753
Cdd:PRK06060   168 ADPLTFVDAMCRKALRLTpEDTGLCSARMYF-AYGLgnSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVP 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  754 ATWRMLCDSERVDLLRGC-TLLCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSARFRLG-EEARP-FLGGPLENTAL 830
Cdd:PRK06060   245 NFFARVIDSCSPDSFRSLrCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRvDEWRLgTLGRVLPPYEI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  831 YILDSEMNPCPPGVAGELLIGGDGLARGYHRRPgltaerflpDPFAADGSRLyRTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:PRK06060   325 RVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  911 GFRIELGEIETRLLEQDSVREAVVVAQPGVAG-PTLVAYLVPTEAALVDAESARQQELRsalknsLLAVLPDYMVPAHML 989
Cdd:PRK06060   395 GVNVDPREVERLIIEDEAVAEAAVVAVRESTGaSTLQAFLVATSGATIDGSVMRDLHRG------LLNRLSAFKVPHRFA 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  990 LLENLPLTPNGKINRKAL-------PL-------------------PDASAVRDAHVAPEGELERAMAAIWSEVLKL--- 1040
Cdd:PRK06060   469 VVDRLPRTPNGKLVRGALrkqsptkPIwelsltepgsgvraqrddlSASNMTIAGGNDGGATLRERLVALRQERQRLvvd 548
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 1041 ---------------GHIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQ 1090
Cdd:PRK06060   549 avcaeaakmlgepdpWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQ 613
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
510-1007 3.65e-31

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 130.75  E-value: 3.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  510 QGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREE-GVGSDVLVGIALERGVPMVVALLAVLKAGGAYV 588
Cdd:PRK06839     2 QGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  589 PLDPQYPADRLQYMIDDSGLRLLLSQ---QSVLARLPQSDGLQSLL-LDDLERLVHgypAENPDLPEAPDSLCYAI-YTS 663
Cdd:PRK06839    82 PLNIRLTENELIFQLKDSGTTVLFVEktfQNMALSMQKVSYVQRVIsITSLKEIED---RKIDNFVEKNESASFIIcYTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  664 GSTGQPKG-VMVRHRALTNFVCSIArQPGMLARDRLLSVTTFsFDIFGLELYV--PLARGASMLLASReqaQDPEALLDL 740
Cdd:PRK06839   159 GTTGKPKGaVLTQENMFWNALNNTF-AIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVPRK---FEPTKALSM 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  741 VERQGVTVLQATPATWRMLCDS---ERVDLLRGCTLLCGGEALAEDL--AARMRGLSASTWnlYGPTETTiwSARFRLGE 815
Cdd:PRK06839   234 IEKHKVTVVMGVPTIHQALINCskfETTNLQSVRWFYNGGAPCPEELmrEFIDRGFLFGQG--FGMTETS--PTVFMLSE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 E--ARPF--LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARY 891
Cdd:PRK06839   310 EdaRRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI------QDG--WLCTGDLARV 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAESarqqelrsa 970
Cdd:PRK06839   382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKKSSSVLIEKD--------- 452
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2183974163  971 LKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06839   453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
510-1007 5.45e-31

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 130.32  E-value: 5.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  510 QGVHRLFEAQAGLTPDAPALLF--GEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAY 587
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  588 VPLDPQYPADRLQYMIDDSGLRLLLSQqsVLARLPQSD---GLQSLLLDDLERLVHGYPAEN--PDLPEAPDSLCYAIYT 662
Cdd:cd05923     81 ALINPRLKAAELAELIERGEMTAAVIA--VDAQVMDAIfqsGVRVLALSDLVGLGEPESAGPliEDPPREPEQPAFVFYT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  663 SGSTGQPKGVMVRHRALTNFVCSIARQPGML--ARDRLLSVTTFSFDI--FGLeLYVPLARGASMLLAsreQAQDPEALL 738
Cdd:cd05923    159 SGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIgfFAV-LVAALALDGTYVVV---EEFDPADAL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  739 DLVERQGVTVLQATPATWRMLCDSE-----RVDLLRgcTLLCGGEALAEDLAARM-RGLSASTWNLYGPTE--TTIWSAR 810
Cdd:cd05923    235 KLIEQERVTSLFATPTHLDALAAAAefaglKLSSLR--HVTFAGATMPDAVLERVnQHLPGEKVNIYGTTEamNSLYMRD 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  811 FRLGEEARPflGGPLENTALYILDSEMNPCPPGVAGELLI--GGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDL 888
Cdd:cd05923    313 ARTGTEMRP--GFFSEVRIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKL------QDG--WYRTGDV 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  889 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPTEAalvdaeSARQ 964
Cdd:cd05923    383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI---GVAderwGQSVTACVVPREG------TLSA 453
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2183974163  965 QELRSALKNSLLAvlpDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05923    454 DELDQFCRASELA---DFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1572-2075 7.54e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 130.82  E-value: 7.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:PRK07788    53 GLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLtqrAARERLPLGEGLPClLLDAEHEWAGYPESDPQSAVGVDNLA----------------- 1714
Cdd:PRK07788   133 FSGPQLAEVAAREGVKALV---YDDEFTDLLSALPP-DLGRLRAWGGNPDDDEPSGSTDETLDdliagsstaplpkppkp 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 --YVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAfdFSVWEIfgALLHGGRLVivpyeTS 1788
Cdd:PRK07788   209 ggIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGEttllPAPMFHATG--WAHLTL--AMALGSTVV-----LR 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1789 R--SPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPL-ALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYG 1865
Cdd:PRK07788   280 RrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTsSLKIIFVSGSALSPELATRALEAFG---PVLYNLYG 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1866 ITETTVHVTYRPLSLADldggAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYlnrpelsctrfvadpf 1945
Cdd:PRK07788   357 STEVAFATIATPEDLAE----APGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY---------------- 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 stTGGR-------LYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGAtQLV 2016
Cdd:PRK07788   417 --TDGRdkqiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgvDDEEFGQ-RLR 493
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2017 GYVVtqaaPSDPAAL-RDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPD 2075
Cdd:PRK07788   494 AFVV----KAPGAALdEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
536-1007 7.64e-31

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 128.79  E-value: 7.64e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQ 615
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SVLARLpqsdglqsllldDLERLVHgypaenpdlpeapdslcyaIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05973     81 ANRHKL------------DSDPFVM-------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPE 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLSVTTFSFdIFGLELYV--PLARGASMLLAsrEQAQDPEALLDLVERQGVTVLQATPATWRML-CDSERVDLLRGCT 772
Cdd:cd05973    130 DSFWNAADPGW-AYGLYYAItgPLALGHPTILL--EGGFSVESTWRVIERLGVTNLAGSPTAYRLLmAAGAEVPARPKGR 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  773 LL---CGGEALAEDLAARMRG-LSASTWNLYGPTETTIWSAR-FRLGEEARP-FLGGPLENTALYILDSEMNPCPPGVAG 846
Cdd:cd05973    207 LRrvsSAGEPLTPEVIRWFDAaLGVPIHDHYGQTELGMVLANhHALEHPVHAgSAGRAMPGWRVAVLDDDGDELGPGEPG 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  847 ELLIGgdglargYHRRPGLTAERF-LPDPFAADGsRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLE 925
Cdd:cd05973    287 RLAID-------IANSPLMWFRGYqLPDTPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIE 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  926 QDSVREAVVVAQPG-VAGPTLVAYLVPTEAAlvDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd05973    359 HPAVAEAAVIGVPDpERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSA----HAYPRTIHFVDELPKTPSGKIQR 432

                   ...
gi 2183974163 1005 KAL 1007
Cdd:cd05973    433 FLL 435
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1574-2066 9.64e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 130.28  E-value: 9.64e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVG-PDVLVGLAAERSlEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK07786    23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQ-------RAARERLPLGEGLPCLLLDAEHEWAGY----PESDPQSA---VGVDNLAYVIY 1718
Cdd:PRK07786   102 TPPEIAFLVSDCGAHVVVTEaalapvaTAVRDIVPLLSTVVVAGGSSDDSVLGYedllAEAGPAHApvdIPNDSPALIMY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1719 TSGSTGKPKGTLLPHGNVL-RLFDATRHWFGFSADD----AWSLFHSYAfdfsVWEIFGALLHGGRLVIVPYEtSRSPED 1793
Cdd:PRK07786   182 TSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDvgfvGVPLFHIAG----IGSMLPGLLLGAPTVIYPLG-AFDPGQ 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1794 FLRLLCRERVTVLNQTPSAFkqlmQVACAGQEVPP--LALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGITETTv 1871
Cdd:PRK07786   257 LLDVLEAEKVTGIFLVPAQW----QAVCAEQQARPrdLALRVLSWGAAPASDTLLRQMAATFPEAQ--ILAAFGQTEMS- 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1872 hvtyrPLSLAdLDGGAA----SPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSctrfvADPFSt 1947
Cdd:PRK07786   330 -----PVTCM-LLGEDAirklGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEAT-----AEAFA- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1948 tgGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGATQLVgyVVTQAAP 2025
Cdd:PRK07786   398 --GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIgrADEKWGEVPVA--VAAVRND 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2183974163 2026 SDPAALRDtLRQALKASLPEHMVPAHLLFLERLPLTANGKL 2066
Cdd:PRK07786   474 DAALTLED-LAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1574-2071 9.93e-31

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 131.22  E-value: 9.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVY-GE-----RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVP 1647
Cdd:TIGR02188   63 VDRHLEARPDKVAIIWeGDepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSV 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRLGYMIEDSGIRLLLTQRAARER---LPL------------------------GEGLPCLLLDAEHEW---- 1696
Cdd:TIGR02188  143 VFGGFSAEALADRINDAGAKLVITADEGLRGgkvIPLkaivdealekcpvsvehvlvvrrtGNPVVPWVEGRDVWWhdlm 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1697 AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW---------FGFSADDAWSLFHSYAfdfsv 1767
Cdd:TIGR02188  223 AKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYvfdikdgdiFWCTADVGWITGHSYI----- 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1768 weIFGALLHGGRLVIvpYE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvacAGQEVP------PLALRHVVfgG 1838
Cdd:TIGR02188  298 --VYGPLANGATTVM--FEgvpTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMR---LGDEWVkkhdlsSLRLLGSV--G 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1839 EALEVQALRPWFERFGDRAPRLVNMYGITETTVHVTyRPL-SLADLDGGAASPigePIPDLSWYLLDAGLNPVPrgcigE 1917
Cdd:TIGR02188  369 EPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMI-TPLpGATPTKPGSATL---PFFGIEPAVVDEEGNPVE-----G 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1918 LYVGGA--------GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEI 1989
Cdd:TIGR02188  440 PGEGGYlvikqpwpGMLRTIYGDHE----RFVDTYFSPFPG-YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEI 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1990 EARLLAQPGVAEAVVL--PHEGPGATqLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLD 2067
Cdd:TIGR02188  515 ESALVSHPAVAEAAVVgiPDDIKGQA-IYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIM 593

                   ....
gi 2183974163 2068 RRAL 2071
Cdd:TIGR02188  594 RRLL 597
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1586-2074 1.07e-30

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 129.82  E-value: 1.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1586 AVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSG 1665
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1666 IRLLLTQ----RAARERLPlgEGLPCLL------------LDAEH--------EWAGY-PESDPQSAVGVDNLAYVIYTS 1720
Cdd:PRK12406    84 ARVLIAHadllHGLASALP--AGVTVLSvptppeiaaayrISPALltppagaiDWEGWlAQQEPYDGPPVPQPQSMIYTS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1721 GSTGKPKGtllphgnvLRLFDAT-----------RHWFGFSADD----AWSLFHS--YAFDFSvweifgALLHGGRLVIV 1783
Cdd:PRK12406   162 GTTGHPKG--------VRRAAPTpeqaaaaeqmrALIYGLKPGIrallTGPLYHSapNAYGLR------AGRLGGVLVLQ 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1784 P-YEtsrsPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPLA-LRHVVFGGEALEVQALRPWFERFGdraPRLV 1861
Cdd:PRK12406   228 PrFD----PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSsLRHVIHAAAPCPADVKRAMIEWWG---PVIY 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1862 NMYGITETTVhVTYrplslADLDGGAASP--IGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLAR-GYLNRPElscT 1938
Cdd:PRK12406   301 EYYGSTESGA-VTF-----ATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE---K 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1939 RFVADPfsttgGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATqLV 2016
Cdd:PRK12406   372 RAEIDR-----GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfgIPDAEFGEA-LM 445
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 2017 GYVVTQA-APSDPAALRDTLrqalKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAP 2074
Cdd:PRK12406   446 AVVEPQPgATLDEADIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
503-956 1.14e-30

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 130.99  E-value: 1.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  503 ASEYPAGQGVHRLFEAQAGLTPDAPALLF----GEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALL 578
Cdd:COG1022      4 FSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  579 AVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL--SQQ------SVLARLPQ------------SDGLQSLLLDDLERL 638
Cdd:COG1022     84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEqldkllEVRDELPSlrhivvldprglRDDPRLLSLDELLAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  639 vhGYPAENPDLPEA------PDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFdIFG-- 710
Cdd:COG1022    164 --GREVADPAELEArraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAH-VFErt 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  711 LELYVpLARGASMLLASreqaqDPEALLDLVERQGVTVLQATPATW---------------------------------R 757
Cdd:COG1022    241 VSYYA-LAAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkrklfrwalavgrryaR 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  758 MLCDSERVDLL----------------------RGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTET----TIWSA-R 810
Cdd:COG1022    315 ARLAGKSPSLLlrlkhaladklvfsklrealggRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETspviTVNRPgD 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  811 FRLGEearpfLGGPLENTALYILDSemnpcppgvaGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLAR 890
Cdd:COG1022    395 NRIGT-----VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDIGE 452
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  891 YRADGVIEYLGRIDHQVKIR-GFRIELGEIETRLLEQDSVREAVVVAQpgvAGPTLVAYLVPTEAAL 956
Cdd:COG1022    453 LDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD---GRPFLAALIVPDFEAL 516
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1551-2071 1.29e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 129.88  E-value: 1.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1551 RADLLQWNPGPQDFTPAS-CLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSL 1629
Cdd:PRK06155     3 PLGAGLAARAVDPLPPSErTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1630 EMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERL----PLGEGLPCL-LLDAEHEWA------- 1697
Cdd:PRK06155    83 EFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadPGDLPLPAVwLLDAPASVSvpagwst 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1698 -GYPESD---PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFHSYAFDfsvwE 1769
Cdd:PRK06155   163 aPLPPLDapaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLyttlPLFHTNALN----A 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1770 IFGALLHGGRLVIVP-YETSRspedFLRLLCRERVTV-----------LNQTPSAFKQLMQVACA-GQEVPPlalrhvvf 1836
Cdd:PRK06155   239 FFQALLAGATYVLEPrFSASG----FWPAVRRHGATVtyllgamvsilLSQPARESDRAHRVRVAlGPGVPA-------- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1837 ggealevQALRPWFERFGdraPRLVNMYGITETTVHVTyrpLSLADLDGGAAspiGEPIPDLSWYLLDAGLNPVPRGCIG 1916
Cdd:PRK06155   307 -------ALHAAFRERFG---VDLLDGYGSTETNFVIA---VTHGSQRPGSM---GRLAPGFEARVVDEHDQELPDGEPG 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1917 ELYVGGA---GLARGYLNRPELSCTRFVADPFsttggrlyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARL 1993
Cdd:PRK06155   371 ELLLRADepfAFATGYFGMPEKTVEAWRNLWF--------HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVL 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1994 LAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALrdtLRQAlKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06155   443 LSHPAVAAAAVfpVPSELGEDEVMAAVVLRDGTALEPVAL---VRHC-EPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2639-2940 1.57e-30

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 127.57  E-value: 1.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2639 PLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLW--------QGALEKP-LQLVR 2708
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGpLDVARLERAVRAVGQRHEALRTCFFTdpedgepmQGVLASSpLRLEH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2709 KRVEVPFSVHDWRDRADLAEaldalaageaglgFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQR 2788
Cdd:cd19532     83 VQISDEAEVEEEFERLKNHV-------------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2789 YRGETPSRSDGRYRDYIAwLQRQD--AGRTE---AFWKQRLQRLGEPTLLVPaFAH-GVRGAeghADRY------RQLDV 2856
Cdd:cd19532    150 YNGQPLLPPPLQYLDFAA-RQRQDyeSGALDedlAYWKSEFSTLPEPLPLLP-FAKvKSRPP---LTRYdthtaeRRLDA 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2857 TTSQRLAEFAREQKVT-----LntlvqAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPCPEQ 2931
Cdd:cd19532    225 ALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQ 297

                   ....*....
gi 2183974163 2932 PIGDWLQAV 2940
Cdd:cd19532    298 TFADVLKET 306
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1590-2071 2.57e-30

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 127.33  E-value: 2.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1590 GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLL 1669
Cdd:cd05907      2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1670 LTqraarerlplgeglpcllldaehewagypeSDPqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGF 1749
Cdd:cd05907     82 FV------------------------------EDP------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1750 SADDAWSLF----HSYAfdfSVWEIFGALLHGGRLVIVPyetsrSPEDFLRLLCRERVTVLNQTPSAFKQlMQVACAGQE 1825
Cdd:cd05907    126 TEGDRHLSFlplaHVFE---RRAGLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEK-VYAAIKVKA 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1826 VPPLA-----------LRHVVFGGEALEVQALRpWFERFGdraprlVNM---YGITETTVHVTYRPlsLADLDGGAaspI 1891
Cdd:cd05907    197 VPGLKrklfdlavggrLRFAASGGAPLPAELLH-FFRALG------IPVyegYGLTETSAVVTLNP--PGDNRIGT---V 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1892 GEPIPDLSWYLLDAglnpvprgciGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVG 1971
Cdd:cd05907    265 GKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITG 327
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RI-DHQVKIRGFRIELGEIEARLLAQPGVAEAVVLpheGPGATQLVGYVV------------TQAAPSDPA------ALR 2032
Cdd:cd05907    328 RKkDLIITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALIVpdpealeawaeeHGIAYTDVAelaanpAVR 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 2033 DTLRQALK---ASLPEHMVPAHLLFLERLP------LTANGKLDRRAL 2071
Cdd:cd05907    405 AEIEAAVEaanARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3099-3183 4.01e-30

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 126.81  E-value: 4.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd17650     81 EDSGA 85
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1559-2071 6.81e-30

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 127.78  E-value: 6.81e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1559 PGPQDFTPASCLHRLieRQAAERPRATAVVY-----GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIV 1633
Cdd:cd05906      2 LHRPEGAPRTLLELL--LRAAERGPTKGITYidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1634 GLLAILKAGGAYVPLDP----RYPSDRLGYM-----IEDSGiRLLLTQRAARERLPLGE--GLPCLLLDAEHEWAGYPES 1702
Cdd:cd05906     80 AFWACVLAGFVPAPLTVpptyDEPNARLRKLrhiwqLLGSP-VVLTDAELVAEFAGLETlsGLPGIRVLSIEELLDTAAD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1703 DPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAwslfhsyafdFSVWEIF---GALLH--- 1776
Cdd:cd05906    159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV----------FLNWVPLdhvGGLVElhl 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1777 -----GGRLVIVPYETS-RSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACagqEVPP-----LALRHVVFGGEALEVQA 1845
Cdd:cd05906    229 ravylGCQQVHVPTEEIlADPLRWLDLIDRYRVTITWAPNFAFALLNDLLE---EIEDgtwdlSSLRYLVNAGEAVVAKT 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1846 LRPW---FERFGDRAPRLVNMYGITETTVHVTY-RPLSLADLDGGAA-SPIGEPIPDLSWYLLDAGLNPVPRGCIGELYV 1920
Cdd:cd05906    306 IRRLlrlLEPYGLPPDAIRPAFGMTETCSGVIYsRSFPTYDHSQALEfVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQV 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1921 GGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLArYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVA 2000
Cdd:cd05906    386 RGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2001 E---AVVLPHEGPGATQL--VGYVVTQAAPSDPAALRDTLRQalKASLPEHMVPAHLLFLER--LPLTANGKLDRRAL 2071
Cdd:cd05906    458 PsftAAFAVRDPGAETEElaIFFVPEYDLQDALSETLRAIRS--VVSREVGVSPAYLIPLPKeeIPKTSLGKIQRSKL 533
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1718-2068 1.22e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 123.16  E-value: 1.22e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1718 YTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAfdfSVWEIFGALLHGGRLVIVpyETSRSPED 1793
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlciPVPLFHCFG---SVLGVLACLTHGATMVFP--SPSFDPLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1794 FLRLLCRERVTVLNQTPSAFkqlmqVACAGQ----EVPPLALRHVVFGGEALEVQALRPWFERFGdrAPRLVNMYGITET 1869
Cdd:cd05917     84 VLEAIEKEKCTALHGVPTMF-----IAELEHpdfdKFDLSSLRTGIMAGAPCPPELMKRVIEVMN--MKDVTIAYGMTET 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1870 TvHVTYRPLSLADLDGGAASpIGEPIPDLSWYLLDAGLNPVP-RGCIGELYVGGAGLARGYLNRPELscTRFVADpfstt 1948
Cdd:cd05917    157 S-PVSTQTRTDDSIEKRVNT-VGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEK--TAEAID----- 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1949 GGRLYRTGDLARYRCDGVVEYVGRIDHQVkIRGFR-IELGEIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQAAP 2025
Cdd:cd05917    228 GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVvgVPDERYG-EEVCAWIRLKEGA 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2183974163 2026 SdpaALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd05917    306 E---LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3087-3182 1.34e-29

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 125.73  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3166
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90
                   ....*....|....*.
gi 2183974163 3167 PEYPEERQAYMLEDSG 3182
Cdd:cd05918     81 PSHPLQRLQEILQDTG 96
AMP-binding pfam00501
AMP-binding enzyme;
3091-3183 1.98e-29

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 123.96  E-value: 1.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3091 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90
                   ....*....|....
gi 2183974163 3170 PEERQAYMLEDSGV 3183
Cdd:pfam00501   81 PAEELAYILEDSGA 94
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1559-2071 3.20e-29

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 125.77  E-value: 3.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1559 PGPQDFTPAscLHRLIERQAAERPRATA-VVYGER-ALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLL 1636
Cdd:PRK05852     9 PMASDFGPR--IADLVEVAATRLPEAPAlVVTADRiAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1637 AILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLL-------------------TQRAARERLPlGEGLPCLLLDAehewA 1697
Cdd:PRK05852    87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidadgphdraepttrwwplTVNVGGDSGP-SGGTLSVHLDA----A 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1698 GYPESDPQSAVGV-DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDA----WSLFHSYAFDFSVWeifg 1772
Cdd:PRK05852   162 TEPTPATSTPEGLrPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDAtvavMPLYHGHGLIAALL---- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1773 ALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVP--PLALRHVVFGGEALEVQALRPWF 1850
Cdd:PRK05852   238 ATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERA-ATEPSGrkPAALRFIRSCSAPLTAETAQALQ 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1851 ERFGdrAPrLVNMYGITETTVHVTYRPLSLADLD---GGAASPIGEPI-PDLSWYLLDAGlnPVPRGCIGELYVGGAGLA 1926
Cdd:PRK05852   317 TEFA--AP-VVCAFGMTEATHQVTTTQIEGIGQTenpVVSTGLVGRSTgAQIRIVGSDGL--PLPAGAVGEVWLRGTTVV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1927 RGYLNRPELSCTRFvadpfstTGGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL- 2005
Cdd:PRK05852   392 RGYLGDPTITAANF-------TDGWL-RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFg 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2006 -PHEGPGATqlVGYVVTQAAPSDPAAlrDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK05852   464 vPDQLYGEA--VAAVIVPRESAPPTA--EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2174-2600 3.48e-29

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 123.47  E-value: 3.48e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQ-MFFE--LDIPRRQHWNQSVL-LEpgQALDGTLLETALQALLAHHDALRLGFRLEdgtWRAE-----HRAVEA 2244
Cdd:cd19543      3 PLSPMQEgMLFHslLDPGSGAYVEQMVItLE--GPLDPDRFRAAWQAVVDRHPILRTSFVWE---GLGEplqvvLKDRKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2245 G-EVLLWQQSVADGQ--ALEALAEQVQ-RSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQ 2320
Cdd:cd19543     78 PwRELDLSHLSEAEQeaELEALAEEDReRGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2321 LQAGQAVALPAKTSaFKAWAERLQAHARdgglEGERGYWLAQLEGVS--TELPCDDREGAQSVRHVRSARTELTEEATRR 2398
Cdd:cd19543    158 LGEGQPPSLPPVRP-YRDYIAWLQRQDK----EAAEAYWREYLAGFEepTPLPKELPADADGSYEPGEVSFELSAELTAR 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2399 LLQEApAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDltRTVGWFTSLFPLR--LSPVAELGASIK 2476
Cdd:cd19543    233 LQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFINTLPVRvrLDPDQTVLELLK 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2477 RI-KEQLRAIPHKGLGFGALRylgsaedraALAALPSPRI----TF-NYLGQFDGSFSADSSALfrpSADAAGSERDSDA 2550
Cdd:cd19543    310 DLqAQQLELREHEYVPLYEIQ---------AWSEGKQALFdhllVFeNYPVDESLEEEQDEDGL---RITDVSAEEQTNY 377
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2551 PLdNWLSLNGqvyaGRLGIDWSFSAARFSEASILRLADAYRDELLALIEH 2600
Cdd:cd19543    378 PL-TVVAIPG----EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1583-2071 4.52e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 124.63  E-value: 4.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1583 RATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIE 1662
Cdd:PRK08276     1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1663 DSGIRLLLTQ-------RAARERLPLgeGLPCLLLDAEHE--WAGYPES-DPQSAVGVDNL---AYVIYTSGSTGKPKGT 1729
Cdd:PRK08276    81 DSGAKVLIVSaaladtaAELAAELPA--GVPLLLVVAGPVpgFRSYEEAlAAQPDTPIADEtagADMLYSSGTTGRPKGI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1730 L--LPH-------GNVLRLFDAtrhWFGFSADDAW----SLFHSYAFDFSVWeifgALLHGGRLVIVPyetSRSPEDFLR 1796
Cdd:PRK08276   159 KrpLPGldpdeapGMMLALLGF---GMYGGPDSVYlspaPLYHTAPLRFGMS----ALALGGTVVVME---KFDAEEALA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1797 LLCRERVTVLNQTPSAFKQLMQVAcagQEVPPL----ALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTVh 1872
Cdd:PRK08276   229 LIERYRVTHSQLVPTMFVRMLKLP---EEVRARydvsSLRVAIHAAAPCPVEVKRAMIDWWG---PIIHEYYASSEGGG- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1873 vtyrpLSLADLDGGAASP--IGEPIpDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTG- 1949
Cdd:PRK08276   302 -----VTVITSEDWLAHPgsVGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGd 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1950 -GRLYRTGDLarYRCDgvveyvgRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGatQLVGYVVTqaaPS 2026
Cdd:PRK08276   376 vGYLDEDGYL--YLTD-------RKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfgVPDEEMG--ERVKAVVQ---PA 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2183974163 2027 DPAALRDTLRQALKASLPEH----MVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08276   442 DGADAGDALAAELIAWLRGRlahyKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
519-1007 4.85e-29

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 124.30  E-value: 4.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  519 QAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADR 598
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  599 LQYMIDDSGLRLLLSQQSVLARLpqsDGLQSLLLDDLERLvhgyPAENPDLPEA--PDSLCYAIYTSGSTGQPKGVMVR- 675
Cdd:PRK03640    91 LLWQLDDAEVKCLITDDDFEAKL---IPGISVKFAELMNG----PKEEAEIQEEfdLDEVATIMYTSGTTGKPKGVIQTy 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 ----HRALtnfvcSIARQPGMLARDRLLSVTTFsFDIFGLELYV-PLARGASMLLasrEQAQDPEALLDLVERQGVTVLQ 750
Cdd:PRK03640   164 gnhwWSAV-----GSALNLGLTEDDCWLAAVPI-FHISGLSILMrSVIYGMRVVL---VEKFDAEKINKLLQTGGVTIIS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  751 ATPAtwrMLCD-SERV------DLLRgCTLLCGGEALAEDL-AARMRGLsaSTWNLYGPTETTiwS---------ARFRL 813
Cdd:PRK03640   235 VVST---MLQRlLERLgegtypSSFR-CMLLGGGPAPKPLLeQCKEKGI--PVYQSYGMTETA--SqivtlspedALTKL 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  814 GEearpfLGGPLENTALYILDsEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYRA 893
Cdd:PRK03640   307 GS-----AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF------QDG--WFKTGDIGYLDE 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  894 DGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTLVAylVPTeAALVDAESARQQELRSALKN 973
Cdd:PRK03640   373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV---GVPDDKWGQ--VPV-AFVVKSGEVTEEELRHFCEE 446
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2183974163  974 SllavLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK03640   447 K----LAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
525-1017 4.87e-29

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 125.39  E-value: 4.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  525 DAPALLF----GEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPL----DPQYPA 596
Cdd:PRK04319    59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVR 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  597 DRLQymidDSGLRLLLSQQSVLARLPQsDGLQSL----LLDDLERLVHGYPAENPDLPEAPDSLCY--------AI--YT 662
Cdd:PRK04319   139 DRLE----DSEAKVLITTPALLERKPA-DDLPSLkhvlLVGEDVEEGPGTLDFNALMEQASDEFDIewtdredgAIlhYT 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  663 SGSTGQPKGV------MVRHRALTNFV----------CSIarQPGMlardrllsVTTFSFDIFGlelyvPLARGASMLLa 726
Cdd:PRK04319   214 SGSTGKPKGVlhvhnaMLQHYQTGKYVldlheddvywCTA--DPGW--------VTGTSYGIFA-----PWLNGATNVI- 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  727 sREQAQDPEALLDLVERQGVTVLQATPATWRML--CDSE---RVDL--LRgcTLLCGGEAL-AEDLAARMRGLSA---ST 795
Cdd:PRK04319   278 -DGGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDlvkKYDLssLR--HILSVGEPLnPEVVRWGMKVFGLpihDN 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  796 WNLygpTET-TIWSARFRlGEEARP-FLGGPLENTALYILDSEMNPCPPGVAGELLI--GGDGLARGYHRRPGLTAERFL 871
Cdd:PRK04319   355 WWM---TETgGIMIANYP-AMDIKPgSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFA 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  872 PDpfaadgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLV 950
Cdd:PRK04319   431 GD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDpVRGEIIKAFVA 502
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  951 ------PTEAAlvdaesarQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINR---KA----LPLPDASAVRD 1017
Cdd:PRK04319   503 lrpgyePSEEL--------KEEIRGFVKKGLGA----HAAPREIEFKDKLPKTRSGKIMRrvlKAwelgLPEGDLSTMED 570
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1712-2068 1.47e-28

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 119.05  E-value: 1.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1712 NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIvpyETSRSP 1791
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1792 EDFLRLLCRERVTVLNQTPSAFKQLMQVacagqEVPPLALRHVVFGGEALEVQAlrpwFERFGDRAPR--LVNMYGITET 1869
Cdd:cd17633     78 KSWIRKINQYNATVIYLVPTMLQALART-----LEPESKIKSIFSSGQKLFEST----KKKLKNIFPKanLIEFYGTSEL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1870 TvHVTYRplsladLDGGAASP--IGEPIPDLSWYLLDAGlnpvpRGCIGELYVGGAGLARGYLNRPELSCTRFvadpfst 1947
Cdd:cd17633    149 S-FITYN------FNQESRPPnsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------- 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1948 tggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGATQLVGYVVTQAAp 2025
Cdd:cd17633    210 -----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgiPDARFGEIAVALYSGDKLT- 283
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2183974163 2026 sdpaalRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd17633    284 ------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
499-1007 1.51e-28

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 123.46  E-value: 1.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  499 SRLPASEypAGQGVHRLFEAQAGLTPDAPALLFGEER--LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVA 576
Cdd:PRK05852     7 AAPMASD--FGPRIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  577 LLAVLKAGGAYVPLDPQYPA----DRLQ------YMIDDSG--------LRLLLSQQSVLARLPQSDGLQSLLLDDLERL 638
Cdd:PRK05852    85 LLAASRADLVVVPLDPALPIaeqrVRSQaagarvVLIDADGphdraeptTRWWPLTVNVGGDSGPSGGTLSVHLDAATEP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  639 VHGYPAenPDLPEAPDSLCyaIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGL--ELYVP 716
Cdd:PRK05852   165 TPATST--PEGLRPDDAMI--MFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPL-YHGHGLiaALLAT 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  717 LARGASMLLASREQAQdPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLL------CGGEALAEDLAARMRG 790
Cdd:PRK05852   240 LASGGAVLLPARGRFS-AHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAAlrfirsCSAPLTAETAQALQTE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  791 LSASTWNLYGPTETTIWSARFRL-----GEEARPFLGGPLENTA--LYILDSEMNPCPPGVAGELLIGGDGLARGYHRRP 863
Cdd:PRK05852   319 FAAPVVCAFGMTEATHQVTTTQIegigqTENPVVSTGLVGRSTGaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDP 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  864 GLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAG 942
Cdd:PRK05852   399 TITAANF------TDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdQLYG 470
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  943 PTLVAYLVPTEAALVDAesarqQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK05852   471 EAVAAVIVPRESAPPTA-----EELVQFCRERLAA----FEIPASFQEASGLPHTAKGSLDRRAV 526
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1578-2071 1.68e-28

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 122.69  E-value: 1.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGIRLLLTQRAAreRLPLGEGLPCLLLDAEHEW------AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLL 1731
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEF--DAIVALETPKIVIDAAAQAdsrrlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMH 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1732 PHGNV-LRLFDATRHwFGFSADD----AWSLFHSYAFDFSVweiFGALLHGGRLVIvpyETSRSPEDFLRLLCRERVTVL 1806
Cdd:PRK06145   170 SYGNLhWKSIDHVIA-LGLTASErllvVGPLYHVGAFDLPG---IAVLWVGGTLRI---HREFDPEAVLAAIERHRLTCA 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1807 NQTPSAFKQLMqvACAGQEVPPL-ALRHVVFGGEALEVQALRPWFERFgdRAPRLVNMYGITETTVHVTyrpLSLADLDG 1885
Cdd:PRK06145   243 WMAPVMLSRVL--TVPDRDRFDLdSLAWCIGGGEKTPESRIRDFTRVF--TRARYIDAYGLTETCSGDT---LMEAGREI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlyRTGDLARYRCDG 1965
Cdd:PRK06145   316 EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1966 VVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL-PHEGPGATQLVGYVVTQAAPSdpaALRDTLRQALKASLP 2044
Cdd:PRK06145   388 FLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVVLNPGAT---LTLEALDRHCRQRLA 464
                          490       500
                   ....*....|....*....|....*..
gi 2183974163 2045 EHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06145   465 SFKVPRQLKVRDELPRNPSGKVLKRVL 491
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1555-2071 1.81e-28

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 124.21  E-value: 1.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1555 LQWNPGPQDF-------TPASclHRLIERQAAERPRATAVVY-GE-----RALDYGELNLRANRLAHRLIELGVGPDVLV 1621
Cdd:cd05966     35 LDWSKGPPFIkwfeggkLNIS--YNCLDRHLKERGDKVAIIWeGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRV 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1622 GLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARER---LPLG-------EGLP----C 1687
Cdd:cd05966    113 AIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGYRGgkvIPLKeivdealEKCPsvekV 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1688 LL---------------LDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW------ 1746
Cdd:cd05966    193 LVvkrtggevpmtegrdLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYvfdyhp 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 ---FGFSADDAWSLFHSYAfdfsvweIFGALLHGGRLVIvpYE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQva 1820
Cdd:cd05966    273 ddiYWCTADIGWITGHSYI-------VYGPLANGATTVM--FEgtpTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMK-- 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1821 cAGQEVPP------LALRHVVfgGEALEVQALRpWFERF--GDRAPrLVNMYGITETTVH-VTYRPlSLADLDGGAASPi 1891
Cdd:cd05966    342 -FGDEWVKkhdlssLRVLGSV--GEPINPEAWM-WYYEVigKERCP-IVDTWWQTETGGImITPLP-GATPLKPGSATR- 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1892 gePIPDLSWYLLDAGLNPVPRGCIGELYVGGA--GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEY 1969
Cdd:cd05966    415 --PFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPG-YYFTGDGARRDEDGYYWI 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1970 VGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATqLVGYVVTQAAPSDPAALRDTLRQALKASLPEHM 2047
Cdd:cd05966    488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVvgRPHDIKGEA-IYAFVTLKDGEEPSDELRKELRKHVRKEIGPIA 566
                          570       580
                   ....*....|....*....|....
gi 2183974163 2048 VPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05966    567 TPDKIQFVPGLPKTRSGKIMRRIL 590
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3113-3183 2.34e-28

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 120.83  E-value: 2.34e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 3113 YAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGA 73
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1594-2071 2.50e-28

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 121.14  E-value: 2.50e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1594 LDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPrypsdrlgymiedsgirlLLTQR 1673
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATT------------------LLTPD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1674 AARERLPLGEGLPCLLLDAEHEwagypeSDPQsavgvdnLAYviYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD 1753
Cdd:cd05974     63 DLRDRVDRGGAVYAAVDENTHA------DDPM-------LLY--FTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 AWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPplaLRH 1833
Cdd:cd05974    128 VHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVK---LRE 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1834 VVFGGEAL--EV--QALRPWFERFGDRaprlvnmYGITETTVHVTYRPLSLAdldggAASPIGEPIPDLSWYLLDAGLNP 1909
Cdd:cd05974    205 VVGAGEPLnpEVieQVRRAWGLTIRDG-------YGQTETTALVGNSPGQPV-----KAGSMGRPLPGYRVALLDPDGAP 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1910 VPRGCIGeLYVGG---AGLARGYLNRPELSCtrfvadpfSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:cd05974    273 ATEGEVA-LDLGDtrpVGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISP 343
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVVLPheGPGATQLV---GYVV-TQAAPSDPAALRDTLRQALKASLPEHMVpAHLLFLErLPLTA 2062
Cdd:cd05974    344 FELESVLIEHPAVAEAAVVP--SPDPVRLSvpkAFIVlRAGYEPSPETALEIFRFSRERLAPYKRI-RRLEFAE-LPKTI 419

                   ....*....
gi 2183974163 2063 NGKLDRRAL 2071
Cdd:cd05974    420 SGKIRRVEL 428
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1578-2071 4.09e-28

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 121.42  E-value: 4.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVlVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:PRK07638    11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGIRLLLTQRAARERLPLGEGlPCLLLDaehEWAGYPESDPQSAVGVDNLA----YVIYTSGSTGKPKGTLLPH 1733
Cdd:PRK07638    90 KERLAISNADMIVTERYKLNDLPDEEG-RVIEID---EWKRMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1734 GNVLRLFDATRHWFGFSADD----AWSLFHSYaFdfsvweIFGAL--LHGGRLVIVpyETSRSPEDFLRLLCRERVTVLN 1807
Cdd:PRK07638   166 QSWLHSFDCNVHDFHMKREDsvliAGTLVHSL-F------LYGAIstLYVGQTVHL--MRKFIPNQVLDKLETENISVMY 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1808 QTPSAFKQLMQVacagQEVPPLALRHVVFGG--EALEVQALRPWFERFgdrapRLVNMYGITETTVhVTYrpLSLADLDG 1885
Cdd:PRK07638   237 TVPTMLESLYKE----NRVIENKMKIISSGAkwEAEAKEKIKNIFPYA-----KLYEFYGASELSF-VTA--LVDEESER 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GAASpIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLN----RPELSctrfvADPFSTtggrlyrTGDLARY 1961
Cdd:PRK07638   305 RPNS-VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIggvlARELN-----ADGWMT-------VRDVGYE 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1962 RCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGaTQLVGYVVTQAApsdpaalRDTLRQAL 2039
Cdd:PRK07638   372 DEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIgvPDSYWG-EKPVAIIKGSAT-------KQQLKSFC 443
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2183974163 2040 KASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK07638   444 LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1716-2068 4.75e-28

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 118.13  E-value: 4.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1716 VIYTSGSTGKPKGTLLPHGN-VLRLFDATRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIvpYETSRSPEDF 1794
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGENTTYKSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1795 LRLLCRERVTVLNQTPSAFKQLM-QVACAGQEVPplALRHVVFGGEALeVQALRPWFERFGDraPRLVNMYGITETTVhV 1873
Cdd:cd17635     84 FKILTTNAVTTTCLVPTLLSKLVsELKSANATVP--SLRLIGYGGSRA-IAADVRFIEATGL--TNTAQVYGLSETGT-A 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSLADLDGGAaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpfsttGGRLY 1953
Cdd:cd17635    158 LCLPTDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVN 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1954 rTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGAtqLVGYVVTQAAPSDPAAL 2031
Cdd:cd17635    228 -TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACyeISDEEFGE--LVGLAVVASAELDENAI 304
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2183974163 2032 RDtLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd17635    305 RA-LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1569-2068 4.89e-28

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 122.19  E-value: 4.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1569 CLHRLIERQAAERPRATAVVYGERAL--DYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYV 1646
Cdd:PRK12583    19 TIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1647 PLDPRYPSDRLGYMIEDSGIRLLLTQRAAR-------------------------ERLPLGEGLpcLLLDAE-------- 1693
Cdd:PRK12583    99 NINPAYRASELEYALGQSGVRWVICADAFKtsdyhamlqellpglaegqpgalacERLPELRGV--VSLAPApppgflaw 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1694 HEWAGYPES-------DPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLR--LFDATRhwFGFSADDAW----SLFHS 1760
Cdd:PRK12583   177 HELQARGETvsrealaERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNngYFVAES--LGLTEHDRLcvpvPLYHC 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1761 YAFdfsVWEIFGALLHGGRLVIvPYEtSRSPEDFLRLLCRERVTVLNQTPSAF--------------KQLMQVACAGQEV 1826
Cdd:PRK12583   255 FGM---VLANLGCMTVGACLVY-PNE-AFDPLATLQAVEEERCTALYGVPTMFiaeldhpqrgnfdlSSLRTGIMAGAPC 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1827 PPLALRHVVFGGEALEVQAlrpwferfgdraprlvnMYGITETTvHVTYRPLSLADLDGGAASpIGEPIPDLSWYLLDAG 1906
Cdd:PRK12583   330 PIEVMRRVMDEMHMAEVQI-----------------AYGMTETS-PVSLQTTAADDLERRVET-VGRTQPHLEVKVVDPD 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfsttgGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:PRK12583   391 GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDED------GWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYP 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQaapSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANG 2064
Cdd:PRK12583   464 REIEEFLFTHPAVADVQVfgVPDEKYG-EEIVAWVRLH---PGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTG 539

                   ....
gi 2183974163 2065 KLDR 2068
Cdd:PRK12583   540 KVQK 543
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3098-3183 5.12e-28

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 121.04  E-value: 5.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3098 TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3177
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                   ....*.
gi 2183974163 3178 LEDSGV 3183
Cdd:cd17656     81 MLDSGV 86
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1578-2071 5.75e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 122.07  E-value: 5.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGIRLLLTQ-------RAARERLPLGEG----------------LPCLLLDAEHEWAGY----------PESDP 1704
Cdd:PRK06178   123 SYELNDAGAEVLLALdqlapvvEQVRAETSLRHVivtsladvlpaeptlpLPDSLRAPRLAAAGAidllpalracTAPVP 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1705 QSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFdATRHWFGFSADDAwSLFHSYAFDFsvW---EIFGALL---HGG 1778
Cdd:PRK06178   203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA-AAAYAVAVVGGED-SVFLSFLPEF--WiagENFGLLFplfSGA 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1779 RLVIVpyeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLMqvacagqEVPPLA------LRHVvfgGEALEVQALRPWF-E 1851
Cdd:PRK06178   279 TLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELM-------DHPRFAeydlssLRQV---RVVSFVKKLNPDYrQ 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1852 RFGDRAPRLV--NMYGITETTVHVTY-RPLSLADLD-GGAASPIGEPIPDLSWYLLD--AGlNPVPRGCIGELYVGGAGL 1925
Cdd:PRK06178   346 RWRALTGSVLaeAAWGMTETHTCDTFtAGFQDDDFDlLSQPVFVGLPVPGTEFKICDfeTG-ELLPLGAEGEIVVRTPSL 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1926 ARGYLNRPELSCTRFVadpfsttGGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL 2005
Cdd:PRK06178   425 LKGYWNKPEATAEALR-------DGWL-HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV 496
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2006 PHEGPGATQL-VGYVVTQ-AAPSDPAALRDTLRQALKAslpeHMVPaHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06178   497 GRPDPDKGQVpVAFVQLKpGADLTAAALQAWCRENMAV----YKVP-EIRIVDALPMTATGKVRKQDL 559
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
520-1024 6.60e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 121.81  E-value: 6.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVG-SDVLVGIALERgVPMVVALLAVLKAGGAYVPLDPQYPADR 598
Cdd:PRK07786    27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNR-TEFVESVLAANMLGAIAVPVNFRLTPPE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  599 LQYMIDDSGLRLLLSQ---QSVLARLPQSDGLQSLLL---DDLERLVHGY--------PAENP-DLPEapDSLCYAIYTS 663
Cdd:PRK07786   106 IAFLVSDCGAHVVVTEaalAPVATAVRDIVPLLSTVVvagGSSDDSVLGYedllaeagPAHAPvDIPN--DSPALIMYTS 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  664 GSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVP-LARGASMLLASReQAQDPEALLDLVE 742
Cdd:PRK07786   184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPL-GAFDPGQLLDVLE 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  743 RQGVTVLQATPATWRMLCDSERV---DL-LRgctLLCGGEALAED-LAARMRGLSASTWNL--YGPTETTIWSARFrLGE 815
Cdd:PRK07786   263 AEKVTGIFLVPAQWQAVCAEQQArprDLaLR---VLSWGAAPASDtLLRQMAATFPEAQILaaFGQTEMSPVTCML-LGE 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 EA---RPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARYR 892
Cdd:PRK07786   339 DAirkLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--WFHSGDLVRQD 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  893 ADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEaalvDAESARQQELRSAL 971
Cdd:PRK07786   411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRN----DDAALTLEDLAEFL 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  972 KNSllavLPDYMVPAHMLLLENLPLTPNGKIN----RKALPLPDASAVRDAHVAPEG 1024
Cdd:PRK07786   487 TDR----LARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGFTE 539
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
491-1007 7.00e-28

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 121.40  E-value: 7.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  491 ERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERG 570
Cdd:PRK06155     2 EPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  571 VPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARlpqsdgLQSLLLDDLER----LVHGYPAEN 646
Cdd:PRK06155    82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAA------LEAADPGDLPLpavwLLDAPASVS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  647 PD-------LPEAPDSLCYA----------IYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLsvTTFS-FDI 708
Cdd:PRK06155   156 VPagwstapLPPLDAPAPAAavqpgdtaaiLYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLY--TTLPlFHT 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  709 FGLELYVP-LARGASMLLASREQAQdpeALLDLVERQGVTV----------LQATPATwrmlcDSERVDLLRGCTLLCGG 777
Cdd:PRK06155   234 NALNAFFQaLLAGATYVLEPRFSAS---GFWPAVRRHGATVtyllgamvsiLLSQPAR-----ESDRAHRVRVALGPGVP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  778 EALAEDLAAR--MRGLSAstwnlYGPTETTI------------WSARFRLGEEARpflggplentalyILDSEMNPCPPG 843
Cdd:PRK06155   306 AALHAAFRERfgVDLLDG-----YGSTETNFviavthgsqrpgSMGRLAPGFEAR-------------VVDEHDQELPDG 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  844 VAGELLIGGD---GLARGYHRRPGLTAErflpdpfaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 920
Cdd:PRK06155   368 EPGELLLRADepfAFATGYFGMPEKTVE--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVE 439
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  921 TRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEA-ALVDAESARQQELRsalknsllavLPDYMVPAHMLLLENLPLTP 998
Cdd:PRK06155   440 QVLLSHPAVAAAAVFPVPSeLGEDEVMAAVVLRDGtALEPVALVRHCEPR----------LAYFAVPRYVEFVAALPKTE 509

                   ....*....
gi 2183974163  999 NGKINRKAL 1007
Cdd:PRK06155   510 NGKVQKFVL 518
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1561-2068 1.23e-27

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 120.68  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1561 PQDFTPAsclHRLIERQAAERPRATAVVY-----GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGL 1635
Cdd:cd05970     13 PENFNFA---YDVVDAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1636 LAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLL-------LTQR--AARERLP-------LGEGLPCLLLDAEHEWAGY 1699
Cdd:cd05970     90 LALHKLGAIAIPATHQLTAKDIVYRIESADIKMIvaiaednIPEEieKAAPECPskpklvwVGDPVPEGWIDFRKLIKNA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1700 PES-----DPQSAVGvDNLAYVIYTSGSTGKPKGT----LLPHGNVL------RLFDATRHWFgfSADDAWSLfhsyafd 1764
Cdd:cd05970    170 SPDferptANSYPCG-EDILLVYFSSGTTGMPKMVehdfTYPLGHIVtakywqNVREGGLHLT--VADTGWGK------- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1765 fSVW-EIFGALLHGGRLVIVPYETSrSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPplALRHVVFGGEALEV 1843
Cdd:cd05970    240 -AVWgKIYGQWIAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS--SLRYCTTAGEALNP 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1844 QALRPWFERFGdraPRLVNMYGITETTvhvtyrpLSLADLDGGAASP--IGEPIPDLSWYLLDAGLNPVPRGCIGELYVG 1921
Cdd:cd05970    316 EVFNTFKEKTG---IKLMEGFGQTETT-------LTIATFPWMEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIR 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1922 GA-----GLARGYLNRPELSCtrfvadpfSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQ 1996
Cdd:cd05970    386 TSkgkpvGLFGGYYKDAEKTA--------EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQH 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 1997 PGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPA-ALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd05970    458 PAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSeELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1578-2071 2.47e-27

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 119.77  E-value: 2.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVV-----YGE-RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:PRK13295    34 VASCPDKTAVTavrlgTGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLTQRAAR--ERLPLGEGLPCLLLDAEH-------------------EWAGYPESDP---QSA 1707
Cdd:PRK13295   114 FRERELSFMLKHAESKVLVVPKTFRgfDHAAMARRLRPELPALRHvvvvggdgadsfeallitpAWEQEPDAPAilaRLR 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1708 VGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFdfsvweIFGALLH---GGRL 1780
Cdd:PRK13295   194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDvilmASPMAHQTGF------MYGLMMPvmlGATA 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1781 VivpYETSRSPEDFLRLLCRERVT--------------VLNQTPSAFKQLMQVACAGQEVPPlalrhvvfggeALEVQAL 1846
Cdd:PRK13295   268 V---LQDIWDPARAAELIRTEGVTftmastpfltdltrAVKESGRPVSSLRTFLCAGAPIPG-----------ALVERAR 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1847 rpwfERFGdraPRLVNMYGITETTVHVTYRPlslADLDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLA 1926
Cdd:PRK13295   334 ----AALG---AKIVSAWGMTENGAVTLTKL---DDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNF 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1927 RGYLNRPELscTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRiDHQVKIRGFR-IELGEIEARLLAQPGVAEAVVL 2005
Cdd:PRK13295   404 GGYLKRPQL--NGTDADGW-------FDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIV 473
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 2006 --PHEGPGaTQLVGYVVTQAAPS-DPAALRDTLRQalkASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK13295   474 ayPDERLG-ERACAFVVPRPGQSlDFEEMVEFLKA---QKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3099-3183 3.72e-27

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 118.16  E-value: 3.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd12116     81 EDAEP 85
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
470-985 4.49e-27

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 119.59  E-value: 4.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  470 LEAVVAEPRRRLGDLPLLDaeeRATLLQRSRLPASEYpagqGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLA 549
Cdd:PRK08279     4 LMDLAARLPRRLPDLPGIL---RGLKRTALITPDSKR----SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  550 WRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL----------------LS 613
Cdd:PRK08279    77 HWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLivgeelveafeearadLA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 QQSVLARLPQSDGLQSLLLDDLERLVHGYPAENPDLPEA--PDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPG 691
Cdd:PRK08279   157 RPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  692 MLARDRLLSVttfsfdifgLELY----------VPLARGASMLLASREQAQdpeALLDLVERQGVTVLQATPATWRMLCD 761
Cdd:PRK08279   237 LTPDDVLYCC---------LPLYhntggtvawsSVLAAGATLALRRKFSAS---RFWDDVRRYRATAFQYIGELCRYLLN 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  762 SERVDLLRG--CTLLCGGealaedlaarmrGLSASTWN-------------LYGPTETTIW---------SARFRLGEEA 817
Cdd:PRK08279   305 QPPKPTDRDhrLRLMIGN------------GLRPDIWDefqqrfgiprileFYAASEGNVGfinvfnfdgTVGRVPLWLA 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  818 RPF--------LGGPLENTalyilDSEMNPCPPGVAGELL--IGGDGLARGYhRRPGLTAERFLPDPFaADGSRLYRTGD 887
Cdd:PRK08279   373 HPYaivkydvdTGEPVRDA-----DGRCIKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVF-KKGDAWFNTGD 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVV--VAQPGVAGPTLVAYLVPTEAALVDaesarqq 965
Cdd:PRK08279   446 LMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADGAEFD------- 518
                          570       580
                   ....*....|....*....|
gi 2183974163  966 elRSALKNSLLAVLPDYMVP 985
Cdd:PRK08279   519 --LAALAAHLYERLPAYAVP 536
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
532-937 5.04e-27

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 117.85  E-value: 5.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  532 GEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL 611
Cdd:cd17640      2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  612 LsqqsvlarlpqsdglqslllddlerlvhgypAENpdlpeAPDSLCYAIYTSGSTGQPKGVMVRHRALT----NFVCSIA 687
Cdd:cd17640     82 V-------------------------------VEN-----DSDDLATIIYTSGTTGNPKGVMLTHANLLhqirSLSDIVP 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  688 RQPGmlarDRLLSVTTfSFDIF--GLElYVPLARGASMLLASreqaqdPEALLDLVERQGVTVLQATPATWRMLcdSERV 765
Cdd:cd17640    126 PQPG----DRFLSILP-IWHSYerSAE-YFIFACGCSQAYTS------IRTLKDDLKRVKPHYIVSVPRLWESL--YSGI 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  766 D----------------LLRGCTL---LCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSARFRLGEEARPFLGGPLE 826
Cdd:cd17640    192 QkqvsksspikqflflfFLSGGIFkfgISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLP 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRI-D 904
Cdd:cd17640    272 GTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAkD 344
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163  905 HQVKIRGFRIELGEIETRLLEQDSVREAVVVAQ 937
Cdd:cd17640    345 TIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ 377
PRK07529 PRK07529
AMP-binding domain protein; Validated
487-1032 5.60e-27

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 119.67  E-value: 5.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  487 LDAEERATLLQRsRLPASEYpagqgvhRLFEAQAGLTPDAPAL---LFGE-----ERLSYAELNALANRLAWRLREEGVG 558
Cdd:PRK07529    10 IEAIEAVPLAAR-DLPASTY-------ELLSRAAARHPDAPALsflLDADpldrpETWTYAELLADVTRTANLLHSLGVG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  559 SDVLVGIALERGVPMVVALLAVLKAGGAyVPLDPQYPADRLQYMIDDSGLRLLL------------SQQSVLARLPqsdG 626
Cdd:PRK07529    82 PGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqKVAEVLAALP---E 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  627 LQSLLLDDLERL-------------------VHGYPAE----------NPDLPEAPDSLCYaIYTSGSTGQPKGVMVRHR 677
Cdd:PRK07529   158 LRTVVEVDLARYlpgpkrlavplirrkaharILDFDAElarqpgdrlfSGRPIGPDDVAAY-FHTGGTTGMPKLAQHTHG 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  678 ALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGL--ELYVPLARGASMLLASREQAQDPEA---LLDLVERQGVTVLQAT 752
Cdd:PRK07529   237 NEVANAWLGALLLGLGPGDTVFCGLPL-FHVNALlvTGLAPLARGAHVVLATPQGYRGPGVianFWKIVERYRINFLSGV 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  753 PATWRML----CDSERVDLLRgcTLLCGGEALAEDLAAR-MRGLSASTWNLYGPTETTIWSAR-FRLGEEARPFLGGPLE 826
Cdd:PRK07529   316 PTVYAALlqvpVDGHDISSLR--YALCGAAPLPVEVFRRfEAATGVRIVEGYGLTEATCVSSVnPPDGERRIGSVGLRLP 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYILDSEMN-----PCPPGVAGELLIGGDGLARGYhrrpgLTAERflpDPFAADGSRLYRTGDLARYRADGVIEYLG 901
Cdd:PRK07529   394 YQRVRVVILDDAgrylrDCAVDEVGVLCIAGPNVFSGY-----LEAAH---NKGLWLEDGWLNTGDLGRIDADGYFWLTG 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  902 RidhqVK---IR-GFRIELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAY--LVP----TEAALVDAESARQQElRSA 970
Cdd:PRK07529   466 R----AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGELPVAYvqLKPgasaTEAELLAFARDHIAE-RAA 540
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  971 lknsllavlpdymVPAHMLLLENLPLTPNGKIN-------------RKAL-----PLPDASAVRD------AHVAPEGEL 1026
Cdd:PRK07529   541 -------------VPKHVRILDALPKTAVGKIFkpalrrdairrvlRAALrdagvEAEVVDVVEDgrrglvAQVALRGAE 607

                   ....*.
gi 2183974163 1027 ERAMAA 1032
Cdd:PRK07529   608 DREAVA 613
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1574-2086 5.85e-27

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 119.34  E-value: 5.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAE-RPRATAVVY------GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYV 1646
Cdd:cd05967     56 LDRHVEAgRGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHS 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1647 PLDPRYPSDRLGYMIEDSGIRLLLTQRAA-------------------------------RERLPLGEGLPCLLLDAEHE 1695
Cdd:cd05967    136 VVFGGFAAKELASRIDDAKPKLIVTASCGiepgkvvpykplldkalelsghkphhvlvlnRPQVPADLTKPGRDLDWSEL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1696 WAGYPESDPQSAVGVDNLaYVIYTSGSTGKPKGTLLPH-GNVLRLFDATRHWFG-------FSADD-AWSLFHSYAfdfs 1766
Cdd:cd05967    216 LAKAEPVDCVPVAATDPL-YILYTSGTTGKPKGVVRDNgGHAVALNWSMRNIYGikpgdvwWAASDvGWVVGHSYI---- 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1767 vweIFGALLHG-------GRLVIVPyetsrSPEDFLRLLCRERVTVLNQTPSAFKQLMQV---ACAGQEVPPLALRHVVF 1836
Cdd:cd05967    291 ---VYGPLLHGattvlyeGKPVGTP-----DPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdGKYIKKYDLSSLRTLFL 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1837 GGEALEVQALRpWFERFGDRAprLVNMYGITETTVHVTYRPLSLADLDGGAASPiGEPIPDLSWYLLDAGLNPVPRGCIG 1916
Cdd:cd05967    363 AGERLDPPTLE-WAENTLGVP--VIDHWWQTETGWPITANPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELG 438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1917 ELYVGGA---GLARGYLNRPElsctRFVADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARL 1993
Cdd:cd05967    439 NIVIKLPlppGCLLTLWKNDE----RFKKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1994 LAQPGVAEAVVL--PHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05967    514 LSHPAVAECAVVgvRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
                          570
                   ....*....|....*.
gi 2183974163 2072 PA-PDasrlQRDYTAP 2086
Cdd:cd05967    594 RKiAD----GEDYTIP 605
PRK05857 PRK05857
fatty acid--CoA ligase;
1566-2073 5.92e-27

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 118.57  E-value: 5.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1566 PASCLHRLIErQAAERPRATAVVY--GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGG 1643
Cdd:PRK05857    13 PSTVLDRVFE-QARQQPEAIALRRcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1644 AYVPLDPRYPS---DRLGYMIEDSGIRLLLTQRAARERLPLG-EGLPCLLLDAEHEWA--------GYPESDPQSavGVD 1711
Cdd:PRK05857    92 IAVMADGNLPIaaiERFCQITDPAAALVAPGSKMASSAVPEAlHSIPVIAVDIAAVTResehsldaASLAGNADQ--GSE 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1712 NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRH----WFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGrLVIVPYET 1787
Cdd:PRK05857   170 DPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKeglnWVTWVVGETTYSPLPATHIGGLWWILTCLMHGG-LCVTGGEN 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1788 SRSpedFLRLLCRERVTVLNQTPSAFKQLM-QVACAGQEVPPlaLRHVVFGGEALEVQALRpWFERFGDRAPRLvnmYGI 1866
Cdd:PRK05857   249 TTS---LLEILTTNAVATTCLVPTLLSKLVsELKSANATVPS--LRLVGYGGSRAIAADVR-FIEATGVRTAQV---YGL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1867 TETTVHVTYRPL---SLADLDGGAaspIGEPIPDLSWYLLDA-GLNPV-----PRGCIGELYVGGAGLARGYLNRPELSc 1937
Cdd:PRK05857   320 SETGCTALCLPTddgSIVKIEAGA---VGRPYPGVDVYLAATdGIGPTapgagPSASFGTLWIKSPANMLGYWNNPERT- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1938 TRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGAtqL 2015
Cdd:PRK05857   396 AEVLIDGW-------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACyeIPDEEFGA--L 466
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2016 VGYVVTQAAPSDPAALRDtLRQALKASL---PEHMV-PAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:PRK05857   467 VGLAVVASAELDESAARA-LKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRASLAA 527
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
512-1017 6.17e-27

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 119.52  E-value: 6.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEER-----LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGA 586
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  587 YVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARlpqsdGLQSLLLDDLERLVHGYP----------AENPDLPEAPDSL 656
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTRR-----GREVNLKEEADKACAQCPtvekvvvvrhLGNDFTPAKGRDL 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  657 CYA---------------------IYTSGSTGQPKGVMVRHRAL-TNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELY 714
Cdd:cd05968    218 SYDeeketagdgaertesedplmiIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIF 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  715 VPLARGASMLLasREQAQD---PEALLDLVERQGVTVLQATPATWRmlcdservdllrgcTLLCGGEAL--AEDLAA-RM 788
Cdd:cd05968    298 GGLILGATMVL--YDGAPDhpkADRLWRMVEDHEITHLGLSPTLIR--------------ALKPRGDAPvnAHDLSSlRV 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  789 RGLSASTWNLygptETTIWSARFRLGEEA---------------------RPF----LGGPLENTALYILDSEMNPCPPG 843
Cdd:cd05968    362 LGSTGEPWNP----EPWNWLFETVGKGRNpiinysggteisggilgnvliKPIkpssFNGPVPGMKADVLDESGKPARPE 437
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  844 VaGELLIGGD--GLARGYHRRPgltaERFLPDPFaadgSRL---YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 918
Cdd:cd05968    438 V-GELVLLAPwpGMTRGFWRDE----DRYLETYW----SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAE 508
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  919 IETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAalVDAESARQQELRSALKNSLLAVLpdymVPAHMLLLENLPLT 997
Cdd:cd05968    509 IESVLNAHPAVLESAAIGVPHpVKGEAIVCFVVLKPG--VTPTEALAEELMERVADELGKPL----SPERILFVKDLPKT 582
                          570       580
                   ....*....|....*....|....*..
gi 2183974163  998 PNGKINRKAL-------PLPDASAVRD 1017
Cdd:cd05968    583 RNAKVMRRVIraaylgkELGDLSSLEN 609
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1698-2071 6.85e-27

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 118.83  E-value: 6.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1698 GYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSAD---------DAWSLFHSYAFDFS-- 1766
Cdd:PRK08751   195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcevviTALPLYHIFALTANgl 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1767 VWEIFGALLHggrLVIVPyetsRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQeVPPLALRHVVFGGEALEVQAL 1846
Cdd:PRK08751   275 VFMKIGGCNH---LISNP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ-IDFSSLKMTLGGGMAVQRSVA 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1847 RPWFERFGdraPRLVNMYGITETTVHVTYRPLSLADLDGGaaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLA 1926
Cdd:PRK08751   347 ERWKQVTG---LTLVEAYGLTETSPAACINPLTLKEYNGS----IGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVM 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1927 RGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE--AVV 2004
Cdd:PRK08751   420 KGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvaAVG 492
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2005 LPHEGPGatQLVGYVVTQaapSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08751   493 VPDEKSG--EIVKVVIVK---KDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2204-2431 7.31e-27

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 116.69  E-value: 7.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2204 ALDGTLLETALQALLAHHDALRLGFRLEDGTWR---AEHRAVEAGEVLL--WQQSVADGQALEALAEQVQRSLDLGSGPL 2278
Cdd:cd19531     35 PLDVAALERALNELVARHEALRTTFVEVDGEPVqviLPPLPLPLPVVDLsgLPEAEREAEAQRLAREEARRPFDLARGPL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2279 LRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGY 2358
Cdd:cd19531    115 LRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAY 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2359 WLAQLEGVST--ELPCD-------DREGAqsvrhvrSARTELTEEATRRLLQEApAAYRTQVNDLLLTALARVIGRWTGQ 2429
Cdd:cd19531    195 WREQLAGAPPvlELPTDrprpavqSFRGA-------RVRFTLPAELTAALRALA-RREGATLFMTLLAAFQVLLHRYSGQ 266

                   ..
gi 2183974163 2430 AD 2431
Cdd:cd19531    267 DD 268
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
535-1007 1.04e-26

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 120.41  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEgVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQ 614
Cdd:PRK08633   641 ELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITS 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  615 QSVLARLPQSDGLQSLLLDD----LERLVHG---------------YPA---ENPDLPE-APDSLCYAIYTSGSTGQPKG 671
Cdd:PRK08633   720 RKFLEKLKNKGFDLELPENVkviyLEDLKAKiskvdkltallaarlLPArllKRLYGPTfKPDDTATIIFSSGSEGEPKG 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGL--ELYVPLARGASMllASREQAQDPEALLDLVERQGVTVL 749
Cdd:PRK08633   800 VMLSHHNILSNIEQISDVFNLRNDDVILSSLPF-FHSFGLtvTLWLPLLEGIKV--VYHPDPTDALGIAKLVAKHRATIL 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 QATPATWRMLCDSERVDLLRGCTL---LCGGEALAEDLAA--RMR-------GlsastwnlYGPTETT------------ 805
Cdd:PRK08633   877 LGTPTFLRLYLRNKKLHPLMFASLrlvVAGAEKLKPEVADafEEKfgirileG--------YGATETSpvasvnlpdvla 948
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 --IWSARF-RLGEearpfLGGPLENTALYILDSE-MNPCPPGVAGELLIGGDGLARGYHRRPGLTAErFLPDpfaADGSR 881
Cdd:PRK08633   949 adFKRQTGsKEGS-----VGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIG 1019
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  882 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRL---LEQDSVREAVVVaqpgvagptlvaylVPTE----- 953
Cdd:PRK08633  1020 WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakaLGGEEVVFAVTA--------------VPDEkkgek 1085
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  954 -AALVDAESARQQELRSALKNSllaVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK08633  1086 lVVLHTCGAEDVEELKRAIKES---GLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
524-1002 1.21e-26

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 117.01  E-value: 1.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGiALERGVP-MVVALLAVLKAGGAYVPLDPQYPADRLQYM 602
Cdd:cd12118     18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVA-VLAPNTPaMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 IDDSGLRLLLSQQSvlarlpqsdglqsLLLDDLerLVHGypaeNPD-LPEAPDSLCYAI---YTSGSTGQPKGVMVRHR- 677
Cdd:cd12118     97 LRHSEAKVLFVDRE-------------FEYEDL--LAEG----DPDfEWIPPADEWDPIalnYTSGTTGRPKGVVYHHRg 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  678 ALTNFVCSIARQpGMlardRLLSVTTFSFDIF-----GLELYVPLARGASMLLasREQaqDPEALLDLVERQGVTVLQAT 752
Cdd:cd12118    158 AYLNALANILEW-EM----KQHPVYLWTLPMFhcngwCFPWTVAAVGGTNVCL--RKV--DAKAIYDLIEKHKVTHFCGA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  753 PATWRMLCD---SERVDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTETT------IWSA---------RFRLg 814
Cdd:cd12118    229 PTVLNMLANappSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKPewdelpteeRARL- 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  815 eEARPFLGGPLEnTALYILDSE-MNPCP-PGV-AGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLARY 891
Cdd:cd12118    308 -KARQGVRYVGL-EEVDVLDPEtMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG--WFHSGDLAVI 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLvpteaALVDAESARQQELRSA 970
Cdd:cd12118    378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEVPCAFV-----ELKEGAKVTEEEIIAF 452
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2183974163  971 LKNSllavLPDYMVPAHMLLLEnLPLTPNGKI 1002
Cdd:cd12118    453 CREH----LAGFMVPKTVVFGE-LPKTSTGKI 479
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
532-1007 1.21e-26

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 117.77  E-value: 1.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  532 GEERLSYAELNALANRLAWRLREEGV--GSDVLVGIALERGVpmVVALLAVLKAGGAYVPLDP----QYPADRLQYM--- 602
Cdd:cd05906     36 SEEFQSYQDLLEDARRLAAGLRQLGLrpGDSVILQFDDNEDF--IPAFWACVLAGFVPAPLTVpptyDEPNARLRKLrhi 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  603 ---------IDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERLVHGYPAEnpdlpeaPDSLCYAIYTSGSTGQPKGVM 673
Cdd:cd05906    114 wqllgspvvLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSR-------PDDLALLMLTSGSTGFPKAVP 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  674 VRHRALTNFVCSIARQPGMLARDRLLSvtTFSFDIFG--LELYV-PLARGASML-LASREQAQDPEALLDLVERQGVTVl 749
Cdd:cd05906    187 LTHRNILARSAGKIQHNGLTPQDVFLN--WVPLDHVGglVELHLrAVYLGCQQVhVPTEEILADPLRWLDLIDRYRVTI- 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  750 qatpaTW------RMLCDSERV------DLLRGCTLLCGGEAL----AEDLAARMR--GLSAS----TWnlyGPTET--- 804
Cdd:cd05906    264 -----TWapnfafALLNDLLEEiedgtwDLSSLRYLVNAGEAVvaktIRRLLRLLEpyGLPPDairpAF---GMTETcsg 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  805 TIWSARFRLGE--EARPF--LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgs 880
Cdd:cd05906    336 VIYSRSFPTYDhsQALEFvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW----- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 rlYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVRE----AVVVAQPGVAGPTLVAYLVPtEAAL 956
Cdd:cd05906    411 --FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVP-EYDL 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  957 VDAESARQQELRSALKNSlLAVLPDYMVPahmLLLENLPLTPNGKINRKAL 1007
Cdd:cd05906    487 QDALSETLRAIRSVVSRE-VGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
510-1007 1.28e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 117.83  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  510 QGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVP 589
Cdd:PRK06710    24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  590 LDPQYPADRLQYMIDDSGLRLLLSQQSVLAR---------------------LPQSDGL--------QSLLLDDLER--L 638
Cdd:PRK06710   104 TNPLYTERELEYQLHDSGAKVILCLDLVFPRvtnvqsatkiehvivtriadfLPFPKNLlypfvqkkQSNLVVKVSEseT 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  639 VHGYPAENPDLPEAPDSLC-------YAIYTSGSTGQPKGVMVRHRAL-TNFVCSIARQPGML-ARDRLLSVTTFsFDIF 709
Cdd:PRK06710   184 IHLWNSVEKEVNTGVEVPCdpendlaLLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKeGEEVVLGVLPF-FHVY 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  710 GLELYVPLA--RGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDSE-----RVDLLRGCtlLCGGEALAE 782
Cdd:PRK06710   263 GMTAVMNLSimQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPllkeyDISSIRAC--ISGSAPLPV 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  783 DLAARMRGLSASTW-NLYGPTETTIWSARFRLGEEARP-FLGGPLENTALYILDSEMNPC-PPGVAGELLIGGDGLARGY 859
Cdd:PRK06710   338 EVQEKFETVTGGKLvEGYGLTESSPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQIMKGY 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  860 HRRPGLTAERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG 939
Cdd:PRK06710   418 WNKPEETAAVL------QDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163  940 -VAGPTLVAYLVpteaaLVDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK06710   490 pYRGETVKAFVV-----LKEGTECSEEELNQFARKYLAA----YKVPKVYEFRDELPKTTVGKILRRVL 549
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
82-371 1.29e-26

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 115.66  E-value: 1.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   82 LDVEALSASLGAIVERHQSLRTVFvedeqLDGFRQQVLASVDVP-VPV---TLAGDDDAQAQIRAFVESETQQPFDLRNG 157
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVF-----LDDGTQQILPEVPWYgITVhdlRGLSEEEAEAALEELRERLSHRVLDVERG 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  158 PLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARrqgiEATLPDLPIQYADYAIWQRHwLEAGERERQL 237
Cdd:cd19535    112 PLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDP----GEPLPPLELSFRDYLLAEQA-LRETAYERAR 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  238 EYWMARLgggqsvLELPTdrqRPALP---------SYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRY 308
Cdd:cd19535    187 AYWQERL------PTLPP---APQLPlakdpeeikEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  309 SGQDEIRVGVPVANRNRV--ETERLIGFFVNTQVLRADLDAQMPFLDllqqtRVAALGAQSHQDL 371
Cdd:cd19535    258 SGQPRFLLNLTLFNRLPLhpDVNDVVGDFTSLLLLEVDGSEGQSFLE-----RARRLQQQLWEDL 317
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
536-1007 1.67e-26

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 115.74  E-value: 1.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQymiddsglrlllsqq 615
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLR--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 svlarlpqsdglqslllDDLERLVHGYPAENpDLPEAPDSLCYaIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05974     66 -----------------DRVDRGGAVYAAVD-ENTHADDPMLL-YFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPG 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLSVTTFSFDIFGLE-LYVPLARGASMLLASrEQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLL 774
Cdd:cd05974    127 DVHWNISSPGWAKHAWScFFAPWNAGATVFLFN-YARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREV 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  775 CG-GEALAEDLAARMRGLsastWNL-----YGPTETTIWSARfRLGEEARP-FLGGPLENTALYILDSEMNPCPPGVAGe 847
Cdd:cd05974    206 VGaGEPLNPEVIEQVRRA----WGLtirdgYGQTETTALVGN-SPGQPVKAgSMGRPLPGYRVALLDPDGAPATEGEVA- 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  848 LLIGGD---GLARGYHRRPGLTAErflpdpfaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLL 924
Cdd:cd05974    280 LDLGDTrpvGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLI 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  925 EQDSVREAVVVAQPgvaGPTLVAylVPTEAALVDAESARQQELRSALKNSLLAVLPDYMVPAHMLLLEnLPLTPNGKINR 1004
Cdd:cd05974    352 EHPAVAEAAVVPSP---DPVRLS--VPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRR 425

                   ...
gi 2183974163 1005 KAL 1007
Cdd:cd05974    426 VEL 428
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
524-1007 1.75e-26

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 117.01  E-value: 1.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGgaYVPLDPQYPADRLQY-- 601
Cdd:PRK10946    37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSELna 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  602 ---------MIDDSGLRLLLSQQSVLARLPQSDGLQSLLLD------DLERLVHGYPAENPDLPEAPDSLCYAIYTSGST 666
Cdd:PRK10946   115 yasqiepalLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLnddgehSLDDAINHPAEDFTATPSPADEVAFFQLSGGST 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  667 GQPKGVMVRH-------RAlTNFVCSIARQPGML-----ARDRLLSvttfSFDIFGlelyVPLARGASMLlasreqAQDP 734
Cdd:PRK10946   195 GTPKLIPRTHndyyysvRR-SVEICGFTPQTRYLcalpaAHNYPMS----SPGALG----VFLAGGTVVL------APDP 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  735 EALL--DLVERQGVTVLQATP---ATW-RMLCDSERVDLLRGCTLL-CGGEALAEDLAARMRG-LSASTWNLYGPTETTI 806
Cdd:PRK10946   260 SATLcfPLIEKHQVNVTALVPpavSLWlQAIAEGGSRAQLASLKLLqVGGARLSETLARRIPAeLGCQLQQVFGMAEGLV 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 WSARFRLGEEaRPFL--GGPL-ENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlY 883
Cdd:PRK10946   340 NYTRLDDSDE-RIFTtqGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------Y 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  884 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAalvdaesA 962
Cdd:PRK10946   412 CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdELMGEKSCAFLVVKEP-------L 484
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2183974163  963 RQQELRSALKNSLLAvlpDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK10946   485 KAVQLRRFLREQGIA---EFKLPDRVECVDSLPLTAVGKVDKKQL 526
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2174-2600 2.29e-26

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 119.58  E-value: 2.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQMFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEVLLWQQS 2253
Cdd:COG1020     21 SAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2254 V-----ADGQALEALAEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVA 2328
Cdd:COG1020    101 VdlealAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLP 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2329 LPAKTSAFKAWAERLQAHARDGGLEGERGYWLAQLEG--VSTELPCDDREGAQSVRHVRSARTELTEEATRRLLQEApAA 2406
Cdd:COG1020    181 LPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGlpPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RR 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2407 YRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGReelfEDIDLTRTVGWFTSLFPLRL-----SPVAELGASIKRikEQ 2481
Cdd:COG1020    260 HGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVdlsgdPSFAELLARVRE--TL 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2482 LRAIPHKGLGFGALRylgsaeDRAALAALPSPRITFNYLGQFDgSFSADSSALfrPSADAAGSERDSDAPlDNWLSLNGQ 2561
Cdd:COG1020    334 LAAYAHQDLPFERLV------EELQPERDLSRNPLFQVMFVLQ-NAPADELEL--PGLTLEPLELDSGTA-KFDLTLTVV 403
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2183974163 2562 VYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEH 2600
Cdd:COG1020    404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1574-2055 3.97e-26

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 116.90  E-value: 3.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP 1653
Cdd:PRK08279    43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1654 SDRLGYMIEDSGIRLLLTQRAARERL-----------------PLGEGLPCLLLDAEHEWAGYPESDPQSAVGV--DNLA 1714
Cdd:PRK08279   123 GAVLAHSLNLVDAKHLIVGEELVEAFeearadlarpprlwvagGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVtaKDTA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 YVIYTSGSTGKPKGTLLPHGNVLRlfdaTRHWFGFSAD--------DAWSLFHSYAFdFSVWEifGALLHGGRLVIVP-Y 1785
Cdd:PRK08279   203 FYIYTSGTTGLPKAAVMSHMRWLK----AMGGFGGLLRltpddvlyCCLPLYHNTGG-TVAWS--SVLAAGATLALRRkF 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1786 ETSRspedFLRLLCRERVTV-----------LNQTPSafkqlmqvacagqevpPLALRH---VVFGgealevQALRP--- 1848
Cdd:PRK08279   276 SASR----FWDDVRRYRATAfqyigelcrylLNQPPK----------------PTDRDHrlrLMIG------NGLRPdiw 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1849 --WFERFGdrAPRLVNMYGITETTVhvtyrplSLADLDG--GA--------ASPI---------GEPIPDlswyllDAG- 1906
Cdd:PRK08279   330 deFQQRFG--IPRILEFYAASEGNV-------GFINVFNfdGTvgrvplwlAHPYaivkydvdtGEPVRD------ADGr 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGCIGELY--VGGAGLARGYlNRPELSCTRFVADPFsTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRI 1984
Cdd:PRK08279   395 CIKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENV 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 1985 ELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGY---VVTQAAPSDPAALRDTLRQAlkasLPEHMVPahlLFL 2055
Cdd:PRK08279   473 ATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMaaiVLADGAEFDLAALAAHLYER----LPAYAVP---LFV 539
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1575-2071 8.11e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 114.79  E-value: 8.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1575 ERQAAERPRATAVVYGE--RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PRK13391     4 GIHAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQRAARE-------RLPlgEGLPCLLLDAEHE---WAGYPESD--------PQSAVGVDNLa 1714
Cdd:PRK13391    84 TPAEAAYIVDDSGARALITSAAKLDvarallkQCP--GVRHRLVLDGDGElegFVGYAEAVaglpatpiADESLGTDML- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 yviYTSGSTGKPKGTL--LPHGNV---LRLFDATRHWFGFSADDAW----SLFHSYAFDFSvweifGALLHGGRLVIVpY 1785
Cdd:PRK13391   161 ---YSSGTTGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDMVYlspaPLYHSAPQRAV-----MLVIRLGGTVIV-M 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1786 ETSrSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPLA-LRHVVFGGEALEVQALRPWFERFGdraPRLVNMY 1864
Cdd:PRK13391   232 EHF-DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSsLEVAIHAAAPCPPQVKEQMIDWWG---PIIHEYY 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1865 GITETTVHVTYRPLSLADLDGGAASPI-GEPipdlswYLLDAGLNPVPRGCIGELYVGGaGLARGYLNRPELSCTRFVAD 1943
Cdd:PRK13391   308 AATEGLGFTACDSEEWLAHPGTVGRAMfGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPD 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1944 PFSTTggrlyrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGatQLVGYVVT 2021
Cdd:PRK13391   381 GTWST------VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfgVPNEDLG--EEVKAVVQ 452
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 2022 QAAPSDP-AALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK13391   453 PVDGVDPgPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1559-2071 9.73e-26

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 114.93  E-value: 9.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1559 PGP----QDFTPASCLHRLIERQAaERPRATAVV--YGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMI 1632
Cdd:cd17642      5 PGPfyplEDGTAGEQLHKAMKRYA-SVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1633 VGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARER-------LPLGEGLpcLLLDAEHEWAGYPESD-- 1703
Cdd:cd17642     84 LPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKvlnvqkkLKIIKTI--IILDSKEDYKGYQCLYtf 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1704 ---------------PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRH-WFGFSADDAWSLFHSYAF--DF 1765
Cdd:cd17642    162 itqnlppgfneydfkPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAILTVIPFhhGF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1766 SVWEIFGALLHGGRLVIVP-YETsrspEDFLRLLCRERVTVLNQTPSAF--------------KQLMQVACAGQevpPLA 1830
Cdd:cd17642    242 GMFTTLGYLICGFRVVLMYkFEE----ELFLRSLQDYKVQSALLVPTLFaffakstlvdkydlSNLHEIASGGA---PLS 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 lRHVvfgGEALEvqalrpwfERFGdrAPRLVNMYGITETTVHVTYRPLSlaDLDGGAaspIGEPIPDLSWYL--LDAG-- 1906
Cdd:cd17642    315 -KEV---GEAVA--------KRFK--LPGIRQGYGLTETTSAILITPEG--DDKPGA---VGKVVPFFYAKVvdLDTGkt 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LNPVPRGcigELYVGGAGLARGYLNRPELSCTRFVADpfsttgGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIEL 1986
Cdd:cd17642    376 LGPNERG---ELCVKGPMIMKGYVNNPEATKALIDKD------GWL-HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPP 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1987 GEIEARLLAQPGVAEAVV--LPHEG----PGA------------TQLVGYVVTQAAPSDpaalrdTLRQALKaslpehmv 2048
Cdd:cd17642    446 AELESILLQHPKIFDAGVagIPDEDagelPAAvvvleagktmteKEVMDYVASQVSTAK------RLRGGVK-------- 511
                          570       580
                   ....*....|....*....|...
gi 2183974163 2049 pahllFLERLPLTANGKLDRRAL 2071
Cdd:cd17642    512 -----FVDEVPKGLTGKIDRRKI 529
PRK07788 PRK07788
acyl-CoA synthetase; Validated
514-1008 2.75e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 113.48  E-value: 2.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQ 593
Cdd:PRK07788    53 GLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  594 YPADRLQYMIDDSGLRLLLSQQSVLARL----------------PQSDGLQSLLLDDLERLVHGYPAENPDLPEAPDSLc 657
Cdd:PRK07788   133 FSGPQLAEVAAREGVKALVYDDEFTDLLsalppdlgrlrawggnPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI- 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  658 yAIYTSGSTGQPKGVMVRH-RALTNFVCSIARQPgmLARDRLLSVTTFSFDIFGL-ELYVPLARGASMLLASReqaQDPE 735
Cdd:PRK07788   212 -VILTSGTTGTPKGAPRPEpSPLAPLAGLLSRVP--FRAGETTLLPAPMFHATGWaHLTLAMALGSTVVLRRR---FDPE 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  736 ALLDLVERQGVTVLQATPATWRMLCD-----SERVDL--LRgcTLLCGGEALAEDLAAR-MRGLSASTWNLYGPTETTIW 807
Cdd:PRK07788   286 ATLEDIAKHKATALVVVPVMLSRILDlgpevLAKYDTssLK--IIFVSGSALSPELATRaLEAFGPVLYNLYGSTEVAFA 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  808 S-ARFRLGEEARPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYhrrpglTAERflpDPFAADGsrLYRTG 886
Cdd:PRK07788   364 TiATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDG--LLSSG 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  887 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPTEAALVDAEsa 962
Cdd:PRK07788   433 DVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI---GVDdeefGQRLRAFVVKAPGAALDED-- 507
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163  963 rqqELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGKINRKALP 1008
Cdd:PRK07788   508 ---AIKDYVRDN----LARYKVPRDVVFLDELPRNPTGKVLKRELR 546
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2204-2597 2.78e-25

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 111.70  E-value: 2.78e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2204 ALDGTLLETALQALLAHHDALRLGF-RLEDGTWRAEHRAVEAGEVLLWQQSVADG---QALEALAEQVQ-RSLDLGSGPL 2278
Cdd:cd19539     35 PLDVEALREALRDVVARHEALRTLLvRDDGGVPRQEILPPGPAPLEVRDLSDPDSdreRRLEELLREREsRGFDLDEEPP 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2279 LRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERLQAHARDGGLEGERGY 2358
Cdd:cd19539    115 IRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDF 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2359 WLAQLEGVS-TELPCDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAyRTQVNDLLLTALARVIGRWTGQADTLIQLE 2437
Cdd:cd19539    195 WRRRLRGAEpTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2438 GHGREElfedIDLTRTVGWFTSLFPLR--LSPVAELGASIKRI-KEQLRAIPHKGLGFGALrylgSAEDRAALAALPSPR 2514
Cdd:cd19539    274 VAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVrKALVDAQRHQELPFQQL----VAELPVDRDAGRHPL 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2515 --ITFNYLGQFDGSFSADSSALFRPsadaaGSERDSDAPLDnwLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRD 2592
Cdd:cd19539    346 vqIVFQVTNAPAGELELAGGLSYTE-----GSDIPDGAKFD--LNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQ 418

                   ....*
gi 2183974163 2593 ELLAL 2597
Cdd:cd19539    419 VLRQL 423
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1697-2071 3.76e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 113.32  E-value: 3.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1697 AGYP--ESDPQSavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDA-------WSLFHSYAFDFSV 1767
Cdd:PRK05677   195 AGQPvtEANPQA----DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGceiliapLPLYHIYAFTFHC 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1768 WEIfgaLLHGGRLVIVPyeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLmqvaCAGQEVPPL---ALRHVVFGGEALEVQ 1844
Cdd:PRK05677   271 MAM---MLIGNHNILIS--NPRDLPAMVKELGKWKFSGFVGLNTLFVAL----CNNEAFRKLdfsALKLTLSGGMALQLA 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1845 ALRPWFERFGdraPRLVNMYGITETTVHVTYRPLSLADLdggaaSPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAG 1924
Cdd:PRK05677   342 TAERWKEVTG---CAICEGYGMTETSPVVSVNPSQAIQV-----GTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQ 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1925 LARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE--A 2002
Cdd:PRK05677   414 VMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcaA 486
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 2003 VVLPHEGPGATQLVgYVVtqaAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK05677   487 IGVPDEKSGEAIKV-FVV---VKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2639-2980 4.12e-25

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 111.32  E-value: 4.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2639 PLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGALEkPLQLVRKRVEVPFSV 2717
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDGGV-PRQEILPPGPAPLEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2718 HDWRDRADLAEALDALAAGEA-GLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSR 2796
Cdd:cd19539     82 RDLSDPDSDRERRLEELLREReSRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2797 S------DGRYRDYIAWLQRQDAGRTEA----FWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQrLAEFA 2866
Cdd:cd19539    162 AaplpelRQQYKEYAAWQREALAAPRAAelldFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAA-LRELA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2867 REQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLA 2946
Cdd:cd19539    241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2183974163 2947 LREFEHTPLYDIQRWAGQVGEA----LFDNILVFENYP 2980
Cdd:cd19539    319 AQRHQELPFQQLVAELPVDRDAgrhpLVQIVFQVTNAP 356
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
512-1113 4.81e-25

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 114.42  E-value: 4.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  512 VHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLD 591
Cdd:COG3319      3 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  592 PQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKG 671
Cdd:COG3319     83 ALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  672 VMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDPEALLDLVERQGVTVLQA 751
Cdd:COG3319    163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDSERVDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLY------GPTETTIWSARFRLGEEARPFLGGPL 825
Cdd:COG3319    243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAaggtatTAAVTTTAAAAAPGVAGALGPIGGGP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  826 ENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDH 905
Cdd:COG3319    323 GLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLR 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  906 QVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAALVDAESARQQelrsalknsLLAVLPDYMVP 985
Cdd:COG3319    403 LQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLL---------LLLLLLPPPLP 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  986 AHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERAMAAIWSEVLKLGHIGRDDNFFELGGHSLLVTQVVSR 1065
Cdd:COG3319    474 PALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLL 553
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 1066 VRRRLDLQVPLRTLFEHSTLRAYAQAVAQLAPAAQGGIVRCARDASPQ 1113
Cdd:COG3319    554 LLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSG 601
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1711-2071 6.61e-25

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 114.64  E-value: 6.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSyaFDFSVwEIFGALLHGGRLVIVPye 1786
Cdd:PRK08633   782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDvilsSLPFFHS--FGLTV-TLWLPLLEGIKVVYHP-- 856
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 tsrSPEDFL---RLLCRERVTVLNQTPSAFKQLMQvacaGQEVPPL---ALRHVVFGGEALEvQALRPWF-ERFGdraPR 1859
Cdd:PRK08633   857 ---DPTDALgiaKLVAKHRATILLGTPTFLRLYLR----NKKLHPLmfaSLRLVVAGAEKLK-PEVADAFeEKFG---IR 925
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1860 LVNMYGITETTVHVTyrpLSLAD-LDGGAAS-------PIGEPIPDLSWYLLDA-GLNPVPRGCIGELYVGGAGLARGYL 1930
Cdd:PRK08633   926 ILEGYGATETSPVAS---VNLPDvLAADFKRqtgskegSVGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQVMKGYL 1002
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1931 NRPELScTRFVADpfsTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIE----ARLLAQPGVAEAVVLP 2006
Cdd:PRK08633  1003 GDPEKT-AEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelaKALGGEEVVFAVTAVP 1078
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 2007 HEGPGaTQLVgyVVTQAAPSDPAALRdtlRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08633  1079 DEKKG-EKLV--VLHTCGAEDVEELK---RAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3087-3183 6.79e-25

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 111.06  E-value: 6.79e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3166
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90
                   ....*....|....*..
gi 2183974163 3167 PEYPEERQAYMLEDSGV 3183
Cdd:COG0318     81 PRLTAEELAYILEDSGA 97
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
66-477 7.27e-25

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 110.08  E-value: 7.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   66 QSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDGFrQQVLAsvDVPVPVTLAGDDDAqaqiraFVE 145
Cdd:cd19545     18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLL-QVVVK--ESPISWTESTSLDE------YLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  146 SETQQPFDLrNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRqgieatlpdlPIQYADYAIWQR 225
Cdd:cd19545     89 EDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP----------VPQPPPFSRFVK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  226 HwLEAGERERQLEYWMARLGGGQSVlelptdrQRPALPSYRG-------ARHELQLPQALGRqlqalaqreGTTLFMLLL 298
Cdd:cd19545    158 Y-LRQLDDEAAAEFWRSYLAGLDPA-------VFPPLPSSRYqprpdatLEHSISLPSSASS---------GVTLATVLR 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  299 ASFQALLHRYSGQDEIRVGVPVANRN----RVetERLIGFFVNTQVLRADLDAQMPFLDLLQQTRvaalgAQSHQDLPFE 374
Cdd:cd19545    221 AAWALVLSRYTGSDDVVFGVTLSGRNapvpGI--EQIVGPTIATVPLRVRIDPEQSVEDFLQTVQ-----KDLLDMIPFE 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  375 QLveALQPERSLS----HSPLFQAMYNHQ-NLGSAGRQSLAAQLPGLSVEDLSWGAHSaqfdLTLDTYESEQGVHAEFTY 449
Cdd:cd19545    294 HT--GLQNIRRLGpdarAACNFQTLLVVQpALPSSTSESLELGIEEESEDLEDFSSYG----LTLECQLSGSGLRVRARY 367
                          410       420
                   ....*....|....*....|....*...
gi 2183974163  450 ATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19545    368 DSSVISEEQVERLLDQFEHVLQQLASAP 395
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
48-476 7.36e-25

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 110.42  E-value: 7.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   48 IPLSYAQerQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQldGFRQQVLASVDVPVP 127
Cdd:cd19534      2 VPLTPIQ--RWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDG--GWQQRIRGDVEELFR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  128 ---VTLAGDDDAQAqIRAFVEsETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYgarRQ 204
Cdd:cd19534     78 levVDLSSLAQAAA-IEALAA-EAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY---EQ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  205 GIEATLPDLP--IQYADYAIWQRHWLEAGERERQLEYWMARLggGQSVLELPTDRQRpalpSYRGARHE-LQLPQALGRQ 281
Cdd:cd19534    153 ALAGEPIPLPskTSFQTWAELLAEYAQSPALLEELAYWRELP--AADYWGLPKDPEQ----TYGDARTVsFTLDEEETEA 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  282 L-QALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETE----RLIGFFVNTQVLRADLDAQMPFLDLLQ 356
Cdd:cd19534    227 LlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGldlsRTVGWFTSMYPVVLDLEASEDLGDTLK 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  357 QTRvAALGAQSHQDLPFEQLVEALQPERS-LSHSPLFQAMYN----HQNLGSAGrqSLAAQLPGLSVEDLSWGAH-SAQF 430
Cdd:cd19534    307 RVK-EQLRRIPNKGIGYGILRYLTPEGTKrLAFHPQPEISFNylgqFDQGERDD--ALFVSAVGGGGSDIGPDTPrFALL 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163  431 DLTLDTYESEqgVHAEFTYATDLFEAATVERLARHWRNLLEAVVAE 476
Cdd:cd19534    384 DINAVVEGGQ--LVITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1570-2071 8.31e-25

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 112.01  E-value: 8.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAerPRATAVVYGERALDYGELNLRANRLAHRLIELGVGP--DVLVGLAAErsLEMIVGLLAILKAGgaYVP 1647
Cdd:PRK10946    27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPgdTALVQLGNV--AEFYITFFALLKLG--VAP 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRL---GY--------MIEDSG---------IRLLLTQ-RAARERLPLGEGLPCLLLDA-EHEWAGYPESdPQ 1705
Cdd:PRK10946   101 VNALFSHQRSelnAYasqiepalLIADRQhalfsdddfLNTLVAEhSSLRVVLLLNDDGEHSLDDAiNHPAEDFTAT-PS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1706 SAvgvDNLAYVIYTSGSTGKPKgtLLP--HGNVLRLFDATRHWFGFSADD----AWSLFHSYAFdfSVWEIFGALLHGGR 1779
Cdd:PRK10946   180 PA---DEVAFFQLSGGSTGTPK--LIPrtHNDYYYSVRRSVEICGFTPQTrylcALPAAHNYPM--SSPGALGVFLAGGT 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1780 LVIVPyetSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPLA-LRHVVFGGEALEvqalrpwfERFGDRAP 1858
Cdd:PRK10946   253 VVLAP---DPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLAsLKLLQVGGARLS--------ETLARRIP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1859 -----RLVNMYGITETTVHVTyrplSLADLDGGAASPIGEPI-PDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNR 1932
Cdd:PRK10946   322 aelgcQLQQVFGMAEGLVNYT----RLDDSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKS 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1933 PELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEA--VVLPHEgp 2010
Cdd:PRK10946   398 PQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAalVSMEDE-- 468
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2011 gatqLVG-----YVVTQaAPSDPAALRDTLRQALKAslpEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK10946   469 ----LMGekscaFLVVK-EPLKAVQLRRFLREQGIA---EFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1570-2071 8.57e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 112.43  E-value: 8.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLL-----------TQRAAR----------ERLPLGEGL---------PCLLLDAE-----H 1694
Cdd:PRK06710   106 PLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKiehvivtriaDFLPFPKNLlypfvqkkqSNLVVKVSesetiH 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1695 EWAGYpESDPQSAVGV-----DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSAD------DAWSLFHSYAF 1763
Cdd:PRK06710   186 LWNSV-EKEVNTGVEVpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgeevvlGVLPFFHVYGM 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1764 DfSVWEIfgALLHGGRLVIVPYETSRSPEDFLRllcRERVTVLNQTPSAFKQLMQVACAgQEVPPLALRHVVFGGEALEV 1843
Cdd:PRK06710   265 T-AVMNL--SIMQGYKMVLIPKFDMKMVFEAIK---KHKVTLFPGAPTIYIALLNSPLL-KEYDISSIRACISGSAPLPV 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1844 QaLRPWFERFgdRAPRLVNMYGITETTvhvtyrPLSLADL--DGGAASPIGEPIPDLSWYL--LDAGlNPVPRGCIGELY 1919
Cdd:PRK06710   338 E-VQEKFETV--TGGKLVEGYGLTESS------PVTHSNFlwEKRVPGSIGVPWPDTEAMImsLETG-EALPPGEIGEIV 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1920 VGGAGLARGYLNRPELSCTRFvadpfstTGGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGV 1999
Cdd:PRK06710   408 VKGPQIMKGYWNKPEETAAVL-------QDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKV 479
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2000 AEAVVLPHEGPGATQLV-GYVVTQaapSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK06710   480 QEVVTIGVPDPYRGETVkAFVVLK---EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PLN02246 PLN02246
4-coumarate--CoA ligase
488-953 1.18e-24

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 111.61  E-value: 1.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  488 DAEERATLLQRSRLPASEYPAGQGVHR-LFEAQAGLtPDAPALLFGE--ERLSYAELNALANRLAWRLREEGVGSDVLVG 564
Cdd:PLN02246     1 EASASEEFIFRSKLPDIYIPNHLPLHDyCFERLSEF-SDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  565 IALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSV---LARLPQSDGLQSLLLDDL-ERLVH 640
Cdd:PLN02246    80 LLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYvdkLKGLAEDDGVTVVTIDDPpEGCLH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  641 GYP---AENPDLPEA---PDSLCYAIYTSGSTGQPKGVMVRHRALtnfVCSIARQ-----P--GMLARDRLLSVTTFsFD 707
Cdd:PLN02246   160 FSEltqADENELPEVeisPDDVVALPYSSGTTGLPKGVMLTHKGL---VTSVAQQvdgenPnlYFHSDDVILCVLPM-FH 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  708 IFGLE--LYVPLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDSERV---DLLRGCTLLCGGEALAE 782
Cdd:PLN02246   236 IYSLNsvLLCGLRVGAAILIMPK---FEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVekyDLSSIRMVLSGAAPLGK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  783 DL--AARMRGLSASTWNLYGPTET-TIWSARFRLGEEarPF------LGGPLENTALYILDSEMN-PCPPGVAGELLIGG 852
Cdd:PLN02246   313 ELedAFRAKLPNAVLGQGYGMTEAgPVLAMCLAFAKE--PFpvksgsCGTVVRNAELKIVDPETGaSLPRNQPGEICIRG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  853 DGLARGYHRRPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREA 932
Cdd:PLN02246   391 PQIMKGYLNDPEATAN-------TIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADA 463
                          490       500
                   ....*....|....*....|..
gi 2183974163  933 VVVAQPG-VAGPTLVAYLVPTE 953
Cdd:PLN02246   464 AVVPMKDeVAGEVPVAFVVRSN 485
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1527-2073 1.35e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 111.24  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1527 LLRSIVARPEARIAELKLLDEAearadllqWNPGPQDFTPASClhrlierQAAERPRATAVVYGERALDYGELNLRANRL 1606
Cdd:PRK13383     9 LVRSGLLNPPSPRAVLRLLREA--------SRGGTNPYTLLAV-------TAARWPGRTAIIDDDGALSYRELQRATESL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1607 AHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPlGEGLP 1686
Cdd:PRK13383    74 ARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIA-GADDA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1687 CLLLDAEHewAGYPESDPQSAVGVDNlAYVIYTSGSTGKPKGtlLPHGNVLR--------LFDATRHWFGFSADDAWSLF 1758
Cdd:PRK13383   153 VAVIDPAT--AGAEESGGRPAVAAPG-RIVLLTSGTTGKPKG--VPRAPQLRsavgvwvtILDRTRLRTGSRISVAMPMF 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1759 HSYAFDFSVWEIfgALlhGGRLVivpyeTSR--SPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPL-ALRHVV 1835
Cdd:PRK13383   228 HGLGLGMLMLTI--AL--GGTVL-----THRhfDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLpQLRVVM 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1836 FGGEALEVQALRPWFERFGDrapRLVNMYGITETTVHVTYRPLSLADldggAASPIGEPIPDLSWYLLDAGLNPVPRGCI 1915
Cdd:PRK13383   299 SSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVGIGALATPADLRD----APETVGKPVAGCPVRILDRNNRPVGPRVT 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1916 GELYVGGaglargylnrpELSCTRfvadpFSTTGGR-----LYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIE 1990
Cdd:PRK13383   372 GRIFVGG-----------ELAGTR-----YTDGGGKavvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVE 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1991 ARLLAQPGVAEAVVL--PHEGPGaTQLVGYVVTQAAPS-DPAALRDTlrqaLKASLPEHMVPAHLLFLERLPLTANGKLD 2067
Cdd:PRK13383   436 NALAAHPAVADNAVIgvPDERFG-HRLAAFVVLHPGSGvDAAQLRDY----LKDRVSRFEQPRDINIVSSIPRNPTGKVL 510

                   ....*.
gi 2183974163 2068 RRALPA 2073
Cdd:PRK13383   511 RKELPG 516
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3099-3182 1.37e-24

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 110.18  E-value: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3177
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                   ....*
gi 2183974163 3178 LEDSG 3182
Cdd:cd17648     81 LEDTG 85
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1590-2008 1.53e-24

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 110.14  E-value: 1.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1590 GERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLL 1669
Cdd:cd17640      2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1670 LTqraarerlplgeglpcllldaehewagypESDPqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLrlfdatrhwfgF 1749
Cdd:cd17640     82 VV-----------------------------ENDS------DDLATIIYTSGTTGNPKGVMLTHANLL-----------H 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1750 SADDAWSLFHSYAFDFSV-----WEIFG------ALLHGGRLVivpYETSRS-PEDFLRLlcreRVTVLNQTP------- 1810
Cdd:cd17640    116 QIRSLSDIVPPQPGDRFLsilpiWHSYErsaeyfIFACGCSQA---YTSIRTlKDDLKRV----KPHYIVSVPrlwesly 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1811 ----------SAFKQ-LMQVACAGQEvpplaLRHVVFGGEALeVQALRPWFERFGdraPRLVNMYGITETTVHVTYRpls 1879
Cdd:cd17640    189 sgiqkqvsksSPIKQfLFLFFLSGGI-----FKFGISGGGAL-PPHVDTFFEAIG---IEVLNGYGLTETSPVVSAR--- 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1880 laDLDGGAASPIGEPIPDLSWYLLDA-GLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDL 1958
Cdd:cd17640    257 --RLKCNVRGSVGRPLPGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDL 327
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 1959 ARYRCDGVVEYVGRI-DHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHE 2008
Cdd:cd17640    328 GWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
529-1004 3.04e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 109.45  E-value: 3.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  529 LLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGL 608
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  609 RLLLSqqsvlarlpqSDglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIAR 688
Cdd:cd05914     81 KAIFV----------SD---------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  689 QPGMLARDRLLSVTTFSfDIFGL--ELYVPLARGASMLLASREqaqdPEALLDLVERQGVTVLQATPATWRML-----CD 761
Cdd:cd05914    124 VVLLGKGDKILSILPLH-HIYPLtfTLLLPLLNGAHVVFLDKI----PSAKIIALAFAQVTPTLGVPVPLVIEkifkmDI 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  762 SERVDLLRGCTLL-----------------------------CGGEALAEDLAARMRGLSASTWNLYGPTET------TI 806
Cdd:cd05914    199 IPKLTLKKFKFKLakkinnrkirklafkkvheafggnikefvIGGAKINPDVEEFLRTIGFPYTIGYGMTETapiisySP 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 WsARFRLGEearpfLGGPLENTALYILDsemnPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTG 886
Cdd:cd05914    279 P-NRIRLGS-----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTG 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  887 DLARYRADGVIEYLGRIDHQ-VKIRGFRIELGEIETRLLEQDSVREAVVVAQPGvagpTLVAYLVPtEAALVDAESARQQ 965
Cdd:cd05914    342 DLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK----KLVALAYI-DPDFLDVKALKQR 416
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2183974163  966 ELRSALKNSLL----AVLPDY-MVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd05914    417 NIIDAIKWEVRdkvnQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1716-2068 3.14e-24

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 106.59  E-value: 3.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1716 VIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFHSYAFDFSVweifgALLH-GGRLVIVPyetSRS 1790
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYlnmlPLFHIAGLNLAL-----ATFHaGGANVVME---KFD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1791 PEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPPLALRHVvFGGEALEVqalrpwFERFGDRAP-RLVNMYGITET 1869
Cdd:cd17637     77 PAEALELIEEEKVTLMGSFPPILSNLLDAA-EKSGVDLSSLRHV-LGLDAPET------IQRFEETTGaTFWSLYGQTET 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1870 TVHVTYRPLSlaDLDGGAaspiGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTrfvadpfsTTG 1949
Cdd:cd17637    149 SGLVTLSPYR--ERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY--------TFR 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1950 GRLYRTGDLARYRCDGVVEYVGRIDHQ--VKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSD 2027
Cdd:cd17637    215 NGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT 294
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2183974163 2028 PAAlrDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd17637    295 LTA--DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2174-2598 3.66e-24

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 108.31  E-value: 3.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQ--MFFELDIPRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDG----TWRAEHRAVEAGEV 2247
Cdd:cd19536      3 PLSSLQEgmLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVPVTEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2248 LLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATLgDGSQRLLLVI--HHLVVDGVSWRILLEDLQTAYRQLQAGQ 2325
Cdd:cd19536     83 DLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRK-DERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2326 AVALPaKTSAFKAWAERLQAHARDGGLEgerGYWLAQLEGVSTELPCDDREGAQSVRHVRSARTELTEEATRrllqEAPA 2405
Cdd:cd19536    162 PLSLP-PAQPYRDFVAHERASIQQAASE---RYWREYLAGATLATLPALSEAVGGGPEQDSELLVSVPLPVR----SRSL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2406 AYRTQVN--DLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDltRTVGWFTSLFPLRLS-PVAELGASIKRIKEQL 2482
Cdd:cd19536    234 AKRSGIPlsTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTlSEETVEDLLKRAQEQE 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2483 R-AIPHKGLGFGALRYLGSAEdraalaalpsPRIT--FNYLgQFDGSFSADS-SALFRPSADAAGSERDSDAPLdnWLSL 2558
Cdd:cd19536    312 LeSLSHEQVPLADIQRCSEGE----------PLFDsiVNFR-HFDLDFGLPEwGSDEGMRRGLLFSEFKSNYDV--NLSV 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2183974163 2559 NGQvyAGRLGIDWSFSAARFSEASILRLADAYRDELLALI 2598
Cdd:cd19536    379 LPK--QDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELA 416
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
520-1007 6.28e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 109.01  E-value: 6.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGE--ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPAD 597
Cdd:PRK13391     7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  598 RLQYMIDDSGLRLLLS---QQSVLARLPQS--DGLQSLLLD---DLERLVhGYPAENPDLPEAP---DSLCYAI-YTSGS 665
Cdd:PRK13391    87 EAAYIVDDSGARALITsaaKLDVARALLKQcpGVRHRLVLDgdgELEGFV-GYAEAVAGLPATPiadESLGTDMlYSSGT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  666 TGQPKGVMvrhraltnfvcsiaRQPGMLARDRLLSVTTFSFDIFGLE----------LY--VPLArgASMLLASR----- 728
Cdd:PRK13391   166 TGRPKGIK--------------RPLPEQPPDTPLPLTAFLQRLWGFRsdmvylspapLYhsAPQR--AVMLVIRLggtvi 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  729 -EQAQDPEALLDLVERQGVTVLQATPATW-RMLCDSERV----DLlrgCTLLCGGEALA---EDLAARM-RGLSASTWNL 798
Cdd:PRK13391   230 vMEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLKLPEEVrdkyDL---SSLEVAIHAAApcpPQVKEQMiDWWGPIIHEY 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  799 YGPTE----TTIWSARF--RLGEEARPFLGgplentALYILDSEMNPCPPGVAGELLIGGdGLARGYHRRPGLTAERFLP 872
Cdd:PRK13391   307 YAATEglgfTACDSEEWlaHPGTVGRAMFG------DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHP 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  873 DPfaadgsRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVP 951
Cdd:PRK13391   380 DG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEEVKAVVQP 453
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163  952 TEAalVDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK13391   454 VDG--VDPGPALAAELIAFCRQRLSR----QKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK07638 PRK07638
acyl-CoA synthetase; Validated
520-1007 8.83e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 108.33  E-value: 8.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGvGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:PRK07638    11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLSQQSVLARLPQSDGlQSLLLDDLERLVHGY---PAENPDLPEAPdslCYAIYTSGSTGQPKGVMVRH 676
Cdd:PRK07638    90 KERLAISNADMIVTERYKLNDLPDEEG-RVIEIDEWKRMIEKYlptYAPIENVQNAP---FYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  677 RA-LTNFVCSiARQPGMLARDRLLSVTTF--SFDIFGL--ELYVplarGASMLLasrEQAQDPEALLDLVERQGVTVLQA 751
Cdd:PRK07638   166 QSwLHSFDCN-VHDFHMKREDSVLIAGTLvhSLFLYGAisTLYV----GQTVHL---MRKFIPNQVLDKLETENISVMYT 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  752 TPATWRMLCDSERVdLLRGCTLLCGG---EALAEDlAARMRGLSASTWNLYGPTETTIWSARFRLGEEARP-FLGGPLEN 827
Cdd:PRK07638   238 VPTMLESLYKENRV-IENKMKIISSGakwEAEAKE-KIKNIFPYAKLYEFYGASELSFVTALVDEESERRPnSVGRPFHN 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  828 TALYILDSEMNPCPPGVAGELLIGGDGLARGYhrrpglTAERFLPDPFAADGsrlYRT-GDLARYRADGVIEYLGRIDHQ 906
Cdd:PRK07638   316 VQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY------IIGGVLARELNADG---WMTvRDVGYEDEEGFIYIVGREKNM 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  907 VKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPtlvaYLVPTEAALVDAeSARQQELRSALKNSllavLPDYMVPA 986
Cdd:PRK07638   387 ILFGGINIFPEEIESVLHEHPAVDEIVVI---GVPDS----YWGEKPVAIIKG-SATKQQLKSFCLQR----LSSFKIPK 454
                          490       500
                   ....*....|....*....|.
gi 2183974163  987 HMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07638   455 EWHFVDEIPYTNSGKIARMEA 475
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
536-1007 9.93e-24

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 107.05  E-value: 9.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLllsqq 615
Cdd:cd05912      2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 svlarlpqsdglqslllddlerlvhgypaenpdlpeapDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLAR 695
Cdd:cd05912     77 --------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  696 DRLLSVTTFsFDIFGLELYV-PLARGASMLLasrEQAQDPEALLDLVERQGVTVLQATPATWRMLCDservDLLRGC--- 771
Cdd:cd05912    119 DNWLCALPL-FHISGLSILMrSVIYGMTVYL---VDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE----ILGEGYpnn 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  772 --TLLCGGEALAEDLAARMRGLSASTWNLYGPTET-------TIWSARFRLGEearpfLGGPLENTALYILDSEMnpcPP 842
Cdd:cd05912    191 lrCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETcsqivtlSPEDALNKIGS-----AGKPLFPVELKIEDDGQ---PP 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  843 GVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETR 922
Cdd:cd05912    263 YEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  923 LLEQDSVREAVVVAQPGVA-GPTLVAYLVpteaalvdaesaRQQELRSA-LKNSLLAVLPDYMVPAHMLLLENLPLTPNG 1000
Cdd:cd05912    335 LLSHPAIKEAGVVGIPDDKwGQVPVAFVV------------SERPISEEeLIAYCSEKLAKYKVPKKIYFVDELPRTASG 402

                   ....*..
gi 2183974163 1001 KINRKAL 1007
Cdd:cd05912    403 KLLRHEL 409
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1585-2071 1.34e-23

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 107.85  E-value: 1.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1585 TAVVYGERALD-----YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGY 1659
Cdd:PRK08008    24 TALIFESSGGVvrrysYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1660 MIEDSGIRLLLTQRAA---------------RERLPLGEGLPCL-------LLDAEHEwagyPESDPQSAVGVDNLAYVI 1717
Cdd:PRK08008   104 ILQNSQASLLVTSAQFypmyrqiqqedatplRHICLTRVALPADdgvssftQLKAQQP----ATLCYAPPLSTDDTAEIL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1718 YTSGSTGKPKGTLLPHGNvLRLFDATRHWFG-FSADDAW-SLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSpedFL 1795
Cdd:PRK08008   180 FTSGTTSRPKGVVITHYN-LRFAGYYSAWQCaLRDDDVYlTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARA---FW 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1796 RLLCRERVTVLNQTPSAFKQLM-QVACAGQEvpPLALRHVVFgGEALEVQALRPWFERFGdraPRLVNMYGITETTVHVt 1874
Cdd:PRK08008   256 GQVCKYRATITECIPMMIRTLMvQPPSANDR--QHCLREVMF-YLNLSDQEKDAFEERFG---VRLLTSYGMTETIVGI- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1875 yrplsLADLDGGAAS--PIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGG-AG--LARGYLNRPELSCTRFVADpfsttg 1949
Cdd:PRK08008   329 -----IGDRPGDKRRwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVLEAD------ 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1950 GRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVlphegpgatqlVGYvvtqaapsdPA 2029
Cdd:PRK08008   398 GWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV-----------VGI---------KD 456
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2030 ALRDtlrQALKA--------SLPE---------HM----VPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08008   457 SIRD---EAIKAfvvlnegeTLSEeeffafceqNMakfkVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1707-2071 1.44e-23

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 108.37  E-value: 1.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1707 AVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAWSLF--------------HSYAFDFSVweiFG 1772
Cdd:PRK12492   203 PVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMkegqevmiaplplyHIYAFTANC---MC 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1773 ALLHGGRLVIVPyetsrSPED---FLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPPLALRHVVFGGEALEVQALRPW 1849
Cdd:PRK12492   280 MMVSGNHNVLIT-----NPRDipgFIKELGKWRFSALLGLNTLFVALMDHP-GFKDLDFSALKLTNSGGTALVKATAERW 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1850 FERFGdraPRLVNMYGITETTVHVTYRPL-SLADLdggaaSPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARG 1928
Cdd:PRK12492   354 EQLTG---CTIVEGYGLTETSPVASTNPYgELARL-----GTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKG 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1929 YLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE--AVVLP 2006
Cdd:PRK12492   426 YWQQPEATAEALDAEGW-------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcaAIGVP 498
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2007 HEGPG-ATQLvgYVVtqaaPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK12492   499 DERSGeAVKL--FVV----ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1711-2078 1.72e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 105.26  E-value: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSyafdFSVWEIFGALLHGGRLVIVP-- 1784
Cdd:cd05944      2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDvllcGLPLFHV----NGSVVTLLTPLASGAHVVLAgp 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1785 --YETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPplALRHVVFGGEALEVQAlrpwFERFGDRAP-RLV 1861
Cdd:cd05944     78 agYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVP-VNADIS--SLRFAMSGAAPLPVEL----RARFEDATGlPVV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1862 NMYGITETTVHVTYRPlsladlDGGAASP--IGEPIP----------DLSWYLLDAGLNPVprgciGELYVGGAGLARGY 1929
Cdd:cd05944    151 EGYGLTEATCLVAVNP------PDGPKRPgsVGLRLPyarvrikvldGVGRLLRDCAPDEV-----GEICVAGPGVFGGY 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1930 LNRpELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEG 2009
Cdd:cd05944    220 LYT-EGNKNAFVADGW-------LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPD 291
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2010 PGATQL-VGYV-VTQAAPSDPAALRDTLRqalkASLPEHM-VPAHLLFLERLPLTANGKLDRRALPAPDASR 2078
Cdd:cd05944    292 AHAGELpVAYVqLKPGAVVEEEELLAWAR----DHVPERAaVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1565-2065 1.75e-23

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 107.38  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1565 TPASclhrLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGA 1644
Cdd:cd12118      5 TPLS----FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1645 YVPLDPRYPSDRLGYMIEDSGIRLLLTqraarerlplgeglpclllDAEHEW-----AGYPESDPQSAVGVDNLAYVIYT 1719
Cdd:cd12118     81 LNALNTRLDAEEIAFILRHSEAKVLFV-------------------DREFEYedllaEGDPDFEWIPPADEWDPIALNYT 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1720 SGSTGKPKGTLLPH-GNVLRLFDATRHW-FGFSADDAWSL--FHSYAFDFsVWEIFGAllhGGRLVIVPyeTSRSPEDFl 1795
Cdd:cd12118    142 SGTTGRPKGVVYHHrGAYLNALANILEWeMKQHPVYLWTLpmFHCNGWCF-PWTVAAV---GGTNVCLR--KVDAKAIY- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1796 RLLCRERVT-------VLN-------QTPSAFKQLMQVACAGqeVPPLAlrHVVFGGEALEVqalrpwferfgdrapRLV 1861
Cdd:cd12118    215 DLIEKHKVThfcgaptVLNmlanappSDARPLPHRVHVMTAG--APPPA--AVLAKMEELGF---------------DVT 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1862 NMYGITETTVHVT---YRP----LSLADLDG-----GAASPIGEPIPdlswyLLDA-GLNPVPRG--CIGELYVGGAGLA 1926
Cdd:cd12118    276 HVYGLTETYGPATvcaWKPewdeLPTEERARlkarqGVRYVGLEEVD-----VLDPeTMKPVPRDgkTIGEIVFRGNIVM 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1927 RGYLNRPElsctrfvADPFSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL- 2005
Cdd:cd12118    351 KGYLKNPE-------ATAEAFRGG-WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVa 422
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 2006 -PHEGPGATqLVGYVVTQAAPSdpaALRDTLRQALKASLPEHMVPAHLLFLErLPLTANGK 2065
Cdd:cd12118    423 rPDEKWGEV-PCAFVELKEGAK---VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
PRK07867 PRK07867
acyl-CoA synthetase; Validated
507-1007 3.27e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 107.07  E-value: 3.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  507 PAGQGVHRLFEAQAGLtpDAPALLFGEERLSYAELNALANRLAWRLREE-GVGSDVLVGIALERGVPMVVALLAVLKAGG 585
Cdd:PRK07867     2 SSAPTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  586 AYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLER---LVHGYPAENPDLPEA-PDSLCYAIY 661
Cdd:PRK07867    80 VPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAwadELAAHRDAEPPFRVAdPDDLFMLIF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  662 TSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARD-RLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQdpeALLDL 740
Cdd:PRK07867   160 TSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDvCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSAS---GFLPD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  741 VERQGVT-----------VLqATPatwrmlcdsERVD----LLRgctLLCGGEALAEDLAARMRGLSASTWNLYGPTETT 805
Cdd:PRK07867   237 VRRYGATyanyvgkplsyVL-ATP---------ERPDdadnPLR---IVYGNEGAPGDIARFARRFGCVVVDGFGSTEGG 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWSARfrlgEEARP--FLGGPLENTAlyILDSEM-NPCPPGVA------------GELL-IGGDGLARGYHRRPGLTAER 869
Cdd:PRK07867   304 VAITR----TPDTPpgALGPLPPGVA--IVDPDTgTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAER 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  870 flpdpfAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAY 948
Cdd:PRK07867   378 ------MRGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQVMAA 449
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  949 LVPTEAALVDAESARQQelrsalknslLAVLPDY---MVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07867   450 LVLAPGAKFDPDAFAEF----------LAAQPDLgpkQWPSYVRVCAELPRTATFKVLKRQL 501
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1621-2073 3.80e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 106.69  E-value: 3.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1621 VGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERL-PLGEGLPCLLLDAEH---EW 1696
Cdd:PRK07867    57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdGLDPGVRVINVDSPAwadEL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1697 AGYPESDPQ-SAVGVDNLAYVIYTSGSTGKPKGTLLPH------GNVLrlfdATRhwFGFSADD----AWSLFHSYAF-- 1763
Cdd:PRK07867   137 AAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHrkvasaGVML----AQR--FGLGPDDvcyvSMPLFHSNAVma 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1764 DFSVweifgaLLHGGRLVIVPYETSRSpeDFLRLLCRERVTVLNQTPSAFKQLMqvacAGQEVPPLA---LRhVVFGGEA 1840
Cdd:PRK07867   211 GWAV------ALAAGASIALRRKFSAS--GFLPDVRRYGATYANYVGKPLSYVL----ATPERPDDAdnpLR-IVYGNEG 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1841 LEVqALRPWFERFGdraPRLVNMYGITETTVHVTYRPlsladldGGAASPIGEPIPDLSWYLLDAGlNPVPRG------- 1913
Cdd:PRK07867   278 APG-DIARFARRFG---CVVVDGFGSTEGGVAITRTP-------DTPPGALGPLPPGVAIVDPDTG-TECPPAedadgrl 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1914 -----CIGELY-VGGAGLARGYLNRPElsctrfvADPFSTTGGRlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELG 1987
Cdd:PRK07867   346 lnadeAIGELVnTAGPGGFEGYYNDPE-------ADAERMRGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTA 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1988 EIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQalKASLPEHMVPAHLLFLERLPLTANGK 2065
Cdd:PRK07867   418 PIERILLRYPDATEVAVyaVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFK 495

                   ....*...
gi 2183974163 2066 LDRRALPA 2073
Cdd:PRK07867   496 VLKRQLSA 503
PRK07529 PRK07529
AMP-binding domain protein; Validated
1566-2071 4.67e-23

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 107.35  E-value: 4.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1566 PAScLHRLIERQAAERPRATAVVYGERA--------LDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLA 1637
Cdd:PRK07529    24 PAS-TYELLSRAAARHPDAPALSFLLDAdpldrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1638 ILKAGGAyVPLDPRYPSDRLGYMIEDSGIRLLLT----------QRAARERLPLGEGLPCLLLD-AEH------------ 1694
Cdd:PRK07529   103 GEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwQKVAEVLAALPELRTVVEVDlARYlpgpkrlavpli 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1695 -------------EWAGYPES--DPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNvlrlfDATRHW-----FGFSADD- 1753
Cdd:PRK07529   182 rrkaharildfdaELARQPGDrlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-----EVANAWlgallLGLGPGDt 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 ---AWSLFHSYAfdfSVWEIFGALLHGGRLVIVPYETSRSPE---DFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVP 1827
Cdd:PRK07529   257 vfcGLPLFHVNA---LLVTGLAPLARGAHVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1828 plALRHVVFGGEALEVQALRpwfeRFGDRAP-RLVNMYGITETTVHVTYRPLSLADLDGGaaspIGEPIPdlswY----- 1901
Cdd:PRK07529   334 --SLRYALCGAAPLPVEVFR----RFEAATGvRIVEGYGLTEATCVSSVNPPDGERRIGS----VGLRLP----Yqrvrv 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1902 --LLDAG--LNPVPRGCIGELYVGGAGLARGYLNrpelscTRFVADPFstTGGRLYRTGDLARYRCDGVVEYVGRidhqV 1977
Cdd:PRK07529   400 viLDDAGryLRDCAVDEVGVLCIAGPNVFSGYLE------AAHNKGLW--LEDGWLNTGDLGRIDADGYFWLTGR----A 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1978 K---IR-GFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQL-VGYV-VTQAAPSDPAALRDTLRQAL--KASLPEHMVP 2049
Cdd:PRK07529   468 KdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVqLKPGASATEAELLAFARDHIaeRAAVPKHVRI 547
                          570       580
                   ....*....|....*....|..
gi 2183974163 2050 ahllfLERLPLTANGKLDRRAL 2071
Cdd:PRK07529   548 -----LDALPKTAVGKIFKPAL 564
PRK09274 PRK09274
peptide synthase; Provisional
514-1007 6.76e-23

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 106.14  E-value: 6.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGE----------ERLSYAELNALANRLAWRLREEGVGSDVlvgialeRGVPMV-------VA 576
Cdd:PRK09274    10 RHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGM-------RAVLMVtpsleffAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  577 LLAVLKAGGAYVPLDPQYPADRLQYMIDDSG------------LRLLL--SQQSVLARLPQSDGLqSLLLDDLERLVHGY 642
Cdd:PRK09274    83 TFALFKAGAVPVLVDPGMGIKNLKQCLAEAQpdafigipkahlARRLFgwGKPSVRRLVTVGGRL-LWGGTTLATLLRDG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  643 PAENPDLPE-APDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSvttfSFDIFGLelyVPLARGA 721
Cdd:PRK09274   162 AAAPFPMADlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLFAL---FGPALGM 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  722 SMLL----ASREQAQDPEALLDLVERQGVTVLQATPATWRML---CDSERVDL--LRgcTLLCGGEALAEDLAARMRGL- 791
Cdd:PRK09274   235 TSVIpdmdPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLgryGEANGIKLpsLR--RVISAGAPVPIAVIERFRAMl 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  792 --SASTWNLYGPTE----TTIwSARFRLGEEARPF-------LGGPLENTALYILD---------SEMNPCPPGVAGELL 849
Cdd:PRK09274   313 ppDAEILTPYGATEalpiSSI-ESREILFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  850 IGGDGLARGYHRRPGLTAERFLPDPfaaDGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSV 929
Cdd:PRK09274   392 VAGPMVTRSYYNRPEATRLAKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  930 -REAVV-VAQPGVAGPTLVaylVPTEAALVDAESARQQELRS-ALKNSLLAVLPDYmvpahmLLLENLPLTP--NGKINR 1004
Cdd:PRK09274   469 kRSALVgVGVPGAQRPVLC---VELEPGVACSKSALYQELRAlAAAHPHTAGIERF------LIHPSFPVDIrhNAKIFR 539

                   ...
gi 2183974163 1005 KAL 1007
Cdd:PRK09274   540 EKL 542
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2742-2941 1.20e-22

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 103.94  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2742 FELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRY----RGETP--SRSDGRYRDYIAWLQRQDAGR 2815
Cdd:cd20484    103 FVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallQGKQPtlASSPASYYDFVAWEQDMLAGA 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2816 T----EAFWKQRLQrlGE-PTLLVPAF--AHGVRGAEGHADRYRqLDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRF 2888
Cdd:cd20484    183 EgeehRAYWKQQLS--GTlPILELPADrpRSSAPSFEGQTYTRR-LPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRY 259
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2889 TGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQ 2941
Cdd:cd20484    260 TGQEDIIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1573-2073 1.42e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 105.11  E-value: 1.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPratAVVYGERALDYGELNLRANRLAHRLIELGVGPDVL-VGLAAERSLEMIVGLLAILKAGGAYVPLDPR 1651
Cdd:PRK13388     9 LRDRAGDDTI---AVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YPSDRLGYMIEDSGIRLLLTQRAARERLPlGEGLPC--LLLDAEHEWA----GYPESDPQSAVGVDNLAYVIYTSGSTGK 1725
Cdd:PRK13388    86 RRGAALAADIRRADCQLLVTDAEHRPLLD-GLDLPGvrVLDVDTPAYAelvaAAGALTPHREVDAMDPFMLIFTSGTTGA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1726 PKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHSYAFdFSVWEIfgALLHGGRLVIVPyetSRSPEDFLRLLCRE 1801
Cdd:PRK13388   165 PKAVRCSHGRLAFAGRALTERFGLTRDDvcyvSMPLFHSNAV-MAGWAP--AVASGAAVALPA---KFSASGFLDDVRRY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1802 RVTVLNQTPSAFKQLMqvacAGQEVPPLA---LRhVVFGGEALEvQALRPWFERFGdraPRLVNMYGITETTVHVTYRPl 1878
Cdd:PRK13388   239 GATYFNYVGKPLAYIL----ATPERPDDAdnpLR-VAFGNEASP-RDIAEFSRRFG---CQVEDGYGSSEGAVIVVREP- 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1879 sladldGGAASPIGEPIPDLSWYLLDAG--------------LNpvPRGCIGELY-VGGAGLARGYLNRPELSCTRFvad 1943
Cdd:PRK13388   309 ------GTPPGSIGRGAPGVAIYNPETLtecavarfdahgalLN--ADEAIGELVnTAGAGFFEGYYNNPEATAERM--- 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1944 pfstTGGRlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVT 2021
Cdd:PRK13388   378 ----RHGM-YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyaVPDERVGDQVMAALVLR 452
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2022 QAAPSDPAALRDTLrqALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:PRK13388   453 DGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1130-1533 1.96e-22

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 102.76  E-value: 1.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1130 HSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHD-GAPRQVIHPTLPIAIEERRppvageDLKGLVETEA 1208
Cdd:cd19545     18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPISWTEST------SLDEYLEEDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1209 HRPFDLQrGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPalaelpiQYADFAAW-QRQW 1287
Cdd:cd19545     92 AAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPP-------PFSRFVKYlRQLD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1288 MDGGErerqlDYWVSRLGGEQPLL--ELPSDRPRPQQQSHRGRRIGIPLPAELaealrrlaqaeQGTLFMLLLASFQALL 1365
Cdd:cd19545    164 DEAAA-----EFWRSYLAGLDPAVfpPLPSSRYQPRPDATLEHSISLPSSASS-----------GVTLATVLRAAWALVL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1366 HRYSGQNDIRVGVPIANRN--REETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQAVVEAqghqdLPFEQLvdALQPE 1443
Cdd:cd19545    228 SRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM-----IPFEHT--GLQNI 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1444 RSLS----HAPLFQVMYNHQRDDHR---GSRFASLGELEVEDLAWDvqtaQFDLTLDTYESSNGLLAELTYATDLFDASS 1516
Cdd:cd19545    301 RRLGpdarAACNFQTLLVVQPALPSstsESLELGIEEESEDLEDFS----SYGLTLECQLSGSGLRVRARYDSSVISEEQ 376
                          410
                   ....*....|....*..
gi 2183974163 1517 AERIAGHWLNLLRSIVA 1533
Cdd:cd19545    377 VERLLDQFEHVLQQLAS 393
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
519-1007 3.00e-22

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 104.08  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  519 QAGLTPDAPALLF----GEE-RLSYAELNALANRLAwrlreegvgsDVLVGI-ALERGVPMVVAL----------LAVLK 582
Cdd:cd05928     20 KAGKRPPNPALWWvngkGDEvKWSFRELGSLSRKAA----------NVLSGAcGLQRGDRVAVILprvpewwlvnVACIR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  583 AGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARL----PQSDGLQS-LLLDDLERlvHGYPAENPDLPEAPDS-L 656
Cdd:cd05928     90 TGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvaSECPSLKTkLLVSEKSR--DGWLNFKELLNEASTEhH 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  657 C--------YAIY-TSGSTGQPKgvMVRHRAltnfvCSIARQPGMLARdRLLSVTtfSFDIF------------GLELYV 715
Cdd:cd05928    168 CvetgsqepMAIYfTSGTTGSPK--MAEHSH-----SSLGLGLKVNGR-YWLDLT--ASDIMwntsdtgwiksaWSSLFE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  716 PLARGASMLLASREQAqDPEALLDLVERQGVTVLQATPATWRMLCD----SERVDLLRGCtlLCGGEALAEDLAARMRGL 791
Cdd:cd05928    238 PWIQGACVFVHHLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQqdlsSYKFPSLQHC--VTGGEPLNPEVLEKWKAQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  792 SA-STWNLYGPTETTIWSARFRlGEEARP-FLGGPLENTALYILDSEMNPCPPGVAGELLIGGD-----GLARGYHRRPG 864
Cdd:cd05928    315 TGlDIYEGYGQTETGLICANFK-GMKIKPgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  865 LTAERFLPDpfaadgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGP 943
Cdd:cd05928    394 KTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDpIRGE 465
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163  944 TLVAYLVPTEAALVDAESARQQELRSALKNsllaVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05928    466 VVKAFVVLAPQFLSHDPEQLTKELQQHVKS----VTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1578-2071 3.13e-22

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 103.23  E-value: 3.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDrl 1657
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA-- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 gymiEDSGIrLLLTQRAARERLPLGEGLPCLLLDAEHEWAGYPESDPQSAVgvdNLAYVIYTSGSTGKPKGTLLPHGNVL 1737
Cdd:cd05929     80 ----EACAI-IEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEA---AGWKMLYSGGTTGRPKGIKRGLPGGP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1738 RLFDATRHW---FGFSADDAW----SLFHSYAFDFSvweiFGALLHGGRLVIVPyetSRSPEDFLRLLCRERVTVLNQTP 1810
Cdd:cd05929    152 PDNDTLMAAalgFGPGADSVYlspaPLYHAAPFRWS----MTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVP 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1811 SAFKQLMQVACAGQEVPPLA-LRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTvhvtyrPLSLADLDGGAAS 1889
Cdd:cd05929    225 TMFVRLLKLPEAVRNAYDLSsLKRVIHAAAPCPPWVKEQWIDWGG---PIIWEYYGGTEGQ------GLTIINGEEWLTH 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1890 P--IGEPI-PDLSwyLLDAGLNPVPRGCIGELYVGGAGlARGYLNRPELSCTRFVADPFSTTGgrlyrtgDLARYRCDGV 1966
Cdd:cd05929    296 PgsVGRAVlGKVH--ILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLG-------DVGYLDEDGY 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1967 VEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGatQLVGYVVtQAAPSDPA--ALRDTLRQALKAS 2042
Cdd:cd05929    366 LYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgVPDEELG--QRVHAVV-QPAPGADAgtALAEELIAFLRDR 442
                          490       500
                   ....*....|....*....|....*....
gi 2183974163 2043 LPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05929    443 LSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK13382 PRK13382
bile acid CoA ligase;
1578-2074 3.45e-22

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 103.68  E-value: 3.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAER-PRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDR 1656
Cdd:PRK13382    52 AAQRcPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1657 LGYMIEDSGIRLL--------LTQRAARER--------LPLGEG-LPCLLLDAEHEWAGYPESDPQSAVgvdnlayVIYT 1719
Cdd:PRK13382   132 LAEVVTREGVDTViydeefsaTVDRALADCpqatrivaWTDEDHdLTVEVLIAAHAGQRPEPTGRKGRV-------ILLT 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1720 SGSTGKPKGTLLP----HGNVLRLFDAT----RHWFGFSAddawSLFHSYAFDFSVweiFGALLhggRLVIVpyeTSR-- 1789
Cdd:PRK13382   205 SGTTGTPKGARRSgpggIGTLKAILDRTpwraEEPTVIVA----PMFHAWGFSQLV---LAASL---ACTIV---TRRrf 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1790 SPEDFLRLLCRERVTVLNQTPSAFKQLMqvacagqEVPP--------LALRHVVFGGEALEVQALRPWFERFGDRaprLV 1861
Cdd:PRK13382   272 DPEATLDLIDRHRATGLAVVPVMFDRIM-------DLPAevrnrysgRSLRFAAASGSRMRPDVVIAFMDQFGDV---IY 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1862 NMYGITETTVHVTYRPlslADLDGgAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNrpelSCTRFV 1941
Cdd:PRK13382   342 NNYNATEAGMIATATP---ADLRA-APDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS----GSTKDF 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1942 ADPFSTTGgrlyrtgDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQ-LVGYVV 2020
Cdd:PRK13382   414 HDGFMASG-------DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQrLAAFVV 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2021 TQAapsDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAP 2074
Cdd:PRK13382   487 LKP---GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
531-1007 4.88e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 103.06  E-value: 4.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  531 FGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRL 610
Cdd:PRK08276     7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  611 LLSQ-------QSVLARLPQsdGLQSLLLDD--------LERLVHGYPAENPDLPEAPDSLcyaIYTSGSTGQPKGVMvr 675
Cdd:PRK08276    87 LIVSaaladtaAELAAELPA--GVPLLLVVAgpvpgfrsYEEALAAQPDTPIADETAGADM---LYSSGTTGRPKGIK-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 hRALTNfvCSIARQPGMLARdrllsVTTFSFDIFGLELYV---PLARGASMLLASREQAQ----------DPEALLDLVE 742
Cdd:PRK08276   160 -RPLPG--LDPDEAPGMMLA-----LLGFGMYGGPDSVYLspaPLYHTAPLRFGMSALALggtvvvmekfDAEEALALIE 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  743 RQGVTVLQATPATW-RMLCDSERV----DL--LRGctLLCGGEALAEDLAARMrglsaSTW------NLYGPTE----TT 805
Cdd:PRK08276   232 RYRVTHSQLVPTMFvRMLKLPEEVraryDVssLRV--AIHAAAPCPVEVKRAM-----IDWwgpiihEYYASSEgggvTV 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWSARF--RLGEEARPFLGGplentaLYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAAdgsrly 883
Cdd:PRK08276   305 ITSEDWlaHPGSVGKAVLGE------VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------ 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  884 rTGDLARYRADGvieYL---GRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPteAAL 956
Cdd:PRK08276   373 -VGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVF---GVPdeemGERVKAVVQP--ADG 443
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  957 VDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK08276   444 ADAGDALAAELIAWLRGRLAH----YKCPRSIDFEDELPRTPTGKLYKRRL 490
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3089-3182 5.50e-22

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 102.00  E-value: 5.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3089 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3168
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90
                   ....*....|....
gi 2183974163 3169 YPEERQAYMLEDSG 3182
Cdd:cd17653     81 LPSARIQAILRTSG 94
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
528-1007 5.70e-22

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 102.85  E-value: 5.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  528 ALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSG 607
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  608 LRLLLSQQSVLA----RLPQsdGLQSLL------------LDDLER------------LVHGYPAENPDLPeAPDSLcya 659
Cdd:PRK12406    84 ARVLIAHADLLHglasALPA--GVTVLSvptppeiaaayrISPALLtppagaidwegwLAQQEPYDGPPVP-QPQSM--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 IYTSGSTGQPKGVmvRHRALT-----NFVCSIARQPGMLARDRLL------SVTTFSFDIFGLELyvplarGASMLLASR 728
Cdd:PRK12406   158 IYTSGTTGHPKGV--RRAAPTpeqaaAAEQMRALIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQPR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  729 eqaQDPEALLDLVERQGVTVLQATPATWRMLCD-----SERVDL--LRGCTLlcGGEALAEDLAARMrglsASTW----- 796
Cdd:PRK12406   230 ---FDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevRAKYDVssLRHVIH--AAAPCPADVKRAM----IEWWgpviy 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  797 NLYGPTETTIwsARFRLGEEA--RP-FLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLAR-GYHRRPGLTAErflp 872
Cdd:PRK12406   301 EYYGSTESGA--VTFATSEDAlsHPgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE---- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  873 dpfaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVP 951
Cdd:PRK12406   375 ----IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfGEALMAVVEP 450
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163  952 TEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK12406   451 QPGATLDEA-----DIRAQLKAR----LAGYKVPKHIEIMAELPREDSGKIFKRRL 497
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1874-2152 6.04e-22

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 99.05  E-value: 6.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSLADLDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTTGGRLY 1953
Cdd:COG3433      3 IATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1954 RTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAALRD 2033
Cdd:COG3433     83 DDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAAL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2034 tlrqALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQRDYTAPRS-----ELEQRLAAIWADVLKLG--R 2106
Cdd:COG3433    163 ----AALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletaLTEEELRADVAELLGVDpeE 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163 2107 VGLDDNFFELGGDSIISIQVVSRARQAGIRLAPRDLFLHQTIRGLA 2152
Cdd:COG3433    239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1686-2071 6.44e-22

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 102.93  E-value: 6.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1686 PCL---LLDAEHEWAGYPE--------SDPQSAVGVDNL-AYVIY-TSGSTGKPKGTLLPHGNV-LRLFDATRHWFGFSA 1751
Cdd:cd05928    136 PSLktkLLVSEKSRDGWLNfkellneaSTEHHCVETGSQePMAIYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTA 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DD-AWSLFHSYAFDFSVWEIFGALLHGGrLVIVPYETSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPplA 1830
Cdd:cd05928    216 SDiMWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFP--S 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1831 LRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITETTvhvtyrpLSLADLDGGAASP--IGEPIPDLSWYLLDAGLN 1908
Cdd:cd05928    293 LQHCVTGGEPLNPEVLEKWKAQTG---LDIYEGYGQTETG-------LICANFKGMKIKPgsMGKASPPYDVQIIDDNGN 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 PVPRGCIGELYVggaglaRGYLNRPELSCTRFVADPFSTTG---GRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIE 1985
Cdd:cd05928    363 VLPPGTEGDIGI------RVKPIRPFGLFSGYVDNPEKTAAtirGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIG 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1986 LGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAP---SDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTA 2062
Cdd:cd05928    437 PFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTV 516

                   ....*....
gi 2183974163 2063 NGKLDRRAL 2071
Cdd:cd05928    517 TGKIQRNEL 525
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2174-2600 6.85e-22

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 101.23  E-value: 6.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQMFFE--LDIPRRqHWNQSVLlEPGQALDGTLLETALQALLAHHDALRLGFrledgtwraehrAVEAGEVLLWQ 2251
Cdd:cd19542      3 PCTPMQEGMLLsqLRSPGL-YFNHFVF-DLDSSVDVERLRNAWRQLVQRHDILRTVF------------VESSAEGTFLQ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2252 ----------QSVADgqALEALAEQVQRSLD---LGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAY 2318
Cdd:cd19542     69 vvlksldppiEEVET--DEDSLDALTRDLLDdptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2319 RQlqagqavALPAKTSAFKAWAERLQAHARDGGLEgergYWLAQLEGVST-ELPC--DDREGAQSVRHVRSARTElteea 2395
Cdd:cd19542    147 NG-------QLLPPAPPFSDYISYLQSQSQEESLQ----YWRKYLQGASPcAFPSlsPKRPAERSLSSTRRSLAK----- 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2396 trrlLQEAPAAYRTQVNDLLLTALARVIGRWTGQAD----TLIqlegHGREELFEDIDltRTVGWFTSLFPLRLS----- 2466
Cdd:cd19542    211 ----LEAFCASLGVTLASLFQAAWALVLARYTGSRDvvfgYVV----SGRDLPVPGID--DIVGPCINTLPVRVKldpdw 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2467 PVAELgasIKRIKEQ-LRAIPHKGLGFGAL-RYLGSAEDRAALAALpspritFNYLGQFD-GSFSADSSALFRPSADAAG 2543
Cdd:cd19542    281 TVLDL---LRQLQQQyLRSLPHQHLSLREIqRALGLWPSGTLFNTL------VSYQNFEAsPESELSGSSVFELSAAEDP 351
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2544 SERDsdapldnwLSLNGQVYAGRLGIDWSFSAARFSEASILRLADAYRDELLALIEH 2600
Cdd:cd19542    352 TEYP--------VAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
524-1017 1.55e-21

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 102.25  E-value: 1.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLF-GEE-----RLSYAELNALANRLAWRLREEGVGSDVLVGIALergvPM----VVALLA---------VLKAG 584
Cdd:cd05966     67 GDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYM----PMipelVIAMLAcarigavhsVVFAG 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  585 gayvpldpqYPADRLQYMIDDSGLRLLLSQQSVLAR-------------LPQSDGLQSLL--------------LD-DLE 636
Cdd:cd05966    143 ---------FSAESLADRINDAQCKLVITADGGYRGgkviplkeivdeaLEKCPSVEKVLvvkrtggevpmtegRDlWWH 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  637 RLVHGYPAENPdlPEAPDSL--CYAIYTSGSTGQPKGVMvrHRaltnfvcsiarQPGMLardrLLSVTTFSF-------D 707
Cdd:cd05966    214 DLMAKQSPECE--PEWMDSEdpLFILYTSGSTGKPKGVV--HT-----------TGGYL----LYAATTFKYvfdyhpdD 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  708 IFGLE------------LYVPLARGASMLLasREQAQ---DPEALLDLVERQGVTVLQATPATWRMLC---DS--ERVDL 767
Cdd:cd05966    275 IYWCTadigwitghsyiVYGPLANGATTVM--FEGTPtypDPGRYWDIVEKHKVTIFYTAPTAIRALMkfgDEwvKKHDL 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  768 --LRgctlLCG--GEALAE-------DLAARMRGLSASTW-----------NLYGPTETTIWSArfrlgeeARPFLGGPL 825
Cdd:cd05966    353 ssLR----VLGsvGEPINPeawmwyyEVIGKERCPIVDTWwqtetggimitPLPGATPLKPGSA-------TRPFFGIEP 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  826 EntalyILDSEMNPCPPGVAGELLIGGD--GLARGYHRRPgltaERFLPDPFAADgSRLYRTGDLARYRADGVIEYLGRI 903
Cdd:cd05966    422 A-----ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKF-PGYYFTGDGARRDEDGYYWITGRV 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  904 DHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAAlvdaesARQQELRSALKNSLLAVLPDY 982
Cdd:cd05966    492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPhDIKGEAIYAFVTLKDGE------EPSDELRKELRKHVRKEIGPI 565
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2183974163  983 MVPAHMLLLENLPLTPNGKINRKAL--------PLPDASAVRD 1017
Cdd:cd05966    566 ATPDKIQFVPGLPKTRSGKIMRRILrkiaageeELGDTSTLAD 608
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3099-3183 1.58e-21

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 101.19  E-value: 1.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd12114     81 ADAGA 85
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
509-1004 1.71e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 101.77  E-value: 1.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  509 GQGVHRLFEAQAGLTPDAPALLFGEE--RLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGA 586
Cdd:PRK12583    17 TQTIGDAFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  587 YVPLDPQYPADRLQYMIDDSGLRLLLSQQS---------VLARLP-----QSDGLQSLLLDDLERLVHGYPAENP----- 647
Cdd:PRK12583    97 LVNINPAYRASELEYALGQSGVRWVICADAfktsdyhamLQELLPglaegQPGALACERLPELRGVVSLAPAPPPgflaw 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  648 -------------DLPEAPDSLCY--AI---YTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIF 709
Cdd:PRK12583   177 helqargetvsreALAERQASLDRddPIniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL-YHCF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  710 GLEL--YVPLARGASMLLASreQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLLCGGEALAEDLAAR 787
Cdd:PRK12583   256 GMVLanLGCMTVGACLVYPN--EAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEV 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  788 MRGL-----SASTWNLYGPTET---TIWSARFRLGEEARPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGY 859
Cdd:PRK12583   334 MRRVmdemhMAEVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  860 HRRPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP- 938
Cdd:PRK12583   414 WNNPEATAE-------SIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPd 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163  939 GVAGPTLVAYLVpteaaLVDAESARQQELRSALKnsllAVLPDYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:PRK12583   487 EKYGEEIVAWVR-----LHPGHAASEEELREFCK----ARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
536-1007 1.96e-21

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 100.87  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAEL--NALAnrLAWRLREEGVGSDvLVGIALERGVPMVVALLAVLKAGgaYVPLDPQYPA--DRLQYMIDDSGLRLL 611
Cdd:cd05909      8 LTYRKLltGAIA--LARKLAKMTKEGE-NVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  612 LSQQSVLARLPQSDGL------QSLLLDDLER----------LVHGY-PAENPDL-----PEAPDSLCYAIYTSGSTGQP 669
Cdd:cd05909     83 LTSKQFIEKLKLHHLFdveydaRIVYLEDLRAkiskadkckaFLAGKfPPKWLLRifgvaPVQPDDPAVILFTSGSEGLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  670 KGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLE--LYVPLARGASMLLASreQAQDPEALLDLVERQGVT 747
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF-FHSFGLTgcLWLPLLSGIKVVFHP--NPLDYKKIPELIYDKKAT 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  748 VLQATPATWRMLCDSERVDLLRGCTL-LCGGEALAEDLA---------ARMRGlsastwnlYGPTET------TIWSARF 811
Cdd:cd05909    240 ILLGTPTFLRGYARAAHPEDFSSLRLvVAGAEKLKDTLRqefqekfgiRILEG--------YGTTECspvisvNTPQSPN 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  812 RLGEearpfLGGPLENTALYILDSE-MNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGDLAR 890
Cdd:cd05909    312 KEGT-----VGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF------GDG--WYDTGDIGK 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  891 YRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLE--QDSVREAVVVAQPGVAGPTLVAYLVPTEAAlvdaesarQQELR 968
Cdd:cd05909    379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEilPEDNEVAVVSVPDGRKGEKIVLLTTTTDTD--------PSSLN 450
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2183974163  969 SALKNSLLAVLpdyMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05909    451 DILKNAGISNL---AKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
508-1007 3.18e-21

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 101.05  E-value: 3.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  508 AGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEgvgSDVLVGIALERGVPMV----VALLAVLKA 583
Cdd:PRK12492    22 AYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQH---TDLVPGDRIAVQMPNVlqypIAVFGALRA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  584 GGAYVPLDPQYPADRLQYMIDDSGLRLLL-------SQQSVLAR--------------LPQSDG-LQSLLLDDLERLVHG 641
Cdd:PRK12492    99 GLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgkLVQEVLPDtgieylieakmgdlLPAAKGwLVNTVVDKVKKMVPA 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  642 YpaenpDLPEAP---------------------DSLCYAIYTSGSTGQPKGVMVRHralTNFVCSIARQPGMLARDRLLS 700
Cdd:PRK12492   179 Y-----HLPQAVpfkqalrqgrglslkpvpvglDDIAVLQYTGGTTGLAKGAMLTH---GNLVANMLQVRACLSQLGPDG 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  701 VTTF----SFDIFGLELYVPLARGAS---MLLASREQA-----QDPEALLDLVERQGVTVLQATPATWRMLCDS---ERV 765
Cdd:PRK12492   251 QPLMkegqEVMIAPLPLYHIYAFTANcmcMMVSGNHNVlitnpRDIPGFIKELGKWRFSALLGLNTLFVALMDHpgfKDL 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  766 DLLRGCTLLCGGEALAEDLAARMRGLSASTW-NLYGPTETTIWSARFRLGEEAR-PFLGGPLENTALYILDSEMNPCPPG 843
Cdd:PRK12492   331 DFSALKLTNSGGTALVKATAERWEQLTGCTIvEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDGNELPLG 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  844 VAGELLIGGDGLARGYHRRPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRL 923
Cdd:PRK12492   411 ERGELCIKGPQVMKGYWQQPEATAE-------ALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  924 LEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALvdaesaRQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKI 1002
Cdd:PRK12492   484 MAHPKVANCAAIGVPDeRSGEAVKLFVVARDPGL------SVEELKAYCKENFTG----YKVPKHIVLRDSLPMTPVGKI 553

                   ....*
gi 2183974163 1003 NRKAL 1007
Cdd:PRK12492   554 LRREL 558
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1716-2067 5.06e-21

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 96.99  E-value: 5.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1716 VIYTSGSTGKPKGTLLPHGNVL----RLFDATRHWFGFSADDAWSLFHSYAFDFSVweifGALLHGGRLVIVPyetSRSP 1791
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLaqalVLAVLQAIDEGTVFLNSGPLFHIGTLMFTL----ATFHAGGTNVFVR---RVDA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1792 EDFLRLLCRERVTVLNQTPSAFKQLMQVACAGqevpPLALRHVVFGGEALEVQALRP-WFERFGdRAPRLvnmYGITETT 1870
Cdd:cd17636     78 EEVLELIEAERCTHAFLLPPTIDQIVELNADG----LYDLSSLRSSPAAPEWNDMATvDTSPWG-RKPGG---YGQTEVM 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1871 VHVTYrplslADLDGGAASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVadpfsttgG 1950
Cdd:cd17636    150 GLATF-----AALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--------G 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1951 RLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVT--QAAPSDP 2028
Cdd:cd17636    217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkPGASVTE 296
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2183974163 2029 AALRDTLRQALkASLPEhmvPAHLLFLERLPLTANGKLD 2067
Cdd:cd17636    297 AELIEHCRARI-ASYKK---PKSVEFADALPRTAGGADD 331
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
534-1007 7.53e-21

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 99.47  E-value: 7.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  534 ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL- 612
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 -------SQQSVLArlpqsDGLQSLLL---------DDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRH 676
Cdd:cd05932     85 gklddwkAMAPGVP-----EGLISISLpppsaancqYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  677 RALTNFVCSIARQPGMLARDRLLSvttfsfdifglelYVPLARGASML------LASREQAQDPEALLDLVE---RQGVT 747
Cdd:cd05932    160 GSFAWAAQAGIEHIGTEENDRMLS-------------YLPLAHVTERVfveggsLYGGVLVAFAESLDTFVEdvqRARPT 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  748 VLQATPATWRML-------CDSERVDLL--------------------RGCTLLCGGEA-LAEDLAARMRGLSASTWNLY 799
Cdd:cd05932    227 LFFSVPRLWTKFqqgvqdkIPQQKLNLLlkipvvnslvkrkvlkglglDQCRLAGCGSApVPPALLEWYRSLGLNILEAY 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  800 GPTETTIWSARFRLGEEARPFLGGPLENTALYILDSemnpcppgvaGELLIGGDGLARGYHRRPGLTAERFLPDPFaadg 879
Cdd:cd05932    307 GMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF---- 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  880 srlYRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIETRLLEQDSVrEAVVVAQPGVAGPtlVAYLVPTEAALVD 958
Cdd:cd05932    373 ---LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAP--LALVVLSEEARLR 446
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  959 AESARQQELRSALKNSLLAVLPDymVPAHMLL-----------LENLPLTPNGKINRKAL 1007
Cdd:cd05932    447 ADAFARAELEASLRAHLARVNST--LDSHEQLagivvvkdpwsIDNGILTPTLKIKRNVL 504
PRK12316 PRK12316
peptide synthase; Provisional
56-521 7.56e-21

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 101.96  E-value: 7.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   56 RQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDeqlDGFRQQVLASvDVPVPVTLAGDDD 135
Cdd:PRK12316  1107 QRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREE---DGGWQQAYAA-PQAGEVLWQRQAA 1182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  136 AQAQIRAFVEsETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYgarrqgiEATLPDLPI 215
Cdd:PRK12316  1183 SEEELLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAY-------ADLDADLPA 1254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  216 QYADYAIWQRHWLE-AGERERQLEYWMARLGGGQSvlELPTDRQRPALPSYRGARHELQLPQALGRQLQALAQRE-GTTL 293
Cdd:PRK12316  1255 RTSSYQAWARRLHEhAGARAEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAyRTQV 1332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  294 FMLLLASFQALLHRYSGQDEIRVGVPVANR----NRVETERLIGFFVNTQVLR----ADLDAQMPFLDllQQTRVA---A 362
Cdd:PRK12316  1333 NDLLLTALARVTCRWSGQASVLVQLEGHGRedlfEDIDLSRTVGWFTSLFPVRltpaADLGESIKAIK--EQLRAVpdkG 1410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  363 LGAQSHQDLPFEQLVEAL----QPERSLSHSPLFQAMYNHQNLGSAGRQSL-AAQLPG------LSVEDLSWGAHsaqfd 431
Cdd:PRK12316  1411 IGYGLLRYLAGEEAAARLaalpQPRITFNYLGQFDRQFDEAALFVPATESAgAAQDPCaplanwLSIEGQVYGGE----- 1485
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  432 ltldtyeseqgVHAEFTYATDLFEAATVERLARHWRNLLEAVV----AEPRRRL--GDLPLldAEERATLLQRSRLPASE 505
Cdd:PRK12316  1486 -----------LSLHWSFSREMFAEATVQRLADDYARELQALIehccDERNRGVtpSDFPL--AGLSQAQLDALPLPAGE 1552
                          490       500
                   ....*....|....*....|....*
gi 2183974163  506 Y-------PAGQGV--HRLFEAQAG 521
Cdd:PRK12316  1553 IadiyplsPMQQGMlfHSLYEQEAG 1577
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2638-2977 7.96e-21

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 98.21  E-value: 7.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2638 YPLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFlwQGALEKPLQLVRKRVEVPFS 2716
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGpVDLAVLERALRQVIAEAETLRLRF--TEEEGEPYQWIDPYTPVPIR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2717 VHDWRDRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRG----- 2791
Cdd:cd19533     80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAllkgr 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2792 ETPSRSDGRYRDYI-AWLQRQDAGRTE---AFWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRyrqLDVTTSQRLAEFAR 2867
Cdd:cd19533    160 PAPPAPFGSFLDLVeEEQAYRQSERFErdrAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAE---LPPELTRTLLEAAE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2868 EQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAelRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGENLAL 2947
Cdd:cd19533    237 AHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLG--AAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSL 314
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2183974163 2948 REFEHTPLYDIQRWAGQVGEA--LFD---NILVFE 2977
Cdd:cd19533    315 LRHQRYRYEDLRRDLGLTGELhpLFGptvNYMPFD 349
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2202-2487 8.13e-21

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 98.33  E-value: 8.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2202 GQALDGTLLETALQALLAHHDALRLGFrLEDGTWRaehraVEAgEVLLWQQSVADG---------QALEALAEQV-QRSL 2271
Cdd:cd19535     34 GEDLDPDRLERAWNKLIARHPMLRAVF-LDDGTQQ-----ILP-EVPWYGITVHDLrglseeeaeAALEELRERLsHRVL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2272 DLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAgqavALPAKTSAFKAWAERLQAHaRDGG 2351
Cdd:cd19535    107 DVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQAL-RETA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2352 LEGERGYWLAQLEgvstELP--------CDdregAQSVRHVRSARTELT-EEATRRLLQEAPAAYRTQVNDLLLTALARV 2422
Cdd:cd19535    182 YERARAYWQERLP----TLPpapqlplaKD----PEEIKEPRFTRREHRlSAEQWQRLKERARQHGVTPSMVLLTAYAEV 253
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2423 IGRWTGQADTLIQLEGHGREELFEDIDltRTVGWFTSLFPL--RLSPVAELGASIKRIKEQL-RAIPH 2487
Cdd:cd19535    254 LARWSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSLLLLevDGSEGQSFLERARRLQQQLwEDLDH 319
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
506-1007 1.03e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 98.93  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  506 YPagqGVHrlfeaqAGLTPDAPALLFGE--ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKA 583
Cdd:PRK13390     2 YP---GTH------AQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  584 GGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVlarlpqsDGLQSLLLDDLE-RLVHG------------YPAENPDLP 650
Cdd:PRK13390    73 GLYITAINHHLTAPEADYIVGDSGARVLVASAAL-------DGLAAKVGADLPlRLSFGgeidgfgsfeaaLAGAGPRLT 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  651 EAPdslCYAI--YTSGSTGQPKGVM--VRHRALTnfvcsiarQPGmlarDRLLSVTTFSFDIFGLELY---------VPL 717
Cdd:PRK13390   146 EQP---CGAVmlYSSGTTGFPKGIQpdLPGRDVD--------APG----DPIVAIARAFYDISESDIYyssapiyhaAPL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  718 -------ARGASMLLASREQAQDPealLDLVERQGVTVLQATPATW-RML-CDSE---RVDL--LRGcTLLCGGEALAED 783
Cdd:PRK13390   211 rwcsmvhALGGTVVLAKRFDAQAT---LGHVERYRITVTQMVPTMFvRLLkLDADvrtRYDVssLRA-VIHAAAPCPVDV 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  784 LAARMRGLSASTWNLYGPTE----TTIWSARF--RLGEEARPFLGgplentALYILDSEMNPCPPGVAGELLIGGDGLAR 857
Cdd:PRK13390   287 KHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWlaHPGSVGRSVLG------DLHICDDDGNELPAGRIGTVYFERDRLPF 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  858 GYHRRPGLTAERFLP-DPFAADgsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVA 936
Cdd:PRK13390   361 RYLNDPEKTAAAQHPaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  937 QPGVAGPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK13390   435 VPDPEMGEQVKAVIQLVEGIRGSD-----ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1587-2068 1.26e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 98.28  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1587 VVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGI 1666
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1667 RLLLTqraarerlplgeglpcllldaehewagypeSDPqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW 1746
Cdd:cd05914     81 KAIFV------------------------------SDE------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 FGFSADDA----WSLFHSY--AFDFSVweifgALLHGGRLVIVpyetSRSPEDFLRLLCRERVTV--------------- 1805
Cdd:cd05914    125 VLLGKGDKilsiLPLHHIYplTFTLLL-----PLLNGAHVVFL----DKIPSAKIIALAFAQVTPtlgvpvplviekifk 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1806 ---LNQTPSA-FKQLMQVACAGQEVPPLALRHVV--FGGEALEV----QALRPWFERFgdraprLVNM-------YGITE 1868
Cdd:cd05914    196 mdiIPKLTLKkFKFKLAKKINNRKIRKLAFKKVHeaFGGNIKEFviggAKINPDVEEF------LRTIgfpytigYGMTE 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1869 TTVHVTYRPLSLADLDGgaaspIGEPIPDLSWYLLDaglnPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFstt 1948
Cdd:cd05914    270 TAPIISYSPPNRIRLGS-----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--- 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1949 ggrlYRTGDLARYRCDGVVEYVGRIDHQ-VKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGY-----VVTQ 2022
Cdd:cd05914    338 ----FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDpdfldVKAL 413
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2183974163 2023 AAPSDPAALRDTLRQALKASLPEH-MVPAHLLFLERLPLTANGKLDR 2068
Cdd:cd05914    414 KQRNIIDAIKWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1592-2046 1.56e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 97.92  E-value: 1.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1592 RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYpsdrlgymiedsGIRLLLT 1671
Cdd:cd05910      1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGM------------GRKNLKQ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1672 qraarerlplgeglpCLLldaehewagypESDPQSAVGV---DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFG 1748
Cdd:cd05910     69 ---------------CLQ-----------EAEPDAFIGIpkaDEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1749 FSADDAwslfhsyafD---FSVWEIFGALLhGGRLVIVPYETSR----SPEDFLRLLCRERVTVLNQTPSAFKQLMQvAC 1821
Cdd:cd05910    123 IRPGEV---------DlatFPLFALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVAR-YC 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 AGQEVPPLALRHVVFGGEALEVqALRPWFERFGDRAPRLVNMYGITE--------------TTVHVTyrplsladlDGGA 1887
Cdd:cd05910    192 AQHGITLPSLRRVLSAGAPVPI-ALAARLRKMLSDEAEILTPYGATEalpvssigsrellaTTTAAT---------SGGA 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1888 ASPIGEPIPDLSWYLLDAGLNP---------VPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPfstTGGRLYRTGDL 1958
Cdd:cd05910    262 GTCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDL 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1959 ARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAAlrdTLRQA 2038
Cdd:cd05910    339 GYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRA---RLEQE 415

                   ....*...
gi 2183974163 2039 LKASLPEH 2046
Cdd:cd05910    416 LRALAKDY 423
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1593-2071 1.72e-20

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 98.76  E-value: 1.72e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1593 ALDYGELNLRANRLAHRLIE-LGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT 1671
Cdd:PLN02574    66 SISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1672 QRAARERLPlGEGLPCLLL-------DAEHEWAGY-------PESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVL 1737
Cdd:PLN02574   146 SPENVEKLS-PLGVPVIGVpenydfdSKRIEFPKFyelikedFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1738 RL------FDATRhwFGFSADD-----AWSLFHSYAFDFSVWeifgALLHGGRLVIVPYETSRSpeDFLRLLCRERVTVL 1806
Cdd:PLN02574   225 AMvelfvrFEASQ--YEYPGSDnvylaALPMFHIYGLSLFVV----GLLSLGSTIVVMRRFDAS--DMVKVIDRFKVTHF 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1807 NQTPSAFKQLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERFgdraPR--LVNMYGITETTVhVTYRPLSLADLD 1884
Cdd:PLN02574   297 PVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL----PHvdFIQGYGMTESTA-VGTRGFNTEKLS 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1885 ggAASPIGEPIPDLSWYLLD---AGLNPvPRGCiGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARY 1961
Cdd:PLN02574   372 --KYSSVGLLAPNMQAKVVDwstGCLLP-PGNC-GELWIQGPGVMKGYLNNPKATQSTIDKDGW-------LRTGDIAYF 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1962 RCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQL-VGYVVTQAApsdpaalrDTLRQALK 2040
Cdd:PLN02574   441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIpVAFVVRRQG--------STLSQEAV 512
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 2183974163 2041 ASLPEHMVPAH-----LLFLERLPLTANGKLDRRAL 2071
Cdd:PLN02574   513 INYVAKQVAPYkkvrkVVFVQSIPKSPAGKILRREL 548
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1121-1533 2.06e-20

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 96.94  E-value: 2.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1121 QWFIWRLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGAPRQVIHPtlpiaIEERRPPVAGEDL 1200
Cdd:cd19534      9 RWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG-----DVEELFRLEVVDL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1201 KGLVE--------TEAHRPFDLQRGPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYAALRHDQPPALAE 1272
Cdd:cd19534     84 SSLAQaaaiealaAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1273 LPiQYADFAAWQRQWMDGGERERQLDYWVSRLGgeQPLLELPSDRPRPQQQShrgRRIGIPLPAELAEALRRLAQAEQGT 1352
Cdd:cd19534    164 KT-SFQTWAELLAEYAQSPALLEELAYWRELPA--ADYWGLPKDPEQTYGDA---RTVSFTLDEEETEALLQEANAAYRT 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1353 LFM-LLLASFQALLHRYSGQNDIRV-----GvpianrnREE-TEGL-----IGFFVNTQVLRAELDGQLPFRELLRQVRQ 1420
Cdd:cd19534    238 EINdLLLAALALAFQDWTGRAPPAIfleghG-------REEiDPGLdlsrtVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1421 AvVEAQGHQDLPFEQLVDALQPERS-LSHAPLFQVMYN----HQRDDHRGSRFASLGELEVEDLAWDVQ-TAQFDLTldt 1494
Cdd:cd19534    311 Q-LRRIPNKGIGYGILRYLTPEGTKrLAFHPQPEISFNylgqFDQGERDDALFVSAVGGGGSDIGPDTPrFALLDIN--- 386
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2183974163 1495 yeSS--NG-LLAELTYATDLFDASSAERIAGHWLNLLRSIVA 1533
Cdd:cd19534    387 --AVveGGqLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1711-2069 2.45e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 95.91  E-value: 2.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLaYVIYTSGSTGKPKGTLLPHGNVLR-LFDATRHWFGFSADDAWS-----------------LFHSYafdfSVWEIFG 1772
Cdd:cd05924      4 DDL-YILYTGGTTGMPKGVMWRQEDIFRmLMGGADFGTGEFTPSEDAhkaaaaaagtvmfpappLMHGT----GSWTAFG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1773 ALLHGGRLVIVPYETsrSPEDFLRLLCRERVTVLNQTPSAF-KQLMQVACAGQEVPPLALRHVVFGGEAL--EVQalrpw 1849
Cdd:cd05924     79 GLLGGQTVVLPDDRF--DPEEVWRTIEKHKVTSMTIVGDAMaRPLIDALRDAGPYDLSSLFAISSGGALLspEVK----- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1850 fERFGDRAPR--LVNMYGITET----TVHVTYRPLSladldggaASPIGEPIPDLSwyLLDAGLNPVPRGCIGELYVGGA 1923
Cdd:cd05924    152 -QGLLELVPNitLVDAFGSSETgftgSGHSAGSGPE--------TGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIARR 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1924 GL-ARGYLNRPELSctrfvADPFSTTGG-RLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE 2001
Cdd:cd05924    221 GHiPLGYYGDEAKT-----AETFPEVDGvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYD 295
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2002 AVV--LPHEGPGatQLVGYVVTQAAPSDP--AALRDTLRQalkaSLPEHMVPAHLLFLERLPLTANGKLDRR 2069
Cdd:cd05924    296 VLVvgRPDERWG--QEVVAVVQLREGAGVdlEELREHCRT----RIARYKLPKQVVFVDEIERSPAGKADYR 361
PRK13382 PRK13382
bile acid CoA ligase;
485-1010 2.71e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 97.91  E-value: 2.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  485 PLLDAEERATLLQRSRLPASEYP------------AGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRL 552
Cdd:PRK13382     6 RLRDTLGLIATLRRAGLIAPMRPdrylrivaamrrEGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAAL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  553 REEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQ--------- 623
Cdd:PRK13382    86 QALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRaladcpqat 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  624 -----SDGLQSLLLddlERLVHGYPAENPdlPEAPDSLCYAIYTSGSTGQPKGVmvRHRALTNF--VCSIARQPGMLARD 696
Cdd:PRK13382   166 rivawTDEDHDLTV---EVLIAAHAGQRP--EPTGRKGRVILLTSGTTGTPKGA--RRSGPGGIgtLKAILDRTPWRAEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  697 RLLSVTTFsFDIFGLELYVPLARGASMLLASREQaqDPEALLDLVERQGVTVLQATPATWRMLCD--SERVDLLRGCTL- 773
Cdd:PRK13382   239 PTVIVAPM-FHAWGFSQLVLAASLACTIVTRRRF--DPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNRYSGRSLr 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  774 --LCGGEALAEDLA-ARMRGLSASTWNLYGPTE----TTIWSARFRlgeeARPFLGG-PLENTALYILDSEMNPCPPGVA 845
Cdd:PRK13382   316 faAASGSRMRPDVViAFMDQFGDVIYNNYNATEagmiATATPADLR----AAPDTAGrPAEGTEIRILDQDFREVPTGEV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  846 GELLIGGDGLARGYhrRPGLTAErfLPDPFAAdgsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLE 925
Cdd:PRK13382   392 GTIFVRNDTQFDGY--TSGSTKD--FHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLAT 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  926 QDSVREAVVVaqpGVA----GPTLVAYLVPTEAAlvdaeSARQQELRSALKNSLlavlPDYMVPAHMLLLENLPLTPNGK 1001
Cdd:PRK13382   461 HPDVAEAAVI---GVDdeqyGQRLAAFVVLKPGA-----SATPETLKQHVRDNL----ANYKVPRDIVVLDELPRGATGK 528

                   ....*....
gi 2183974163 1002 INRKALPLP 1010
Cdd:PRK13382   529 ILRRELQAR 537
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1559-2071 3.70e-20

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 97.78  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1559 PGPQDFTPASCLHRLIE---RQAAERPratAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGL 1635
Cdd:PRK07059    14 PAEIDASQYPSLADLLEesfRQYADRP---AFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAI 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1636 LAILKAGGAYVPLDPRYPSDRLGYMIEDSG---IRLL------LTQRAARERLP------LGE--GLPCLLL-------- 1690
Cdd:PRK07059    91 AAVLRAGYVVVNVNPLYTPRELEHQLKDSGaeaIVVLenfattVQQVLAKTAVKhvvvasMGDllGFKGHIVnfvvrrvk 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1691 ---------------DAEHEWAGYPESDPqsAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLR-----------LFDATR 1744
Cdd:PRK07059   171 kmvpawslpghvrfnDALAEGARQTFKPV--KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmeawlqpAFEKKP 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1745 HWFGFSADDAWSLFHSYAFdfSVWEIFGALLhGGRLVIVPyetsrSPED---FLRLLCRERVTVLNQTPSAFKQLMQVAc 1821
Cdd:PRK07059   249 RPDQLNFVCALPLYHIFAL--TVCGLLGMRT-GGRNILIP-----NPRDipgFIKELKKYQVHIFPAVNTLYNALLNNP- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1822 agqEVPPLALRHVVF---GGEALEVQALRPWFERFGdrAPrLVNMYGITETTVHVTYRPLSLADLDGgaasPIGEPIPDL 1898
Cdd:PRK07059   320 ---DFDKLDFSKLIVangGGMAVQRPVAERWLEMTG--CP-ITEGYGLSETSPVATCNPVDATEFSG----TIGLPLPST 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1899 SWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRIDHQVK 1978
Cdd:PRK07059   390 EVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMIL 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1979 IRGFRIELGEIEARLLAQPGVAE--AVVLPHEGPG-ATQLvgYVVTQaapsDPAALRDTLRQALKASLPEHMVPAHLLFL 2055
Cdd:PRK07059   463 VSGFNVYPNEIEEVVASHPGVLEvaAVGVPDEHSGeAVKL--FVVKK----DPALTEEDVKAFCKERLTNYKRPKFVEFR 536
                          570
                   ....*....|....*.
gi 2183974163 2056 ERLPLTANGKLDRRAL 2071
Cdd:PRK07059   537 TELPKTNVGKILRREL 552
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
500-1008 4.16e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 96.99  E-value: 4.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  500 RLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLA 579
Cdd:PRK13383    25 RLLREASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  580 VLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLPQSDglQSLLLDDlerlvhgyPA-----ENPDLPEAPD 654
Cdd:PRK13383   105 VGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGAD--DAVAVID--------PAtagaeESGGRPAVAA 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIArqpgMLARDRL-----LSVTTFSFDIFGL-ELYVPLARGASMLLASR 728
Cdd:PRK13383   175 PGRIVLLTSGTTGKPKGVPRAPQLRSAVGVWVT----ILDRTRLrtgsrISVAMPMFHGLGLgMLMLTIALGGTVLTHRH 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  729 EQAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGC--TLLCGGEALAEDLAAR-MRGLSASTWNLYGPTETT 805
Cdd:PRK13383   251 FDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQlrVVMSSGDRLDPTLGQRfMDTYGDILYNGYGSTEVG 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWS----ARFRLGEEArpfLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTaerflpdpfAADGsr 881
Cdd:PRK13383   331 IGAlatpADLRDAPET---VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKA---------VVDG-- 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  882 LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAE 960
Cdd:PRK13383   397 MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVVLHPGSGVDAA 476
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163  961 sarqqELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGKINRKALP 1008
Cdd:PRK13383   477 -----QLRDYLKDR----VSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1711-2071 5.25e-20

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 97.05  E-value: 5.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVL-RLFDATRHWFGFSADD------AWSLFHSYAFDFSvweifgALLH---GGRL 1780
Cdd:PRK08974   206 EDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPLLHPGkelvvtALPLYHIFALTVN------CLLFielGGQN 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1781 VIVPyetsrSPED---FLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDRa 1857
Cdd:PRK08974   280 LLIT-----NPRDipgFVKELKKYPFTAITGVNTLFNALLNNE-EFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQY- 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1858 prLVNMYGITETTVHVTYRPLSLADLDGGaaspIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPElSC 1937
Cdd:PRK08974   353 --LLEGYGLTECSPLVSVNPYDLDYYSGS----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPE-AT 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1938 TRFVADpfsttgGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE--AVVLPHEGPGATQL 2015
Cdd:PRK08974   426 DEVIKD------GWL-ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvaAVGVPSEVSGEAVK 498
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2016 VgYVVtqaaPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK08974   499 I-FVV----KKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
660-1004 6.59e-20

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 93.87  E-value: 6.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 IYTSGSTGQPKGVMVRHRaltNFVCS---IARQPGMLARDRLLSVTTFsFDIFGLEL-YVPLARGASMLLASReqaQDPE 735
Cdd:cd17637      6 IHTAAVAGRPRGAVLSHG---NLIAAnlqLIHAMGLTEADVYLNMLPL-FHIAGLNLaLATFHAGGANVVMEK---FDPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  736 ALLDLVERQGVTVLQATPATWRMLCDSER---VDL--LRGCTllcGGEAlaEDLAARMRGLSAST-WNLYGPTET----T 805
Cdd:cd17637     79 EALELIEEEKVTLMGSFPPILSNLLDAAEksgVDLssLRHVL---GLDA--PETIQRFEETTGATfWSLYGQTETsglvT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWSARFRLGEEARPflgGPLENTAlyILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRT 885
Cdd:cd17637    154 LSPYRERPGSAGRP---GPLVRVR--IVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF------RNG--WHHT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  886 GDLARYRADGVIEYLGRIDHQ--VKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGP----------TLVAYLVPTE 953
Cdd:cd17637    221 GDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI---GVPDPkwgegikavcVLKPGATLTA 297
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  954 AALVDAESARqqelrsalknsllavLPDYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd17637    298 DELIEFVGSR---------------IARYKKPRYVVFVEALPKTADGSIDR 333
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2639-2922 1.43e-19

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 94.41  E-value: 1.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2639 PLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFlwQGALEKPLQLVR--KRVEVPF 2715
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGaLDVDALRAALADVVARHESLRTVF--PEDDGGPYQVVLpaAEARPDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2716 SVHDwrdraDLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRgetpS 2795
Cdd:cd19540     81 TVVD-----VTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYA----A 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2796 RSDGR----------YRDYIAWlQRQ----------DAGRTEAFWKQRLQRLGEPTLLV-----PAFAHGvRGAEGHADr 2850
Cdd:cd19540    152 RRAGRapdwaplpvqYADYALW-QREllgdeddpdsLAARQLAYWRETLAGLPEELELPtdrprPAVASY-RGGTVEFT- 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2851 yrqLDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLP 2922
Cdd:cd19540    229 ---IDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLV 295
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1149-1431 1.82e-19

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 94.09  E-value: 1.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1149 DALQGALDLLVQRHETLRTTFVEhDGapRQVIHPTLPiaieerRPPVAGEDLKGLVETEA------------HRPFDLQR 1216
Cdd:cd19535     40 DRLERAWNKLIARHPMLRAVFLD-DG--TQQILPEVP------WYGITVHDLRGLSEEEAeaaleelrerlsHRVLDVER 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1217 GPLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDELIRVYaalrHDQPPALAELPIQYADFAAWQRQwMDGGERERQ 1296
Cdd:cd19535    111 GPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQA-LRETAYERA 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1297 LDYWVSRL----GGEQ-PLLELPSDRPRPQQQSHRGRrigipLPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQ 1371
Cdd:cd19535    186 RAYWQERLptlpPAPQlPLAKDPEEIKEPRFTRREHR-----LSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 1372 NDIRVGVPIANRNR--EETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQavveaQGHQDL 1431
Cdd:cd19535    261 PRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQ-----QLWEDL 317
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1712-2066 2.08e-19

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 92.18  E-value: 2.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1712 NLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFHSYAFDFSvweIFGALLHGGrlVIVPYET 1787
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYliinPFFHTFGYKAG---IVACLLTGA--TVVPVAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1788 SrSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPPLALRHVVFGGEALEVQALRPWFERFGDRAprLVNMYGIT 1867
Cdd:cd17638     76 F-DVDAILEAIERERITVLPGPPTLFQSLLDHP-GRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFET--VLTAYGLT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1868 ETTVHVTYRPLSLADLdggAASPIGEPIPDLSWYLLDAglnpvprgciGELYVGGAGLARGYLNRPELSCTRFVADpfst 1947
Cdd:cd17638    152 EAGVATMCRPGDDAET---VATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDAD---- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1948 tgGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHEGPGAtqlVG--YVVTQa 2023
Cdd:cd17638    215 --GWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgvPDERMGE---VGkaFVVAR- 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2183974163 2024 apsDPAALRDtlrQALKASLPEHM----VPAHLLFLERLPLTANGKL 2066
Cdd:cd17638    288 ---PGVTLTE---EDVIAWCRERLanykVPRFVRFLDELPRNASGKV 328
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
520-935 2.43e-19

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 94.17  E-value: 2.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDvlVGIALeRG---VPMVVALLAVLKAGGAYVPLDPQYPA 596
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEG--SGVAL-RGknsPETLLAYLALLQCGARVLPLNPQLPQ 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  597 DRLQYMIDDSGLRLLLsqqsVLARLPQSDGLQSLLLDdlerlvhgYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRH 676
Cdd:PRK09029    90 PLLEELLPSLTLDFAL----VLEGENTFSALTSLHLQ--------LVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  677 RA-LTNfvcsiarqpgmlARDrLLSVTTFS-----------FDIFGLE-LYVPLARGASMLLasREQAQDPEALldlver 743
Cdd:PRK09029   158 QAhLAS------------AEG-VLSLMPFTaqdswllslplFHVSGQGiVWRWLYAGATLVV--RDKQPLEQAL------ 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  744 QGVT--VLQATPAtWRMLCDSERVDLLRgcTLLCGGEALAEDLAARMRGLSASTWNLYGPTE--TTIWSARfrlgEEARP 819
Cdd:PRK09029   217 AGCThaSLVPTQL-WRLLDNRSEPLSLK--AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEmaSTVCAKR----ADGLA 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 FLGGPLENTALYIldsemnpcppgVAGELLIGGDGLARGYHRRPGLTaerflpdPFA-ADGsrLYRTGDLARYRaDGVIE 898
Cdd:PRK09029   290 GVGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVnDEG--WFATRDRGEWQ-NGELT 348
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2183974163  899 YLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVV 935
Cdd:PRK09029   349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1591-2065 5.05e-19

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 93.19  E-value: 5.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1591 ERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAyvpldprypsdrlGYMIEdsgirllL 1670
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-------------AALIN-------Y 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1671 TQRaarerlplGEGLP-CL-LLDAEHewagypesdpqsaVGVDnLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFG 1748
Cdd:cd05940     61 NLR--------GESLAhCLnVSSAKH-------------LVVD-AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGG 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1749 FSADD----AWSLFHSYAfdfSVWEIFGALLHGGRLVIvpyETSRSPEDFLRLLCRERVTV-----------LNQTPSAF 1813
Cdd:cd05940    119 ALPSDvlytCLPLYHSTA---LIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIfqyigelcrylLNQPPKPT 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLMQVACagqevpplalrhvVFGgealevQALRP--W--F-ERFGDraPRLVNMYGITETTVhvtyrplSLADLDG--- 1885
Cdd:cd05940    193 ERKHKVRM-------------IFG------NGLRPdiWeeFkERFGV--PRIAEFYAATEGNS-------GFINFFGkpg 244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 --GAASPI----------------GEPIPDLSWYLLdaglnPVPRGCIGEL--YVGGAGLARGYLNrPELSCTRFVADPF 1945
Cdd:cd05940    245 aiGRNPSLlrkvaplalvkydlesGEPIRDAEGRCI-----KVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF 318
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1946 StTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGY---VVTQ 2022
Cdd:cd05940    319 K-KGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMaaiVLQP 397
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2183974163 2023 AAPSDPAALRDTLRQAlkasLPEHMVPAHLLFLERLPLTANGK 2065
Cdd:cd05940    398 NEEFDLSALAAHLEKN----LPGYARPLFLRLQPEMEITGTFK 436
PRK08315 PRK08315
AMP-binding domain protein; Validated
514-1002 8.60e-19

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 93.34  E-value: 8.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  514 RLFEAQAGLTPDAPALLFGEE--RLSYAELNALANRLAWRLREEGVGSDVLVGI-ALERgVPMVVALLAVLKAGGAYVPL 590
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIwAPNV-PEWVLTQFATAKIGAILVTI 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  591 DPQYPADRLQYMIDDSGLRLLLSQ------------QSVLARLPQSD--GLQSLLLDDLERLVH---------------- 640
Cdd:PRK08315    99 NPAYRLSELEYALNQSGCKALIAAdgfkdsdyvamlYELAPELATCEpgQLQSARLPELRRVIFlgdekhpgmlnfdell 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  641 --GYPAENPDLPEAPDSL-CY-AI---YTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLEL 713
Cdd:PRK08315   179 alGRAVDDAELAARQATLdPDdPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL-YHCFGMVL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  714 YV--PLARGASMLLASreQAQDPEALLDLVERQGVTVLQATPAtwrM------LCDSERVDL--LRgcTLLCGGEALAED 783
Cdd:PRK08315   258 GNlaCVTHGATMVYPG--EGFDPLATLAAVEEERCTALYGVPT---MfiaeldHPDFARFDLssLR--TGIMAGSPCPIE 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  784 LAAR------MRGLSAStwnlYGPTETTIWSARFRLGEearPF------LGGPLENTALYILDSEMN-PCPPGVAGELLI 850
Cdd:PRK08315   331 VMKRvidkmhMSEVTIA----YGMTETSPVSTQTRTDD---PLekrvttVGRALPHLEVKIVDPETGeTVPRGEQGELCT 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  851 GGDGLARGYHRRPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVkIRGfrielG------EIETRLL 924
Cdd:PRK08315   404 RGYSVMKGYWNDPEKTAE-------AIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLY 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  925 EQDSVREAVVVaqpGVA----GPTLVAYLVPTEAALVDAEsarqqELRSALKNSllavLPDYMVPAHMLLLENLPLTPNG 1000
Cdd:PRK08315   471 THPKIQDVQVV---GVPdekyGEEVCAWIILRPGATLTEE-----DVRDFCRGK----IAHYKIPRYIRFVDEFPMTVTG 538

                   ..
gi 2183974163 1001 KI 1002
Cdd:PRK08315   539 KI 540
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
501-1007 9.49e-19

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 93.16  E-value: 9.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  501 LPASEYPAgqgVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAV 580
Cdd:PRK07059    17 IDASQYPS---LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  581 LKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL-------SQQSVLARLP--------QSD--GLQSLLLDDLERLVH--- 640
Cdd:PRK07059    94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKTAvkhvvvasMGDllGFKGHIVNFVVRRVKkmv 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  641 ------GYPAENPDLPE-----------APDSLCYAIYTSGSTGQPKGVMVRHRaltNFVCSIAR-----QPGMLARDRL 698
Cdd:PRK07059   174 pawslpGHVRFNDALAEgarqtfkpvklGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVLQmeawlQPAFEKKPRP 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  699 LSVTTfsfdIFGLELYVPLARGASMLLASREQA--------QDPEALLDLVERQGVTVLQATPATWRMLCDSE---RVDL 767
Cdd:PRK07059   251 DQLNF----VCALPLYHIFALTVCGLLGMRTGGrnilipnpRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPdfdKLDF 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  768 LRGCTLLCGGEALAEDLAARMR-----------GLSAS----TWNlygPTETTIWSARfrlgeearpfLGGPLENTALYI 832
Cdd:PRK07059   327 SKLIVANGGGMAVQRPVAERWLemtgcpitegyGLSETspvaTCN---PVDATEFSGT----------IGLPLPSTEVSI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  833 LDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGF 912
Cdd:PRK07059   394 RDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGF 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  913 RIELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAYLVPTEAALVDAEsarqqelrsaLKNSLLAVLPDYMVPAHMLLL 991
Cdd:PRK07059   467 NVYPNEIEEVVASHPGVLEVAAVGVPDEhSGEAVKLFVVKKDPALTEED----------VKAFCKERLTNYKRPKFVEFR 536
                          570
                   ....*....|....*.
gi 2183974163  992 ENLPLTPNGKINRKAL 1007
Cdd:PRK07059   537 TELPKTNVGKILRREL 552
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
660-1002 1.01e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 90.25  E-value: 1.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 IYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLE--LYVPLARGASMLlasREQAQDPEAL 737
Cdd:cd17638      6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKagIVACLLTGATVV---PVAVFDVDAI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  738 LDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTL---LCGGEALAEDLAARMRG-LSAST-WNLYGPTETTIwsarfr 812
Cdd:cd17638     82 LEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraaVTGAATVPVELVRRMRSeLGFETvLTAYGLTEAGV------ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  813 lGEEARPflGGPLENTAlyildsemNPCPPGVAG-ELLIGGDG--LARGYHRRPGltaerFLPDPFA------ADGsrLY 883
Cdd:cd17638    156 -ATMCRP--GDDAETVA--------TTCGRACPGfEVRIADDGevLVRGYNVMQG-----YLDDPEAtaeaidADG--WL 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  884 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPTEAALVDA 959
Cdd:cd17638    218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI---GVPdermGEVGKAFVVARPGVTLTE 294
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2183974163  960 ESArqqelrSALKNSLLAvlpDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:cd17638    295 EDV------IAWCRERLA---NYKVPRFVRFLDELPRNASGKV 328
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2639-2921 1.50e-18

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 91.56  E-value: 1.50e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2639 PLSPMQQGMLFHSLYQQNSGDYINQMRLDVEG-LDPQRFREAWQAALDAHEVLRSGFLWQGALekPLQLVR--KRVEVPF 2715
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDGV--PYQLILeeDEATPKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2716 SVhdwrdRADLAEALDALAAGEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYR----G 2791
Cdd:cd19538     81 EI-----KEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRarckG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2792 ETPSRS--DGRYRDYIAWlQRQDAGRTE----------AFWKQRLQRLGEPTLLV-----PAfahgVRGAEGHADRYrQL 2854
Cdd:cd19538    156 EAPELAplPVQYADYALW-QQELLGDESdpdsliarqlAYWKKQLAGLPDEIELPtdyprPA----ESSYEGGTLTF-EI 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2855 DVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTL 2921
Cdd:cd19538    230 DSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTL 294
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1576-2066 1.56e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 91.99  E-value: 1.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAERPRATAVVYGERaLDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSD 1655
Cdd:PRK13390     8 QIAPDRPAVIVAETGEQ-VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1656 RLGYMIEDSGIRLLLTQrAARERLPLGEGLPC-LLLDAEHEWAGYPESDPQSAVGVDNL------AYVIYTSGSTGKPKG 1728
Cdd:PRK13390    87 EADYIVGDSGARVLVAS-AALDGLAAKVGADLpLRLSFGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1729 TL--LPHGNVLRLFDA----TRHWFGFSADDAW----SLFHSYAFDFSvweifgALLH--GGRLVIVpyeTSRSPEDFLR 1796
Cdd:PRK13390   166 IQpdLPGRDVDAPGDPivaiARAFYDISESDIYyssaPIYHAAPLRWC------SMVHalGGTVVLA---KRFDAQATLG 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1797 LLCRERVTVLNQTPSAFKQLMQVAC---AGQEVPplALRHVVFGGEALEV---QALRPWFerfgdrAPRLVNMYGITEtt 1870
Cdd:PRK13390   237 HVERYRITVTQMVPTMFVRLLKLDAdvrTRYDVS--SLRAVIHAAAPCPVdvkHAMIDWL------GPIVYEYYSSTE-- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1871 VH---VTYRPLSLADLDGGAASPIGepipdlSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPELSC-TRFVADPFS 1946
Cdd:PRK13390   307 AHgmtFIDSPDWLAHPGSVGRSVLG------DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAaAQHPAHPFW 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1947 TTggrlyrTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPS 2026
Cdd:PRK13390   381 TT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI 454
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2183974163 2027 DPA-ALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKL 2066
Cdd:PRK13390   455 RGSdELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
509-1007 1.97e-18

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 92.05  E-value: 1.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  509 GQGVHRLFEAQAGLTPDAPALLF----GEER-LSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKA 583
Cdd:PRK08008     6 GQHLRQMWDDLADVYGHKTALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  584 GGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVL---ARLPQSDG--LQSLLLDDLerlvhGYPAENP------DLPEA 652
Cdd:PRK08008    86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYpmyRQIQQEDAtpLRHICLTRV-----ALPADDGvssftqLKAQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  653 PDSLCYA-----------IYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTfSFDI-FGLELYVP-LAR 719
Cdd:PRK08008   161 PATLCYApplstddtaeiLFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMP-AFHIdCQCTAAMAaFSA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  720 GASMLLASREQAQdpeALLDLVERQGVTVLQATPATWRML-----CDSERVDLLRGCTL-LCGGEALAEDLAARmrgLSA 793
Cdd:PRK08008   240 GATFVLLEKYSAR---AFWGQVCKYRATITECIPMMIRTLmvqppSANDRQHCLREVMFyLNLSDQEKDAFEER---FGV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  794 STWNLYGPTETTIWSARFRLGEEAR-PFLGGPLENTALYILDSEMNPCPPGVAGELLIG---GDGLARGYHRRPGLTAER 869
Cdd:PRK08008   314 RLLTSYGMTETIVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKV 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  870 FLPDPFaadgsrLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGP----TL 945
Cdd:PRK08008   394 LEADGW------LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV---GIKDSirdeAI 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  946 VAYLVPTEaalvdAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK08008   464 KAFVVLNE-----GETLSEEEFFAFCEQNMAK----FKVPSYLEIRKDLPRNCSGKIIKKNL 516
PLN02574 PLN02574
4-coumarate--CoA ligase-like
524-1007 2.21e-18

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 91.83  E-value: 2.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALL--FGEERLSYAELNALANRLAWRLREEG--VGSDVlVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRL 599
Cdd:PLN02574    53 NGDTALIdsSTGFSISYSELQPLVKSMAAGLYHVMgvRQGDV-VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEI 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  600 QYMIDDSGLRLLLSQQSVLARLPqSDGLQSLLLDD-------------LERLVHGYPAENPDLPEAPDSLCYAIYTSGST 666
Cdd:PLN02574   132 KKRVVDCSVGLAFTSPENVEKLS-PLGVPVIGVPEnydfdskriefpkFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTT 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  667 GQPKGVMVRHRaltNFVCSI-------ARQPGMLARDRLLSVTTFSFDIFGLELYVP--LARGASMLLASREQAQDpeaL 737
Cdd:PLN02574   211 GASKGVVLTHR---NLIAMVelfvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGSTIVVMRRFDASD---M 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  738 LDLVERQGVTVLQATPATWRMLCDSER---VDLLRGCTLLCGGEA-----LAEDLAARMRGLSASTWnlYGPTETTIWSA 809
Cdd:PLN02574   285 VKVIDRFKVTHFPVVPPILMALTKKAKgvcGEVLKSLKQVSCGAAplsgkFIQDFVQTLPHVDFIQG--YGMTESTAVGT 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  810 RFRLGEEARPF--LGGPLENTALYILDSEMNPC-PPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTG 886
Cdd:PLN02574   363 RGFNTEKLSKYssVGLLAPNMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------LRTG 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  887 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAYLVPTEaalvdaESARQQ 965
Cdd:PLN02574   436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKeCGEIPVAFVVRRQ------GSTLSQ 509
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2183974163  966 ElrsALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PLN02574   510 E---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1596-2058 3.16e-18

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 90.99  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLL----- 1670
Cdd:cd05932      9 WGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgkld 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1671 ----TQRAARERLPLGEGLPCLLLDAEHEW----AGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDA 1742
Cdd:cd05932     89 dwkaMAPGVPEGLISISLPPPSAANCQYQWddliAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1743 TRHWFGFSADDAWSLFHSYAFDFSVWEIFGALLHGGRLVIVPYETSRSPEDflrlLCRERVTVLNQTP---SAFKQLMQv 1819
Cdd:cd05932    169 GIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVED----VQRARPTLFFSVPrlwTKFQQGVQ- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1820 acagQEVPP-----------------------LALRHV--VFGGEALEVQALRPWFERFGdraPRLVNMYGITETTV--H 1872
Cdd:cd05932    244 ----DKIPQqklnlllkipvvnslvkrkvlkgLGLDQCrlAGCGSAPVPPALLEWYRSLG---LNILEAYGMTENFAysH 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1873 VTYrPLSlaDLDGgaasPIGEPIPDLSwylldaglnpVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrl 1952
Cdd:cd05932    317 LNY-PGR--DKIG----TVGNAGPGVE----------VRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF------- 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1953 YRTGDLARYRCDGVVEYVGRIDHQVKI-RGFRIELGEIEARLLAQPGVAEAVVLpheGPGATQLVGYVVTQAAPSDPAAL 2031
Cdd:cd05932    373 LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI---GSGLPAPLALVVLSEEARLRADA 449
                          490       500
                   ....*....|....*....|....*....
gi 2183974163 2032 RDtlRQALKASLPEHM--VPAHLLFLERL 2058
Cdd:cd05932    450 FA--RAELEASLRAHLarVNSTLDSHEQL 476
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2205-2495 3.28e-18

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 90.21  E-value: 3.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2205 LDGTL----LETALQALLAHHDALRLGFR------------LEDGTWRAEHRAVEAgevllwqqsvaDGQALEALAEQVQ 2268
Cdd:cd19532     32 LTGPLdvarLERAVRAVGQRHEALRTCFFtdpedgepmqgvLASSPLRLEHVQISD-----------EAEVEEEFERLKN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2269 RSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQagqavaLPAKTSAFKAWAERLQAHAR 2348
Cdd:cd19532    101 HVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQP------LLPPPLQYLDFAARQRQDYE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2349 DGGLEGERGYWLAQLEGVSTELPcddregAQSVRHVRSaRTELTEEATRRLLQEAPAAYRTQVNDL-----------LLT 2417
Cdd:cd19532    175 SGALDEDLAYWKSEFSTLPEPLP------LLPFAKVKS-RPPLTRYDTHTAERRLDAALAARIKEAsrklrvtpfhfYLA 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2418 ALARVIGRWTGQADTLIQLEGHGReelfEDIDLTRTVGWFTSLFPLRL--SPVAELGASIKRIKEQLR-AIPHKGLGFGA 2494
Cdd:cd19532    248 ALQVLLARLLDVDDICIGIADANR----TDEDFMETIGFFLNLLPLRFrrDPSQTFADVLKETRDKAYaALAHSRVPFDV 323

                   .
gi 2183974163 2495 L 2495
Cdd:cd19532    324 L 324
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1566-2070 3.41e-18

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 91.73  E-value: 3.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1566 PASCLHRLIERQAAERprATAVVYgeRALDYGE------LNLRANRLAHRLIELG------VGPDVLVGLAAERSLEMIV 1633
Cdd:PRK12476    32 PGTTLISLIERNIANV--GDTVAY--RYLDHSHsaagcaVELTWTQLGVRLRAVGarlqqvAGPGDRVAILAPQGIDYVA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1634 GLLAILKAGGAYVPL-DPRYP--SDRLGYMIEDSGIRLLLTQRAARE-------RLPLGEGLPCLLLDAEHEWAGypESD 1703
Cdd:PRK12476   108 GFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEavegflrNLPRLRRPRVIAIDAIPDSAG--ESF 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1704 PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNV----------LRLFDATRHwfGFSaddaW-SLFHsyafDFSVWEIFG 1772
Cdd:PRK12476   186 VPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgtnlvqmilsIDLLDRNTH--GVS----WlPLYH----DMGLSMIGF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1773 ALLHGGRLVIV-PYETSRSPEDFLRLL---CRERVTVLNQTPSAFKqlmqvACAGQEVPP----LALRHVVF--GGEALE 1842
Cdd:PRK12476   256 PAVYGGHSTLMsPTAFVRRPQRWIKALsegSRTGRVVTAAPNFAYE-----WAAQRGLPAegddIDLSNVVLiiGSEPVS 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1843 VQALRPW---FERFGDRAPRLVNMYGITETTVHV-TYRP--------LSLADLDGGAASPI-------------GEPIPD 1897
Cdd:PRK12476   331 IDAVTTFnkaFAPYGLPRTAFKPSYGIAEATLFVaTIAPdaepsvvyLDREQLGAGRAVRVaadapnavahvscGQVARS 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1898 LSWYLLDAGL-NPVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFSTT-----------GGRLYRTGDLARYRcDG 1965
Cdd:PRK12476   411 QWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRLaegshadgaadDGTWLRTGDLGVYL-DG 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1966 VVEYVGRIDHQVKIRGFR-----IELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALK 2040
Cdd:PRK12476   490 ELYITGRIADLIVIDGRNhypqdIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVS 569
                          570       580       590
                   ....*....|....*....|....*....|...
gi 2183974163 2041 AslpEHMVP-AHLLFLER--LPLTANGKLDRRA 2070
Cdd:PRK12476   570 R---RHGLAvADVRLVPAgaIPRTTSGKLARRA 599
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
525-1007 4.72e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 90.86  E-value: 4.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  525 DAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVL-VGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:PRK13388    16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQQsvlARLPQSDGL-----QSLLLDDLE--RLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRH 676
Cdd:PRK13388    96 RRADCQLLVTDA---EHRPLLDGLdlpgvRVLDVDTPAyaELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  677 RALTNFVCSIARQPGMLARDrllsVTTFSFDIFG----LELYVP-LARGASMLLASREQAQdpeALLDLVERQGVT---- 747
Cdd:PRK13388   173 GRLAFAGRALTERFGLTRDD----VCYVSMPLFHsnavMAGWAPaVASGAAVALPAKFSAS---GFLDDVRRYGATyfny 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  748 ------VLQATPatwrmlcdsERVD-----LLRGctllCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSARfrlgEE 816
Cdd:PRK13388   246 vgkplaYILATP---------ERPDdadnpLRVA----FGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVR----EP 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  817 ARP--FLGGPLENTALYILDSeMNPCPPGV---AGELL-----IG------GDGLARGYHRRPGLTAERFlpdpfaADGs 880
Cdd:PRK13388   309 GTPpgSIGRGAPGVAIYNPET-LTECAVARfdaHGALLnadeaIGelvntaGAGFFEGYYNNPEATAERM------RHG- 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 rLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVD- 958
Cdd:PRK13388   381 -MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPdERVGDQVMAALVLRDGATFDp 459
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  959 AESARqqelrsalknsLLAVLPDY---MVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK13388   460 DAFAA-----------FLAAQPDLgtkAWPRYVRIAADLPSTATNKVLKREL 500
PLN02246 PLN02246
4-coumarate--CoA ligase
1570-2020 6.58e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 90.42  E-value: 6.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1570 LHRLIERQAAERPRATAVVYGE--RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVP 1647
Cdd:PLN02246    25 LHDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1648 LDPRYPSDRLGYMIEDSGIRLLLTQRAARERLP---LGEGLPCLLLDAEHE----WAGYPESD----PQSAVGVDNLAYV 1716
Cdd:PLN02246   105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKglaEDDGVTVVTIDDPPEgclhFSELTQADenelPEVEISPDDVVAL 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1717 IYTSGSTGKPKGTLLPHGN----VLRLFDATRHWFGFSADDA----WSLFHSYAFDfSVweIFGALLHGGRLVIVP-YET 1787
Cdd:PLN02246   185 PYSSGTTGLPKGVMLTHKGlvtsVAQQVDGENPNLYFHSDDVilcvLPMFHIYSLN-SV--LLCGLRVGAAILIMPkFEI 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1788 SRspedFLRLLCRERVTVlnqtpSAFkqlmqvacagqeVPPLAL----------------RHVVFG----GEALEvqalr 1847
Cdd:PLN02246   262 GA----LLELIQRHKVTI-----APF------------VPPIVLaiakspvvekydlssiRMVLSGaaplGKELE----- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1848 pwfERFGDRAPRLV--NMYGITET-----------------------TVhVTYRPLSLADLDGGAASPIGEPipdlswyl 1902
Cdd:PLN02246   316 ---DAFRAKLPNAVlgQGYGMTEAgpvlamclafakepfpvksgscgTV-VRNAELKIVDPETGASLPRNQP-------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1903 ldaglnpvprgciGELYVGGAGLARGYLNRPElsCTRFVADpfstTGGRLYrTGDLARYRCDGVVEYVGRIDHQVKIRGF 1982
Cdd:PLN02246   384 -------------GEICIRGPQIMKGYLNDPE--ATANTID----KDGWLH-TGDIGYIDDDDELFIVDRLKELIKYKGF 443
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2183974163 1983 RIELGEIEARLLAQPGVAEAVVLPHEGPGATQL-VGYVV 2020
Cdd:PLN02246   444 QVAPAELEALLISHPSIADAAVVPMKDEVAGEVpVAFVV 482
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1715-2071 8.66e-18

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 90.59  E-value: 8.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 YVIYTSGSTGKPKGTLLPHGNVLrLFDATRHWFGF----------SADDAWSLFHSYAfdfsvweIFGALLHGGRLVIvp 1784
Cdd:PRK00174   249 FILYTSGSTGKPKGVLHTTGGYL-VYAAMTMKYVFdykdgdvywcTADVGWVTGHSYI-------VYGPLANGATTLM-- 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1785 YE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvacAGQEVP------PLALRHVVfgGEALEVQALRpWFERF-- 1853
Cdd:PRK00174   319 FEgvpNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMK---EGDEHPkkydlsSLRLLGSV--GEPINPEAWE-WYYKVvg 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1854 GDRAPrLVNMYGITETTVHVTyRPL-SLADLDGGAASPigePIPDLSWYLLDAGLNPVPRGCIGELYVGGA--GLARGYL 1930
Cdd:PRK00174   393 GERCP-IVDTWWQTETGGIMI-TPLpGATPLKPGSATR---PLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIY 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1931 NRPElsctRFVADPFSTTGGRlYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--PHE 2008
Cdd:PRK00174   468 GDHE----RFVKTYFSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVgrPDD 542
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 2009 --GPGatqLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK00174   543 ikGQG---IYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2203-2464 9.27e-18

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 88.91  E-value: 9.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2203 QALDGTLLETALQALLAHHDALRLGFRLEDGTwraEHRAVEAGEVLLWQQ----SVADGQALEALAEQVQRSLDLGSGPL 2278
Cdd:cd20484     34 SKLDVEKFKQACQFVLEQHPILKSVIEEEDGV---PFQKIEPSKPLSFQEedisSLKESEIIAYLREKAKEPFVLENGPL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2279 LRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVAL---PAKTSAFKAWAERLQAhardgGLEGE 2355
Cdd:cd20484    111 MRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLassPASYYDFVAWEQDMLA-----GAEGE 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2356 --RGYWLAQLEGV--STELPCDdregaqsvrHVRSARTELTEEATRRLLQEA--------PAAYRTQVNDLLLTALARVI 2423
Cdd:cd20484    186 ehRAYWKQQLSGTlpILELPAD---------RPRSSAPSFEGQTYTRRLPSElsnqiksfARSQSINLSTVFLGIFKLLL 256
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2183974163 2424 GRWTGQADTLIQLEGHGR-EELFEDIdltrtVGWFTSLFPLR 2464
Cdd:cd20484    257 HRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIR 293
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3090-3183 1.08e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 89.56  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                           90
                   ....*....|....
gi 2183974163 3170 PEERQAYMLEDSGV 3183
Cdd:PRK07798    88 VEDELRYLLDDSDA 101
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1589-2065 1.16e-17

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 89.03  E-value: 1.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1589 YGERALDYGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIR 1667
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1668 LLLtqraarerlplgeglpcllldaehewagypeSDPqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWF 1747
Cdd:cd05937     81 FVI-------------------------------VDP------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1748 GFSADDAW----SLFHSYAFdfsvweIFGA---LLHGGRLVIVP-----------YETSRSPEDFLRLLCRervTVLNQT 1809
Cdd:cd05937    124 NLKNGDRTytcmPLYHGTAA------FLGAcncLMSGGTLALSRkfsasqfwkdvRDSGATIIQYVGELCR---YLLSTP 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1810 PSAFKQLMQVACAgqevpplalrhvvFGgealevQALRP--WfERFGDR--APRLVNMYGITETtvhvtyrPLSLADLDG 1885
Cdd:cd05937    195 PSPYDRDHKVRVA-------------WG------NGLRPdiW-ERFRERfnVPEIGEFYAATEG-------VFALTNHNV 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1886 GA--ASPIGEPIPDLSWYLLDaGLNPV---------------------PRGCIGELYV----GGAGLARGYLNRPELSCT 1938
Cdd:cd05937    248 GDfgAGAIGHHGLIRRWKFEN-QVVLVkmdpetddpirdpktgfcvraPVGEPGEMLGrvpfKNREAFQGYLHNEDATES 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1939 RFVADPFSTtGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGY 2018
Cdd:cd05937    327 KLVRDVFRK-GDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGC 405
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2019 VVTQAAPSdpAALRDTLRQALKAS-----LPEHMVPAHLLFLERLPLTANGK 2065
Cdd:cd05937    406 AAITLEES--SAVPTEFTKSLLASlarknLPSYAVPLFLRLTEEVATTDNHK 455
PRK08315 PRK08315
AMP-binding domain protein; Validated
1572-2065 1.58e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 89.10  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGERAL--DYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLD 1649
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1650 PRYPSDRLGYMIEDSGIRLLLTQRAAR------------------ERLPL-GEGLPCL----LLDAEHEWAGYPESD-PQ 1705
Cdd:PRK08315   100 PAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcEPGQLqSARLPELrrviFLGDEKHPGMLNFDElLA 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1706 SAVGVDNLAY-----------VI---YTSGSTGKPKGTLLPHGNVLR--LFDATRhwFGFSADDAW----SLFHSYAfdf 1765
Cdd:PRK08315   180 LGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFIGEA--MKLTEEDRLcipvPLYHCFG--- 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1766 SVWEIFGALLHGGRLVIvPYEtSRSPEDFLRLLCRERVTVLNQTPSAFkqlmqvaCAGQEVPPLA------LRHVVFGGE 1839
Cdd:PRK08315   255 MVLGNLACVTHGATMVY-PGE-GFDPLATLAAVEEERCTALYGVPTMF-------IAELDHPDFArfdlssLRTGIMAGS 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1840 ALEVQALRpwferfgdRAPRLVNM------YGITETTvhvtyrPLSLADldgGAASPI-------GEPIPDLSWYLLDAG 1906
Cdd:PRK08315   326 PCPIEVMK--------RVIDKMHMsevtiaYGMTETS------PVSTQT---RTDDPLekrvttvGRALPHLEVKIVDPE 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1907 LN-PVPRGCIGELYVGGAGLARGYLNRPELscTRFVADPfsttGGRLyRTGDLARYRCDGVVEYVGRIDHQVkIRGfrie 1985
Cdd:PRK08315   389 TGeTVPRGEQGELCTRGYSVMKGYWNDPEK--TAEAIDA----DGWM-HTGDLAVMDEEGYVNIVGRIKDMI-IRG---- 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1986 lG------EIEARLLAQPGVAEAVV--LPHEGPGaTQLVGYVVTQA-APSDPAALRDTLRqalkASLPEHMVPAHLLFLE 2056
Cdd:PRK08315   457 -GeniyprEIEEFLYTHPKIQDVQVvgVPDEKYG-EEVCAWIILRPgATLTEEDVRDFCR----GKIAHYKIPRYIRFVD 530

                   ....*....
gi 2183974163 2057 RLPLTANGK 2065
Cdd:PRK08315   531 EFPMTVTGK 539
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
660-1004 2.26e-17

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 86.55  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 IYTSGSTGQPKGVMVRHR-ALTNFVCSIARQPGMLARDRLLSVTTFSFDIFGLELYVPL-ARGASMLLASREQAQdpeAL 737
Cdd:cd17635      7 IFTSGTTGEPKAVLLANKtFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLiHGGLCVTGGENTTYK---SL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  738 LDLVERQGVTVLQATPATWRMLCdSERVDLLRGCTLL----CGGE-ALAEDLAARMRGLSASTWNLYGPTETT-IWSARF 811
Cdd:cd17635     84 FKILTTNAVTTTCLVPTLLSKLV-SELKSANATVPSLrligYGGSrAIAADVRFIEATGLTNTAQVYGLSETGtALCLPT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  812 RLGEEARPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlyRTGDLARY 891
Cdd:cd17635    163 DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------NTGDLGER 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEaalVDAESArqqelRSA 970
Cdd:cd17635    235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISdEEFGELVGLAVVASA---ELDENA-----IRA 306
                          330       340       350
                   ....*....|....*....|....*....|....
gi 2183974163  971 LKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd17635    307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK09192 PRK09192
fatty acyl-AMP ligase;
1591-2068 2.59e-17

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 88.52  E-value: 2.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1591 ERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP-------SDRLGYMIED 1663
Cdd:PRK09192    47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLAS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1664 SGIRLLLTQR-------AARERLPLGEGLPCLLLDAEHEWAG-YPESDPqsavgvDNLAYVIYTSGSTGKPKGTLLPHGN 1735
Cdd:PRK09192   127 AQPAAIITPDellpwvnEATHGNPLLHVLSHAWFKALPEADVaLPRPTP------DDIAYLQYSSGSTRFPRGVIITHRA 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1736 VL-RLFDATRHWFGFSADD---AW-SLFHsyafDFSVWEIFGALLHGGrlVIVPY----ETSRSPEDFLRLLCRERVTVl 1806
Cdd:PRK09192   201 LMaNLRAISHDGLKVRPGDrcvSWlPFYH----DMGLVGFLLTPVATQ--LSVDYlptrDFARRPLQWLDLISRNRGTI- 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1807 NQTPSAFKQLMQVACAGQEVPPLAL---RHVVFGGEALEVQALRPWFERFGD---RAPRLVNMYGITETTVHVTYRPLS- 1879
Cdd:PRK09192   274 SYSPPFGYELCARRVNSKDLAELDLscwRVAGIGADMIRPDVLHQFAEAFAPagfDDKAFMPSYGLAEATLAVSFSPLGs 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1880 -----LADLD----GGAASPI-------------GEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRPElsc 1937
Cdd:PRK09192   354 givveEVDRDrleyQGKAVAPgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE--- 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1938 trfVADPFSTTGgrLYRTGDLArYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGV--AEAVVLPHEGPGATQL 2015
Cdd:PRK09192   431 ---SQDVLAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQENGEKI 504
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 2016 VgyVVTQAAPSDP---AALRDTLRQALKAslpEH-------MVPAHllfleRLPLTANGKLDR 2068
Cdd:PRK09192   505 V--LLVQCRISDEerrGQLIHALAALVRS---EFgveaaveLVPPH-----SLPRTSSGKLSR 557
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1562-2086 2.98e-17

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 88.27  E-value: 2.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1562 QDFtPASClHRLIE---RQAAERPRATAVVYGE--RAlDYGELNLRANRLAHRLIELGVGP-DVLVGLA--AERSLEMIV 1633
Cdd:PRK06018     6 QDW-PLLC-HRIIDhaaRIHGNREVVTRSVEGPivRT-TYAQIHDRALKVSQALDRDGIKLgDRVATIAwnTWRHLEAWY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1634 GLLAIlkaGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQ-------RAARERLPLGEGLpCLLLDAEH------------ 1694
Cdd:PRK06018    83 GIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVITDltfvpilEKIADKLPSVERY-VVLTDAAHmpqttlknavay 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1695 -----------EWAGYPEsdpqsavgvDNLAYVIYTSGSTGKPKGTLLPH-GNVLR-LFDATRHWFGFSADDAW----SL 1757
Cdd:PRK06018   159 eewiaeadgdfAWKTFDE---------NTAAGMCYTSGTTGDPKGVLYSHrSNVLHaLMANNGDALGTSAADTMlpvvPL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1758 FHSYAfdfsvWEI-FGALLHGGRLVIvP---------YEtsrspedflrLLCRERVTVLNQTPSAFKQLMQ-VACAGQEV 1826
Cdd:PRK06018   230 FHANS-----WGIaFSAPSMGTKLVM-PgakldgasvYE----------LLDTEKVTFTAGVPTVWLMLLQyMEKEGLKL 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1827 PplALRHVVFGGEALEvqalRPWFERFGDRAPRLVNMYGITETTVHVTYRPLS--LADLDGGAASPI----GEPIPDLSW 1900
Cdd:PRK06018   294 P--HLKMVVCGGSAMP----RSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKppFSKLPGDARLDVlqkqGYPPFGVEM 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1901 YLLDAGLNPVPRG--CIGELYVGGAGLARGYLnrpelsctRFVADPFSTTGgrLYRTGDLARYRCDGVVEYVGRIDHQVK 1978
Cdd:PRK06018   368 KITDDAGKELPWDgkTFGRLKVRGPAVAAAYY--------RVDGEILDDDG--FFDTGDVATIDAYGYMRITDRSKDVIK 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1979 IRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLvgyVVTQAAPSDPAAlRDTLRQALKASLPEHMVPAHLLFLE 2056
Cdd:PRK06018   438 SGGEWISSIDLENLAVGHPKVAEAAVigVYHPKWDERPL---LIVQLKPGETAT-REEILKYMDGKIAKWWMPDDVAFVD 513
                          570       580       590
                   ....*....|....*....|....*....|.
gi 2183974163 2057 RLPLTANGKLDRRALpapdasRLQ-RDYTAP 2086
Cdd:PRK06018   514 AIPHTATGKILKTAL------REQfKDYKLP 538
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3095-3182 3.09e-17

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 87.69  E-value: 3.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3174
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                   ....*...
gi 2183974163 3175 AYMLEDSG 3182
Cdd:cd05945     81 REILDAAK 88
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
653-1007 3.13e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 86.38  E-value: 3.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  653 PDSLCYAIYTSGSTGQPKgvMVRHRaltnfVCSIARQPGMLARDRLLSVTTFS------FDIFGL--ELYVPLARGASML 724
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPK--LAQHT-----HSNEVYNAWMLALNSLFDPDDVLlcglplFHVNGSvvTLLTPLASGAHVV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  725 LASREQAQDPEALLD---LVERQGVTVLQATPATWRMLC---DSERVDLLRGCtlLCGGEALAEDLAARMR-GLSASTWN 797
Cdd:cd05944     74 LAGPAGYRNPGLFDNfwkLVERYRITSLSTVPTVYAALLqvpVNADISSLRFA--MSGAAPLPVELRARFEdATGLPVVE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  798 LYGPTETTIWSARFRLGEEARPFLGG---PLENTALYILDSEMN---PCPPGVAGELLIGGDGLARGYhrrpgLTAERFL 871
Cdd:cd05944    152 GYGLTEATCLVAVNPPDGPKRPGSVGlrlPYARVRIKVLDGVGRllrDCAPDEVGEICVAGPGVFGGY-----LYTEGNK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  872 pDPFAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGV-AGPTLVAY-- 948
Cdd:cd05944    227 -NAFVADG--WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAhAGELPVAYvq 303
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163  949 LVP----TEAALVDAESARQQElRSAlknsllavlpdymVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05944    304 LKPgavvEEEELLAWARDHVPE-RAA-------------VPKHIEVLEELPVTAVGKVFKPAL 352
PRK09274 PRK09274
peptide synthase; Provisional
1572-2071 3.22e-17

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 88.42  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1572 RLIERQAAERPRATAVVYGE----------RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKA 1641
Cdd:PRK09274    10 RHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1642 GGAYVPLDPRYPSDRLGYMIEDS------GI------RLLL--TQRAARERLPLGEGL----PCLL-LDAEHEWAGYPES 1702
Cdd:PRK09274    90 GAVPVLVDPGMGIKNLKQCLAEAqpdafiGIpkahlaRRLFgwGKPSVRRLVTVGGRLlwggTTLAtLLRDGAAAPFPMA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1703 DPQSavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDawslfhsyaFD---FSVWEIFGALLhGGR 1779
Cdd:PRK09274   170 DLAP----DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE---------IDlptFPLFALFGPAL-GMT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1780 LVIVPYETSR----SPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPPlALRHVVFGGEALEVQALrpwfERFGD 1855
Cdd:PRK09274   236 SVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLP-SLRRVISAGAPVPIAVI----ERFRA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1856 RAP---RLVNMYGITE--------------TTVHVTyrplsladlDGGAASPIGEPIPDLSWYLLDAGLNP--------- 1909
Cdd:PRK09274   311 MLPpdaEILTPYGATEalpissiesreilfATRAAT---------DNGAGICVGRPVDGVEVRIIAISDAPipewddalr 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1910 VPRGCIGELYVGGAGLARGYLNRPElsCTRF--VADPfstTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELG 1987
Cdd:PRK09274   382 LATGEIGEIVVAGPMVTRSYYNRPE--ATRLakIPDG---QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTI 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1988 EIEARLLAQPGVAEAVVLPHEGPGATQLVgyVVTQAAPSDpAALRDTLRQALKASLPEHMVPA---HLLFLERLPLTA-- 2062
Cdd:PRK09274   457 PCERIFNTHPGVKRSALVGVGVPGAQRPV--LCVELEPGV-ACSKSALYQELRALAAAHPHTAgieRFLIHPSFPVDIrh 533

                   ....*....
gi 2183974163 2063 NGKLDRRAL 2071
Cdd:PRK09274   534 NAKIFREKL 542
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2188-2485 3.90e-17

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 87.04  E-value: 3.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2188 PRRQHWNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGT---WRAEHRAVEAGEVLLWQQSVADGQALEALA 2264
Cdd:cd19533     19 PEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEpyqWIDPYTPVPIRHIDLSGDPDPEGAAQQWMQ 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2265 EQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVALPAKTSAFKAWAERlQ 2344
Cdd:cd19533     99 EDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPPAPFGSFLDLVEEE-Q 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2345 AHARDGGLEGERGYWLAQLEGVSTELPCDDREGAQSVRHVRsaRT-ELTEEATRRLLqEAPAAYRTQVNDLLLTALARVI 2423
Cdd:cd19533    178 AYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLR--RTaELPPELTRTLL-EAAEAHGASWPSFFIALVAAYL 254
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2424 GRWTGQADTLIQLEGHGReelfEDIDLTRTVGWFTSLFPLRLS-----PVAELgasIKRIKEQLRAI 2485
Cdd:cd19533    255 HRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLTvdpqqTFAEL---VAQVSRELRSL 314
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1711-2071 4.28e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 85.87  E-value: 4.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSAddAWSL----FHSYAFDFSVweifGALLHGGRLVIVPYE 1786
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG--QWLLalpaHHIAGLQVLV----RSVIAGSEPVELDVS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 TSRSPEDFLRLLCR----ERVTVLNQTpsafkQLMQVACAGQEVPPLA-LRHVVFGGEALEvqalRPWFERFGDRAPRLV 1861
Cdd:PRK07824   109 AGFDPTALPRAVAElgggRRYTSLVPM-----QLAKALDDPAATAALAeLDAVLVGGGPAP----APVLDAAAAAGINVV 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1862 NMYGITETTVHVTY--RPLSladldgGAASPIGEpipdlswylldaglnpvprgciGELYVGGAGLARGYLNRPElsctr 1939
Cdd:PRK07824   180 RTYGMSETSGGCVYdgVPLD------GVRVRVED----------------------GRIALGGPTLAKGYRNPVD----- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1940 fvADPFSTTGgrLYRTGDLARYRcDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGaTQLVG 2017
Cdd:PRK07824   227 --PDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVfgLPDDRLG-QRVVA 300
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2018 YVVTQAAPSDPAalrDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK07824   301 AVVGDGGPAPTL---EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1592-2071 4.49e-17

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 87.73  E-value: 4.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1592 RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT 1671
Cdd:PLN02330    54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1672 QRAARERLPlGEGLPCLLLDAEH-----EWAGYPESDPQSAVGVDN-------LAYVIYTSGSTGKPKGTLLPHGNVL-- 1737
Cdd:PLN02330   134 NDTNYGKVK-GLGLPVIVLGEEKiegavNWKELLEAADRAGDTSDNeeilqtdLCALPFSSGTTGISKGVMLTHRNLVan 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1738 ---RLFDATRHWFGFSADDAW-SLFHSYAFdfsVWEIFGALLHGGRLVIVPYETSRSpedFLRLLCRERVTVLNQTPSAF 1813
Cdd:PLN02330   213 lcsSLFSVGPEMIGQVVTLGLiPFFHIYGI---TGICCATLRNKGKVVVMSRFELRT---FLNALITQEVSFAPIVPPII 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLMQVACAGQ-EVPPLALRHVVFGGEALEVQALRPWFERFGDraPRLVNMYGITETTVhVTyrpLSLADLDGGAA---- 1888
Cdd:PLN02330   287 LNLVKNPIVEEfDLSKLKLQAIMTAAAPLAPELLTAFEAKFPG--VQVQEAYGLTEHSC-IT---LTHGDPEKGHGiakk 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1889 SPIGEPIPDLSWYLL--DAGLNpVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADpfsttgGRLYrTGDLARYRCDGV 1966
Cdd:PLN02330   361 NSVGFILPNLEVKFIdpDTGRS-LPKNTPGELCVRSQCVMQGYYNNKEETDRTIDED------GWLH-TGDIGYIDDDGD 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1967 VEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQLVGYVVTQAAPSDpaalRDTLRQALKASLP 2044
Cdd:PLN02330   433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVvpLPDEEAGEIPAACVVINPKAKES----EEDILNFVAANVA 508
                          490       500
                   ....*....|....*....|....*..
gi 2183974163 2045 EHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PLN02330   509 HYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1578-2006 5.90e-17

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 86.85  E-value: 5.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1578 AAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRL 1657
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1658 GYMIEDSGIRLLLTqraarerLPLGEGLPCLLLDAEHEWAGYPESDPQSavgvDNLAYVIYTSGSTGKPKGTLLPHGN-- 1735
Cdd:PRK09029    93 EELLPSLTLDFALV-------LEGENTFSALTSLHLQLVEGAHAVAWQP----QRLATMTLTSGSTGLPKAAVHTAQAhl 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1736 -----VLRLFDatrhwfgFSADDAW----SLFHsyafdFS----VWEifgALLHGGRLVIvpyetsRSPEDFLRLLcrER 1802
Cdd:PRK09029   162 asaegVLSLMP-------FTAQDSWllslPLFH-----VSgqgiVWR---WLYAGATLVV------RDKQPLEQAL--AG 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1803 VTVLNQTPSAFKQLMQvacagQEVPPLALRHVVFGG--------EALEVQALRPWferFGdraprlvnmYGITETTVHVT 1874
Cdd:PRK09029   219 CTHASLVPTQLWRLLD-----NRSEPLSLKAVLLGGaaipveltEQAEQQGIRCW---CG---------YGLTEMASTVC 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1875 YRPlslADLDGGAaspiGEPIPDLSWYLLDaglnpvprgciGELYVGGAGLARGYLNRPELSctrfvadPFSTTGGrLYR 1954
Cdd:PRK09029   282 AKR---ADGLAGV----GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEG-WFA 335
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 1955 TGDLARYRcDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLP 2006
Cdd:PRK09029   336 TRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVP 386
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1126-1476 8.88e-17

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 85.57  E-value: 8.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1126 RLDPHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVeHDG--APRQVIHPTLPIAIEERRPP---VAGEDL 1200
Cdd:cd19544     16 LLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAIL-WEGlsEPVQVVWRQAELPVEELTLDpgdDALAQL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1201 KGLVETEAHRpFDLQRG-PLLRVLLLPLATDECVLVLTLHHIIADGWSMQVLVDElIRVYAALRHDQPPAlaelPIQYAD 1279
Cdd:cd19544     95 RARFDPRRYR-LDLRQApLLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAGRAAALPP----PVPYRN 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1280 FAAWQRQwmdGGERERQLDYWVSRLGG-EQP-----LLELPSDrprpqqqshrGRRIG---IPLPAELAEALRRLAQAEQ 1350
Cdd:cd19544    169 FVAQARL---GASQAEHEAFFREMLGDvDEPtapfgLLDVQGD----------GSDITearLALDAELAQRLRAQARRLG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1351 ---GTLFML----LLAsfqallhRYSGQNDI--------RVGvpianrNREETEGLIGFFVNTQVLRAELDGQlPFRELL 1415
Cdd:cd19544    236 vspASLFHLawalVLA-------RCSGRDDVvfgtvlsgRMQ------GGAGADRALGMFINTLPLRVRLGGR-SVREAV 301
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 1416 RQVRQAVVEAqghqdLPFEQLvdalqperSLSHA----------PLFQVM--YNHQRDDHRGSRFASLGELEV 1476
Cdd:cd19544    302 RQTHARLAEL-----LRHEHA--------SLALAqrcsgvpaptPLFSALlnYRHSAAAAAAAALAAWEGIEL 361
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
653-1001 9.12e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 85.13  E-value: 9.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  653 PDSLcYAIYTSGSTGQPKGVMVRH----RAL---TNFVCSIARQPGMLARDRLLSVTTFSFDIfglelyVPLARGASMLL 725
Cdd:cd05924      3 ADDL-YILYTGGTTGMPKGVMWRQedifRMLmggADFGTGEFTPSEDAHKAAAAAAGTVMFPA------PPLMHGTGSWT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  726 A------------SREQAqDPEALLDLVERQGVTVLQAT-PATWRMLCDSER----VDLLRGCTLLCGGEALAEDLAARM 788
Cdd:cd05924     76 AfggllggqtvvlPDDRF-DPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRdagpYDLSSLFAISSGGALLSPEVKQGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  789 RGL--SASTWNLYGPTET--TIWSARFRLGEEARPFLggpLENTALYILDSEMNPCPPGVAGELLIGGDGL-ARGYHRRP 863
Cdd:cd05924    155 LELvpNITLVDAFGSSETgfTGSGHSAGSGPETGPFT---RANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDE 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  864 GLTAERFlpdpFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-G 942
Cdd:cd05924    232 AKTAETF----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERwG 307
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163  943 PTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGK 1001
Cdd:cd05924    308 QEVVAVVQLREGAGVDLE-----ELREHCRTRIAR----YKLPKQVVFVDEIERSPAGK 357
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2204-2431 1.02e-16

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 85.55  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2204 ALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALL 2283
Cdd:cd19540     35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2284 ATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQA---VALPAKTSAFKAWAERLQAHARDGG--LEGERGY 2358
Cdd:cd19540    115 FRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRApdwAPLPVQYADYALWQRELLGDEDDPDslAARQLAY 194
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2359 WLAQLEGV--STELPCDDREGAqsVRHVRSARTELT-EEATRRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQAD 2431
Cdd:cd19540    195 WRETLAGLpeELELPTDRPRPA--VASYRGGTVEFTiDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDD 268
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
655-1004 1.05e-16

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 83.99  E-value: 1.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLCYAIYTSGSTGQPKGVMVRHRA-LTNFVCSiarQPGML--ARDRLLSVTTFSFDIFGLELYVPLARGASMLLASReqa 731
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCN---EDLFNisGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK--- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  732 QDPEALLDLVERQGVTVLQATPATWRMLCDSERVDL-LRgcTLLCGGEALAEDLAARMRGLS--ASTWNLYGPTETTIWS 808
Cdd:cd17633     75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESkIK--SIFSSGQKLFESTKKKLKNIFpkANLIEFYGTSELSFIT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  809 ARFRlGEEARPF-LGGPLENTALYILDSEmnpcpPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaadgsrlYRTGD 887
Cdd:cd17633    153 YNFN-QESRPPNsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSVGD 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGPTLVaylvpteAALVDAESARQQEL 967
Cdd:cd17633    215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-------VALYSGDKLTYKQL 287
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2183974163  968 RSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKINR 1004
Cdd:cd17633    288 KRFLKQKLSR----YEIPKKIIFVDSLPYTSSGKIAR 320
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2205-2403 1.54e-16

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 85.01  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2205 LDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLA 2284
Cdd:cd19538     36 LDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLF 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2285 TLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQA---VALPAKTSAFKAWAERLQAHARDGG--LEGERGYW 2359
Cdd:cd19538    116 ELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEApelAPLPVQYADYALWQQELLGDESDPDslIARQLAYW 195
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2183974163 2360 LAQLEGV--STELPCDDREGAQSVRHVRSARTELTEEATRRLLQEA 2403
Cdd:cd19538    196 KKQLAGLpdEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
505-1007 1.79e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 85.97  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  505 EYPAGQGVhrlFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEgvgSDVLVG--IALErgVPMV----VALL 578
Cdd:PRK05677    22 EYPNIQAV---LKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQH---TDLKPGdrIAVQ--LPNVlqypVAVF 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  579 AVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL--LSQQSVLAR--LPQSDGLQSL------LLDDLERLV--------- 639
Cdd:PRK05677    94 GAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALvcLANMAHLAEkvLPKTGVKHVIvtevadMLPPLKRLLinavvkhvk 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  640 ---------------------HGYPAENPDLpeAPDSLCYAIYTSGSTGQPKGVMVRHRaltNFVCSIARQPGMLARD-- 696
Cdd:PRK05677   174 kmvpayhlpqavkfndalakgAGQPVTEANP--QADDVAVLQYTGGTTGVAKGAMLTHR---NLVANMLQCRALMGSNln 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  697 ----------RLLSVTTFSFDIFGLELYvplarGASMLLASreQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE--- 763
Cdd:PRK05677   249 egceiliaplPLYHIYAFTFHCMAMMLI-----GNHNILIS--NPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEafr 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLLRGCTLLCGGEALAEDLAARMRGLSA-STWNLYGPTETTIWSA-----RFRLGEearpfLGGPLENTALYILDSEM 837
Cdd:PRK05677   322 KLDFSALKLTLSGGMALQLATAERWKEVTGcAICEGYGMTETSPVVSvnpsqAIQVGT-----IGIPVPSTLCKVIDDDG 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  838 NPCPPGVAGELLIGGDGLARGYHRRPGLTAERflpdpFAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 917
Cdd:PRK05677   397 NELPLGEVGELCVKGPQVMKGYWQRPEATDEI-----LDSDG--WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPN 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  918 EIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDAEsarqqELRSALKNSLLAvlpdYMVPAHMLLLENLPL 996
Cdd:PRK05677   470 ELEDVLAALPGVLQCAAIGVPDEKsGEAIKVFVVVKPGETLTKE-----QVMEHMRANLTG----YKVPKAVEFRDELPT 540
                          570
                   ....*....|.
gi 2183974163  997 TPNGKINRKAL 1007
Cdd:PRK05677   541 TNVGKILRREL 551
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
653-956 1.79e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 85.73  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  653 PDSLCYAIYTSGSTGQPKGVMVRHRaltNFVCSIArqpGMLAR--------DRLLSvttfsfdifglelYVPLA------ 718
Cdd:cd17639     87 PDDLACIMYTSGSTGNPKGVMLTHG---NLVAGIA---GLGDRvpellgpdDRYLA-------------YLPLAhifela 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  719 -------RGASMLLASreqaqdPEALL---------DLVERQGvTVLQATPATW-------------------------- 756
Cdd:cd17639    148 aenvclyRGGTIGYGS------PRTLTdkskrgckgDLTEFKP-TLMVGVPAIWdtirkgvlaklnpmgglkrtlfwtay 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  757 -------RMLCDSERVDL-------------LRGCtlLCGGEALAEDLAARMRGLSASTWNLYGPTETTIWSARFRLGEE 816
Cdd:cd17639    221 qsklkalKEGPGTPLLDElvfkkvraalggrLRYM--LSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDL 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  817 ARPFLGGPLENTALYILDSE------MNPCPpgvAGELLIGGDGLARGYHRRPGLTAERFLPDpfaadgsRLYRTGDLAR 890
Cdd:cd17639    299 ETGRVGPPLPCCEIKLVDWEeggystDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAFDGD-------GWFHTGDIGE 368
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  891 YRADGVIEYLGRIDHQVKIR-GFRIELGEIETRLLEQDSVREAVVVAQPgvAGPTLVAYLVPTEAAL 956
Cdd:cd17639    369 FHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADP--DKSYPVAIVVPNEKHL 433
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
830-1099 1.99e-16

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 82.88  E-value: 1.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  830 LYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKI 909
Cdd:COG3433     26 QARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQ 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  910 RGFRIELGEIET-----RLLEQDSVREAVVVAQPGVAGPTLVAYLVPTEAALVDAESARQqelrsalknsllAVLPDYMV 984
Cdd:COG3433    106 VVIRAERGEEEElllvlRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAAL------------DKVPPDVV 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  985 PAHMLLLENLPLTPNGKINRKALPLPDASAVRDAHVAPEGELERA-----MAAIWSEVLKLG--HIGRDDNFFELGGHSL 1057
Cdd:COG3433    174 AASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVDpeEIDPDDNLFDLGLDSI 253
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2183974163 1058 LVTQVVSRVRRRlDLQVPLRTLFEHSTLRAYAQAVAQLAPAA 1099
Cdd:COG3433    254 RLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAA 294
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3091-3182 2.33e-16

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 84.58  E-value: 2.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3091 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                           90
                   ....*....|...
gi 2183974163 3170 PEERQAYMLEDSG 3182
Cdd:cd17631     80 TPPEVAYILADSG 92
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
657-960 2.56e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 83.12  E-value: 2.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  657 CYAIYTSGSTGQPKGVMVRHRAL------TNFVCSIARQPGMLARDRL-----LSVTTFSFDIFGLELYVPLArgasmll 725
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALlaqalvLAVLQAIDEGTVFLNSGPLfhigtLMFTLATFHAGGTNVFVRRV------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  726 asreqaqDPEALLDLVERQGVTVLQATPATwrmlcdserVDLLRgctllcggEALAE---DLAARMRGLSASTWNLYGPT 802
Cdd:cd17636     76 -------DAEEVLELIEAERCTHAFLLPPT---------IDQIV--------ELNADglyDLSSLRSSPAAPEWNDMATV 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  803 ETTIWSARFR---------------LGEEARPFLGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTA 867
Cdd:cd17636    132 DTSPWGRKPGgygqtevmglatfaaLGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNA 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  868 ERFlpdpfaADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTLV- 946
Cdd:cd17636    212 RRT------RGG--WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI---GVPDPRWAq 280
                          330
                   ....*....|....*..
gi 2183974163  947 ---AYLVPTEAALVDAE 960
Cdd:cd17636    281 svkAIVVLKPGASVTEA 297
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
502-1007 2.67e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 85.27  E-value: 2.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  502 PASEYPAGQGVHRLFEAQAGLtPDAPALL--FGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLA 579
Cdd:cd17642     10 PLEDGTAGEQLHKAMKRYASV-PGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  580 VLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQ----QSVLARLPQSDGLQSLLLDDLERLVHGYPAEN--------- 646
Cdd:cd17642     89 GLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSkkglQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYtfitqnlpp 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  647 --------PDLPEAPDSLCYAIYTSGSTGQPKGVMVRHR-ALTNFvcSIARQP----GMLARDRLLSVTTF--SFDIFGL 711
Cdd:cd17642    169 gfneydfkPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKnIVARF--SHARDPifgnQIIPDTAILTVIPFhhGFGMFTT 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  712 ELYvpLARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDSERV---DLLRGCTLLCGGEALA---EDLA 785
Cdd:cd17642    247 LGY--LICGFRVVLMYK---FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVdkyDLSNLHEIASGGAPLSkevGEAV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  786 ARMRGLSASTWNlYGPTETTiwSARFRLGEE-ARPFLGG---PLENTALYILDSEmNPCPPGVAGELLIGGDGLARGYHR 861
Cdd:cd17642    322 AKRFKLPGIRQG-YGLTETT--SAILITPEGdDKPGAVGkvvPFFYAKVVDLDTG-KTLGPNERGELCVKGPMIMKGYVN 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  862 RPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAvvvaqpGVA 941
Cdd:cd17642    398 NPEATKA-------LIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDA------GVA 464
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  942 G-PTLVAYLVPteAALVDAESARQQElrsalKNSLLAVLPDYMVPAHML-----LLENLPLTPNGKINRKAL 1007
Cdd:cd17642    465 GiPDEDAGELP--AAVVVLEAGKTMT-----EKEVMDYVASQVSTAKRLrggvkFVDEVPKGLTGKIDRRKI 529
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
535-972 3.91e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 84.05  E-value: 3.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSglrlllsq 614
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEA-------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  615 qsvlarlpqsdglqslllddlerlvhgypaeNPD----LPEAPDSLCyAIYTSGSTGQPKGVMVRHRALTNFVCSIARQP 690
Cdd:cd05910     74 -------------------------------EPDafigIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  691 GMLARDRLLSvtTFS-FDIFGLELyvPLARGASMLLASREQAQDPEALLDLVERQGVTVLQATPATWRML---CDSERVD 766
Cdd:cd05910    122 GIRPGEVDLA--TFPlFALFGPAL--GLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVaryCAQHGIT 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  767 LLRGCTLLCGGEALAEDLAARMRGL---SASTWNLYGPTE----TTIWSARFRLGEEARP------FLGGPLENTALYIL 833
Cdd:cd05910    198 LPSLRRVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEalpvSSIGSRELLATTTAATsggagtCVGRPIPGVRVRII 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  834 DSEMNP---------CPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPfaaDGSRLYRTGDLARYRADGVIEYLGRID 904
Cdd:cd05910    278 EIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKA 354
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  905 HQVKIRGFRIELGEIETRLLEQDSV-REAVV-VAQPGVAGPTLVAYLVPteaaLVDAESAR-QQELRSALK 972
Cdd:cd05910    355 HRVITTGGTLYTEPVERVFNTHPGVrRSALVgVGKPGCQLPVLCVEPLP----GTITPRARlEQELRALAK 421
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
533-1001 5.25e-16

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 83.56  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  533 EERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL 612
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 SQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeapdsLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGM 692
Cdd:cd05940     81 VD-----------------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGA 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  693 LARDRLLSVttfsfdifgLELY----------VPLARGASMLLASREQAQDpeaLLDLVERQGVTVLQATPATWRMLCDS 762
Cdd:cd05940    120 LPSDVLYTC---------LPLYhstalivgwsACLASGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLLNQ 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  763 ERVDLLRG--CTLLCGGealaedlaarmrGLSASTWN-------------LYGPTETTIWSARF--RLGEEAR-PFLGGP 824
Cdd:cd05940    188 PPKPTERKhkVRMIFGN------------GLRPDIWEefkerfgvpriaeFYAATEGNSGFINFfgKPGAIGRnPSLLRK 255
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  825 LENTALYILDSE-----------MNPCPPGVAGELL--IGGDGLARGYhRRPGLTAERFLPDPFaADGSRLYRTGDLARY 891
Cdd:cd05940    256 VAPLALVKYDLEsgepirdaegrCIKVPRGEPGLLIsrINPLEPFDGY-TDPAATEKKILRDVF-KKGDAWFNTGDLMRL 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVV--VAQPGVAGPTLVaylvpteAALVDAESarQQELRS 969
Cdd:cd05940    334 DGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGM-------AAIVLQPN--EEFDLS 404
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2183974163  970 ALKNSLLAVLPDYMVPAHMLLLENLPLTPNGK 1001
Cdd:cd05940    405 ALAAHLEKNLPGYARPLFLRLQPEMEITGTFK 436
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
506-1007 6.85e-16

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 84.16  E-value: 6.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  506 YPAG----------QGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLA-WRLREEGVGSDVLVGIALERGVPMV 574
Cdd:PRK08751    11 YPAGvaaeidleqfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAaYLLGELQLKKGDRVALMMPNCLQYP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  575 VALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL-------SQQSVLARLPQ----SDGLQSLL-----------L 632
Cdd:PRK08751    91 IATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnfgtTVQQVIADTPVkqviTTGLGDMLgfpkaalvnfvV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  633 DDLERLVHGYPAEN----------------PDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRaltNFVCSiarqpgMLARD 696
Cdd:PRK08751   171 KYVKKLVPEYRINGairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVAN------MQQAH 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  697 RLLSVTTFSFD-----IFGLELYVPLARGASMLLASR--------EQAQDPEALLDLVERQGVTVLQATPATWRMLCDSE 763
Cdd:PRK08751   242 QWLAGTGKLEEgcevvITALPLYHIFALTANGLVFMKiggcnhliSNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDLLRGCTLLC---GGEALAEDLAARMRGLSASTW-NLYGPTETTIWSARFRLG-EEARPFLGGPLENTALYILDSEMN 838
Cdd:PRK08751   322 GFDQIDFSSLKMtlgGGMAVQRSVAERWKQVTGLTLvEAYGLTETSPAACINPLTlKEYNGSIGLPIPSTDACIKDDAGT 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  839 PCPPGVAGELLIGGDGLARGYHRRPGLTAErflpdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 918
Cdd:PRK08751   402 VLAIGEIGELCIKGPQVMKGYWKRPEETAK-------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  919 IETrlleqdsvreaVVVAQPGVAgpTLVAYLVPTEAA--LVDAESARQQELRSA--LKNSLLAVLPDYMVPAHMLLLENL 994
Cdd:PRK08751   475 IED-----------VIAMMPGVL--EVAAVGVPDEKSgeIVKVVIVKKDPALTAedVKAHARANLTGYKQPRIIEFRKEL 541
                          570
                   ....*....|...
gi 2183974163  995 PLTPNGKINRKAL 1007
Cdd:PRK08751   542 PKTNVGKILRREL 554
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3089-3183 7.64e-16

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 83.38  E-value: 7.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3089 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 3167
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90
                   ....*....|....*.
gi 2183974163 3168 EYPEERQAYMLEDSGV 3183
Cdd:cd05936     82 LYTPRELEHILNDSGA 97
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
470-1000 8.14e-16

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 84.04  E-value: 8.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  470 LEAVVAEPRRRLGDLPLLDAE------ERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTpdapallfgeerlsYAELNA 543
Cdd:cd17632     10 LEAVTEAIRRPGLRLAQIIATvmtgyaDRPALGQRATELVTDPATGRTTLRLLPRFETIT--------------YAELWE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  544 LANRLAWRLR-EEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLL--------LSQ 614
Cdd:cd17632     76 RVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLavsaehldLAV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  615 QSVL----------------------------ARLPQSDGLQSLLLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGST 666
Cdd:cd17632    156 EAVLeggtpprlvvfdhrpevdahraalesarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGST 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  667 GQPKGVMVRHRALTNFvcsiARQPGMLARDRLLSVTTFSF----DIFG-LELYVPLARGASMLLASreqAQDPEALLDLV 741
Cdd:cd17632    236 GTPKGAMYTERLVATF----WLKVSSIQDIRPPASITLNFmpmsHIAGrISLYGTLARGGTAYFAA---ASDMSTLFDDL 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  742 ERQGVTVLQATPATWRML-------------------CDSERV------DLLRG--CTLLCGGEALAEDLAARMRG-LSA 793
Cdd:cd17632    309 ALVRPTELFLVPRVCDMLfqryqaeldrrsvagadaeTLAERVkaelreRVLGGrlLAAVCGSAPLSAEMKAFMESlLDL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  794 STWNLYGPTETtiwSARFRLGEEARPflggPlentalyILDSEMNPCP---------PGVAGELLIGGDGLARGYHRRPG 864
Cdd:cd17632    389 DLHDGYGSTEA---GAVILDGVIVRP----P-------VLDYKLVDVPelgyfrtdrPHPRGELLVKTDTLFPGYYKRPE 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  865 LTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHQVKirgfrIELGEIET--RLleqdsvrEAVVVAQPGV-- 940
Cdd:cd17632    455 VTAEVFDEDGF-------YRTGDVMAELGPDRLVYVDRRNNVLK-----LSQGEFVTvaRL-------EAVFAASPLVrq 515
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163  941 -------AGPTLVAYLVPTEAALVDAESARqqeLRSALKNSLLAV-----LPDYMVPAHmLLLENLPLTP-NG 1000
Cdd:cd17632    516 ifvygnsERAYLLAVVVPTQDALAGEDTAR---LRAALAESLQRIareagLQSYEIPRD-FLIETEPFTIaNG 584
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1576-2070 8.69e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 83.51  E-value: 8.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1576 RQAAERPRA--TAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYP 1653
Cdd:PRK07768    10 ANARTSPRGmvTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1654 SDRLGYMIEDSGIRL-LLTQRAARERLPLGEGLPCL------LLDAEHEWAGYPESDPQsaVGVDNLAYVIYTSGSTGKP 1726
Cdd:PRK07768    90 RTDLAVWAEDTLRVIgMIGAKAVVVGEPFLAAAPVLeekgirVLTVADLLAADPIDPVE--TGEDDLALMQLTSGSTGSP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1727 KGTLLPHGNVLRLFDATRHWFGFSADD----AW-SLFHSYAFD--FSVWEIFGALLhggrLVIVPYETSRSPEDFLRLLC 1799
Cdd:PRK07768   168 KAVQITHGNLYANAEAMFVAAEFDVETdvmvSWlPLFHDMGMVgfLTVPMYFGAEL----VKVTPMDFLRDPLLWAELIS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1800 RERVTVL---NQTPSAFKQLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFE---RFGDRAPRLVNMYGITETTVHV 1873
Cdd:PRK07768   244 KYRGTMTaapNFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRPEAILPAYGMAEATLAV 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1874 TYRPLSL--------ADL----------DGGAASP---IGEPIPDLSWYLLDAGLNPVPRGCIGELYVGGAGLARGYLnr 1932
Cdd:PRK07768   324 SFSPCGAglvvdevdADLlaalrravpaTKGNTRRlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-- 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1933 pelsctrfvadpfsTTGGRL--------YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEaRLLA-----QPGV 1999
Cdd:PRK07768   402 --------------TMDGFIpaqdadgwLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE-RAAArvegvRPGN 466
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2000 AEAVVLPHEGPGATQLVgyVVTQAAPSDPAALRDTLRQALKASLPEHMV-PAHLLFLE--RLPLTANGKLDRRA 2070
Cdd:PRK07768   467 AVAVRLDAGHSREGFAV--AVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNVVVLGpgSIPKTPSGKLRRAN 538
PLN03102 PLN03102
acyl-activating enzyme; Provisional
1564-2093 9.97e-16

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 83.53  E-value: 9.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1564 FTPASCLHRlierqAAE-RPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAG 1642
Cdd:PLN03102    14 LTPITFLKR-----ASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1643 GAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRA----ARERLPL------GEGLPCLLL------------DAEHE---WA 1697
Cdd:PLN03102    89 AVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplAREVLHLlssedsNLNLPVIFIheidfpkrpsseELDYEcliQR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1698 GYP-------------ESDPQSavgvdnlayVIYTSGSTGKPKGTLLPH-GNVLRLFDATRHW-FGFSADDAWSL--FHS 1760
Cdd:PLN03102   169 GEPtpslvarmfriqdEHDPIS---------LNYTSGTTADPKGVVISHrGAYLSTLSAIIGWeMGTCPVYLWTLpmFHC 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1761 YAFDFSvWeifGALLHGGRLVIVPYETSrsPEDFlRLLCRERVTVLNQTPSAFKQLMQVACAGQ--EVPPLalrHVVFGG 1838
Cdd:PLN03102   240 NGWTFT-W---GTAARGGTSVCMRHVTA--PEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLspRSGPV---HVLTGG 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1839 EALEVqALRPWFERFGDRaprLVNMYGITETTVHVTY------------------------RPLSLADLDGGAASPigep 1894
Cdd:PLN03102   310 SPPPA-ALVKKVQRLGFQ---VMHAYGLTEATGPVLFcewqdewnrlpenqqmelkarqgvSILGLADVDVKNKET---- 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1895 ipdlswylldagLNPVPRG--CIGELYVGGAGLARGYLNRPELSCTRFvadpfstTGGRLyRTGDLARYRCDGVVEYVGR 1972
Cdd:PLN03102   382 ------------QESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAF-------KHGWL-NTGDVGVIHPDGHVEIKDR 441
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1973 IDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPHEGPGATQlVGYVVTQAAPSDPAALRDTLR-------QALKASL 2043
Cdd:PLN03102   442 SKDIIISGGENISSVEVENVLYKYPKVLETAVvaMPHPTWGETP-CAFVVLEKGETTKEDRVDKLVtrerdliEYCRENL 520
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2044 PEHMVPAHLLFLERLPLTANGKLDRRALPAPDASRLQRDYTAPRSELEQR 2093
Cdd:PLN03102   521 PHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDEDNVIKKVHQR 570
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
2639-2941 1.10e-15

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 82.23  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2639 PLSPMQQGMLFHslYQQNSG------DYINQMRLDVeglDPQRFREAWQAALDAHEVLRSGFlwqgaLEKPLQLVRK--- 2709
Cdd:cd19537      3 ALSPIEREWWHK--YQLSTGtssfnvSFACRLSGDV---DRDRLASAWNTVLARHRILRSRY-----VPRDGGLRRSyss 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2710 ---RVEVPFSVHDWRdradlaealdalaagEAGLGFELAEAPLLRLVLVRTgerrhHLIYTNHHILMDGWSNSQLLGEVL 2786
Cdd:cd19537     73 sppRVQRVDTLDVWK---------------EINRPFDLEREDPIRVFISPD-----TLLVVMSHIICDLTTLQLLLREVS 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2787 QRYRGETPSRSDGRYRDYIAWlQRQDAGRTEAFWKQRLQrlGEPTLLVPAFAhGVRGAEGhADRYRQLDVTTSQRLAEFA 2866
Cdd:cd19537    133 AAYNGKLLPPVRREYLDSTAW-SRPASPEDLDFWSEYLS--GLPLLNLPRRT-SSKSYRG-TSRVFQLPGSLYRSLLQFS 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2867 REQKVTLNTLVQAAWLILLQRFTGQDTVAFGATVSGRPAElrGIEEQIGLFINTLPV-VASPCPEQP-IGDWLQAVQ 2941
Cdd:cd19537    208 TSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIrIRFPSSSDAsAADFLRAVR 282
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1129-1436 1.24e-15

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 82.36  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1129 PHSAAYNIPVALRLKGPLRRDALQGALDLLVQRHETLRTTFVEHDGA-PRQVIHPTLpiaieerRPPVAGEDLKGlvETE 1207
Cdd:cd19547     19 PDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAePLQYVRDDL-------APPWALLDWSG--EDP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1208 AHRPFDLQRgPLLRVLLLPLATDECVLV-LTL--------------HHIIADGWSMQVLVDELIRVYAALRHDQPPALAe 1272
Cdd:cd19547     90 DRRAELLER-LLADDRAAGLSLADCPLYrLTLvrlgggrhyllwshHHILLDGWCLSLIWGDVFRVYEELAHGREPQLS- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1273 lPIQ-YADFAAWQR-QWMDGGERERqldYWVSRLG--GEQPLLELPSDRprpQQQSHrgrrigiPLPAELAEALRRL-AQ 1347
Cdd:cd19547    168 -PCRpYRDYVRWIRaRTAQSEESER---FWREYLRdlTPSPFSTAPADR---EGEFD-------TVVHEFPEQLTRLvNE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1348 AEQG---TLFMLLLASFQALLHRYSGQNDIRVGVPIANR--NREETEGLIGFFVNTQVLRAELDGQLPFRELLRQVRQ-- 1420
Cdd:cd19547    234 AARGygvTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRdl 313
                          330
                   ....*....|....*.
gi 2183974163 1421 AVVEAQGHqdLPFEQL 1436
Cdd:cd19547    314 ATTAAHGH--VPLAQI 327
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1563-2070 1.34e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 83.24  E-value: 1.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1563 DFTPASCLHRLIERQAAERPRATAVVY--------GE-RALDYGELNLRANRLAHRLIELGvGPDVLVGLAAERSLEMIV 1633
Cdd:PRK07769    16 RFPPNTNLVRHVERWAKVRGDKLAYRFldfsterdGVaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLI 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1634 GLLAILKAGGAYVPL-DPRYP--SDRLGYMIEDSGIRLLLTQRAARER-------LPLGEGLPCLLLDAEHEWAGypESD 1703
Cdd:PRK07769    95 AFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGvrkffraRPAKERPRVIAVDAVPDEVG--ATW 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1704 PQSAVGVDNLAYVIYTSGSTGKPKGTLLPH----GNVLRLFDAtrhwFGFSADD---AW-SLFHsyafDFSVWEIFGALL 1775
Cdd:PRK07769   173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHlnlpTNVLQVIDA----LEGQEGDrgvSWlPFFH----DMGLITVLLPAL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1776 HGGRLVIV-PYETSRSPEDFLRLLCRE---RVTVLNQTPS-AFKQLMQVACAGQEVPPLALRHV---VFGGEALEVQALR 1847
Cdd:PRK07769   245 LGHYITFMsPAAFVRRPGRWIRELARKpggTGGTFSAAPNfAFEHAAARGLPKDGEPPLDLSNVkglLNGSEPVSPASMR 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1848 PWFERF---GDRAPRLVNMYGITETTVHVTYRP---------LSLADLDGGAASPIGE----PIPDLS--------W-YL 1902
Cdd:PRK07769   325 KFNEAFapyGLPPTAIKPSYGMAEATLFVSTTPmdeeptviyVDRDELNAGRFVEVPAdapnAVAQVSagkvgvseWaVI 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1903 LDA-GLNPVPRGCIGELYVGGAGLARGYLNRPELSCTRF------VADPFSTTG----GRLYRTGDLARYrCDGVVEYVG 1971
Cdd:PRK07769   405 VDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksRLSESHAEGapddALWVRTGDYGVY-FDGELYITG 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1972 RIDHQVKIRGFR-----IELGEIEARLLAQPGVAEAVVLP------------HEG----PGAT--QLVgyVVTQAAP--- 2025
Cdd:PRK07769   484 RVKDLVIIDGRNhypqdLEYTAQEATKALRTGYVAAFSVPanqlpqvvfddsHAGlkfdPEDTseQLV--IVAERAPgah 561
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 2183974163 2026 -SDPAALRDTLRQALKASlpeHMVPAHLLFLE---RLPLTANGKLDRRA 2070
Cdd:PRK07769   562 kLDPQPIADDIRAAIAVR---HGVTVRDVLLVpagSIPRTSSGKIARRA 607
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
49-477 1.43e-15

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 81.97  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   49 PLSYAQERQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDGFRqqvLASVDVPVPV 128
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQ---YVRDDLAPPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  129 TL---AGDD-DAQAQI-RAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARR 203
Cdd:cd19547     80 ALldwSGEDpDRRAELlERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  204 QGIEATL-PDLPiqYADYAIWQRHWLEAG-ERERQLEYWMARLgGGQSVLELPTDRQrpalPSYRGARHElqLPQALGRQ 281
Cdd:cd19547    160 HGREPQLsPCRP--YRDYVRWIRARTAQSeESERFWREYLRDL-TPSPFSTAPADRE----GEFDTVVHE--FPEQLTRL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  282 LQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANR--NRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTR 359
Cdd:cd19547    231 VNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIH 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  360 --VAALGAQSHqdLPFEQLVEALQPERsLSHSPLFQAMYNHQNLGSagrqslaAQLPG--LSVEDLSWGAHS-AQFDLTL 434
Cdd:cd19547    311 rdLATTAAHGH--VPLAQIKSWASGER-LSGGRVFDNLVAFENYPE-------DNLPGddLSIQIIDLHAQEkTEYPIGL 380
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2183974163  435 DTYESEQgVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEP 477
Cdd:cd19547    381 IVLPLQK-LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PLN02654 PLN02654
acetate-CoA ligase
1591-2071 1.91e-15

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 83.02  E-value: 1.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1591 ERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLL 1670
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1671 TQRAARERLPL---------------GEGLP---CLLLDAEH-------EW------------AGYPESDPQSAVGVDNL 1713
Cdd:PLN02654   198 TCNAVKRGPKTinlkdivdaaldesaKNGVSvgiCLTYENQLamkredtKWqegrdvwwqdvvPNYPTKCEVEWVDAEDP 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1714 AYVIYTSGSTGKPKGTLLPHGNVLrLFDATRHWFGF----------SADDAWSLFHSYAfdfsvweIFGALLHGGRLVIv 1783
Cdd:PLN02654   278 LFLLYTSGSTGKPKGVLHTTGGYM-VYTATTFKYAFdykptdvywcTADCGWITGHSYV-------TYGPMLNGATVLV- 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1784 pYETSRSPEDFLR---LLCRERVTVLNQTPSAFKQLMQvacAGQEvppLALRHV-----VFG--GEALEVQALRPWFERF 1853
Cdd:PLN02654   349 -FEGAPNYPDSGRcwdIVDKYKVTIFYTAPTLVRSLMR---DGDE---YVTRHSrkslrVLGsvGEPINPSAWRWFFNVV 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1854 GDRAPRLVNMYGITET-TVHVTYRPLSLADLDGGAASPIGEPIPdlswYLLDAGLNPVPRGCIGELYVGGA--GLARG-Y 1929
Cdd:PLN02654   422 GDSRCPISDTWWQTETgGFMITPLPGAWPQKPGSATFPFFGVQP----VIVDEKGKEIEGECSGYLCVKKSwpGAFRTlY 497
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1930 LNRPELSCTRFvaDPFSTtggrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVV--LPH 2007
Cdd:PLN02654   498 GDHERYETTYF--KPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVvgIEH 571
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2008 EGPGATqLVGYVVTQAAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PLN02654   572 EVKGQG-IYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PRK09192 PRK09192
fatty acyl-AMP ligase;
533-1023 2.19e-15

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 82.36  E-value: 2.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  533 EERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLdpQYPA---------DRLQYMI 603
Cdd:PRK09192    47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMgfggresyiAQLRGML 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQQSVLARLPQSDGLQSLLLDDLERLVHGYPAENPDLPEA-PDSLCYAIYTSGSTGQPKGVMVRHRALTNF 682
Cdd:PRK09192   125 ASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALPRPtPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  683 VCSIARQpGMLAR--DRLLSVTTFSFDIfGLE--LYVPLARGASM-LLASREQAQDPEALLDLVERQGVTVLQATPATWR 757
Cdd:PRK09192   205 LRAISHD-GLKVRpgDRCVSWLPFYHDM-GLVgfLLTPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYE 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  758 mLC-------DSERVDLLRGCTLLCGGE--------ALAEDLAArmRGLSASTW-NLYGPTETTIW-------------- 807
Cdd:PRK09192   283 -LCarrvnskDLAELDLSCWRVAGIGADmirpdvlhQFAEAFAP--AGFDDKAFmPSYGLAEATLAvsfsplgsgivvee 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  808 ---------SARFRLGEEARPF-----LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTaerflpD 873
Cdd:PRK09192   360 vdrdrleyqGKAVAPGAETRRVrtfvnCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQ------D 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  874 PFAADGsrLYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVR--EAVVVAQPGVAGPTLVAyLVp 951
Cdd:PRK09192   434 VLAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVL-LV- 508
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163  952 tEAALVDAEsARQQeLRSALKNSLLA-----VLPDyMVPAHmllleNLPLTPNGKINR-KALPLPDASAVRDAHVAPE 1023
Cdd:PRK09192   509 -QCRISDEE-RRGQ-LIHALAALVRSefgveAAVE-LVPPH-----SLPRTSSGKLSRaKAKKRYLSGAFASLDVAAS 577
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3085-3161 3.82e-15

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 81.84  E-value: 3.82e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 3085 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 3161
Cdd:PRK08279    37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3090-3183 3.85e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 81.49  E-value: 3.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3168
Cdd:PRK07656    10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                           90
                   ....*....|....*
gi 2183974163 3169 YPEERQAYMLEDSGV 3183
Cdd:PRK07656    89 YTADEAAYILARGDA 103
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2206-2599 6.30e-15

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 80.00  E-value: 6.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2206 DGTLLETALQALLAHHDALRLGFrlEDGTWRAEHRAVEAGEVLL----WQQSVADGQALEALAEQVQRS-LDLGSGPLLR 2280
Cdd:cd20483     37 DVNLLQKALSELVRRHEVLRTAY--FEGDDFGEQQVLDDPSFHLividLSEAADPEAALDQLVRNLRRQeLDIEEGEVIR 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2281 ALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQAVA-LPAKT---SAFKAWAE-RLQAHARDGGLEge 2355
Cdd:cd20483    115 GWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLAtVPPPPvqyIDFTLWHNaLLQSPLVQPLLD-- 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2356 rgYWLAQLEG---VSTELP---CDDREGAQSvrHVRSARTELTEEATRRL------LQEAPAAYrtqvndlLLTALARVI 2423
Cdd:cd20483    193 --FWKEKLEGipdASKLLPfakAERPPVKDY--ERSTVEATLDKELLARMkricaqHAVTPFMF-------LLAAFRAFL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2424 GRWTGQADTLIQL----EGHGreelfediDLTRTVGWFTSLFPLRL--SPVAELGASIKRIKEQ-LRAIPHKGLGFGALr 2496
Cdd:cd20483    262 YRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCrmDCDMSFDDLLESTKTTcLEAYEHSAVPFDYI- 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2497 ylgsaedraaLAALPSPR---------ITFNYlgQFDGSFSADSSALFRPSADaagseRDSDAPLDNWLSLNGQVYA-GR 2566
Cdd:cd20483    333 ----------VDALDVPRstshfpigqIAVNY--QVHGKFPEYDTGDFKFTDY-----DHYDIPTACDIALEAEEDPdGG 395
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2183974163 2567 LGIDWSFSAARFSEASILRLADAYRDELLALIE 2599
Cdd:cd20483    396 LDLRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
536-1007 7.27e-15

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 80.72  E-value: 7.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  536 LSYAELNALANRLAWRLREEGV--GSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS 613
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 QqsvlarlpqsDGLQSLLLDDLERLVHGYPAENPdlPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSI----ARQ 689
Cdd:cd05927     86 D----------AGVKVYSLEEFEKLGKKNKVPPP--PPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEIL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  690 PGMLARDRLLSvttfsfdifglelYVPLA---------------------RGASMLLASREQAQDP-------------- 734
Cdd:cd05927    154 NKINPTDVYIS-------------YLPLAhifervvealflyhgakigfySGDIRLLLDDIKALKPtvfpgvprvlnriy 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  735 EALLDLVERQGV-------------------TVLQATPaTWRMLCDSERVDLLRGCT--LLCGGEALAEDLAARMRG-LS 792
Cdd:cd05927    221 DKIFNKVQAKGPlkrklfnfalnyklaelrsGVVRASP-FWDKLVFNKIKQALGGNVrlMLTGSAPLSPEVLEFLRVaLG 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  793 ASTWNLYGPTETTIWSARFRLGEEARPFLGGPLENtALYILDS--EMN-----PCPpgvAGELLIGGDGLARGYHRRPGL 865
Cdd:cd05927    300 CPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPC-AEVKLVDvpEMNydakdPNP---RGEVCIRGPNVFSGYYKDPEK 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  866 TAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHqvkIrgFRIELGE-IETRLLEQDSVReAVVVAQPGVAG-- 942
Cdd:cd05927    376 TAEALDEDGW-------LHTGDIGEWLPNGTLKIIDRKKN---I--FKLSQGEyVAPEKIENIYAR-SPFVAQIFVYGds 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  943 --PTLVAYLVPTEAALVD------------AESARQQELRSALKNSLLAV-----------LPDYMVPAHMLLLENLPLT 997
Cdd:cd05927    443 lkSFLVAIVVPDPDVLKEwaaskgggtgsfEELCKNPEVKKAILEDLVRLgkenglkgfeqVKAIHLEPEPFSVENGLLT 522
                          570
                   ....*....|
gi 2183974163  998 PNGKINRKAL 1007
Cdd:cd05927    523 PTFKLKRPQL 532
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3078-3182 8.42e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 80.23  E-value: 8.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3078 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILK 3157
Cdd:PRK06187     1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                           90       100
                   ....*....|....*....|....*
gi 2183974163 3158 AGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:PRK06187    79 IGAVLHPINIRLKPEEIAYILNDAE 103
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1988-2065 1.63e-14

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 70.65  E-value: 1.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1988 EIEARLLAQPGVAEAVV--LPHEGPGATqLVGYVVtqaAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGK 2065
Cdd:pfam13193    1 EVESALVSHPAVAEAAVvgVPDELKGEA-PVAFVV---LKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1596-2068 1.70e-14

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 79.42  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGvgPDVLVGLAAERSLEMIVGLLAILKAGGAYVPL-------DPRYPSDRLGYMIEDSGIRL 1668
Cdd:PRK05851    34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrgaDDGRWADATLTRFAGIGVRT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1669 LLTQRAARERL-PLGEGLPCLLLDaehEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLR----LFDAT 1743
Cdd:PRK05851   112 VLSHGSHLERLrAVDSSVTVHDLA---TAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSnlrgLNARV 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1744 RhwFGFSADDAWS---LFHSYAFDFsvweIFGALLHGGRLVIVPYET-SRSPEDFLRLLCRERVTVLNQTPSAFKQLMQV 1819
Cdd:PRK05851   189 G--LDAATDVGCSwlpLYHDMGLAF----LLTAALAGAPLWLAPTTAfSASPFRWLSWLSDSRATLTAAPNFAYNLIGKY 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1820 ACAGQEVPPLALRHVVFGGEALEVQALRPWFE---RFGDRAPRLVNMYGITETTVHVT-------YRPLSLADLDGGAA- 1888
Cdd:PRK05851   263 ARRVSDVDLGALRVALNGGEPVDCDGFERFATamaPFGFDAGAAAPSYGLAESTCAVTvpvpgigLRVDEVTTDDGSGAr 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1889 --SPIGEPIPDLSwYLLDAGLNPVPRGC--IGELYVGGAGLARGYLNRPELsctrfvaDPfsttgGRLYRTGDLArYRCD 1964
Cdd:PRK05851   343 rhAVLGNPIPGME-VRISPGDGAAGVAGreIGEIEIRGASMMSGYLGQAPI-------DP-----DDWFPTGDLG-YLVD 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1965 GVVEYVGRIDHQVKIRGFRIELGEIEaRLLAQ-PGVAE-AVVLPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQALKAS 2042
Cdd:PRK05851   409 GGLVVCGRAKELITVAGRNIFPTEIE-RVAAQvRGVREgAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVVQRVASE 487
                          490       500
                   ....*....|....*....|....*...
gi 2183974163 2043 LpeHMVPAHLLFLE--RLPLTANGKLDR 2068
Cdd:PRK05851   488 C--GVVPSDVVFVApgSLPRTSSGKLRR 513
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1711-2067 2.03e-14

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 80.01  E-value: 2.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVL--RLFDATRhwFGFSADD----AWSLFHSyafdfsvweiFG-------ALLHG 1777
Cdd:PRK06814   793 DDPAVILFTSGSEGTPKGVVLSHRNLLanRAQVAAR--IDFSPEDkvfnALPVFHS----------FGltgglvlPLLSG 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1778 GRLVIVPyetsrSPEDFlRLLcRERVTVLNQT----PSAFkqLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERF 1853
Cdd:PRK06814   861 VKVFLYP-----SPLHY-RII-PELIYDTNATilfgTDTF--LNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKF 931
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1854 GdraPRLVNMYGITETTvhvtyrP-LSLADLDGGAASPIGEPIPdlswyLLDAGLNPVP---RGciGELYVGGAGLARGY 1929
Cdd:PRK06814   932 G---IRILEGYGVTETA------PvIALNTPMHNKAGTVGRLLP-----GIEYRLEPVPgidEG--GRLFVRGPNVMLGY 995
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1930 LnRPElscTRFVADPFSttgGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEArlLAQ---PGVAEAVV-L 2005
Cdd:PRK06814   996 L-RAE---NPGVLEPPA---DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAelwPDALHAAVsI 1066
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2006 PHEGPGaTQLVgyVVTQAAPSDPAALrdtLRQALKASLPEHMVPAHLLFLERLPLTANGKLD 2067
Cdd:PRK06814  1067 PDARKG-ERII--LLTTASDATRAAF---LAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
485-891 2.31e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 79.32  E-value: 2.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  485 PLLDAEERA--TLLQRSRLPASEYPagQGVHRLFEAQAGLTPDAPALLFGE------ERLSYAELNALANRLAWRLREEG 556
Cdd:PRK12582    24 PDISVERRAdgSIVIKSRHPLGPYP--RSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  557 VGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPA-----DRLQYMIDDSGLRLLLSQQSVlarlPQSDGLQSLL 631
Cdd:PRK12582   102 LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGA----PFARALAALD 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  632 LDDLERLVHGYPAE-NPDLPEA-------------------PDSLCYAIYTSGSTGQPKGVMVRHRALtnfvCS-IARQP 690
Cdd:PRK12582   178 LLDVTVVHVTGPGEgIASIAFAdlaatpptaavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMM----CAnIAMQE 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  691 GMLARDRLLSVTTfSFD------IFG--LELYVPLARGASMLL-ASREQAQDPEALLDLVERQGVTVLQATPATWRMLCD 761
Cdd:PRK12582   254 QLRPREPDPPPPV-SLDwmpwnhTMGgnANFNGLLWGGGTLYIdDGKPLPGMFEETIRNLREISPTVYGNVPAGYAMLAE 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  762 S-ERVDLLRGC------TLLCGGEALAEDLAARMRGLSAST-------WNLYGPTET------TIWSARfRLGEearpfL 821
Cdd:PRK12582   333 AmEKDDALRRSffknlrLMAYGGATLSDDLYERMQALAVRTtghripfYTGYGATETaptttgTHWDTE-RVGL-----I 406
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  822 GGPLENTALYILdsemnpcPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaaDGSRLYRTGDLARY 891
Cdd:PRK12582   407 GLPLPGVELKLA-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAF-------DEEGFYRLGDAARF 462
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
63-421 2.56e-14

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 78.25  E-value: 2.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   63 MDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEdEQLDGFRQQVLASVDVPV-PVTLAGDDDAQAQIR 141
Cdd:cd19544     17 LAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILW-EGLSEPVQVVWRQAELPVeELTLDPGDDALAQLR 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  142 AFVESEtQQPFDLRNGP-LLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALygarRQGIEATLPDlPIQYADY 220
Cdd:cd19544     96 ARFDPR-RYRLDLRQAPlLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAI----LAGRAAALPP-PVPYRNF 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  221 AIWQRHwleAGERERQLEYWMARLGGgqsVLElptdrqrPALP---------SYRGARHELQLPQALGRQLQALAQREGT 291
Cdd:cd19544    170 VAQARL---GASQAEHEAFFREMLGD---VDE-------PTAPfglldvqgdGSDITEARLALDAELAQRLRAQARRLGV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  292 TlfmllLASfqaLLH--------RYSGQDEIRVGVPVANRNR--VETERLIGFFVNTQVLRADLDaQMPFLDLLQQT--R 359
Cdd:cd19544    237 S-----PAS---LFHlawalvlaRCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRLG-GRSVREAVRQThaR 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  360 VAALgaqshqdLPFEQ--LVEAlQPERSLSHS-PLFQAMYNHQNLGSAGRQSLAAQLPG---------------LSVEDL 421
Cdd:cd19544    308 LAEL-------LRHEHasLALA-QRCSGVPAPtPLFSALLNYRHSAAAAAAAALAAWEGiellggeertnypltLSVDDL 379
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1021-1095 2.91e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 70.27  E-value: 2.91e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 1021 APEGELERAMAAIWSEVLKL--GHIGRDDNFF-ELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQL 1095
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1596-2040 3.12e-14

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 78.41  E-value: 3.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGgayVPLDPRYpsDRLGymieDSGIRLLLTQRAA 1675
Cdd:cd17639      8 YAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY--ATLG----EDALIHSLNETEC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1676 RerlplgeglpCLLLDAEHewagypesdpqsavgvDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHW-FGFSADDA 1754
Cdd:cd17639     79 S----------AIFTDGKP----------------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvPELLGPDD 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1755 WSLfhSY-----AFDFSVWEIFgaLLHGGRL------VIVPYETSRSPEDFL-----------RLLCRERVTVLNQTPSA 1812
Cdd:cd17639    133 RYL--AYlplahIFELAAENVC--LYRGGTIgygsprTLTDKSKRGCKGDLTefkptlmvgvpAIWDTIRKGVLAKLNPM 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1813 -------FKQLMQVACAGQEVPPLA--LRHVVF----------------GGEALEVQALRpWFERFGdrAPrLVNMYGIT 1867
Cdd:cd17639    209 gglkrtlFWTAYQSKLKALKEGPGTplLDELVFkkvraalggrlrymlsGGAPLSADTQE-FLNIVL--CP-VIQGYGLT 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1868 ETTVHVTYrpLSLADLDGGAaspIGEPIPDLSWYLLD---AGL---NPVPRGcigELYVGGAGLARGYLNRPELSCTRFv 1941
Cdd:cd17639    285 ETCAGGTV--QDPGDLETGR---VGPPLPCCEIKLVDweeGGYstdKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF- 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1942 adpfstTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIR-GFRIELGEIEARLLAQPGVAEAVVLPHegPGATQLVGYVV 2020
Cdd:cd17639    356 ------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYAD--PDKSYPVAIVV 427
                          490       500
                   ....*....|....*....|
gi 2183974163 2021 TqaapsDPAALRDTLRQALK 2040
Cdd:cd17639    428 P-----NEKHLTKLAEKHGV 442
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
575-1007 5.10e-14

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 78.17  E-value: 5.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  575 VALLAVLKAGGAYVPLDPQYPADRLQYMIDDSG-------------LRLLLSQQSV----LAR----LPQSDG-LQSLLL 632
Cdd:PRK08974    89 IALFGILRAGMIVVNVNPLYTPRELEHQLNDSGakaivivsnfahtLEKVVFKTPVkhviLTRmgdqLSTAKGtLVNFVV 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  633 DDLERLVHGYpaenpDLPEA---------------------PDSLCYAIYTSGSTGQPKGVMVRHR-ALTN-FVCSIARQ 689
Cdd:PRK08974   169 KYIKRLVPKY-----HLPDAisfrsalhkgrrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRnMLANlEQAKAAYG 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  690 PgMLARDRLLSVTTFS-FDIFGLE----LYVPLarGASMLLASreQAQDPEALLDLVERQGVTVLQATPATWRMLCDSER 764
Cdd:PRK08974   244 P-LLHPGKELVVTALPlYHIFALTvnclLFIEL--GGQNLLIT--NPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEE 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  765 VDLLRGCTL---LCGGEALAEDLAARMRGLSAStwNL---YGPTETTIWSArfrlgeeARPF--------LGGPLENTAL 830
Cdd:PRK08974   319 FQELDFSSLklsVGGGMAVQQAVAERWVKLTGQ--YLlegYGLTECSPLVS-------VNPYdldyysgsIGLPVPSTEI 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  831 YILDSEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAErFLPDPFAAdgsrlyrTGDLARYRADGVIEYLGRIDHQVKIR 910
Cdd:PRK08974   390 KLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVS 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  911 GFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVdaesarQQELRSALKNSLLAvlpdYMVPAHML 989
Cdd:PRK08974   462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPsEVSGEAVKIFVVKKDPSLT------EEELITHCRRHLTG----YKVPKLVE 531
                          490
                   ....*....|....*...
gi 2183974163  990 LLENLPLTPNGKINRKAL 1007
Cdd:PRK08974   532 FRDELPKSNVGKILRREL 549
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
523-1007 5.41e-14

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 78.13  E-value: 5.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLF-----GEER-LSYAELNALANRLAWRLREEGVGSDVLVGIALergvPMV----VALLAVLKAGGAYVPLDP 592
Cdd:cd05967     64 RGDQIALIYdspvtGTERtYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYM----PMIpeaaIAMLACARIGAIHSVVFG 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  593 QYPADRLQYMIDDSGLRLLLSQQSVLA---------------RLPQSDGLQSLLLD---------------DLERLVHGY 642
Cdd:cd05967    140 GFAAKELASRIDDAKPKLIVTASCGIEpgkvvpykplldkalELSGHKPHHVLVLNrpqvpadltkpgrdlDWSELLAKA 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  643 PAENPDLPEAPDSLcYAIYTSGSTGQPKGVmVRHRA--LTNFVCSIARQPGMLARDRLLS------VTTFSFDIFGlely 714
Cdd:cd05967    220 EPVDCVPVAATDPL-YILYTSGTTGKPKGV-VRDNGghAVALNWSMRNIYGIKPGDVWWAasdvgwVVGHSYIVYG---- 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  715 vPLARGASMLL--ASREQAQDPEALLDLVERQGVTVLQATPATWRML-CDSERVDLLRGC------TLLCGGEALAEDLA 785
Cdd:cd05967    294 -PLLHGATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrKEDPDGKYIKKYdlsslrTLFLAGERLDPPTL 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  786 ARMRG-LSASTWNLYGPTETTiWS-ARFRLGEEARPFLGG----PLENTALYILDSEMNPCPPGVAGELLIGGD---GLA 856
Cdd:cd05967    373 EWAENtLGVPVIDHWWQTETG-WPiTANPVGLEPLPIKAGspgkPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCL 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  857 RGYHRRPgltaERFLpDPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVA 936
Cdd:cd05967    452 LTLWKND----ERFK-KLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  937 QP-GVAGPTLVAYLVPTEAALVDAESArQQELRSALKNSLLAVlpdyMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05967    527 VRdELKGQVPLGLVVLKEGVKITAEEL-EKELVALVREQIGPV----AAFRLVIFVKRLPKTRSGKILRRTL 593
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2085-2152 5.71e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 69.50  E-value: 5.71e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2085 APRSELEQRLAAIWADVLKL--GRVGLDDNFF-ELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIRGLA 2152
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
PRK08162 PRK08162
acyl-CoA synthetase; Validated
524-1007 7.13e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 77.68  E-value: 7.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMI 603
Cdd:PRK08162    32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  604 DDSGLRLLLSQQ--SVLAR--LPQSDGLQSLLLD---------------DLERLV-HGypaeNPDLP-EAPDSLCYAI-- 660
Cdd:PRK08162   112 RHGEAKVLIVDTefAEVAReaLALLPGPKPLVIDvddpeypggrfigalDYEAFLaSG----DPDFAwTLPADEWDAIal 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  661 -YTSGSTGQPKGVMVRHR-----ALTNFV-CSIARQPGMlardrLLSVTTFSFDIFGLELYVPLARGASMLLasreQAQD 733
Cdd:PRK08162   188 nYTSGTTGNPKGVVYHHRgaylnALSNILaWGMPKHPVY-----LWTLPMFHCNGWCFPWTVAARAGTNVCL----RKVD 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  734 PEALLDLVERQGVTVLQATPATWRMLC---DSERVDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTET----TI 806
Cdd:PRK08162   259 PKLIFDLIREHGVTHYCGAPIVLSALInapAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpaTV 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 ------WSArfrLGEEARPFLGG------PLENtALYILDSE-MNPCPPG--VAGELLIGGDGLARGYHRRPGLTAERFl 871
Cdd:PRK08162   339 cawqpeWDA---LPLDERAQLKArqgvryPLQE-GVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATEEAF- 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  872 pdpfaADGsrLYRTGDLARYRADGVIeylgridhQVKIR--------GFRIELGEIETRLLEQDSVREAVVVAQPGVA-G 942
Cdd:PRK08162   414 -----AGG--WFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKwG 478
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  943 PTLVAYLvpteaALVDAESARQQELRSALKnsllAVLPDYMVPAHMLLLEnLPLTPNGKINRKAL 1007
Cdd:PRK08162   479 EVPCAFV-----ELKDGASATEEEIIAHCR----EHLAGFKVPKAVVFGE-LPKTSTGKIQKFVL 533
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1547-1961 1.21e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 77.01  E-value: 1.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1547 EAEARAD--LLQWNPGPQDFTPASCLHRLIER--QAAERP---RATAVVYGERALDYGELNLRANRLAHRLIELGVGPDV 1619
Cdd:PRK12582    27 SVERRADgsIVIKSRHPLGPYPRSIPHLLAKWaaEAPDRPwlaQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGR 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1620 LVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY---PSD--RLGYMIEDSGIRLLLTQRAAR-ER--------------- 1678
Cdd:PRK12582   107 PVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGAPfARalaaldlldvtvvhv 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1679 LPLGEGLPCLLLDaehEWAGYPESD----PQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDA 1754
Cdd:PRK12582   187 TGPGEGIASIAFA---DLAATPPTAavaaAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPP 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1755 wslfHSYAFDFSVWE-------IFGALL-HGGRLVI-----VP---YETSR-----SPedflrllcrervTVLNQTPSAF 1813
Cdd:PRK12582   264 ----PPVSLDWMPWNhtmggnaNFNGLLwGGGTLYIddgkpLPgmfEETIRnlreiSP------------TVYGNVPAGY 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLmqvACAGQEVPPLA------LRHVVFGGEAL------EVQALRpwFERFGDRAPrLVNMYGITET-----TVH-VTY 1875
Cdd:PRK12582   328 AML---AEAMEKDDALRrsffknLRLMAYGGATLsddlyeRMQALA--VRTTGHRIP-FYTGYGATETaptttGTHwDTE 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1876 RPlsladldggaaSPIGEPIPDLSwylldagLNPVPRGCIGELYVGGAGLARGYLNRPELSctrfvADPFSTTGgrLYRT 1955
Cdd:PRK12582   402 RV-----------GLIGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELT-----AAAFDEEG--FYRL 456

                   ....*.
gi 2183974163 1956 GDLARY 1961
Cdd:PRK12582   457 GDAARF 462
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
532-1027 1.85e-13

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 76.36  E-value: 1.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  532 GEERLSYAELNALANRLAWRLREE-GVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRL 610
Cdd:PRK05620    35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  611 LLSQQSVLAR----LPQSDGLQSLLL-------------------DDLERLVHGYPAEN--PDLPE-APDSLCYaiyTSG 664
Cdd:PRK05620   115 IVADPRLAEQlgeiLKECPCVRAVVFigpsdadsaaahmpegikvYSYEALLDGRSTVYdwPELDEtTAAAICY---STG 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  665 STGQPKGVMVRHRALtnFVCSIarqpGMLARDRlLSVTTFSFDIFGLELY------VPLA---RGASMLLASREqaQDPE 735
Cdd:PRK05620   192 TTGAPKGVVYSHRSL--YLQSL----SLRTTDS-LAVTHGESFLCCVPIYhvlswgVPLAafmSGTPLVFPGPD--LSAP 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  736 ALLDLVERQGVTVLQATPATWRMLC------DSERVDLLrgcTLLCGGEALAEDLaarmrglsASTW---------NLYG 800
Cdd:PRK05620   263 TLAKIIATAMPRVAHGVPTLWIQLMvhylknPPERMSLQ---EIYVGGSAVPPIL--------IKAWeerygvdvvHVWG 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  801 PTETTiwsarfRLGEEARPFLGGPLENTALY---------------ILDSEMNPCPPGVAGELLIGGDGLARGYHRRP-- 863
Cdd:PRK05620   332 MTETS------PVGTVARPPSGVSGEARWAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPte 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  864 --GLTAERF-------LPDPFAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVV 934
Cdd:PRK05620   406 egGGAASTFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  935 VaqpGVAGPTLVAYlvPTEAALVDAESARQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKALplpdasa 1014
Cdd:PRK05620   484 I---GYPDDKWGER--PLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL------- 551
                          570
                   ....*....|...
gi 2183974163 1015 vrDAHVApEGELE 1027
Cdd:PRK05620   552 --RQHLA-DGDFE 561
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
523-1018 2.12e-13

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 76.16  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLFGEE----RLSYAELNALANRLAWRLREEGVG-SDVLVGIaLERGVPMVVALLAVLKAGGAYVPLDPQYPA- 596
Cdd:cd05943     82 ADDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKpGDRVAGY-LPNIPEAVVAMLATASIGAIWSSCSPDFGVp 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  597 ---DRLQyMIDDsglRLLLSQQSVL---ARLPQSDGLQSLL--LDDLERLVH---GYPAENPDLPEAPDSLCYA------ 659
Cdd:cd05943    161 gvlDRFG-QIEP---KVLFAVDAYTyngKRHDVREKVAELVkgLPSLLAVVVvpyTVAAGQPDLSKIAKALTLEdflatg 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  660 ------------------IYTSGSTGQPK-------GVMVRHRALTNFVCSIarQPGmlarDRLLSVTT-----FSFDIF 709
Cdd:cd05943    237 aagelefeplpfdhplyiLYSSGTTGLPKcivhgagGTLLQHLKEHILHCDL--RPG----DRLFYYTTcgwmmWNWLVS 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  710 GlelyvpLARGASMLLASREQ-AQDPEALLDLVERQGVTVLqATPATWRMLCD------SERVDLLRGCTLLCGGEALA- 781
Cdd:cd05943    311 G------LAVGATIVLYDGSPfYPDTNALWDLADEEGITVF-GTSAKYLDALEkaglkpAETHDLSSLRTILSTGSPLKp 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  782 -------EDLAARMRGLSAStwnlyGPTEttIWSArFRLGEEARPFLGGPLE----NTALYILDSEMNPCpPGVAGELLI 850
Cdd:cd05943    384 esfdyvyDHIKPDVLLASIS-----GGTD--IISC-FVGGNPLLPVYRGEIQcrglGMAVEAFDEEGKPV-WGEKGELVC 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  851 ggdglARGYHRRPgltaERFLPDPfaaDGSR-----------LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 919
Cdd:cd05943    455 -----TKPFPSMP----VGFWNDP---DGSRyraayfakypgVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  920 ETRLLEQDSVREAVVVAQPGVAGPT-LVAYLVPTEAALVDAEsaRQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTP 998
Cdd:cd05943    523 YRVVEKIPEVEDSLVVGQEWKDGDErVILFVKLREGVELDDE--LRKRIRSTIRSALSP----RHVPAKIIAVPDIPRTL 596
                          570       580
                   ....*....|....*....|....*..
gi 2183974163  999 NGKIN----RKAL---PLPDASAVRDA 1018
Cdd:cd05943    597 SGKKVevavKKIIagrPVKNAGALANP 623
prpE PRK10524
propionyl-CoA synthetase; Provisional
1571-2073 2.65e-13

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 76.14  E-value: 2.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1571 HRLIERQAAERPRATAVVY------GERALDYGELNLRANRLAHRLIELGV--GPDVLVGLA--AERSLEMivglLAILK 1640
Cdd:PRK10524    56 HNAVDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVqrGDRVLIYMPmiAEAAFAM----LACAR 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1641 AGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRA-AR------------ERLPLGEGLP--CLLLD-----------AEH 1694
Cdd:PRK10524   132 IGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAgSRggkvvpykplldEAIALAQHKPrhVLLVDrglapmarvagRDV 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1695 EWAGYPESDPQSAVGVDNL-----AYVIYTSGSTGKPKGtllphgnVLR--------LFDATRHWFG-------FSADD- 1753
Cdd:PRK10524   212 DYATLRAQHLGARVPVEWLesnepSYILYTSGTTGKPKG-------VQRdtggyavaLATSMDTIFGgkagetfFCASDi 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1754 AWSLFHSYAfdfsvweIFGALLHGgrLVIVPYE---TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQvacagQEVPPL- 1829
Cdd:PRK10524   285 GWVVGHSYI-------VYAPLLAG--MATIMYEglpTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKK-----QDPALLr 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1830 -----ALRHVVFGGEALE-------VQAL-RP-----------W-----FERFGDRAPRL----VNMYG-----ITETTv 1871
Cdd:PRK10524   351 khdlsSLRALFLAGEPLDeptaswiSEALgVPvidnywqtetgWpilaiARGVEDRPTRLgspgVPMYGynvklLNEVT- 429
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1872 hvtyrplsladldggaaspiGEPI-PDLSWYLLDAGlnPVPRGCIGELYVGGAglargylnrpelsctRFVADPFSTTGG 1950
Cdd:PRK10524   430 --------------------GEPCgPNEKGVLVIEG--PLPPGCMQTVWGDDD---------------RFVKTYWSLFGR 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1951 RLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAE-AVVlphegpG-ATQLVGYV-VTQAAPSD 2027
Cdd:PRK10524   473 QVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEvAVV------GvKDALKGQVaVAFVVPKD 546
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 2028 PAALRDT-LRQALKASLPEHMV--------PAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:PRK10524   547 SDSLADReARLALEKEIMALVDsqlgavarPARVWFVSALPKTRSGKLLRRAIQA 601
PLN03102 PLN03102
acyl-activating enzyme; Provisional
661-1037 3.90e-13

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 75.44  E-value: 3.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  661 YTSGSTGQPKGVMVRHRA--LTNFVCSIARQPGMLARdRLLSVTTFSFDIFGLELYVPlARGASMLLASREQAqdPEALL 738
Cdd:PLN03102   193 YTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCPV-YLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTA--PEIYK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  739 DlVERQGVTVLQATPATWRMLCDSERVDLLRGCT---LLCGGEALAEDLAARMRGLSASTWNLYGPTETT------IWSA 809
Cdd:PLN03102   269 N-IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgpvlfcEWQD 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  810 RF-RLGEEARPFLGGP--LENTALYILD------SEMNPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaadGS 880
Cdd:PLN03102   348 EWnRLPENQQMELKARqgVSILGLADVDvknketQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF--------KH 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLV-----PTEA 954
Cdd:PLN03102   420 GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHpTWGETPCAFVVlekgeTTKE 499
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  955 ALVDAESARQQELRSALKNSLlavlPDYMVPAHMLLLENLPLTPNGKINRKAL-PLPDASAVRDAHVAPEGELERAMAAI 1033
Cdd:PLN03102   500 DRVDKLVTRERDLIEYCRENL----PHFMCPRKVVFLQELPKNGNGKILKPKLrDIAKGLVVEDEDNVIKKVHQRPVEHF 575

                   ....
gi 2183974163 1034 WSEV 1037
Cdd:PLN03102   576 SSRL 579
PRK05857 PRK05857
fatty acid--CoA ligase;
499-1007 5.22e-13

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 74.66  E-value: 5.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  499 SRLPASEypagqgVHRLFEaQAGLTPDAPALLF--GEERLSYAELNALANRLAWRLREEGV--GSDVLVgiALERGVPMV 574
Cdd:PRK05857    10 PQLPSTV------LDRVFE-QARQQPEAIALRRcdGTSALRYRELVAEVGGLAADLRAQSVsrGSRVLV--ISDNGPETY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  575 VALLAVLKAGGAYVPLDPQYPA---DRLQYMIDDSGlrLLLSQQSVLARLPQSDGLQSL------LLDDLERLVHG---- 641
Cdd:PRK05857    81 LSVLACAKLGAIAVMADGNLPIaaiERFCQITDPAA--ALVAPGSKMASSAVPEALHSIpviavdIAAVTRESEHSldaa 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  642 YPAENPDLpeAPDSLCYAIYTSGSTGQPKGVMVRHRalTNF-VCSIARQPGMLARDRLLSVTTFS----FDIFGL-ELYV 715
Cdd:PRK05857   159 SLAGNADQ--GSEDPLAMIFTSGTTGEPKAVLLANR--TFFaVPDILQKEGLNWVTWVVGETTYSplpaTHIGGLwWILT 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  716 PLARGASMLLASREQAqdpeALLDLVERQGVTVLQATPATWRMLCDSER-----VDLLRgctLLCGGEALAedLAARMRG 790
Cdd:PRK05857   235 CLMHGGLCVTGGENTT----SLLEILTTNAVATTCLVPTLLSKLVSELKsanatVPSLR---LVGYGGSRA--IAADVRF 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  791 LSAS---TWNLYGPTETTIWS----------ARFRLGEEARPFLGgplenTALYILDSE-MNPCPPGVA-----GELLIG 851
Cdd:PRK05857   306 IEATgvrTAQVYGLSETGCTAlclptddgsiVKIEAGAVGRPYPG-----VDVYLAATDgIGPTAPGAGpsasfGTLWIK 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  852 GDGLARGYHRRPGLTAErflpdpFAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEtRLLEQDS-VR 930
Cdd:PRK05857   381 SPANMLGYWNNPERTAE------VLIDG--WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSgVR 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  931 EAVVVAQPGVAGPTLVAYLVpTEAALVDAESARqqelrsALKNSLLAVL---PDYMV-PAHMLLLENLPLTPNGKINRKA 1006
Cdd:PRK05857   452 EAACYEIPDEEFGALVGLAV-VASAELDESAAR------ALKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRAS 524

                   .
gi 2183974163 1007 L 1007
Cdd:PRK05857   525 L 525
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
2879-3174 5.83e-13

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 75.49  E-value: 5.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2879 AAWLILLQRFTGQDTVAFG--ATVSGRPAELRgieeqigLFINtlpvvaspcPEQPIGDWLQAVQGEnlalrefehtply 2956
Cdd:TIGR03443   54 AAFAALVYRLTGDEDIVLGtsSNKSGRPFVLR-------LNIT---------PELSFLQLYAKVSEE------------- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2957 dIQRWAGQVGEAlFDNILvfeNYPVSAALAEETPADMRI---DALSNQE---QTHYPLTL---LVSAGETLELHYSYSRQ 3027
Cdd:TIGR03443  105 -EKEGASDIGVP-FDELS---EHIQAAKKLERTPPLFRLafqDAPDNQQttySTGSTTDLtvfLTPSSPELELSIYYNSL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3028 AFDEAAIECLAERLERLLLGMCENPGASLGELDSLAVAERYQLLE-----GWnataAEYplqRG-VHRLFEEQVER---- 3097
Cdd:TIGR03443  180 LFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdr 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3098 -----TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3172
Cdd:TIGR03443  253 tcvveTPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPA 332

                   ..
gi 2183974163 3173 RQ 3174
Cdd:TIGR03443  333 RQ 334
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
498-1007 6.95e-13

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 74.25  E-value: 6.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  498 RSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGE--ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVV 575
Cdd:PLN02330    16 RSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  576 ALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQSVLARLpQSDGLQSLLLDdlERLVHGypAEN-PDLPEAPD 654
Cdd:PLN02330    96 VALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKV-KGLGLPVIVLG--EEKIEG--AVNwKELLEAAD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 --------------SLCYAIYTSGSTGQPKGVMVRHRALTNFVCS--IARQPGMLARDRLLSVTTFsFDIFGLE--LYVP 716
Cdd:PLN02330   171 ragdtsdneeilqtDLCALPFSSGTTGISKGVMLTHRNLVANLCSslFSVGPEMIGQVVTLGLIPF-FHIYGITgiCCAT 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  717 LARGASMLLASReqaQDPEALLDLVERQGVTVLQATPATWRMLCDS---ERVDL--LRGCTLLCGGEALAEDL--AARMR 789
Cdd:PLN02330   250 LRNKGKVVVMSR---FELRTFLNALITQEVSFAPIVPPIILNLVKNpivEEFDLskLKLQAIMTAAAPLAPELltAFEAK 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  790 GLSASTWNLYGPTE---TTIWSARFRLGE--EARPFLGGPLENTALYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRP 863
Cdd:PLN02330   327 FPGVQVQEAYGLTEhscITLTHGDPEKGHgiAKKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCVMQGYYNNK 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  864 GLTAERFlpdpfaaDGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVAGP 943
Cdd:PLN02330   407 EETDRTI-------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163  944 TLVAylvpteAALVDAESARQQElrSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PLN02330   480 EIPA------ACVVINPKAKESE--EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1947-2077 7.41e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 73.53  E-value: 7.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1947 TTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQLVGYVVTQAAPS 2026
Cdd:PRK08308   287 KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI 366
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 2027 DPAALRDTLRQalkaSLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDAS 2077
Cdd:PRK08308   367 DPVQLREWCIQ----HLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVT 413
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1711-2067 8.72e-13

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 74.36  E-value: 8.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD----AWSLFHsyAFDFSVwEIFGALLHGGRLVIVPye 1786
Cdd:PRK08043   365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDrfmsALPLFH--SFGLTV-GLFTPLLTGAEVFLYP-- 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1787 tsrSPEDFL---RLLCRERVTVLNQTpSAFkqLMQVACAGQEVPPLALRHVVFGGEALEVQALRPWFERFGdraPRLVNM 1863
Cdd:PRK08043   440 ---SPLHYRivpELVYDRNCTVLFGT-STF--LGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG---LRILEG 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1864 YGITETTVHVTYR-PLsladldggAASP--IGEPIPDLswyllDAGLNPVP---RGciGELYVGGAGLARGYL--NRPEL 1935
Cdd:PRK08043   511 YGVTECAPVVSINvPM--------AAKPgtVGRILPGM-----DARLLSVPgieQG--GRLQLKGPNIMNGYLrvEKPGV 575
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1936 SCTRFVADPFSTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEA-RLLAQPGVAEAVVLPHEGPGATQ 2014
Cdd:PRK08043   576 LEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKGEA 655
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 2015 LVGYVvtqaapSDPAALRDTLRQALKAS-LPEHMVPAHLLFLERLPLTANGKLD 2067
Cdd:PRK08043   656 LVLFT------TDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2672-2952 8.93e-13

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 73.45  E-value: 8.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2672 DPQRFREAWQAALDAHEVLRSGFLWQGalEKPLQLVRKRVEVPFSVHDWRDRADLAEALDALAAGEAGLGFELAEAPLLR 2751
Cdd:cd20483     37 DVNLLQKALSELVRRHEVLRTAYFEGD--DFGEQQVLDDPSFHLIVIDLSEAADPEAALDQLVRNLRRQELDIEEGEVIR 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2752 LVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRYRGETPSRSDG-------RYRDYIAWLQR--QDAGRTE--AFW 2820
Cdd:cd20483    115 GWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLAtvppppvQYIDFTLWHNAllQSPLVQPllDFW 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2821 KQRLQRLGEPTLLVPaFAHGVR--GAEGHADRYRQ-LDVTTSQRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAFG 2897
Cdd:cd20483    195 KEKLEGIPDASKLLP-FAKAERppVKDYERSTVEAtLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIG 273
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 2898 ATVSGRP-AELrgiEEQIGLFINTLPVVASPCPEQPIGDWLQAVQGenLALREFEH 2952
Cdd:cd20483    274 MVDGDRPhPDF---DDLVGFFVNMLPIRCRMDCDMSFDDLLESTKT--TCLEAYEH 324
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1028-1087 9.59e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 65.28  E-value: 9.59e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 1028 RAMAAIWSEVLKLGH--IGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRA 1087
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
535-1014 1.15e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 73.63  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEGVGS-DVLVGIALERGVPMVvALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS 613
Cdd:PRK06018    39 RTTYAQIHDRALKVSQALDRDGIKLgDRVATIAWNTWRHLE-AWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 QQSVLARLPQ-SDGLQSLllddlER-LVHGYPAENPDlPEAPDSLCYAI-----------------------YTSGSTGQ 668
Cdd:PRK06018   118 DLTFVPILEKiADKLPSV-----ERyVVLTDAAHMPQ-TTLKNAVAYEEwiaeadgdfawktfdentaagmcYTSGTTGD 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  669 PKGVMVRHRalTNFVCS-IARQP---GMLARDRLLSVT-TFSFDIFGLELYVPlARGASMLLASreqAQ-DPEALLDLVE 742
Cdd:PRK06018   192 PKGVLYSHR--SNVLHAlMANNGdalGTSAADTMLPVVpLFHANSWGIAFSAP-SMGTKLVMPG---AKlDGASVYELLD 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  743 RQGVTVLQATPATWRMLC---DSERVDLLRGCTLLCGGEALAEDLAARMRGLSASTWNLYGPTETtiwSARFRLGEEARP 819
Cdd:PRK06018   266 TEKVTFTAGVPTVWLMLLqymEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEM---SPLGTLAALKPP 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 FLGGPLE--------------NTALYILDSEMNPCP-PGVA-GELLIGGDGLARGYHRRPGltaerflpDPFAADGsrLY 883
Cdd:PRK06018   343 FSKLPGDarldvlqkqgyppfGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYRVDG--------EILDDDG--FF 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  884 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA---GPTLVAYLVPteaalvdAE 960
Cdd:PRK06018   413 DTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKwdeRPLLIVQLKP-------GE 485
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  961 SARQQELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGKINRKAL-------PLPDASA 1014
Cdd:PRK06018   486 TATREEILKYMDGK----IAKWWMPDDVAFVDAIPHTATGKILKTALreqfkdyKLPTAAA 542
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3076-3183 1.29e-12

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 73.60  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3076 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVV 3150
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2183974163 3151 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:COG1022     81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGA 113
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
1596-2086 2.51e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 72.43  E-value: 2.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAA---ERSLEMIVGllaILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLL--- 1669
Cdd:PRK07008    42 YRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYG---VSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVlfd 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1670 -----LTQRAA--------------RERLPlGEGLPCL----LLDAEHEWAGYPESDPQSAvgvdnlAYVIYTSGSTGKP 1726
Cdd:PRK07008   119 ltflpLVDALApqcpnvkgwvamtdAAHLP-AGSTPLLcyetLVGAQDGDYDWPRFDENQA------SSLCYTSGTTGNP 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1727 KGTLLPH-GNVLRLF-----DAtrhwFGFSADDAW----SLFHSYAfdfsvWEI-FGALLHGGRLVIV-PYETSRSpedF 1794
Cdd:PRK07008   192 KGALYSHrSTVLHAYgaalpDA----MGLSARDAVlpvvPMFHVNA-----WGLpYSAPLTGAKLVLPgPDLDGKS---L 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1795 LRLLCRERVTVLNQTPSAFKQLMQ-VACAGQEVPPlaLRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITE----- 1868
Cdd:PRK07008   260 YELIEAERVTFSAGVPTVWLGLLNhMREAGLRFST--LRRTVIGGSACPPAMIRTFEDEYG---VEVIHAWGMTEmsplg 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1869 TTVHVTYRPLSLADldgGAASPI----GEPIPDLSWYLLDAGLNPVPRG--CIGELYVGGAGLARGYLNRPelsctrfvA 1942
Cdd:PRK07008   335 TLCKLKWKHSQLPL---DEQRKLlekqGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVIDRYFRGD--------A 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1943 DPFSTtggRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEA--VVLPHegPGATQLVGYVV 2020
Cdd:PRK07008   404 SPLVD---GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAacIACAH--PKWDERPLLVV 478
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2021 TQAAPSDpaALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALpapdasRLQ-RDYTAP 2086
Cdd:PRK07008   479 VKRPGAE--VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL------REQfRDYVLP 537
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
531-1007 4.25e-12

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 71.69  E-value: 4.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  531 FGEERLSYAELNALANRLA-WRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLR 609
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAhWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  610 LLLSQqsvlarlpqsdglqslllddlerlvhgypaenpdlpeaPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQ 689
Cdd:cd05937     81 FVIVD--------------------------------------PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHD 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  690 PGMLARDRLLSVttfsfdifglelyVPLARGASMLLAsreqaqdpeALLDLVERQGVTVLQATPAT--WRMLCDSERVDL 767
Cdd:cd05937    123 LNLKNGDRTYTC-------------MPLYHGTAAFLG---------ACNCLMSGGTLALSRKFSASqfWKDVRDSGATII 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  768 L---RGCTLLCGGEALAEDLAARMR-----GLSASTWN-------------LYGPTETTIWSARFRLGeearPFLGGPLE 826
Cdd:cd05937    181 QyvgELCRYLLSTPPSPYDRDHKVRvawgnGLRPDIWErfrerfnvpeigeFYAATEGVFALTNHNVG----DFGAGAIG 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  827 NTALYI------------LDSE-----MNP-------CPPGVAGELLI----GGDGLARGYHRRPGLTAERFLPDPFAAd 878
Cdd:cd05937    257 HHGLIRrwkfenqvvlvkMDPEtddpiRDPktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRK- 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  879 GSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVV--VAQPGVAGPTLVAYLVPTEAAL 956
Cdd:cd05937    336 GDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSA 415
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  957 VDAEsARQQELRS-ALKNsllavLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05937    416 VPTE-FTKSLLASlARKN-----LPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
643-1007 4.66e-12

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 71.25  E-value: 4.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  643 PAENPDLPEAPDSL-CYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQP---GMLARDRLLSV------TTFSFDIFGLE 712
Cdd:cd05929    113 EGGSPETPIEDEAAgWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAAlgfGPGADSVYLSPaplyhaAPFRWSMTALF 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  713 LyvplarGASMLLASReqaQDPEALLDLVERQGVTVLQATPATW-RMLCDSERVdllRGctllcggealAEDLAARMRGL 791
Cdd:cd05929    193 M------GGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAV---RN----------AYDLSSLKRVI 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  792 SAST------------------WNLYGPTE----TTIWSARF--RLGEEARPFLGGplentaLYILDSEMNPCPPGVAGE 847
Cdd:cd05929    251 HAAApcppwvkeqwidwggpiiWEYYGGTEgqglTIINGEEWltHPGSVGRAVLGK------VHILDEDGNEVPPGEIGE 324
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  848 L-LIGGDGLArgYHRRPGLTAERFLPDPFAAdgsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQ 926
Cdd:cd05929    325 VyFANGPGFE--YTNDPEKTAAARNEGGWST-------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  927 DSVREAVVVaqpGVAGPTL---VAYLVPTeAALVDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNGKIN 1003
Cdd:cd05929    396 PKVLDAAVV---GVPDEELgqrVHAVVQP-APGADAGTALAEELIAFLRDRLSR----YKCPRSIEFVAELPRDDTGKLY 467

                   ....
gi 2183974163 1004 RKAL 1007
Cdd:cd05929    468 RRLL 471
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2174-2507 6.51e-12

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 70.40  E-value: 6.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQMFFELDIPRRQHW-NQSVLLEPgQALDGTLLETALQALLAHHDALRLGFRLEDGtwraeHRAVEA--GEVLLW 2250
Cdd:cd19545      3 PCTPLQEGLMALTARQPGAYvGQRVFELP-PDIDLARLQAAWEQVVQANPILRTRIVQSDS-----GGLLQVvvKESPIS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2251 QQSVADGQalEALAEQVQRSLDLGsGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQavalp 2330
Cdd:cd19545     77 WTESTSLD--EYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ----- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2331 akTSAFKAWAERLQAHARDGGlegeRGYWLAQLEGV-STELPCddregAQSVRHVRSARTELteEATRRLLQEAPAAYRT 2409
Cdd:cd19545    149 --PPPFSRFVKYLRQLDDEAA----AEFWRSYLAGLdPAVFPP-----LPSSRYQPRPDATL--EHSISLPSSASSGVTL 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2410 QVndLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDL----TRTVgwftslFPLR--LSPVAELGASIKRIKEQL- 2482
Cdd:cd19545    216 AT--VLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQivgpTIAT------VPLRvrIDPEQSVEDFLQTVQKDLl 287
                          330       340
                   ....*....|....*....|....*
gi 2183974163 2483 RAIPHKGLGFGALRYLGSaEDRAAL 2507
Cdd:cd19545    288 DMIPFEHTGLQNIRRLGP-DARAAC 311
prpE PRK10524
propionyl-CoA synthetase; Provisional
494-1007 7.64e-12

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 71.13  E-value: 7.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  494 TLLQRSRLP-ASEYPAGQ------GVHRLFEAQagltPDAPALLF-----GEER-LSYAELNALANRLAWRLREEGV--G 558
Cdd:PRK10524    34 QVLDYSNPPfARWFVGGRtnlchnAVDRHLAKR----PEQLALIAvstetDEERtYTFRQLHDEVNRMAAMLRSLGVqrG 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  559 SDVLVGIalergvPMV----VALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQQS------VLA--------- 619
Cdd:PRK10524   110 DRVLIYM------PMIaeaaFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAgsrggkVVPykplldeai 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  620 RLPQSDGLQSLLLD---DLERLVHG----YPAE-----NPDLP----EAPDSlCYAIYTSGSTGQPKGVmvrHR------ 677
Cdd:PRK10524   184 ALAQHKPRHVLLVDrglAPMARVAGrdvdYATLraqhlGARVPvewlESNEP-SYILYTSGTTGKPKGV---QRdtggya 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  678 -ALTNFVCSI-ARQPG--MLARDRLLSVTTFSFDIFGlelyvPLARG-ASMLLASREQAQDPEALLDLVERQGVTVLQAT 752
Cdd:PRK10524   260 vALATSMDTIfGGKAGetFFCASDIGWVVGHSYIVYA-----PLLAGmATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSA 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  753 PATWRMLCDSE-----RVDL--LRgcTLLCGGEALAEDLAAR-MRGLSASTWNLYGPTETTiWS--ARFRlGEEARPF-L 821
Cdd:PRK10524   335 PTAIRVLKKQDpallrKHDLssLR--ALFLAGEPLDEPTASWiSEALGVPVIDNYWQTETG-WPilAIAR-GVEDRPTrL 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  822 GGPleNTALY-----ILDSEM-NPCPPGVAGELLIGGDglargyhRRPGLTA------ERFLPDPFAADGSRLYRTGDLA 889
Cdd:PRK10524   411 GSP--GVPMYgynvkLLNEVTgEPCGPNEKGVLVIEGP-------LPPGCMQtvwgddDRFVKTYWSLFGRQVYSTFDWG 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  890 RYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVA----GPTLVAYLVPTEAALVDAESAR-- 963
Cdd:PRK10524   482 IRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVV---GVKdalkGQVAVAFVVPKDSDSLADREARla 558
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 2183974163  964 -QQELRSALKNSLLAVlpdyMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK10524   559 lEKEIMALVDSQLGAV----ARPARVWFVSALPKTRSGKLLRRAI 599
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2092-2149 8.72e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.58  E-value: 8.72e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 2092 QRLAAIWADVLKL--GRVGLDDNFFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIR 2149
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
524-1006 9.32e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 70.80  E-value: 9.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  524 PDAPallfgeERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLdpQYPADR--LQY 601
Cdd:PRK07768    24 PDAP------VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML--HQPTPRtdLAV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  602 MIDDSGLRL-LLSQQSVL--------ARLPQSDGLQSLLLDDLerlVHGYPAENPDLPEapDSLCYAIYTSGSTGQPKGV 672
Cdd:PRK07768    96 WAEDTLRVIgMIGAKAVVvgepflaaAPVLEEKGIRVLTVADL---LAADPIDPVETGE--DDLALMQLTSGSTGSPKAV 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  673 MVRHRaltNFVCSIArqpGMLAR-------DRLLSVTTFSFDIfGLE--LYVPLARGASMLLAS-REQAQDPEALLDLVE 742
Cdd:PRK07768   171 QITHG---NLYANAE---AMFVAaefdvetDVMVSWLPLFHDM-GMVgfLTVPMYFGAELVKVTpMDFLRDPLLWAELIS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  743 RQGVTVLQATPATWRMLC-------DSERVDL--LRgcTLLCGGE----ALAEDL--AARMRGLSASTW-NLYGPTETTI 806
Cdd:PRK07768   244 KYRGTMTAAPNFAYALLArrlrrqaKPGAFDLssLR--FALNGAEpidpADVEDLldAGARFGLRPEAIlPAYGMAEATL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  807 ------WSARFRLGE------------------EARPF--LGGPLENTALYILDSEMNPCPPGVAGELLIGGDGLARGYh 860
Cdd:PRK07768   322 avsfspCGAGLVVDEvdadllaalrravpatkgNTRRLatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY- 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  861 rrpgLTAERFLPdpfAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-- 938
Cdd:PRK07768   401 ----LTMDGFIP---AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRld 473
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  939 -GVAGPTLvAYLVPTEAALVDAESARqqeLRSALKNSLLAVLPdyMVPAHMLLLE--NLPLTPNGKINRKA 1006
Cdd:PRK07768   474 aGHSREGF-AVAVESNAFEDPAEVRR---IRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTPSGKLRRAN 538
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2666-2941 1.10e-11

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 69.82  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2666 LDVEGLDPQRFREAWQAALDAHEVLRSGFLWQGalekpLQLVRKRVEVP-FSVHDWRDRADLAEaldalaagEAGLG--- 2741
Cdd:cd19535     32 FDGEDLDPDRLERAWNKLIARHPMLRAVFLDDG-----TQQILPEVPWYgITVHDLRGLSEEEA--------EAALEelr 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2742 -------FELAEAPLLRLVLVRTGERRHHLiytnhHI-----LMDGWSNSQLLGEVLQRYR--GETPSRSDGRYRDYIAW 2807
Cdd:cd19535     99 erlshrvLDVERGPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEdpGEPLPPLELSFRDYLLA 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2808 LQRQDAGRTE---AFWKQRLQRL-GEPTLLV---------PAFAHgvrgaeghadRYRQLDVTTSQRLAEFAREQKVTLN 2874
Cdd:cd19535    174 EQALRETAYErarAYWQERLPTLpPAPQLPLakdpeeikePRFTR----------REHRLSAEQWQRLKERARQHGVTPS 243
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2875 TLVQAAWLILLQRFTGQDTVAFGATVSGRPAELRGIEEQIGLFINTLPVVASPCPEQPIGDWLQAVQ 2941
Cdd:cd19535    244 MVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQ 310
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1592-2071 1.14e-11

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 70.15  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1592 RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAG--GAYVPLDPRYPSdrLGYMIEDSGIRLL 1669
Cdd:cd05939      2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGveTALINSNLRLES--LLHCITVSKAKAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1670 LTQraarerlplgeglpclLLDAEHEWAgypESDPQSAVGV---DNLAYvIYTSGSTGKPKGTLLPHGNVLRLFDATRHW 1746
Cdd:cd05939     80 IFN----------------LLDPLLTQS---STEPPSQDDVnfrDKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1747 FGFSADD----AWSLFHSYAfdfsvwEIFG---ALLHGGRLVIvpyETSRSPEDFLRLLCRERVTV-----------LNQ 1808
Cdd:cd05939    140 FGMRPEDvvydCLPLYHSAG------GIMGvgqALLHGSTVVI---RKKFSASNFWDDCVKYNCTIvqyigeicrylLAQ 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1809 TPSAFKQLMQVacagqevpplalRHVVfgGEALEVQALRPWFERFgdRAPRLVNMYGITETTVhvtyrplSLADLDG--G 1886
Cdd:cd05939    211 PPSEEEQKHNV------------RLAV--GNGLRPQIWEQFVRRF--GIPQIGEFYGATEGNS-------SLVNIDNhvG 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1887 AAS----------PI---------GEPIPDlswylldaglnpvPRG-CI----GE--LYVG----GAGLAR--GYLNRPE 1934
Cdd:cd05939    268 ACGfnsrilpsvyPIrlikvdedtGELIRD-------------SDGlCIpcqpGEpgLLVGkiiqNDPLRRfdGYVNEGA 334
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1935 lSCTRFVADPFsTTGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGPGATQ 2014
Cdd:cd05939    335 -TNKKIARDVF-KKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEG 412
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 2015 LVGyvvtQAAPSDPAALRDT--LRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:cd05939    413 RAG----MAAIVDPERKVDLdrFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
619-1002 1.40e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 70.12  E-value: 1.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  619 ARLPQSdglqSLLLDDLERLVHGYPAEN--PDLPE-APDSLCYaiyTSGSTGQPKGVMVRHRA--LTNFVCSIARQPGML 693
Cdd:PRK07008   145 AHLPAG----STPLLCYETLVGAQDGDYdwPRFDEnQASSLCY---TSGTTGNPKGALYSHRStvLHAYGAALPDAMGLS 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  694 ARDRLLSVT-TFSFDIFGLELYVPLArGASMLLASReqAQDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCT 772
Cdd:PRK07008   218 ARDAVLPVVpMFHVNAWGLPYSAPLT-GAKLVLPGP--DLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFST 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  773 L---LCGG--------EALAEDLAARMRglsastwNLYGPTE-------TTIWSARFRLGEEARPFL----GGPLENTAL 830
Cdd:PRK07008   295 LrrtVIGGsacppamiRTFEDEYGVEVI-------HAWGMTEmsplgtlCKLKWKHSQLPLDEQRKLlekqGRVIYGVDM 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  831 YILDSEMNPCP-PGVA-GELLIGGDGLARGYHRRpgltaerflpdpfaaDGSRLYR----TGDLARYRADGVIEYLGRID 904
Cdd:PRK07008   368 KIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG---------------DASPLVDgwfpTGDVATIDADGFMQITDRSK 432
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  905 HQVKIRGFRIELGEIETrlleqdsvreaVVVAQPGVAGPTLVAYLVP--TEAALV------DAESARQQelrsalknsLL 976
Cdd:PRK07008   433 DVIKSGGEWISSIDIEN-----------VAVAHPAVAEAACIACAHPkwDERPLLvvvkrpGAEVTREE---------LL 492
                          410       420       430
                   ....*....|....*....|....*....|
gi 2183974163  977 AV----LPDYMVPAHMLLLENLPLTPNGKI 1002
Cdd:PRK07008   493 AFyegkVAKWWIPDDVVFVDAIPHTATGKL 522
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3077-3183 1.48e-11

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 70.07  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3077 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 3155
Cdd:PRK06178    24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
                           90       100
                   ....*....|....*....|....*...
gi 2183974163 3156 LKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:PRK06178   104 LKLGAVHVPVSPLFREHELSYELNDAGA 131
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
644-936 1.92e-11

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 69.44  E-value: 1.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  644 AENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFDIfGLELY--VPLARGA 721
Cdd:cd05908     96 TEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM-GLIAFhlAPLIAGM 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  722 S-MLLASREQAQDPEALLDLVERQGVTVLQATPATWRMLCD------SERVDLLRGCTLLCGGEALAEDLAAR-MRGLSA 793
Cdd:cd05908    175 NqYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpekANDWDLSSIRMILNGAEPIDYELCHEfLDHMSK 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  794 ------STWNLYGPTETTIWSARFRLGEEARPF----------------------------LGGPLENTALYILDSEMNP 839
Cdd:cd05908    255 yglkrnAILPVYGLAEASVGASLPKAQSPFKTItlgrrhvthgepepevdkkdsecltfveVGKPIDETDIRICDEDNKI 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  840 CPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEI 919
Cdd:cd05908    335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDI 406
                          330
                   ....*....|....*..
gi 2183974163  920 ETRLLEQDSVREAVVVA 936
Cdd:cd05908    407 ERIAEELEGVELGRVVA 423
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3063-3165 3.21e-11

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 69.02  E-value: 3.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3063 AVAERYQllegwnatAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVgVA 3141
Cdd:COG1021     11 EFAARYR--------EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQ 81
                           90       100
                   ....*....|....*....|....
gi 2183974163 3142 MERSIEMVVALMAILKAGGayVPV 3165
Cdd:COG1021     82 LPNVAEFVIVFFALFRAGA--IPV 103
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3091-3173 3.22e-11

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 68.77  E-value: 3.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3091 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3170
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                   ...
gi 2183974163 3171 EER 3173
Cdd:PRK04813    88 AER 90
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1674-2066 3.57e-11

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 69.02  E-value: 3.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1674 AARERLP-LGEGLPCLLLDAEHEWAGYPESDPQSAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLfdatrhWFGFSAD 1752
Cdd:cd17632    185 SARERLAaVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATF------WLKVSSI 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1753 DAWSLFHSYAFDF--------SVWeIFGALLHGGrlviVPYETSRSpeDFLRL---LCRERVTVLNQTPSAFKQLMQ--- 1818
Cdd:cd17632    259 QDIRPPASITLNFmpmshiagRIS-LYGTLARGG----TAYFAAAS--DMSTLfddLALVRPTELFLVPRVCDMLFQryq 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1819 -----VACAGQEVPPLA------LRHVVFGGE---ALEVQA-----LRPWFERFGDRapRLVNMYGITETTV----HVTY 1875
Cdd:cd17632    332 aeldrRSVAGADAETLAervkaeLRERVLGGRllaAVCGSAplsaeMKAFMESLLDL--DLHDGYGSTEAGAvildGVIV 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1876 RP----LSLADldggaaspigepIPDLSWYLLDaglNPVPRGcigELYVGGAGLARGYLNRPELSCTRFVADPFsttggr 1951
Cdd:cd17632    410 RPpvldYKLVD------------VPELGYFRTD---RPHPRG---ELLVKTDTLFPGYYKRPEVTAEVFDEDGF------ 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1952 lYRTGD-LARYRCDGVVeYVGRIDHQVKI-RGFRIELGEIEARLLAQPGVAE-------------AVVLPHEGPgatqLV 2016
Cdd:cd17632    466 -YRTGDvMAELGPDRLV-YVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPTQDA----LA 539
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 2017 GYVVTQAAPsdpaALRDTL-RQALKASLPEHMVPAHLLfLERLPLT-ANGKL 2066
Cdd:cd17632    540 GEDTARLRA----ALAESLqRIAREAGLQSYEIPRDFL-IETEPFTiANGLL 586
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1574-2046 4.14e-11

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 68.61  E-value: 4.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1574 IERQAAERPRATAVVYGE-----RALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPL 1648
Cdd:cd05921      1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1649 DPRYPS-----DRLGYMIEDSGIRLLLTQ------RAARERLPLG----------EGLPCLLLDAEHEWAGYPESDPQ-S 1706
Cdd:cd05921     81 SPAYSLmsqdlAKLKHLFELLKPGLVFAQdaapfaRALAAIFPLGtplvvsrnavAGRGAISFAELAATPPTAAVDAAfA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1707 AVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADD--------AWSlfHSYAFDfsvwEIFGALLH-G 1777
Cdd:cd05921    161 AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvdwlPWN--HTFGGN----HNFNLVLYnG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1778 GRLVIvpYETSRSPEDF---LRLLCRERVTVLNQTPSAFKQLMQvacAGQEVPPLA------LRHVVFGGEAL------E 1842
Cdd:cd05921    235 GTLYI--DDGKPMPGGFeetLRNLREISPTVYFNVPAGWEMLVA---ALEKDEALRrrffkrLKLMFYAGAGLsqdvwdR 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1843 VQALRpwFERFGDRAPrLVNMYGITET--TVHVTYRPLSLADLdggaaspIGEPIPDLSWYLldaglnpVPRGCIGELYV 1920
Cdd:cd05921    310 LQALA--VATVGERIP-MMAGLGATETapTATFTHWPTERSGL-------IGLPAPGTELKL-------VPSGGKYEVRV 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1921 GGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCD-----GVVeYVGRIDHQVKIR-GFRIELGEIEARLL 1994
Cdd:cd05921    373 KGPNVTPGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAV 444
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 1995 AQ--PGVAEAVVLPHEG--------PGATQLVGYVVTQAAPSDPAALRDTLRQALKASLPEH 2046
Cdd:cd05921    445 AAcaPLVHDAVVAGEDRaevgalvfPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAAL 506
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1567-2005 4.86e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 68.29  E-value: 4.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1567 ASCLHRLierqAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYV 1646
Cdd:PLN02860    10 CQCLTRL----ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1647 PLDPRYPSDRLGYMIEDSGIRLLLTQRAAR---ERLPLGE----------GLPCL--------LLDAEHEWA---GYPES 1702
Cdd:PLN02860    86 PLNYRWSFEEAKSAMLLVRPVMLVTDETCSswyEELQNDRlpslmwqvflESPSSsvfiflnsFLTTEMLKQralGTTEL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1703 DPQSAvgVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFH----SYAfdfsvweiFGAL 1774
Cdd:PLN02860   166 DYAWA--PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYlhtaPLCHigglSSA--------LAML 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1775 LHGGRLVIVP-YETSRSpedfLRLLCRERVTVLNQTPSAFKQLMQVA---CAGQEVPplALRHVVFGGEALEVQALRPWF 1850
Cdd:PLN02860   236 MVGACHVLLPkFDAKAA----LQAIKQHNVTSMITVPAMMADLISLTrksMTWKVFP--SVRKILNGGGSLSSRLLPDAK 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1851 ERFgDRApRLVNMYGITETTVHVTYRPLSLADLDGGAASPIGEPIPDLSwylldagLNPVPRG-CIG------ELYVG-- 1921
Cdd:PLN02860   310 KLF-PNA-KLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSS-------SVHQPQGvCVGkpaphvELKIGld 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1922 -----GAGLARGylnrPELsCTRFVADPFSTTGGRL----YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEAR 1992
Cdd:PLN02860   381 essrvGRILTRG----PHV-MLGYWGQNSETASVLSndgwLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV 455
                          490
                   ....*....|...
gi 2183974163 1993 LLAQPGVAEAVVL 2005
Cdd:PLN02860   456 LSQHPGVASVVVV 468
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1596-2071 5.87e-11

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 68.27  E-value: 5.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPL-----------------------DPR 1651
Cdd:PRK05620    41 FAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLnkqlmndqivhiinhaedevivaDPR 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1652 YpSDRLGYMIED----SGIRLLLTQRAARERLPLGEGLPCL----LLD---AEHEWAGYPESDPqsavgvdnlAYVIYTS 1720
Cdd:PRK05620   121 L-AEQLGEILKEcpcvRAVVFIGPSDADSAAAHMPEGIKVYsyeaLLDgrsTVYDWPELDETTA---------AAICYST 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1721 GSTGKPKGTLLPHgNVLRLfdatrHWFGFSADDAWSLFHSYAFDFSV-------WEI-FGALLHGGRLVIVPYETsrSPE 1792
Cdd:PRK05620   191 GTTGAPKGVVYSH-RSLYL-----QSLSLRTTDSLAVTHGESFLCCVpiyhvlsWGVpLAAFMSGTPLVFPGPDL--SAP 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1793 DFLRLLCRERVTVLNQTPSAFKQLMqvaCAGQEVPP--LALRHVVFGGEALEVQALRPWFERFGdraPRLVNMYGITET- 1869
Cdd:PRK05620   263 TLAKIIATAMPRVAHGVPTLWIQLM---VHYLKNPPerMSLQEIYVGGSAVPPILIKAWEERYG---VDVVHVWGMTETs 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1870 TVHVTYRPLSLADLDGGAASPIGE---PIpDLSWYLLDAG--LNPVPRGCiGELYVGGAGLARGYLNRP----------- 1933
Cdd:PRK05620   337 PVGTVARPPSGVSGEARWAYRVSQgrfPA-SLEYRIVNDGqvMESTDRNE-GEIQVRGNWVTASYYHSPteegggaastf 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1934 -----ELSCTRFVADpfsttgGRLyRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL--P 2006
Cdd:PRK05620   415 rgedvEDANDRFTAD------GWL-RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIgyP 487
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2007 HEGPGATQLvgyVVTQAAPSDP--AALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRAL 2071
Cdd:PRK05620   488 DDKWGERPL---AVTVLAPGIEptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2196-2464 6.17e-11

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 67.50  E-value: 6.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2196 SVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWRAEHRAVEAGEVLLWQQSVADGQALEALAEQVQRSLDLGS 2275
Cdd:cd19546     30 SVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPVVPATEEELPALLADRAAHLFDLTR 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2276 GPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQA---VALPAKTSAFKAWAERLQAHARDG-G 2351
Cdd:cd19546    110 ETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAperAPLPLQFADYALWERELLAGEDDRdS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2352 LEGER-GYWLAQLEGV--STELPCDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTQVNdLLLTALARVIGRWTG 2428
Cdd:cd19546    190 LIGDQiAYWRDALAGApdELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFT-VVQAALAMLLTRLGA 268
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2183974163 2429 QADTLIQLEGHGREELfedIDLTRTVGWFTSLFPLR 2464
Cdd:cd19546    269 GTDVTVGTVLPRDDEE---GDLEGMVGPFARPLALR 301
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3101-3183 7.81e-11

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 67.31  E-value: 7.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3101 APALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGkdLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd05941     81 TDSEP 85
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2637-3035 8.26e-11

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 67.28  E-value: 8.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2637 LYPLSPMQQgmLFHSLYQQNSGDYiNQ-MRLDV-EGLDPQRFREAWQAALDAHEVLRSGFL-----WQGALEKPLQLVrk 2709
Cdd:cd19534      1 EVPLTPIQR--WFFEQNLAGRHHF-NQsVLLRVpQGLDPDALRQALRALVEHHDALRMRFRredggWQQRIRGDVEEL-- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2710 rveVPFSVHDWRDRADLAEALDALAagEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRY 2789
Cdd:cd19534     76 ---FRLEVVDLSSLAQAAAIEALAA--EAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2790 RGE--------TPSRSdgrYRDYIAWLqrQDAGRTEAFWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYR-QLDV-TTS 2859
Cdd:cd19534    151 EQAlagepiplPSKTS---FQTWAELL--AEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGDARTVSfTLDEeETE 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2860 QRLAEFAREQKVTLNTLVQAAWLILLQRFTGQDTVAfgatVS----GRPAELRGIE--EQIGLFINTLPVVASPCPEQPI 2933
Cdd:cd19534    226 ALLQEANAAYRTEINDLLLAALALAFQDWTGRAPPA----IFleghGREEIDPGLDlsRTVGWFTSMYPVVLDLEASEDL 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2934 GDWLQAVQgENLalrefEHTPL----YDIQRWAGQVGEALFDNIL----VFeNY------PVSAALAEETPADMRIDALS 2999
Cdd:cd19534    302 GDTLKRVK-EQL-----RRIPNkgigYGILRYLTPEGTKRLAFHPqpeiSF-NYlgqfdqGERDDALFVSAVGGGGSDIG 374
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2183974163 3000 NQEQTHYPL--TLLVSAGEtLELHYSYSRQAFDEAAIE 3035
Cdd:cd19534    375 PDTPRFALLdiNAVVEGGQ-LVITVSYSRNMYHEETIQ 411
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2213-2431 8.78e-11

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 67.08  E-value: 8.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2213 ALQALLAHHDALRLGFRLEDGT------WRaehRAVEAGEVLLWQQSVADGQALEALAEQVQRSLDLGSGPLLRALLATL 2286
Cdd:cd19544     44 ALQQVIDRHDILRTAILWEGLSepvqvvWR---QAELPVEELTLDPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAED 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2287 GDGSQRLLLV-IHHLVVDGVSWRILLEDLQtayrQLQAGQAVALPAKTSaFKawaeRLQAHARDGGLEGE-RGYWLAQLE 2364
Cdd:cd19544    121 PANGRWLLLLlFHHLISDHTSLELLLEEIQ----AILAGRAAALPPPVP-YR----NFVAQARLGASQAEhEAFFREMLG 191
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 2365 GVsTE--LPCDDREGAQSVRHVRSARTELTEEATRRLLQEA------PAAyrtqvndLLLTALARVIGRWTGQAD 2431
Cdd:cd19544    192 DV-DEptAPFGLLDVQGDGSDITEARLALDAELAQRLRAQArrlgvsPAS-------LFHLAWALVLARCSGRDD 258
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
485-891 9.19e-11

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 67.60  E-value: 9.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  485 PLLDAEERA--TLLQRSRLPASEYPAGQGvHRLfEAQAGLTPDAPAL-----LFGEERLSYAELNALANRLAWRLREEGV 557
Cdd:PRK08180    14 PAVEVERRAdgTIYLRSAEPLGDYPRRLT-DRL-VHWAQEAPDRVFLaergaDGGWRRLTYAEALERVRAIAQALLDRGL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  558 GSD----VLVGIALERGVPMvvalLAVLKAGGAYVPLDPQY---PAD--RLQYMID---------DSGLR-------LLL 612
Cdd:PRK08180    92 SAErplmILSGNSIEHALLA----LAAMYAGVPYAPVSPAYslvSQDfgKLRHVLElltpglvfaDDGAAfaralaaVVP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 SQQSVLARLPQSDGLQSLLLDDLERlvhgyPAENPDLPEA-----PDSLCYAIYTSGSTGQPKGVMVRHRALtnfvCSIA 687
Cdd:PRK08180   168 ADVEVVAVRGAVPGRAATPFAALLA-----TPPTAAVDAAhaavgPDTIAKFLFTSGSTGLPKAVINTHRML----CANQ 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  688 RqpgMLARdrllsvtTFSFD---------------------IFGLELYvplaRGASMLLASRE--QAQDPEALLDLVERQ 744
Cdd:PRK08180   239 Q---MLAQ-------TFPFLaeeppvlvdwlpwnhtfggnhNLGIVLY----NGGTLYIDDGKptPGGFDETLRNLREIS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  745 GvTVLQATPATWRMLCDSERVDllrgctllcggEALAEDLAARMR-------GLSASTWNL------------------Y 799
Cdd:PRK08180   305 P-TVYFNVPKGWEMLVPALERD-----------AALRRRFFSRLKllfyagaALSQDVWDRldrvaeatcgerirmmtgL 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  800 GPTETTIwSARFRLGEEARP-FLGGPLENTALYILdsemnpcPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaad 878
Cdd:PRK08180   373 GMTETAP-SATFTTGPLSRAgNIGLPAPGCEVKLV-------PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY--- 441
                          490
                   ....*....|...
gi 2183974163  879 gsrlYRTGDLARY 891
Cdd:PRK08180   442 ----YRSGDAVRF 450
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2193-2431 1.03e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 68.15  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2193 WNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWR----AEHRAVEAGEVLLWQQSVADGQALEALAEQVQ 2268
Cdd:PRK10252    30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWqwvdPALTFPLPEIIDLRTQPDPHAAAQALMQADLQ 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2269 RSLDLGSG-PLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQAGQavalPAKTSAFKAWAERL---Q 2344
Cdd:PRK10252   110 QDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE----PTPASPFTPFADVVeeyQ 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2345 AHARDGGLEGERGYWLAQLEGVS--TELPCDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRTqvnDLLLTALARV 2422
Cdd:PRK10252   186 RYRASEAWQRDAAFWAEQRRQLPppASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRP---DLALALVALW 262

                   ....*....
gi 2183974163 2423 IGRWTGQAD 2431
Cdd:PRK10252   263 LGRLCGRMD 271
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1546-2065 1.22e-10

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 67.30  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1546 DEAEARADLLQWNPGPQ-DFtpASCLHRlierqAAERPRATAVVYGE----RALDYGELNLRANRLAHRLIELGVGP-DV 1619
Cdd:cd05943     53 VVSGRIMPGARWFPGARlNY--AENLLR-----HADADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPgDR 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1620 LVGLAAErSLEMIVGLLAILKAGGAYVPLDPRYPS----DRLG------------YMIEDSGIRLLLTQRAARERLPLGE 1683
Cdd:cd05943    126 VAGYLPN-IPEAVVAMLATASIGAIWSSCSPDFGVpgvlDRFGqiepkvlfavdaYTYNGKRHDVREKVAELVKGLPSLL 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1684 G---LPCLLLDAEHEWAGYPES--------DPQSA------VGVDNLAYVIYTSGSTGKPK-------GTLLPHGNVLRL 1739
Cdd:cd05943    205 AvvvVPYTVAAGQPDLSKIAKAltledflaTGAAGelefepLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHIL 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1740 -FDATRH--WFGFSADdAWSLFHsyafdfsvWEIfGALLHGGRLVIvpYETS---RSPEDFLRLLCRERVTVLNQTPsaf 1813
Cdd:cd05943    285 hCDLRPGdrLFYYTTC-GWMMWN--------WLV-SGLAVGATIVL--YDGSpfyPDTNALWDLADEEGITVFGTSA--- 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLMqvACAGQEVPP------LALRHVVFGGEALEVQALRpWFERfgdraprlvnmygitettvHVTYRpLSLADLDGGA 1887
Cdd:cd05943    350 KYLD--ALEKAGLKPaethdlSSLRTILSTGSPLKPESFD-YVYD-------------------HIKPD-VLLASISGGT 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1888 aspigepipDL-SWYLLDAGLNPVPRGCIGELYVGGAGLARGYLNRP------ELSCTR--------FVADP-------- 1944
Cdd:cd05943    407 ---------DIiSCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPvwgekgELVCTKpfpsmpvgFWNDPdgsryraa 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1945 -FSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVLPHEGP-GATQLVGYVVTQ 2022
Cdd:cd05943    478 yFAKYPG-VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKdGDERVILFVKLR 556
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2183974163 2023 AAPSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGK 2065
Cdd:cd05943    557 EGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
PRK05850 PRK05850
acyl-CoA synthetase; Validated
520-911 1.24e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 67.27  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  520 AGLTPDAPALLFGE---------ERLSYAELNALANRLAWRLREEGVGSDVLVgIALERGVPMVVALLAVLKAGGAYVPL 590
Cdd:PRK05850    11 ASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  591 D-PQYPA--DRLQYMIDDSGLRLLLSQQSV---LARLPQSDGLQS----LLLD--DLERlvhgyPAENPDLPEAPDSLCY 658
Cdd:PRK05850    90 SvPQGGAhdERVSAVLRDTSPSVVLTTSAVvddVTEYVAPQPGQSappvIEVDllDLDS-----PRGSDARPRDLPSTAY 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  659 AIYTSGSTGQPKGVMVRHRALT-NFVCSIA---RQPGMLARDRLLSVTTFSF--DIfGLELYV--PLARGASMLLASreq 730
Cdd:PRK05850   165 LQYTSGSTRTPAGVMVSHRNVIaNFEQLMSdyfGDTGGVPPPDTTVVSWLPFyhDM-GLVLGVcaPILGGCPAVLTS--- 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  731 aqdPEALLdlvERqgvtvlqatPATW-RMLC------------------------DSERVDLLRGCTLLCGGE----ALA 781
Cdd:PRK05850   241 ---PVAFL---QR---------PARWmQLLAsnphafsaapnfafelavrktsddDMAGLDLGGVLGIISGSErvhpATL 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  782 EDLAARMrglsaSTWNL--------YGPTETTIWSARFRLGE-----------------EARPFLGG-PL------ENTA 829
Cdd:PRK05850   306 KRFADRF-----APFNLretairpsYGLAEATVYVATREPGQppesvrfdyeklsaghaKRCETGGGtPLvsygspRSPT 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  830 LYILDSEMN-PCPPGVAGELLIGGDGLARGYHRRPGLTAERF-----LPDPFAADGSRLyRTGDLArYRADGVIEYLGRI 903
Cdd:PRK05850   381 VRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWL-RTGDLG-FISEGELFIVGRI 458

                   ....*...
gi 2183974163  904 DHQVKIRG 911
Cdd:PRK05850   459 KDLLIVDG 466
PLN02479 PLN02479
acetate-CoA ligase
1573-2073 1.26e-10

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 67.18  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1573 LIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY 1652
Cdd:PLN02479    25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1653 PSDRLGYMIEDSGIRLLLTQRaarERLPLGEGL-------------PCLLL----------------------------- 1690
Cdd:PLN02479   105 NAPTIAFLLEHSKSEVVMVDQ---EFFTLAEEAlkilaekkkssfkPPLLIvigdptcdpkslqyalgkgaieyekflet 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1691 -DAEHEWAGyPESDPQS-AVGvdnlayviYTSGSTGKPKGTLLPH-GNVLRLFDATRHW-FGFSADDAWSL--FHSYAFD 1764
Cdd:PLN02479   182 gDPEFAWKP-PADEWQSiALG--------YTSGTTASPKGVVLHHrGAYLMALSNALIWgMNEGAVYLWTLpmFHCNGWC 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1765 FSvWEIfgALLHGGRLVIVPYETsrspEDFLRLLCRERVTVLNQTPSAFKQLMQvACAGQEVPPLA-LRHVVFGGEALEV 1843
Cdd:PLN02479   253 FT-WTL--AALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIVN-APKSETILPLPrVVHVMTAGAAPPP 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1844 QALrpwfERFGDRAPRLVNMYGITETtvhvtYRPLSLAdldggAASPIGEPIPDLSWYLLDA----------GLN----- 1908
Cdd:PLN02479   325 SVL----FAMSEKGFRVTHTYGLSET-----YGPSTVC-----AWKPEWDSLPPEEQARLNArqgvryigleGLDvvdtk 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 ---PVPR--GCIGELYVGGAGLARGYLNRPELSCTRFvadpfsttGGRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFR 1983
Cdd:PLN02479   391 tmkPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF--------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGEN 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1984 IELGEIEARLLAQPGVAEAVVL--PHEGPGATQlVGYVVTQ--AAPSDPAALRDTLRQALKASLPEHMVPAHLLFlERLP 2059
Cdd:PLN02479   463 ISSLEVENVVYTHPAVLEASVVarPDERWGESP-CAFVTLKpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLP 540
                          570
                   ....*....|....
gi 2183974163 2060 LTANGKLDRRALPA 2073
Cdd:PLN02479   541 KTATGKIQKHVLRA 554
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2174-2477 1.96e-10

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 65.80  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2174 PLLPIQQ--MFFELDIPRRQ-HWNQSVLLEPGqALDGTLLETALQALLAHHDALRLGFRLEDgtwRAEHRAVEAGEV--- 2247
Cdd:cd19547      3 PLAPMQEgmLFRGLFWPDSDaYFNQNVLELVG-GTDEDVLREAWRRVADRYEILRTGFTWRD---RAEPLQYVRDDLapp 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2248 ---LLWQQSVADGQA--LEAL-AEQVQRSLDLGSGPLLRALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQL 2321
Cdd:cd19547     79 walLDWSGEDPDRRAelLERLlADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2322 QAGQAVALpAKTSAFKAWAERLQAHARDGGlEGERgYWLAQLEGVS----TELPCdDREGA-QSVRHvrsartELTEEAT 2396
Cdd:cd19547    159 AHGREPQL-SPCRPYRDYVRWIRARTAQSE-ESER-FWREYLRDLTpspfSTAPA-DREGEfDTVVH------EFPEQLT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2397 rRLLQEAPAAYRTQVNDLLLTALARVIGRWTGQADTLIQLEGHGREELFEDIDLtrTVGWFTSLFPL--RLSP---VAEL 2471
Cdd:cd19547    229 -RLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPLriRLDPdqtVTGL 305

                   ....*.
gi 2183974163 2472 GASIKR 2477
Cdd:cd19547    306 LETIHR 311
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
509-1004 2.22e-10

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 66.36  E-value: 2.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  509 GQGVHRLfeaqAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYV 588
Cdd:PLN02860    10 CQCLTRL----ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  589 PLDPQYPADRLQYMIDDSGLRLLLSQQSV--------LARLPqSDGLQSLLLDDLERLVH--------------GYPAEN 646
Cdd:PLN02860    86 PLNYRWSFEEAKSAMLLVRPVMLVTDETCsswyeelqNDRLP-SLMWQVFLESPSSSVFIflnsflttemlkqrALGTTE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  647 PDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTnfVCSIARqpgmlardrlLSVTTFSFDifglELYV---PLAR--GA 721
Cdd:PLN02860   165 LDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAK----------IAIVGYGED----DVYLhtaPLCHigGL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  722 S----MLLASREQAQDPE----ALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGC-----TLLCGGEALAEDL--AA 786
Cdd:PLN02860   229 SsalaMLMVGACHVLLPKfdakAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVfpsvrKILNGGGSLSSRLlpDA 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  787 RMRGLSASTWNLYGPTETTIWSARFRLGEEARPFLGGPLENTALYILDSEMNP---C----PPGVagELLIGGDG----- 854
Cdd:PLN02860   309 KKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPqgvCvgkpAPHV--ELKIGLDEssrvg 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  855 --LARGYHrrpglTAERFLPDPFAADGSRL----YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDS 928
Cdd:PLN02860   387 riLTRGPH-----VMLGYWGQNSETASVLSndgwLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  929 VREAVVVAQPGVAGPTLVAYLVP-------TEAALVDAESARQ---QELR--SALKNsllavLPDYMVPAHMLLLEN-LP 995
Cdd:PLN02860   462 VASVVVVGVPDSRLTEMVVACVRlrdgwiwSDNEKENAKKNLTlssETLRhhCREKN-----LSRFKIPKLFVQWRKpFP 536

                   ....*....
gi 2183974163  996 LTPNGKINR 1004
Cdd:PLN02860   537 LTTTGKIRR 545
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
598-1009 2.90e-10

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 66.29  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  598 RLQYMiDDSGLRLLLSqqsvlarLPQSDGLQSLLLDDLERLVHGYPAEnPDLPeAPDSLCYAIYTSGSTGQPKGVMVRHR 677
Cdd:PLN02387   204 RVIYM-DDEGVDSDSS-------LSGSSNWTVSSFSEVEKLGKENPVD-PDLP-SPNDIAVIMYTSGSTGLPKGVMMTHG 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  678 altNFVCSIARQ----PGMLARDRLLSvttfsfdifglelYVPLA----------------------------------R 719
Cdd:PLN02387   274 ---NIVATVAGVmtvvPKLGKNDVYLA-------------YLPLAhilelaaesvmaavgaaigygspltltdtsnkikK 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  720 G----ASMLLASREQAQdpEALLDLVeRQGV--TV------------------LQATPATW-------RMLCDSE----- 763
Cdd:PLN02387   338 GtkgdASALKPTLMTAV--PAILDRV-RDGVrkKVdakgglakklfdiaykrrLAAIEGSWfgawgleKLLWDALvfkki 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  764 RVDL---LRGctLLCGGEALAEDLAARMR-GLSASTWNLYGPTETTIWSARFRLGEEARPFLGGPLENTALYILDSEM-- 837
Cdd:PLN02387   415 RAVLggrIRF--MLSGGAPLSGDTQRFINiCLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEgg 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  838 -----NPCPpgvAGELLIGGDGLARGYHRRPGLTAERFLPDpfaADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIR-G 911
Cdd:PLN02387   493 ylisdKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhG 566
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  912 FRIELGEIETRLLEQDSVREAVVVAQPgvAGPTLVAYLVPTEAA-----------------LVDAESARQQELRSALKNS 974
Cdd:PLN02387   567 EYVSLGKVEAALSVSPYVDNIMVHADP--FHSYCVALVVPSQQAlekwakkagidysnfaeLCEKEEAVKEVQQSLSKAA 644
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2183974163  975 LLAVLPDYMVPAHMLLLENlPLTPNGKINRKALPL 1009
Cdd:PLN02387   645 KAARLEKFEIPAKIKLLPE-PWTPESGLVTAALKL 678
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
658-1007 4.26e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 65.53  E-value: 4.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  658 YAIYTSGSTGQPKGVmVRHRAlTNFVCSIARQPGMLARD---RLLSVTTFSFDIFGLELYVPLARGASMLLASREQAQDP 734
Cdd:PTZ00237   258 YILYTSGTTGNSKAV-VRSNG-PHLVGLKYYWRSIIEKDiptVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNK 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  735 EALLDL---VERQGVTVLQATPATWRMLC----DSERV----DLLRGCTLLCGGEALAEDLAARMRG-LSASTWNLYGPT 802
Cdd:PTZ00237   336 HIEDDLwntIEKHKVTHTLTLPKTIRYLIktdpEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENkLKIKSSRGYGQT 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  803 ETTIWSArFRLGEEARPF--LGGPLENTALYILDS---EMN-----------PCPPGVAGELLIGGDGLARGYHRRPGLt 866
Cdd:PTZ00237   416 EIGITYL-YCYGHINIPYnaTGVPSIFIKPSILSEdgkELNvneigevafklPMPPSFATTFYKNDEKFKQLFSKFPGY- 493
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  867 aerflpdpfaadgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTL- 945
Cdd:PTZ00237   494 ----------------YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI---GIYDPDCy 554
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163  946 ---VAYLVpteaaLVDAESARQQELrSALKNSLLAVLPD----YMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PTZ00237   555 nvpIGLLV-----LKQDQSNQSIDL-NKLKNEINNIITQdiesLAVLRKIIIVNQLPKTKTGKIPRQII 617
PLN02479 PLN02479
acetate-CoA ligase
661-1007 4.71e-10

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 65.25  E-value: 4.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  661 YTSGSTGQPKGVMVRHRALTNFVCSIARQPGM-LARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQaqdpEALLD 739
Cdd:PLN02479   202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMnEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTA----KAIYS 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  740 LVERQGVTVLQATPATWRMLCDSERVD----LLRGCTLLCGGEALAEDLAARM--RGLSAS-TWNL---YGPTETTIWSA 809
Cdd:PLN02479   278 AIANYGVTHFCAAPVVLNTIVNAPKSEtilpLPRVVHVMTAGAAPPPSVLFAMseKGFRVThTYGLsetYGPSTVCAWKP 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  810 ---RFRLGEEARPFLGGPLENTALYILD----SEMNPCPP--GVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGs 880
Cdd:PLN02479   358 ewdSLPPEEQARLNARQGVRYIGLEGLDvvdtKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ANG- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 rLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQPGVA-GPTLVAYLVPTEAALVDA 959
Cdd:PLN02479   431 -WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERwGESPCAFVTLKPGVDKSD 509
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163  960 ESARQQELRSALKNSllavLPDYMVPAHmLLLENLPLTPNGKINRKAL 1007
Cdd:PLN02479   510 EAALAEDIMKFCRER----LPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1561-2071 6.61e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 64.58  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1561 PQDFTPASCLhRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILK 1640
Cdd:PRK08162    12 AANYVPLTPL-SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1641 AGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRA----ARERLPLGEGLPCLLLDAEHewAGYPESDPQSAV-------- 1708
Cdd:PRK08162    91 AGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEfaevAREALALLPGPKPLVIDVDD--PEYPGGRFIGALdyeaflas 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1709 GVDNLAYVI-----------YTSGSTGKPKGTLLPH--------GNVLRlFDATRHwfgfsADDAWSL--FHSYAFDFSv 1767
Cdd:PRK08162   169 GDPDFAWTLpadewdaialnYTSGTTGNPKGVVYHHrgaylnalSNILA-WGMPKH-----PVYLWTLpmFHCNGWCFP- 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1768 WEIfgALLHGgrlVIVPYETSRsPEDFLRLLCRERVT-------VLN---QTPSAFK----QLMQVACAGQeVPPLAlrh 1833
Cdd:PRK08162   242 WTV--AARAG---TNVCLRKVD-PKLIFDLIREHGVThycgapiVLSaliNAPAEWRagidHPVHAMVAGA-APPAA--- 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1834 VVFGGEALEVqalrpwferfgdrapRLVNMYGITEttvhvTYRPLSL-ADLDGGAASPIGEPIPDLSW----YLLDAGLN 1908
Cdd:PRK08162   312 VIAKMEEIGF---------------DLTHVYGLTE-----TYGPATVcAWQPEWDALPLDERAQLKARqgvrYPLQEGVT 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1909 --------PVPRG--CIGELYVGGAGLARGYLNRPELSCTRFvadpfstTGGrLYRTGDLARYRCDGvveYVgridhQVK 1978
Cdd:PRK08162   372 vldpdtmqPVPADgeTIGEIMFRGNIVMKGYLKNPKATEEAF-------AGG-WFHTGDLAVLHPDG---YI-----KIK 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1979 IR--------GFRIELGEIEARLLAQPGVAEA--VVLPHEGPGATQLVGYVVTQAAPSDPAALRDTLRQalkaSLPEHMV 2048
Cdd:PRK08162   436 DRskdiiisgGENISSIEVEDVLYRHPAVLVAavVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCRE----HLAGFKV 511
                          570       580
                   ....*....|....*....|...
gi 2183974163 2049 PAHLLFLErLPLTANGKLDRRAL 2071
Cdd:PRK08162   512 PKAVVFGE-LPKTSTGKIQKFVL 533
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
535-977 8.54e-10

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 64.38  E-value: 8.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPA-----DRLQYMIDdsglr 609
Cdd:cd05921     25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFE----- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  610 lLLSQQSVLAR--LPQSDGLQSLLLDDLERLVHGYPAENP---------------DLPEA-----PDSLCYAIYTSGSTG 667
Cdd:cd05921    100 -LLKPGLVFAQdaAPFARALAAIFPLGTPLVVSRNAVAGRgaisfaelaatpptaAVDAAfaavgPDTVAKFLFTSGSTG 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  668 QPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVT------TFSFD-IFGLELYvplaRGASMLL-ASREQAQDPEALLD 739
Cdd:cd05921    179 LPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDwlpwnhTFGGNhNFNLVLY----NGGTLYIdDGKPMPGGFEETLR 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  740 LVERQGVTVLQATPATWRMLcdserVDLLRGCTLLC------------GGEALAEDLAARMRGLSAST-------WNLYG 800
Cdd:cd05921    255 NLREISPTVYFNVPAGWEML-----VAALEKDEALRrrffkrlklmfyAGAGLSQDVWDRLQALAVATvgeripmMAGLG 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  801 PTETTIwSARFRLGEEARP-FLGGPLENTALYILdsemnpcPPGVAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadg 879
Cdd:cd05921    330 ATETAP-TATFTHWPTERSgLIGLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF---- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  880 srlYRTGDLARYrAD------GVIeYLGRIDHQVKIR-GFRIELGEIETRLLEQDS--VREAVVVAQPG-------VAGP 943
Cdd:cd05921    398 ---YCLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAACAplVHDAVVAGEDRaevgalvFPDL 472
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2183974163  944 TLVAYLVPTEAAlVDAESARQQELRSALKNSLLA 977
Cdd:cd05921    473 LACRRLVGLQEA-SDAEVLRHAKVRAAFRDRLAA 505
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1707-2043 8.60e-10

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 64.01  E-value: 8.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1707 AVGVDNLAYVIYTSGSTGKPKGTLL-------PHGNVLRLFdatrHWFGFSADDAwsLFHSYAFDFSVWeifGALLHGG- 1778
Cdd:COG1541     79 AVPLEEIVRIHASSGTTGKPTVVGYtrkdldrWAELFARSL----RAAGVRPGDR--VQNAFGYGLFTG---GLGLHYGa 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1779 -RL--VIVPYeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACA-GQEVPPLALRHVVFGGEALeVQALRPWFE-RF 1853
Cdd:COG1541    150 eRLgaTVIPA-GGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEeGIDPRDLSLKKGIFGGEPW-SEEMRKEIEeRW 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1854 GDRAprlVNMYGITETTVHVTYrplSLADLDGGAaspIGEP--IPDlswyLLD-AGLNPVPRGCIGELYVggaglargyl 1930
Cdd:COG1541    228 GIKA---YDIYGLTEVGPGVAY---ECEAQDGLH---IWEDhfLVE----IIDpETGEPVPEGEEGELVV---------- 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1931 nrpelsctrfvadpfsTTGGR----L--YRTGDLARY------------RCDGVveyVGRIDHQVKIRGFRIELGEIEAR 1992
Cdd:COG1541    285 ----------------TTLTKeampLirYRTGDLTRLlpepcpcgrthpRIGRI---LGRADDMLIIRGVNVFPSQIEEV 345
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 1993 LLAQPGVAEA--VVLPHEGPGATQLVgyVVTQAAPSDPAALRDTLRQALKASL 2043
Cdd:COG1541    346 LLRIPEVGPEyqIVVDREGGLDELTV--RVELAPGASLEALAEAIAAALKAVL 396
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3099-3183 1.01e-09

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 64.03  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLD----YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3174
Cdd:cd17654      1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80

                   ....*....
gi 2183974163 3175 AYMLEDSGV 3183
Cdd:cd17654     81 LTVMKKCHV 89
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1706-2073 1.02e-09

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 64.07  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1706 SAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSADDAW----SLFHSYAFDFSVweIFGALlhGGRLV 1781
Cdd:PRK06334   178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMmsflPPFHAYGFNSCT--LFPLL--SGVPV 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1782 IVPYeTSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVAcAGQEVPPLALRHVVFGGEALEvQALRPWFER-FGDRAPRl 1860
Cdd:PRK06334   254 VFAY-NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTA-KKQESCLPSLRFVVIGGDAFK-DSLYQEALKtFPHIQLR- 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1861 vNMYGITETTVHVTYRPLSladldggaaSP-----IGEPIPDLSWYLLDAGLN-PVPRGCIGELYVGGAGLARGYLNrpe 1934
Cdd:PRK06334   330 -QGYGTTECSPVITINTVN---------SPkhescVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG--- 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1935 lsctrfvADP---FSTTGGRL-YRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAvvlPHEGP 2010
Cdd:PRK06334   397 -------EDFgqgFVELGGETwYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA---DHAGP 466
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2011 GAT-----QLVGYVVTQAAPSDPAALRDTLRQALKASLpehMVPAHLLFLERLPLTANGKLDRRALPA 2073
Cdd:PRK06334   467 LVVcglpgEKVRLCLFTTFPTSISEVNDILKNSKTSSI---LKISYHHQVESIPMLGTGKPDYCSLNA 531
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3088-3182 1.37e-09

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 63.59  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3088 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGA 3161
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                           90       100
                   ....*....|....*....|.
gi 2183974163 3162 YVPVDPEYPEERQAYMLEDSG 3182
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAE 111
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
662-1007 1.39e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 62.76  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  662 TSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARdRLLSVTTFSfdIFGLELYV-PLARGASMLLASREQAQDPEALLDL 740
Cdd:PRK07824    43 TSGTTGTPKGAMLTAAALTASADATHDRLGGPGQ-WLLALPAHH--IAGLQVLVrSVIAGSEPVELDVSAGFDPTALPRA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  741 VERQG-------VTVLQATPAtwrmLCDSERVDLLRGC-TLLCGGEALAEDLAARMRGLSASTWNLYGPTETTiwsarfr 812
Cdd:PRK07824   120 VAELGggrrytsLVPMQLAKA----LDDPAATAALAELdAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETS------- 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  813 lgeearpflGG------PLENTALYILDsemnpcppgvaGELLIGGDGLARGYHRRPGltaerflPDPFAADGsrLYRTG 886
Cdd:PRK07824   189 ---------GGcvydgvPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAEPG--WFRTD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  887 DLARYrADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVaqpGVAGPTLVAYLVpteAALVDAESARqqE 966
Cdd:PRK07824   240 DLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF---GLPDDRLGQRVV---AAVVGDGGPA--P 310
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2183974163  967 LRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:PRK07824   311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
918-1001 1.40e-09

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 56.78  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  918 EIETRLLEQDSVREAVVVAQPG-VAGPTLVAYLVPTEAALVDAEsarqqELRSALKnsllAVLPDYMVPAHMLLLENLPL 996
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDeLKGEAPVAFVVLKPGVELLEE-----ELVAHVR----EELGPYAVPKEVVFVDELPK 71

                   ....*
gi 2183974163  997 TPNGK 1001
Cdd:pfam13193   72 TRSGK 76
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3095-3183 2.11e-09

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 63.03  E-value: 2.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 3173
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                           90
                   ....*....|
gi 2183974163 3174 QAYMLEDSGV 3183
Cdd:PRK08316   100 LAYILDHSGA 109
PRK08308 PRK08308
acyl-CoA synthetase; Validated
879-1014 2.31e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 62.36  E-value: 2.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  879 GSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGpTLVAYLVPTEAAlV 957
Cdd:PRK08308   289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKdPVAG-ERVKAKVISHEE-I 366
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  958 DAESARQQelrsALKNsllavLPDYMVPAHMLLLENLPLTPNGKINRKALPLPDASA 1014
Cdd:PRK08308   367 DPVQLREW----CIQH-----LAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
832-1007 3.90e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 62.47  E-value: 3.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  832 ILDSEMNPCPPGVAGELLIGGD--GLARGYHRRPgltaERFLPDPFAADGSRlYRTGDLARYRADGVIEYLGRIDHQVKI 909
Cdd:PRK00174   437 VVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNV 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  910 RGFRIELGEIETRLLEQDSVREAVVVAQP-GVAGPTLVAYLVPTEAALVDAesarqqELRSALKNSLLAVLPDYMVPAHM 988
Cdd:PRK00174   512 SGHRLGTAEIESALVAHPKVAEAAVVGRPdDIKGQGIYAFVTLKGGEEPSD------ELRKELRNWVRKEIGPIAKPDVI 585
                          170
                   ....*....|....*....
gi 2183974163  989 LLLENLPLTPNGKINRKAL 1007
Cdd:PRK00174   586 QFAPGLPKTRSGKIMRRIL 604
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3113-3174 5.66e-09

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 61.76  E-value: 5.66e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 3113 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3174
Cdd:cd17647     23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ 84
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3099-3182 5.67e-09

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 61.56  E-value: 5.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLD--YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3176
Cdd:cd05926      1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                   ....*.
gi 2183974163 3177 MLEDSG 3182
Cdd:cd05926     81 YLADLG 86
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1711-2029 5.98e-09

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 62.06  E-value: 5.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1711 DNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWF-GFSADDAW----SLFH--SYAFDFSVWEIFGALLHGGRLVIV 1783
Cdd:PLN02387   250 NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYlaylPLAHilELAAESVMAAVGAAIGYGSPLTLT 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1784 pyETS-------RSPEDFLR---------LLCRERVTVLNQTPS---AFKQLMQVACAGQEVpplALRHVVFGGEALE-- 1842
Cdd:PLN02387   330 --DTSnkikkgtKGDASALKptlmtavpaILDRVRDGVRKKVDAkggLAKKLFDIAYKRRLA---AIEGSWFGAWGLEkl 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1843 ---VQALRPWFERFGDR--------AP------RLVNM---------YGITETTVHVTYrplslADLDGGAASPIGEPIP 1896
Cdd:PLN02387   405 lwdALVFKKIRAVLGGRirfmlsggAPlsgdtqRFINIclgapigqgYGLTETCAGATF-----SEWDDTSVGRVGPPLP 479
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1897 D-----LSW----YLL-DAglnPVPRGcigELYVGGAGLARGYLNRPELSCTRFVADpfsTTGGRLYRTGDLARYRCDGV 1966
Cdd:PLN02387   480 CcyvklVSWeeggYLIsDK---PMPRG---EIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIGQFHPDGC 550
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 1967 VEYVGRIDHQVKIR-GFRIELGEIEARLLAQPGVAEAVVlpHEGPGATQLVGYVVtqaaPSDPA 2029
Cdd:PLN02387   551 LEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMV--HADPFHSYCVALVV----PSQQA 608
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
537-935 1.89e-08

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 60.13  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  537 SYAELNALANRLAWRLREEGVGSDVLVGIaLERGVP-MVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS-- 613
Cdd:cd17641     13 TWADYADRVRAFALGLLALGVGRGDVVAI-LGDNRPeWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAed 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 QQSVLARLPQSDGLQSLL--------------------LDDLERLVHGYPAENPDLPEA------PDSLCYAIYTSGSTG 667
Cdd:cd17641     92 EEQVDKLLEIADRIPSVRyviycdprgmrkyddprlisFEDVVALGRALDRRDPGLYERevaagkGEDVAVLCTTSGTTG 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  668 QPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFSFdiFGLELYVPlarGASMLLASREQ-AQDPEALLDLVERQGV 746
Cdd:cd17641    172 KPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW--IGEQMYSV---GQALVCGFIVNfPEEPETMMEDLREIGP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  747 TVLQATPATW---------RMLcDSERVD--LLRgctllCGGEALAEDLAARMRGLSASTWN----------LYGPTETT 805
Cdd:cd17641    247 TFVLLPPRVWegiaadvraRMM-DATPFKrfMFE-----LGMKLGLRALDRGKRGRPVSLWLrlaswladalLFRPLRDR 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  806 IWSARFR--------LGEEARPF---LGGPL-------ENTALYIL------DSEMNPCP-PGV------AGELLIGGDG 854
Cdd:cd17641    321 LGFSRLRsaatggaaLGPDTFRFfhaIGVPLkqlygqtELAGAYTVhrdgdvDPDTVGVPfPGTevrideVGEILVRSPG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  855 LARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRI-DHQVKIRGFRIELGEIETRLLEQDSVREAV 933
Cdd:cd17641    401 VFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAV 473

                   ..
gi 2183974163  934 VV 935
Cdd:cd17641    474 VL 475
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1596-1736 2.59e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 59.54  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGV--GPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLdprYpsDRLG-----YMIEDSGIRL 1668
Cdd:cd05927      8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---Y--DTLGpeaieYILNHAEISI 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163 1669 LLTQraarerlplgEGLPCLLL-DAEHEWAGYPESDPQSAVgvDNLAYVIYTSGSTGKPKGTLLPHGNV 1736
Cdd:cd05927     83 VFCD----------AGVKVYSLeEFEKLGKKNKVPPPPPKP--EDLATICYTSGTTGNPKGVMLTHGNI 139
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1594-1981 2.89e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 59.57  E-value: 2.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1594 LDYGELNLRANRLAHRLIELGVGPDVLVGLAAErSLEMIVGLLAILKAGGAYVPLDPRYPS---DRLGYMIEDSGIRLLL 1670
Cdd:PRK05850    36 LTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQ-GLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1671 TQRAARE------RLPLGEGLPCLL------LDAEHEwagyPESDPQSAvgvDNLAYVIYTSGSTGKPKGTLLPHGNVLR 1738
Cdd:PRK05850   115 TTSAVVDdvteyvAPQPGQSAPPVIevdlldLDSPRG----SDARPRDL---PSTAYLQYTSGSTRTPAGVMVSHRNVIA 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1739 LFD-ATRHWFGFSADDA--------W-SLFHSYAFdfsVWEIFGALLHGGRLVIVpyetsrSPEDFLrllcrervtvlnQ 1808
Cdd:PRK05850   188 NFEqLMSDYFGDTGGVPppdttvvsWlPFYHDMGL---VLGVCAPILGGCPAVLT------SPVAFL------------Q 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1809 TPSAFKQLMQVACAGQEVPP------------------LALRHV---VFGGEALEVQALRPWFERFG-----DRAPRlvN 1862
Cdd:PRK05850   247 RPARWMQLLASNPHAFSAAPnfafelavrktsdddmagLDLGGVlgiISGSERVHPATLKRFADRFApfnlrETAIR--P 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1863 MYGITETTVHVTYRPLSLA---------DLDGGAASPIGepiPDLSWYLLDAGL--NPV------------PRGCIGELY 1919
Cdd:PRK05850   325 SYGLAEATVYVATREPGQPpesvrfdyeKLSAGHAKRCE---TGGGTPLVSYGSprSPTvrivdpdtciecPAGTVGEIW 401
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 1920 VGGAGLARGYLNRPELSCTRF---VADPFS-TTGGRLYRTGDLArYRCDGVVEYVGRIDHQVKIRG 1981
Cdd:PRK05850   402 VHGDNVAAGYWQKPEETERTFgatLVDPSPgTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDG 466
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
489-958 3.52e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 59.47  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  489 AEERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTP-----DAPALLFGEERLSYAELNALANRL---------AWRLRE 554
Cdd:PLN02861     2 AETYTVKVEESRPATGGKPSAGPVYRSIYAKDGLLDlpadiDSPWQFFSDAVKKYPNNQMLGRRQvtdskvgpyVWLTYK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  555 EGVGSDVLVGIALE-RGV--------------PMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLSQ----Q 615
Cdd:PLN02861    82 EVYDAAIRIGSAIRsRGVnpgdrcgiygsncpEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQeskiS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  616 SVLARLPQSDG----------LQSLLLDDLERL-VHGYPAE--------NPDLP-EAPDSLCYAIYTSGSTGQPKGVMVR 675
Cdd:PLN02861   162 SILSCLPKCSSnlktivsfgdVSSEQKEEAEELgVSCFSWEefslmgslDCELPpKQKTDICTIMYTSGTTGEPKGVILT 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  676 HRALTnfvcsiarqPGMLARDRLLSVTT---------FSF----DIFG--LELYVpLARGASM--------LLASREQAQ 732
Cdd:PLN02861   242 NRAII---------AEVLSTDHLLKVTDrvateedsyFSYlplaHVYDqvIETYC-ISKGASIgfwqgdirYLMEDVQAL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  733 DP----------------------------EALLDLVE-------RQGVTVLQATPATWRMLCDSERVDLL-RGCTLLCG 776
Cdd:PLN02861   312 KPtifcgvprvydriytgimqkissggmlrKKLFDFAYnyklgnlRKGLKQEEASPRLDRLVFDKIKEGLGgRVRLLLSG 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  777 GEALAEDLAARMRGLSASTWNL-YGPTETTiwSARFRLGEEARPFLG--GPLENTALYILDS--EM-----NPCPpgvAG 846
Cdd:PLN02861   392 AAPLPRHVEEFLRVTSCSVLSQgYGLTESC--GGCFTSIANVFSMVGtvGVPMTTIEARLESvpEMgydalSDVP---RG 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  847 ELLIGGDGLARGYHRRPGLTAERFLpdpfaaDGsrLYRTGDLARYRADGVIEYlgrIDHQVKIrgFRIELGE-IETRLLE 925
Cdd:PLN02861   467 EICLRGNTLFSGYHKRQDLTEEVLI------DG--WFHTGDIGEWQPNGAMKI---IDRKKNI--FKLSQGEyVAVENLE 533
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 2183974163  926 QDSVReAVVVAQPGVAGPT----LVAYLVPTEAALVD 958
Cdd:PLN02861   534 NTYSR-CPLIASIWVYGNSfesfLVAVVVPDRQALED 569
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1547-1961 3.64e-08

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 59.12  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1547 EAEARAD--LLQWNPGPQDFTPASCLHRLiERQAAERPRATAVVY-----GERALDYGELNLRANRLAHRLIELGVGPDV 1619
Cdd:PRK08180    17 EVERRADgtIYLRSAEPLGDYPRRLTDRL-VHWAQEAPDRVFLAErgadgGWRRLTYAEALERVRAIAQALLDRGLSAER 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1620 LVGLAAERSLEMIVGLLAILKAGGAYVPLDPRY---PSD--RLGYMIEdsgirlLLT------------QRAARERLPLG 1682
Cdd:PRK08180    96 PLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvSQDfgKLRHVLE------LLTpglvfaddgaafARALAAVVPAD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1683 ----------EGLPCLLLDAEHEWAGYPESDPQ-SAVGVDNLAYVIYTSGSTGKPKGTLLPHGNVLRLFDATRHWFGFSA 1751
Cdd:PRK08180   170 vevvavrgavPGRAATPFAALLATPPTAAVDAAhAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLA 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1752 DD--------AWSlfHSYAFDFsvweIFG-ALLHGGRLVI-----VP---YETsrspedfLRLLcRE-RVTVLNQTPSAF 1813
Cdd:PRK08180   250 EEppvlvdwlPWN--HTFGGNH----NLGiVLYNGGTLYIddgkpTPggfDET-------LRNL-REiSPTVYFNVPKGW 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1814 KQLmqvacagqeVPPL----ALRHVVF--------GGEALEvQALRPWFERFGDRA----PRLVNMYGITET--TVHVTY 1875
Cdd:PRK08180   316 EML---------VPALerdaALRRRFFsrlkllfyAGAALS-QDVWDRLDRVAEATcgerIRMMTGLGMTETapSATFTT 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1876 RPLSLadldggaASPIGEPIPDLSWYLldaglnpVPRGCIGELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRT 1955
Cdd:PRK08180   386 GPLSR-------AGNIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRS 444

                   ....*.
gi 2183974163 1956 GDLARY 1961
Cdd:PRK08180   445 GDAVRF 450
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3096-3182 4.68e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 58.82  E-value: 4.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3096 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3170
Cdd:PRK08314    21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
                           90
                   ....*....|..
gi 2183974163 3171 EERQAYMLEDSG 3182
Cdd:PRK08314    97 EEELAHYVTDSG 108
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1715-2068 4.69e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 58.98  E-value: 4.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1715 YVIYTSGSTGKPKGTLLPHGNVLRLFdaTRHWFGFSADD-----------AWSLFHSYafdfsvweIFGALLHGGRLVIv 1783
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGPHLVGL--KYYWRSIIEKDiptvvfshssiGWVSFHGF--------LYGSLSLGNTFVM- 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1784 pYE-----TSRSPEDFLRLLCRERVTVLNQTPSAFKQLMQVACAGQEVPP----LALRHVVFGGEALEvQALRPWFE-RF 1853
Cdd:PTZ00237   327 -FEggiikNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSkydlSNLKEIWCGGEVIE-ESIPEYIEnKL 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1854 GDRAPRLvnmYGITET--TVHVTYRPLSLAdldggaASPIGEPIPDLSWYLLDAGLNPVPRGCIGELYVGgaglargyLN 1931
Cdd:PTZ00237   405 KIKSSRG---YGQTEIgiTYLYCYGHINIP------YNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK--------LP 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1932 RPELSCTRFVADP------FSTTGGrLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGVAEAVVL 2005
Cdd:PTZ00237   468 MPPSFATTFYKNDekfkqlFSKFPG-YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 2006 PHEGPG-ATQLVGYVVTQAAPSDPAA----LRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDR 2068
Cdd:PTZ00237   547 GIYDPDcYNVPIGLLVLKQDQSNQSIdlnkLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3101-3182 4.88e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 58.76  E-value: 4.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3101 APALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3180
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81

                   ..
gi 2183974163 3181 SG 3182
Cdd:PRK08276    82 SG 83
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3113-3182 4.94e-08

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 58.38  E-value: 4.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3113 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd05911     13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1596-2016 5.23e-08

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 58.59  E-value: 5.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1596 YGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLT--QR 1673
Cdd:cd17641     14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAedEE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1674 AARERLPLGEGLPCL------------------LLDAEHEWA---GYPESDPQ------SAVGVDNLAYVIYTSGSTGKP 1726
Cdd:cd17641     94 QVDKLLEIADRIPSVryviycdprgmrkyddprLISFEDVVAlgrALDRRDPGlyerevAAGKGEDVAVLCTTSGTTGKP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1727 KGTLLPHGNVLRLfDATRHWFGFSADDAWSLfhSY-------AFDFSVweifGALLHGGRLVIVPYETSRSPEDfLR--- 1796
Cdd:cd17641    174 KLAMLSHGNFLGH-CAAYLAADPLGPGDEYV--SVlplpwigEQMYSV----GQALVCGFIVNFPEEPETMMED-LReig 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1797 -------------LLCRERVTVLNQTP---SAFKQLMQVACAG------QEVPPLALRHVVFGGEALEVQALRpwfERFG 1854
Cdd:cd17641    246 ptfvllpprvwegIAADVRARMMDATPfkrFMFELGMKLGLRAldrgkrGRPVSLWLRLASWLADALLFRPLR---DRLG 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1855 DRAPR-----------------------LVNMYGITETTVHVTYRPLSLADLDggaasPIGEPIPDLSWYLLDAGlnpvp 1911
Cdd:cd17641    323 FSRLRsaatggaalgpdtfrffhaigvpLKQLYGQTELAGAYTVHRDGDVDPD-----TVGVPFPGTEVRIDEVG----- 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1912 rgcigELYVGGAGLARGYLNRPELSCTRFVADPFsttggrlYRTGDLARYRCDGVVEYVGRI-DHQVKIRGFRIELGEIE 1990
Cdd:cd17641    393 -----EILVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIE 460
                          490       500
                   ....*....|....*....|....*.
gi 2183974163 1991 ARLLAQPGVAEAVVLPHEGPGATQLV 2016
Cdd:cd17641    461 NKLKFSPYIAEAVVLGAGRPYLTAFI 486
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
563-1006 6.10e-08

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 58.60  E-value: 6.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  563 VGIALERGVPMVVALLAVLKAGGAYVPL-DPQYP--ADRLQYMIDDSGLRLLLSQQSV-------LARLPQSDGLQSLLL 632
Cdd:PRK12476    95 VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAaeavegfLRNLPRLRRPRVIAI 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  633 DDL-ERLVHGYPAENPDLpeapDSLCYAIYTSGSTGQPKGVMVRHRAL-TNFVCSIarqpgmlardrlLSVTTFSFDIFG 710
Cdd:PRK12476   175 DAIpDSAGESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQMI------------LSIDLLDRNTHG 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  711 ---LELY---------VPLARGASMLLAS-----REQAQDPEALLDlvERQGVTVLQATP------ATWRML-CDSERVD 766
Cdd:PRK12476   239 vswLPLYhdmglsmigFPAVYGGHSTLMSptafvRRPQRWIKALSE--GSRTGRVVTAAPnfayewAAQRGLpAEGDDID 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  767 lLRGCTLLCGGEALAEDlAARMRGLSASTWNL--------YGPTETTIWSA--------------RFRLG---------- 814
Cdd:PRK12476   317 -LSNVVLIIGSEPVSID-AVTTFNKAFAPYGLprtafkpsYGIAEATLFVAtiapdaepsvvyldREQLGagravrvaad 394
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  815 -EEARPFL--GGPLENTALYILDSEM-NPCPPGVAGELLIGGDGLARGYHRRPGLTAERF-------LPDPFAADGS--- 880
Cdd:PRK12476   395 aPNAVAHVscGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAEGSHADGAadd 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  881 -RLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQD-SVREAVVVA--QPGVAGPTLVayLVPTEAA- 955
Cdd:PRK12476   475 gTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEASpMVRRGYVTAftVPAEDNERLV--IVAERAAg 551
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163  956 --LVDAESArQQELRSALKNS-LLAVLPDYMVPAHMlllenLPLTPNGKINRKA 1006
Cdd:PRK12476   552 tsRADPAPA-IDAIRAAVSRRhGLAVADVRLVPAGA-----IPRTTSGKLARRA 599
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3110-3181 8.59e-08

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 57.78  E-value: 8.59e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 3110 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3181
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA 72
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3087-3182 1.57e-07

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 57.11  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 3161
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                           90       100
                   ....*....|....*....|.
gi 2183974163 3162 YVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAE 163
PLN02654 PLN02654
acetate-CoA ligase
533-1023 1.59e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 57.21  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  533 EERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLL 612
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  613 SQQSVlARLPQSDGLQSLLLDDLERLV-HGYPA------EN-----------------------PDLP--------EAPD 654
Cdd:PLN02654   198 TCNAV-KRGPKTINLKDIVDAALDESAkNGVSVgicltyENqlamkredtkwqegrdvwwqdvvPNYPtkcevewvDAED 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  655 SLcYAIYTSGSTGQPKGV-------MVRhrALTNFVCSIARQPGML--ARDRLLSVTTFSFDIFGlelyvPLARGASMLL 725
Cdd:PLN02654   277 PL-FLLYTSGSTGKPKGVlhttggyMVY--TATTFKYAFDYKPTDVywCTADCGWITGHSYVTYG-----PMLNGATVLV 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  726 -ASREQAQDPEALLDLVERQGVTVLQATPATWRMLCDServdllrgctllcGGEALAEDLAARMRGL---------SAST 795
Cdd:PLN02654   349 fEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD-------------GDEYVTRHSRKSLRVLgsvgepinpSAWR 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  796 W--NLYG----PTETTIWSAR---FRL-----------GEEARPFLG-GPLentalyILDSEMNPCPPGVAGELLIGGD- 853
Cdd:PLN02654   416 WffNVVGdsrcPISDTWWQTEtggFMItplpgawpqkpGSATFPFFGvQPV------IVDEKGKEIEGECSGYLCVKKSw 489
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  854 -GLAR---GYHRRPGLTAERflpdPFAAdgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSV 929
Cdd:PLN02654   490 pGAFRtlyGDHERYETTYFK----PFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  930 REAVVVA-QPGVAGPTLVAYLvpteaALVDAESaRQQELRSALKNSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL- 1007
Cdd:PLN02654   562 AEAAVVGiEHEVKGQGIYAFV-----TLVEGVP-YSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILr 635
                          570       580
                   ....*....|....*....|....
gi 2183974163 1008 --------PLPDASAVRDAHVAPE 1023
Cdd:PLN02654   636 kiasrqldELGDTSTLADPGVVDQ 659
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
842-1008 2.07e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 56.54  E-value: 2.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  842 PGVAGELLIGGDGLARGYHrrpgltaerflpdPFAADGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIET 921
Cdd:PRK07445   298 ANQTGNITIQAQSLALGYY-------------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  922 RLLEQDSVREAVVVAQP-GVAGPTLVAYLVPteaalvDAESARQQELRSALKNSLLAvlpdYMVPAHMLLLENLPLTPNG 1000
Cdd:PRK07445   365 AILATGLVQDVCVLGLPdPHWGEVVTAIYVP------KDPSISLEELKTAIKDQLSP----FKQPKHWIPVPQLPRNPQG 434

                   ....*...
gi 2183974163 1001 KINRKALP 1008
Cdd:PRK07445   435 KINRQQLQ 442
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3097-3183 2.13e-07

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 56.59  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3097 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3175
Cdd:PRK07470    19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97

                   ....*...
gi 2183974163 3176 YMLEDSGV 3183
Cdd:PRK07470    98 YLAEASGA 105
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3110-3182 2.76e-07

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 55.95  E-value: 2.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 3110 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSG 73
PRK08315 PRK08315
AMP-binding domain protein; Validated
3089-3183 2.85e-07

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 56.36  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3089 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 3164
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
                           90
                   ....*....|....*....
gi 2183974163 3165 VDPEYPEERQAYMLEDSGV 3183
Cdd:PRK08315    98 INPAYRLSELEYALNQSGC 116
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3108-3182 2.85e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 55.76  E-value: 2.85e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 3108 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG 75
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3063-3165 6.28e-07

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 55.03  E-value: 6.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3063 AVAERYqllegwnaTAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVA 3141
Cdd:cd05920      1 EFARRY--------RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQ 71
                           90       100
                   ....*....|....*....|....
gi 2183974163 3142 MERSIEMVVALMAILKAGGayVPV 3165
Cdd:cd05920     72 LPNVAEFVVLFFALLRLGA--VPV 93
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3097-3182 7.97e-07

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 54.51  E-value: 7.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3097 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3176
Cdd:PRK06145    14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93

                   ....*.
gi 2183974163 3177 MLEDSG 3182
Cdd:PRK06145    94 ILGDAG 99
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3108-3161 9.12e-07

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 54.28  E-value: 9.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 3108 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 3161
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV 54
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3090-3183 1.01e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 54.39  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3167
Cdd:PRK12583    23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                           90
                   ....*....|....*.
gi 2183974163 3168 EYPEERQAYMLEDSGV 3183
Cdd:PRK12583   103 AYRASELEYALGQSGV 118
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
534-1007 1.46e-06

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 53.97  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  534 ERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRLLLS 613
Cdd:cd05939      2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  614 QqsvlarlpqsdglqslLLDDLERLVHGYPAENPDLpEAPDSLCYaIYTSGSTGQPKGVMVRHraltnfvcsiarqpgml 693
Cdd:cd05939     82 N----------------LLDPLLTQSSTEPPSQDDV-NFRDKLFY-IYTSGTTGLPKAAVIVH----------------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  694 arDRLLSVTTFSFDIFGLE----LYVPL----------ARGASMLLAS----REQAQDPEALLDLVeRQGVTVLQATPAT 755
Cdd:cd05939    127 --SRYYRIAAGAYYAFGMRpedvVYDCLplyhsaggimGVGQALLHGStvviRKKFSASNFWDDCV-KYNCTIVQYIGEI 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  756 WRML-----CDSERVDLLRgctLLCGGealaedlaarmrGLSASTWN-------------LYGPTETTIWSARF--RLGe 815
Cdd:cd05939    204 CRYLlaqppSEEEQKHNVR---LAVGN------------GLRPQIWEqfvrrfgipqigeFYGATEGNSSLVNIdnHVG- 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  816 eARPFLGGPL------------ENTALYILDSE--MNPCPPGVAGEL---LIGGDGLAR--GYHRRpGLTAERFLPDPFA 876
Cdd:cd05939    268 -ACGFNSRILpsvypirlikvdEDTGELIRDSDglCIPCQPGEPGLLvgkIIQNDPLRRfdGYVNE-GATNKKIARDVFK 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  877 AdGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVV--VAQPGVAGPTLVaylvpteA 954
Cdd:cd05939    346 K-GDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGM-------A 417
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2183974163  955 ALVDAESARQQELRSAlknSLLAVLPDYMVPAHMLLLENLPLTPNGKINRKAL 1007
Cdd:cd05939    418 AIVDPERKVDLDRFSA---VLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
535-1004 1.72e-06

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 53.62  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  535 RLSYAELNALA-NRLAWRLREEGVGSDVLVGialERGVPMVVALLAVLKAGGAYVPL-------DPQYPADRLQYMIDDS 606
Cdd:PRK05851    31 RHPWPEVHGRAeNVAARLLDRDRPGAVGLVG---EPTVELVAAIQGAWLAGAAVSILpgpvrgaDDGRWADATLTRFAGI 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  607 GLRLLLSQQSVLARLPQSDGlqSLLLDDLERLVHgypAENPDLPEAPDSLCYAIY--TSGSTGQPKGVMVRHRALTNFVC 684
Cdd:PRK05851   108 GVRTVLSHGSHLERLRAVDS--SVTVHDLATAAH---TNRSASLTPPDSGGPAVLqgTAGSTGTPRTAILSPGAVLSNLR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  685 SIARQPGM-LARDRLLSVTTFSFDIfGLELYVPLA-RGASMLLA-SREQAQDPEALLDLVERQGVTVLQATPATWRMLCD 761
Cdd:PRK05851   183 GLNARVGLdAATDVGCSWLPLYHDM-GLAFLLTAAlAGAPLWLApTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGK 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  762 SER----VDLLRGCTLLCGGEALAEDLAARMR------GLSA-STWNLYGPTETTIWSARFRLGEEAR------------ 818
Cdd:PRK05851   262 YARrvsdVDLGALRVALNGGEPVDCDGFERFAtamapfGFDAgAAAPSYGLAESTCAVTVPVPGIGLRvdevttddgsga 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  819 ---PFLGGPLENTALYILDSEMnpcPPGVA----GELLIGGDGLARGYhrrpgltaerFLPDPFAADGsrLYRTGDLArY 891
Cdd:PRK05851   342 rrhAVLGNPIPGMEVRISPGDG---AAGVAgreiGEIEIRGASMMSGY----------LGQAPIDPDD--WFPTGDLG-Y 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  892 RADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVREAVVVA---QPGVAGPTLVaylVPTEAALVDAESArqqelR 968
Cdd:PRK05851   406 LVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgtGEGSARPGLV---IAAEFRGPDEAGA-----R 477
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2183974163  969 SALKNSLLAVLPdyMVPAHMLLLE--NLPLTPNGKINR 1004
Cdd:PRK05851   478 SEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRR 513
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3090-3183 2.01e-06

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 53.35  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3167
Cdd:PRK05852    21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                           90
                   ....*....|....*.
gi 2183974163 3168 EYPEERQAYMLEDSGV 3183
Cdd:PRK05852   101 ALPIAEQRVRSQAAGA 116
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
531-760 2.03e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 53.45  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  531 FGEERLSYAELNALANRLAWRLREE-GVGSDVLVGIALERGvPMVVAL-LAVLKAGGAYVPLDPQYPADRLQYMIDDSGL 608
Cdd:cd05938      1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNE-PAFLWIwLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  609 RLLLS----QQSVLARLP--QSDGLQSLLL---------DDLERLVHGYPAENP--DL--PEAPDSLCYAIYTSGSTGQP 669
Cdd:cd05938     80 KVLVVapelQEAVEEVLPalRADGVSVWYLshtsntegvISLLDKVDAASDEPVpaSLraHVTIKSPALYIYTSGTTGLP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  670 KGVMVRHRALTnFVCSIARQPGMLARDRL-LSVTTFSFDIFGLELYVPLARGASMLLASREQAQDpeaLLDLVERQGVTV 748
Cdd:cd05938    160 KAARISHLRVL-QCSGFLSLCGVTADDVIyITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQ---FWDDCRKHNVTV 235
                          250
                   ....*....|..
gi 2183974163  749 LQATPATWRMLC 760
Cdd:cd05938    236 IQYIGELLRYLC 247
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3082-3169 2.03e-06

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 53.73  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3082 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAIL 3156
Cdd:PRK08180    36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                           90
                   ....*....|...
gi 2183974163 3157 KAGGAYVPVDPEY 3169
Cdd:PRK08180   116 YAGVPYAPVSPAY 128
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
254-793 2.04e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.11  E-value: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  254 PTDRQRPALPSYRGARHELQLPQALGRQLQALAQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIG 333
Cdd:COG3321    855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  334 FFVNTQVLRADLDAQMPFLDLLQQTRVAALGAQSHQDLPFEQLVEALQPERSLShsplfqamynhqnLGSAGRQSLAAQL 413
Cdd:COG3321    935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAA-------------AAAAAAALAAAAA 1001
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  414 PGLSVEDLSWGAHSAQFDLTLDTYESEQGVHAEFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERA 493
Cdd:COG3321   1002 LALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAA 1081
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  494 TLLQRSRLPASEYPAGQGVHRLFEAQAGLTPDAPALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPM 573
Cdd:COG3321   1082 AALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAA 1161
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  574 VVALLAVLKAGGAYVPLDPQYPADRLQYMIDDSGLRL--LLSQQSVLARLPQSDGLQSLLLDDLERLVHGYPAENPDLPE 651
Cdd:COG3321   1162 ALAAALLAAAALLLALALALAAALAAALAGLAALLLAalLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAA 1241
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  652 APDSLCYAIYTSGSTGQPKGVMVRHRALTnfvcsiARQPGMLARDRLLSVTTFSFDIFGLELYVPLARGASMLLASREQA 731
Cdd:COG3321   1242 AAAVAALAAAAAALLAALAALALLAAAAG------LAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAA 1315
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163  732 QDPEALLDLVERQGVTVLQATPATWRMLCDSERVDLLRGCTLLCGGEALAEDLAARMRGLSA 793
Cdd:COG3321   1316 AAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
631-1003 2.15e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 53.82  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  631 LLDDLERLVHGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRA-LTNFVCSIARQPgMLARDRLLSVTTFsFDIF 709
Cdd:PRK06814   770 LADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNlLANRAQVAARID-FSPEDKVFNALPV-FHSF 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  710 GLE--LYVPLARGASMLLAsreqaqdPEAL-----LDLVERQGVTVLQATPAtwrMLCDSERV----DL--LRGCTllcg 776
Cdd:PRK06814   848 GLTggLVLPLLSGVKVFLY-------PSPLhyriiPELIYDTNATILFGTDT---FLNGYARYahpyDFrsLRYVF---- 913
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  777 geALAEDLAARMRGLSASTWNL-----YGPTETTIWSA-----RFRLGEEARpflggplentALYILDSEMNPCPpGV-- 844
Cdd:PRK06814   914 --AGAEKVKEETRQTWMEKFGIrilegYGVTETAPVIAlntpmHNKAGTVGR----------LLPGIEYRLEPVP-GIde 980
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  845 AGELLIGGDGLARGYHR--RPGLTAErflpdpfAADGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETR 922
Cdd:PRK06814   981 GGRLFVRGPNVMLGYLRaeNPGVLEP-------PADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL 1051
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  923 LLEQDSVREAVVVAQP-GVAGPTLVayLVPTEAalvDAEsaRQQELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGK 1001
Cdd:PRK06814  1052 AAELWPDALHAAVSIPdARKGERII--LLTTAS---DAT--RAAFLAHAKAAG----ASELMVPAEIITIDEIPLLGTGK 1120

                   ..
gi 2183974163 1002 IN 1003
Cdd:PRK06814  1121 ID 1122
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3111-3183 2.36e-06

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 52.98  E-value: 2.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2183974163 3111 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3087-3182 3.22e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 52.73  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3087 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3166
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                           90
                   ....*....|....*.
gi 2183974163 3167 PEYPEERQAYMLEDSG 3182
Cdd:PRK06710   106 PLYTERELEYQLHDSG 121
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3058-3179 4.48e-06

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 52.36  E-value: 4.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3058 ELDSLAVAERYQLlegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERG 3131
Cdd:PRK13295     2 EFDAVLLPPRRAA-----SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLG 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2183974163 3132 IGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3179
Cdd:PRK13295    77 VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLK 124
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3109-3182 5.99e-06

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 51.66  E-value: 5.99e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 3109 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSG 78
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3095-3182 6.03e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 52.00  E-value: 6.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3172
Cdd:PRK13391     7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90
                   ....*....|
gi 2183974163 3173 RQAYMLEDSG 3182
Cdd:PRK13391    87 EAAYIVDDSG 96
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
662-979 6.30e-06

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 51.69  E-value: 6.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  662 TSGSTGQPKGVMVRHRALTNFVCSIAR---QPGMLARDRLLSvtTFSFDIF--------GLElyvplARGASMLLASreq 730
Cdd:COG1541     91 SSGTTGKPTVVGYTRKDLDRWAELFARslrAAGVRPGDRVQN--AFGYGLFtgglglhyGAE-----RLGATVIPAG--- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  731 AQDPEALLDLVERQGVTVLQATPATWRMLCDSER---VDL----LRgcTLLCGGEALAEDLAARM-RGLSASTWNLYGPT 802
Cdd:COG1541    161 GGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEeegIDPrdlsLK--KGIFGGEPWSEEMRKEIeERWGIKAYDIYGLT 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  803 ETTIWSArfrlGE-EARpflGGPLENTALY---ILDSEM-NPCPPGVAGELLIggdglargyhrrpglTaerflpdPFAA 877
Cdd:COG1541    239 EVGPGVA----YEcEAQ---DGLHIWEDHFlveIIDPETgEPVPEGEEGELVV---------------T-------TLTK 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  878 DGSRL--YRTGDLARY------------RADGVieyLGRIDHQVKIRGFRIELGEIetrlleqdsvrEAVVVAQPGVAGp 943
Cdd:COG1541    290 EAMPLirYRTGDLTRLlpepcpcgrthpRIGRI---LGRADDMLIIRGVNVFPSQI-----------EEVLLRIPEVGP- 354
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2183974163  944 tlvAYL--VPTEAAL----VDAESAR---QQELRSALKNSLLAVL 979
Cdd:COG1541    355 ---EYQivVDREGGLdeltVRVELAPgasLEALAEAIAAALKAVL 396
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3101-3183 6.46e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 51.53  E-value: 6.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3101 APALAFGEERLDYAELNRRANRLAhaliERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3180
Cdd:PRK07787    16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90

                   ...
gi 2183974163 3181 SGV 3183
Cdd:PRK07787    91 SGA 93
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3104-3181 6.50e-06

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 51.67  E-value: 6.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 3104 LAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3181
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS 78
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3095-3175 7.22e-06

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 51.86  E-value: 7.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPe 3168
Cdd:cd05931      3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLPP- 80

                   ....*..
gi 2183974163 3169 yPEERQA 3175
Cdd:cd05931     81 -PTPGRH 86
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2087-2153 9.28e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 46.09  E-value: 9.28e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  2087 RSELEQRLAAIWADVLKLG---RVGLDDNFFELGGDSIISIQVVSRARQA-GIRLAPRDLFLHQTIRGLAG 2153
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAE 80
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
649-1001 1.03e-05

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 51.25  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  649 LPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIARQPGMLARDRLLSVTTFsFDIFGLE--LYVPLARGASMLLA 726
Cdd:PRK08043   360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPL-FHSFGLTvgLFTPLLTGAEVFLY 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  727 sreqaqdPEALL-----DLVERQGVTVLQATpATWrmLCDSERV----DLLRGCTLLCGGEALAEdlaaRMRGLSASTWN 797
Cdd:PRK08043   439 -------PSPLHyrivpELVYDRNCTVLFGT-STF--LGNYARFanpyDFARLRYVVAGAEKLQE----STKQLWQDKFG 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  798 L-----YGPTETTIWSArFRLGEEARPFLGGPLentaLYILDSEMNPCpPGVA--GELLIGGDGLARGYHR--RPGLtae 868
Cdd:PRK08043   505 LrilegYGVTECAPVVS-INVPMAAKPGTVGRI----LPGMDARLLSV-PGIEqgGRLQLKGPNIMNGYLRveKPGV--- 575
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  869 rfLPDPFAADG-----SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIETRLLEQDSVRE-AVVVAQPGVAG 942
Cdd:PRK08043   576 --LEVPTAENArgemeRGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQhATAIKSDASKG 653
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2183974163  943 PTLVayLVPTeaalvDAESARQQELRSALKNSllavLPDYMVPAHMLLLENLPLTPNGK 1001
Cdd:PRK08043   654 EALV--LFTT-----DSELTREKLQQYAREHG----VPELAVPRDIRYLKQLPLLGSGK 701
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3063-3165 1.03e-05

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 51.14  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3063 AVAERYQLLEGWNataaEYPLQRgvhrLFEEQVErtPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAM 3142
Cdd:PRK10946    11 EFARRYREKGYWQ----DLPLTD----ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQL 80
                           90       100
                   ....*....|....*....|...
gi 2183974163 3143 ERSIEMVVALMAILKAGgaYVPV 3165
Cdd:PRK10946    81 GNVAEFYITFFALLKLG--VAPV 101
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
3107-3182 1.56e-05

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 50.47  E-value: 1.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2183974163 3107 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:PRK12406     8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3076-3182 1.60e-05

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 50.53  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3076 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 3155
Cdd:PRK06155    12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                           90       100
                   ....*....|....*....|....*..
gi 2183974163 3156 LKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:PRK06155    92 AWLGAIAVPINTALRGPQLEHILRNSG 118
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
645-953 1.96e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 50.58  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  645 ENPD--LPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSI-----ARQPGMLARDRLLSvttfsfdifglelYVPL 717
Cdd:PLN02430   209 ENPSetNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLS-------------FLPL 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  718 A-------------RGASM------LLASREQAQD--------------------PEALLDL--VERQGVTVLQATPATW 756
Cdd:PLN02430   276 AhildrmieeyffrKGASVgyyhgdLNALRDDLMElkptllagvprvferihegiQKALQELnpRRRLIFNALYKYKLAW 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  757 RMLCDSER-----VDLL-----------RGCTLLCGGEALAEDLAARMRGLS-ASTWNLYGPTETtiwsarfrLGEEARP 819
Cdd:PLN02430   356 MNRGYSHKkaspmADFLafrkvkaklggRLRLLISGGAPLSTEIEEFLRVTScAFVVQGYGLTET--------LGPTTLG 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  820 F---------LGGPLENTALYILD-SEM--NPCPPGVAGELLIGGDGLARGYHRRPGLTAERFlpdpfaADGsrLYRTGD 887
Cdd:PLN02430   428 FpdemcmlgtVGAPAVYNELRLEEvPEMgyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM------KDG--WFHTGD 499
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  888 LARYRADGVIEYLGRIDHQVKI-RGFRIELGEIETRLLEQDSVREAVVVAQPgvAGPTLVAYLVPTE 953
Cdd:PLN02430   500 IGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVYGDS--FKSMLVAVVVPNE 564
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
47-586 2.08e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 50.64  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   47 RIPL-SYAQERQWflwqmdpqSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDEQLDGFRQQVLASVDVP 125
Cdd:COG3321    860 RVPLpTYPFQRED--------AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLA 931
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  126 VPVTLAGDDDAQAQIRAFVESETQQPFDLRNGPLLRARLLRLAADDHVLTLTIHHVAADGWSMRVLVEELIALYGARRQG 205
Cdd:COG3321    932 LVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALL 1011
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  206 IEATLPdlpiqyadyaiwQRHWLEAGERERQLEYWMARLGGGQSVLELPTDRQRPALPSYRGARHELQLPQALGRQLQAL 285
Cdd:COG3321   1012 LAAAAA------------AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELAL 1079
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  286 AQREGTTLFMLLLASFQALLHRYSGQDEIRVGVPVANRNRVETERLIGFFVNTQVLRADLDAQMPFLDLLQQTRVAALGA 365
Cdd:COG3321   1080 AAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAAL 1159
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  366 QSHQDLPFEQLVEALQPERSLSHSPLFQAMYNHQNLGSAGRQSLAAQLPGLSVEDLSWGAHSAQFDLTLDTYESEQGVHA 445
Cdd:COG3321   1160 AAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALA 1239
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  446 EFTYATDLFEAATVERLARHWRNLLEAVVAEPRRRLGDLPLLDAEERATLLQRSRLPASEYPAGQGVHRLFEAQAGLTPD 525
Cdd:COG3321   1240 AAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAA 1319
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  526 APALLFGEERLSYAELNALANRLAWRLREEGVGSDVLVGIALERGVPMVVALLAVLKAGGA 586
Cdd:COG3321   1320 ALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAA 1380
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3096-3159 2.14e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 50.31  E-value: 2.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163 3096 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAG 3159
Cdd:PRK07788    60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3095-3183 2.39e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 49.98  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3174
Cdd:PRK06188    22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101

                   ....*....
gi 2183974163 3175 AYMLEDSGV 3183
Cdd:PRK06188   102 AYVLEDAGI 110
PRK09274 PRK09274
peptide synthase; Provisional
3097-3167 2.41e-05

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 49.90  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3097 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGIGA-DRLvgVAMER-SIEMVVALMAILKAGGAYVP 3164
Cdd:PRK09274    18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRA--VLMVTpSLEFFALTFALFKAGAVPVL 95

                   ...
gi 2183974163 3165 VDP 3167
Cdd:PRK09274    96 VDP 98
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
532-903 2.45e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 49.97  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  532 GEERLSYAelnalanrlawrLREEGVGSDVLVGialeRGVPMVVALLAVLKAGGAYVPLDPQYPADrlqymIDDSGLRLL 611
Cdd:PTZ00216   181 GEDALAYA------------LRETECKAIVCNG----KNVPNLLRLMKSGGMPNTTIIYLDSLPAS-----VDTEGCRLV 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  612 lSQQSVLArlpqsdglqsllLDDLERLVHGYPaenpdLPEAPDSLCYAIYTSGSTGQPKGVMVRHRALTNFVCSIArqpg 691
Cdd:PTZ00216   240 -AWTDVVA------------KGHSAGSHHPLN-----IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALE---- 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  692 mlarDRLLsvttfsfDIFG----LELYV---PLA-------------RGASMLLASreqaqdPEALL--------DLVE- 742
Cdd:PTZ00216   298 ----DRLN-------DLIGppeeDETYCsylPLAhimefgvtniflaRGALIGFGS------PRTLTdtfarphgDLTEf 360
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  743 ---------------RQGVTVLQATPATW-RMLCDSERVDLLRGctLLCGGE---------ALAED-LAARMRG------ 790
Cdd:PTZ00216   361 rpvfligvprifdtiKKAVEAKLPPVGSLkRRVFDHAYQSRLRA--LKEGKDtpywnekvfSAPRAvLGGRVRAmlsggg 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  791 -LSASTWNL-----------YGPTETTIWSARFRLGEEArPFLGGPLENTA-LYILDSEM-----NPCPpgvAGELLIGG 852
Cdd:PTZ00216   439 pLSAATQEFvnvvfgmviqgWGLTETVCCGGIQRTGDLE-PNAVGQLLKGVeMKLLDTEEykhtdTPEP---RGEILLRG 514
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2183974163  853 DGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRI 903
Cdd:PTZ00216   515 PFLFKGYYKQEELTREVLDEDGW-------FHTGDVGSIAANGTLRIIGRV 558
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1589-1805 2.65e-05

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 49.98  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1589 YGERALDYGELNLRANRLAHRLI-ELGVGPDVLVGLAAERSLEMIVGLLAILKAGGAYVPLDPRYPSDRLGYMIEDSGIR 1667
Cdd:cd05938      1 FEGETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1668 LLLTQRAARERLPlgEGLPCLLLDAEHEWAGYPESDPQsavGVDNL-------------------------AYVIYTSGS 1722
Cdd:cd05938     81 VLVVAPELQEAVE--EVLPALRADGVSVWYLSHTSNTE---GVISLldkvdaasdepvpaslrahvtikspALYIYTSGT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1723 TGKPKGTLLPHGNVLRLfDATRHWFGFSADD----AWSLFHSYAFdfsVWEIFGALLHGGRLVIVP-YETSRSPEDflrl 1797
Cdd:cd05938    156 TGLPKAARISHLRVLQC-SGFLSLCGVTADDviyiTLPLYHSSGF---LLGIGGCIELGATCVLKPkFSASQFWDD---- 227

                   ....*....
gi 2183974163 1798 lCRE-RVTV 1805
Cdd:cd05938    228 -CRKhNVTV 235
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3109-3169 2.73e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 50.04  E-value: 2.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 3109 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:PRK12582    79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAY 139
PRK12467 PRK12467
peptide synthase; Provisional
56-401 2.73e-05

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 50.54  E-value: 2.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   56 RQWFLWQMDPQSAAYNIPSALRLRGELDVEALSASLGAIVERHQSLRTVFVEDeqldgfrqqvlasvdvPVPVTLAGDDd 135
Cdd:PRK12467  3657 RDLMSAPTIAELAGYSPLGDVPVNLLLDLNRLETGFPALFCRHEGLGTVFDYE----------------PLAVILEGDR- 3719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  136 aqaqirafvesetqqpfdlrngpllrarllrlaaddHVLTLTIHHVAADGWSmrvlveelialygarrqgiEATLPDLPI 215
Cdd:PRK12467  3720 ------------------------------------HVLGLTCRHLLDDGWQ-------------------DTSLQAMAV 3744
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  216 QYADYAIWQRHWLEAGERErqleyWmaRLGGgqsvlelptdrqrpalpsyrgarhelqlpqALGRQLQALAQREGttlfm 295
Cdd:PRK12467  3745 QYADYILWQQAKGPYGLLG-----W--SLGG------------------------------TLARLVAELLEREG----- 3782
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  296 lllasfqallhrysgqdeirvgvpvanrnrvETERLIGFFVNTQVLRADLDAQMPFLDLLQQtrVAALGAQSHQDL---- 371
Cdd:PRK12467  3783 -------------------------------ESEAFLGLFDNTLPLPDEFVPQAEFLELLRQ--LGELIGRANRLLrgle 3829
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2183974163  372 -----PFEQLVEALQPERSLSHSPLFQAMYNHQNL 401
Cdd:PRK12467  3830 eggvgPDVLVGIAIQRCFDIAPLELYTPLLDAGEL 3864
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1773-2082 2.95e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 49.61  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1773 ALLHGGRLVIVPY-------ETSRSPEDFlrllcrervtVLNQTPSAFKQLMQVAcagqeVPPLALRHVVFGGEAlevqa 1845
Cdd:PRK07445   181 SFLTGGKLVILPYkrlksgqELPPNPSDF----------FLSLVPTQLQRLLQLR-----PQWLAQFRTILLGGA----- 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1846 lRPWFERFgDRAP----RLVNMYGITETTVHV-TYRPlslAD-LDGGAASpiGEPIPDlswylldAGLNpVPRGCIGELY 1919
Cdd:PRK07445   241 -PAWPSLL-EQARqlqlRLAPTYGMTETASQIaTLKP---DDfLAGNNSS--GQVLPH-------AQIT-IPANQTGNIT 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1920 VGGAGLARGYLnrPELSCTRfvadpfsttggRLYRTGDLARYRCDGVVEYVGRIDHQVKIRGFRIELGEIEARLLAQPGV 1999
Cdd:PRK07445   306 IQAQSLALGYY--PQILDSQ-----------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2000 AEAVVLphegpG-ATQLVGYVVTQAA-PSDPAALRDTLRQALKASLPEHMVPAHLLFLERLPLTANGKLDRRALPAPDAS 2077
Cdd:PRK07445   373 QDVCVL-----GlPDPHWGEVVTAIYvPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447

                   ....*
gi 2183974163 2078 RLQRD 2082
Cdd:PRK07445   448 RLGLP 452
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2736-2923 5.64e-05

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 48.63  E-value: 5.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2736 GEAGLGFELAEAPLLRLVLVRTGERRHHLIYTNHHILMDGWSNSQLLGEVLQRY----RGETPSRSDG--RYRDYIAWLQ 2809
Cdd:cd19546     99 DRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRAPERAPLplQFADYALWER 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2810 RQDAGRTE---------AFWKQRLQRLGEPTLLVPAFAHGVRGAEGHADRYRQLDVTTSQRLAEFAREQKVTLNTLVQAA 2880
Cdd:cd19546    179 ELLAGEDDrdsligdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAA 258
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2183974163 2881 WLILLQRFTGQDTVAFGaTVSGRPAELRGIEEQIGLFINTLPV 2923
Cdd:cd19546    259 LAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLAL 300
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
2193-2434 5.88e-05

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 48.34  E-value: 5.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2193 WNQSVLLEPGQALDGTLLETALQALLAHHDALRLGFRLEDGTWR---AEH--RAVEAGEVLLWqqsvadgqalealaEQV 2267
Cdd:cd19537     24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRrsySSSppRVQRVDTLDVW--------------KEI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2268 QRSLDLGSGPLLRALLAtlgdgSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQlqaGQAVALPAKTSAFKAWAERLQAHA 2347
Cdd:cd19537     90 NRPFDLEREDPIRVFIS-----PDTLLVVMSHIICDLTTLQLLLREVSAAYNG---KLLPPVRREYLDSTAWSRPASPED 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2348 RDgglegergYWLAQLEGVSteLPCDDREGAQSVRHVRSARTELTEEATRRLLQEAPAAYRT--QvndLLLTALARVIGR 2425
Cdd:cd19537    162 LD--------FWSEYLSGLP--LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITlhQ---LALAAVALALQD 228

                   ....*....
gi 2183974163 2426 WTGQADTLI 2434
Cdd:cd19537    229 LSDRTDIVL 237
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3094-3182 9.46e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 48.23  E-value: 9.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3094 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 3168
Cdd:PRK07786    22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
                           90
                   ....*....|....
gi 2183974163 3169 YPEERQAYMLEDSG 3182
Cdd:PRK07786   101 LTPPEIAFLVSDCG 114
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3107-3181 1.14e-04

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 47.63  E-value: 1.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 3107 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3181
Cdd:cd12119     22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHA 96
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1023-1094 1.24e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.01  E-value: 1.24e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163  1023 EGELERAMAAIWSEVLKLG---HIGRDDNFFELGGHSLLVTQVVSRVRRRLDLQVPLRTLFEHSTLRAYAQAVAQ 1094
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
75-300 1.38e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.40  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163   75 ALRLRGELDVEALSASLGAIVERHQSLRTVFvedEQLDGFRQQVLASvDVPVPVTLAGDDDAQAQIRAFVESETQQPFDL 154
Cdd:PRK09294    27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHL---EQDSDGGWELVAD-DLLHPGIVVVDGDAARPLPELQLDQGVSLLAL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  155 RNGPLLrarllrlaaDDHVLTLTIHHVAADGWSMRVLVEELIALYGAR-RQGIEATLPDLPI-QYADYAIWQRhwleaGE 232
Cdd:PRK09294   103 DVVPDD---------GGARVTLYIHHSIADAHHSASLLDELWSRYTDVvTTGDPGPIRPQPApQSLEAVLAQR-----GI 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2183974163  233 RERQLEyWMARLGGGQSVLELP-----TDRQRPALPS-YRGARHELQlpQALGRQLQALAQREGTTLFMLLLAS 300
Cdd:PRK09294   169 RRQALS-GAERFMPAMYAYELPptptaAVLAKPGLPQaVPVTRCRLS--KAQTSSLAAFGRRHRLTVNALVSAA 239
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3111-3165 1.80e-04

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 47.13  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2183974163 3111 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3165
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL 55
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3090-3182 1.99e-04

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 46.94  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:PRK07059    28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                           90
                   ....*....|...
gi 2183974163 3170 PEERQAYMLEDSG 3182
Cdd:PRK07059   108 TPRELEHQLKDSG 120
PLN02736 PLN02736
long-chain acyl-CoA synthetase
618-687 2.79e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 46.63  E-value: 2.79e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  618 LARLPQSDGLQSLLLDDLERLvhGYPAENPDLPEAPDSLCYAIYTSGSTGQPKGVMVRHRaltNFVCSIA 687
Cdd:PLN02736   187 LPSLPSGTGVEIVTYSKLLAQ--GRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG---NLIANVA 251
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3099-3183 3.09e-04

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 46.14  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3099 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3178
Cdd:cd12118     18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97

                   ....*
gi 2183974163 3179 EDSGV 3183
Cdd:cd12118     98 RHSEA 102
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
2204-2422 3.21e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 46.24  E-value: 3.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2204 ALDGTLLETALQALLAHHDALRLgfRLE---DGTWRaehraVEAGEVLLWQQSVADGQALEALAEqvqrsLDLGSGPLLR 2280
Cdd:PRK09294    33 VLDIDALSDAFDALLRAHPVLAA--HLEqdsDGGWE-----LVADDLLHPGIVVVDGDAARPLPE-----LQLDQGVSLL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2281 ALLATLGDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQL----QAGQAVALPAKTSAFKAWAER-LQAHARDGGLEGE 2355
Cdd:PRK09294   101 ALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVvttgDPGPIRPQPAPQSLEAVLAQRgIRRQALSGAERFM 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163 2356 RGYWLAQLEGVSTELPCDDREGAQSVRHVrsaRTELTEEATRRLLQEAPAAyRTQVNDLLLTALARV 2422
Cdd:PRK09294   181 PAMYAYELPPTPTAAVLAKPGLPQAVPVT---RCRLSKAQTSSLAAFGRRH-RLTVNALVSAAILLA 243
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3102-3182 3.56e-04

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 46.21  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3102 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3181
Cdd:cd05959     21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100

                   .
gi 2183974163 3182 G 3182
Cdd:cd05959    101 R 101
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
772-924 3.93e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 46.25  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  772 TLLCGGEALAEDLAARMRGL-SASTWNLYGPTETTiwSARFrlGEEARPF----LGGPLENTALYILDS----EMNPCPP 842
Cdd:PTZ00342   465 VILNGGGKLSPKIAEELSVLlNVNYYQGYGLTETT--GPIF--VQHADDNntesIGGPISPNTKYKVRTwetyKATDTLP 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  843 gvAGELLIGGDGLARGYHRRPGLTAERFLPDPFaadgsrlYRTGDLARYRADGVIEYLGRIDHQVKirgfrIELGE-IET 921
Cdd:PTZ00342   541 --KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY-------FKTGDIVQINKNGSLTFLDRSKGLVK-----LSQGEyIET 606

                   ...
gi 2183974163  922 RLL 924
Cdd:PTZ00342   607 DML 609
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1237-1714 4.05e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 46.40  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1237 TLHHIIADGWSMQVLVDelirvYAALRHDQPPALAELPiQYAdfaaWQRQWMDGGERERQLDYWVSRLGGEQPLLELPsd 1316
Cdd:COG3321    832 QLLTALAQLWVAGVPVD-----WSALYPGRGRRRVPLP-TYP----FQREDAAAALLAAALAAALAAAAALGALLLAA-- 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1317 rPRPQQQSHRGRRIGIPLPAELAEALRRLAQAEQGTLFMLLLASFQALLHRYSGQNDIRVGVPIANRNREETEGLIGFFV 1396
Cdd:COG3321    900 -LAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAA 978
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1397 NTQVLRAELDGQLPFRELLRQVRQAVVEAQGHQDLPFEQLVDALQPERSLSHAPLFQVMYNHQRDDHRGSRFASLGELEV 1476
Cdd:COG3321    979 AAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAA 1058
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1477 EDLAWDVQTAQFDLTLDTYESSNGLLAELTYATDLFDASSAERIAGHWLNLLRSIVARPEARIAELKLLDEAEARADLLQ 1556
Cdd:COG3321   1059 AALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAA 1138
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 1557 WNPGPQDFTPASCLHRLIERQAAERPRATAVVYGERALDYGELNLRANRLAHRLIELGVGPDVLVGLAAERSLEMIVGLL 1636
Cdd:COG3321   1139 ALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAA 1218
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2183974163 1637 AILKAGGAYVPLDPRYPSDRLGYMIEDSGIRLLLTQRAARERLPLGEGLPCLLLDAEHEWAGYPESDPQSAVGVDNLA 1714
Cdd:COG3321   1219 AAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAA 1296
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3096-3180 4.89e-04

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 45.63  E-value: 4.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3096 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3175
Cdd:PRK09029    14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93

                   ....*
gi 2183974163 3176 YMLED 3180
Cdd:PRK09029    94 ELLPS 98
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3090-3182 5.10e-04

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 45.50  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3090 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3169
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                           90
                   ....*....|...
gi 2183974163 3170 PEERQAYMLEDSG 3182
Cdd:PRK06164    95 RSHEVAHILGRGR 107
PRK03584 PRK03584
acetoacetate--CoA ligase;
523-754 6.42e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 45.56  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  523 TPDAPALLF-----GEERLSYAELNALANRLAWRLREEGVGS-DVLVGIalergVP----MVVALLAVLKAGGAYVPLDP 592
Cdd:PRK03584    97 RDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-----LPnipeTVVAMLATASLGAIWSSCSP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  593 QYpadrlqymiddsglrlllSQQSVLARLPQ--------SDG-------------LQSLL--LDDLERLVH-GYPAENPD 648
Cdd:PRK03584   172 DF------------------GVQGVLDRFGQiepkvliaVDGyryggkafdrrakVAELRaaLPSLEHVVVvPYLGPAAA 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163  649 LPEAPDSLCYA------------------------IYTSGSTGQPK-------GVMVRHRALTNFVCSIarQPGmlarDR 697
Cdd:PRK03584   234 AAALPGALLWEdflapaeaaelefepvpfdhplwiLYSSGTTGLPKcivhghgGILLEHLKELGLHCDL--GPG----DR 307
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2183974163  698 LLSVTTFS-----FDIFGlelyvpLARGASMLL-----AsreqAQDPEALLDLVERQGVTVLQATPA 754
Cdd:PRK03584   308 FFWYTTCGwmmwnWLVSG------LLVGATLVLydgspF----YPDPNVLWDLAAEEGVTVFGTSAK 364
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
652-680 1.09e-03

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 44.66  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*....
gi 2183974163  652 APDSLCYAIYTSGSTGQPKGVMVRHRALT 680
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHDNIT 176
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3101-3180 1.65e-03

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 44.01  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3101 APALAFGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3179
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                   .
gi 2183974163 3180 D 3180
Cdd:cd05958     81 K 81
PRK12467 PRK12467
peptide synthase; Provisional
2738-3003 2.90e-03

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 43.61  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2738 AGLGFELAEAPLLRLVlvrtGERRHHLIYTNHHILMDGWSNSQLLGEVLQryrgetpsrsdgrYRDYIAWLQRQDagrte 2817
Cdd:PRK12467  3700 EGLGTVFDYEPLAVIL----EGDRHVLGLTCRHLLDDGWQDTSLQAMAVQ-------------YADYILWQQAKG----- 3757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2818 afwkqrlqrlgeptllvpafAHGVRGAEghadryrqLDVTTSQRLAEFAREQkvtlntlvqaawlillqrftGQDtvafg 2897
Cdd:PRK12467  3758 --------------------PYGLLGWS--------LGGTLARLVAELLERE--------------------GES----- 3784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 2898 atvsgrpaelrgiEEQIGLFINTLPVVASPCPEQPIGDWLQAVQG----ENLALREFEHTPLYDIQRwAGQVGEALFDNI 2973
Cdd:PRK12467  3785 -------------EAFLGLFDNTLPLPDEFVPQAEFLELLRQLGEligrANRLLRGLEEGGVGPDVL-VGIAIQRCFDIA 3850
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2183974163 2974 LVFENYPV--SAALAEETPADMRIDALSNQEQ 3003
Cdd:PRK12467  3851 PLELYTPLldAGELAHIFDVAMRLKLLSLQLQ 3882
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3113-3182 3.73e-03

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 42.95  E-value: 3.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3113 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:cd17634     87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
PRK03584 PRK03584
acetoacetate--CoA ligase;
3091-3154 4.11e-03

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 42.86  E-value: 4.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2183974163 3091 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGIGA-DRLVGVaMERSIEMVVALMA 3154
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLA 158
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3095-3183 4.67e-03

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 42.61  E-value: 4.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3095 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3172
Cdd:cd05904     15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90
                   ....*....|.
gi 2183974163 3173 RQAYMLEDSGV 3183
Cdd:cd05904     95 EIAKQVKDSGA 105
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3113-3182 5.75e-03

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 42.43  E-value: 5.75e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3113 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:PRK06087    52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQ 121
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3074-3182 5.81e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 42.29  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183974163 3074 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVAL 3152
Cdd:PRK05605    22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
                           90       100       110
                   ....*....|....*....|....*....|
gi 2183974163 3153 MAILKAGGAYVPVDPEYPEERQAYMLEDSG 3182
Cdd:PRK05605   100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHG 129
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3113-3183 6.96e-03

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 41.95  E-value: 6.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183974163 3113 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3183
Cdd:cd05912      4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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