|
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
|
|
|