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Conserved domains on  [gi|1573930569|gb|RZE14726|]
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KR domain-containing protein [Streptomyces albidoflavus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 8-2201 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 911.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPD-EMPV 86
Cdd:PRK12467    49 RIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSlTIPL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   87 HRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:PRK12467   129 DDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EEPPPAGFE--SADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRALDE 241
Cdd:PRK12467   209 REPSLPALPiqYAD-YAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELpTDRPRPAVPSYrgARLRVDLPQALSAGLKA 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  242 AAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRG 321
Cdd:PRK12467   288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  322 LRAHQRHRGESI------RRDLGvlgrgrrvHGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPG-------- 387
Cdd:PRK12467   368 AQAHQDLPFEQLvealqpERSLS--------HSPLFQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTAqfdlaldt 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  388 -AEADTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEELpLGETPVLLPGEEP--VRRDEPAPRV--TRTLPQLF 462
Cdd:PRK12467   440 yESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR-LGELPLLDAEERAreLVRWNAPATEyaPDCVHQLI 518

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  463 EARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPA 542
Cdd:PRK12467   519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  543 ERLALVMADAEPVAVVTDTAGSGRLP-ATDARVVVVDDArtVADLAGRAPHDLTDAdragaTGPYDTAYVIHTSGSTGRP 621
Cdd:PRK12467   599 DRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEP--ADLLCGYSGHNPEVA-----LDPDNLAYVIYTSGSTGQP 671

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVL 701
Cdd:PRK12467   672 KGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVL 751

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  702 NQTPSAFEQLvLADAATDRATGsLRYVVLGGEALVAERLRPWadRHGLDAPELVNMYGITETTVHVTFHRLvrADLEDPR 781
Cdd:PRK12467   752 KIVPSHLQAL-LQASRVALPRP-QRALVCGGEALQVDLLARV--RALGPGARLINHYGPTETTVGVSTYEL--SDEERDF 825

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  782 RRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGT 861
Cdd:PRK12467   826 GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGV 905

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  862 LVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVaGGAVVPRAAEDGLTQLVAYAVPAE-----EGGADPAGLRAHLAARL 936
Cdd:PRK12467   906 IEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV-REAVVLAQPGDAGLQLVAYLVPAAvadgaEHQATRDELKAQLRQVL 984

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  937 PAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSL 1015
Cdd:PRK12467   985 PDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTElEKRLAAIWADVLKV--ERVGLTDNFFELGGHSL 1062

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1016 LATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADAGrpLPALTASERPSLVPASFAQERMWFLSRMDGAAATYN 1095
Cdd:PRK12467  1063 LATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGA--QPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYH 1140

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1096 IPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTL---RPELHVVDCPDEERAAHVAAAMRRSF 1172
Cdd:PRK12467  1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLtleEPLLLAADKDEAQLKVYVEAEARQPF 1220

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1173 DLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApap 1251
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEhVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMD--- 1297

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1252 egPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNR 1331
Cdd:PRK12467  1298 --AGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHR 1375

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1332 WGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPA 1411
Cdd:PRK12467  1376 YSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLS 1455

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1412 RHPLFQVMLALQNN-ERAVLTLGEDRVPLRPAATGTAKFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGA 1490
Cdd:PRK12467  1456 HSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQASLTYATDLFEASTIERLAGH 1529

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1491 LRDLLTVVCADPEVRTGALPRADrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragAADRTEQ 1570
Cdd:PRK12467  1530 WLNLLQGLVADPERRLGELDLLD--------------------------------------------------EAERRQI 1559

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1571 VVSSLAPGTRVVAISGLPRTAEggldegalkdlpviDQVaagawrerlarlpgvreaevvleevpeelerrhvgrpraag 1650
Cdd:PRK12467  1560 LEGWNATHTGYPLARLVHQLIE--------------DQA----------------------------------------- 1584

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1651 gAAEPDAPSVerpasvpalsegpalpepsVSGwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRG 1730
Cdd:PRK12467  1585 -AATPEAVAL-------------------VFG------------------------EQELTYGELNRRANRLAHRLIALG 1620

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1731 LRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVP-----VSYATTSAAVSKLEGIWEMLDRpwiVTSAAGEPGLrEL 1805
Cdd:PRK12467  1621 VGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEyprerLAYMIEDSGIELLLTQSHLQAR---LPLPDGLRSL-VL 1696

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1806 AARREWSGLRLTTADALREEpedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWI 1885
Cdd:PRK12467  1697 DQEDDWLEGYSDSNPAVNLA----------PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFT 1766

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1886 PLDHVTGVVMFhLRDVYLGCRQIHAPtSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfqDRDWDLSPVRLVM 1965
Cdd:PRK12467  1767 SFAFDVSVWEL-FWPLINGARLVIAP-PGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD----EQVEHPLSLRRVV 1840

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1966 NAGEVVVASAARRFLHVLAPFGLpqdvmHPGWGMSETCSVVTDSvLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLP 2045
Cdd:PRK12467  1841 CGGEALEVEALRPWLERLPDTGL-----FNLYGPTETAVDVTHW-TCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVP 1914

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2046 EGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEA 2117
Cdd:PRK12467  1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEA 1994

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2118 CVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAP----GQDPAGALREIAGKVTREIgvSPAFLIP---VEAEAIPK 2190
Cdd:PRK12467  1995 RLREQGGV----REAVVIAQDGANGKQLVAYVVPTDPglvdDDEAQVALRAILKNHLKAS--LPEYMVPahlVFLARMPL 2068

                         2250
                   ....*....|.
gi 1573930569 2191 TEIGKIQRTKL 2201
Cdd:PRK12467  2069 TPNGKLDRKAL 2079
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 2301-2705 1.87e-40

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd08953:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 436  Bit Score: 157.14  E-value: 1.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2301 RPGEAGDLAAVLERLEADGRTPDTVvhlAATEDA---EDGAAPGSDVSLLV-LAQALAGRTGGERPVdLLFVTAGAQAVT 2376
Cdd:cd08953     41 APAALASAFLALAYEAALLGLAAAE---AALLDAlsaLDPAAALQLLESLQrLLKAGLLAARASGRA-LLQVVTGLPGAL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2377 PEERPTASHAAAGALLKSLREELPWLRGVHLDLSGGSAG-DRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAPR 2455
Cdd:cd08953    117 GLDALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASaEALARELAAELAAPGAAEVRYRDGLRYVQTLEPLPLPAGA 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2456 TAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERhladagpassriEAFRRLRGLG-EVRY 2534
Cdd:cd08953    197 AASAPLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKA------------QTLAALEALGaRVLY 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2535 ETADVTDAAQVRAAVRRAADAWGvPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSS 2614
Cdd:cd08953    265 ISADVTDAAAVRRLLEKVRERYG-AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSS 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2615 VNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLA--WSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLAR 2692
Cdd:cd08953    344 VSAFFGGAGQADYAAANAFLDAFAAYLRQRGPQGRVLSinWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALEQAL 423

                          410
                   ....*....|...
gi 1573930569 2693 TLDLPHLLIGADR 2705
Cdd:cd08953    424 SSDLPQVLVSPGD 436
PRK12467 super family cl36129
peptide synthase; Provisional
 2776-2839 1.38e-11

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 70.96  E-value: 1.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALA 2839
Cdd:PRK12467  3606 VEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 8-2201 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 911.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPD-EMPV 86
Cdd:PRK12467    49 RIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSlTIPL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   87 HRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:PRK12467   129 DDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EEPPPAGFE--SADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRALDE 241
Cdd:PRK12467   209 REPSLPALPiqYAD-YAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELpTDRPRPAVPSYrgARLRVDLPQALSAGLKA 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  242 AAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRG 321
Cdd:PRK12467   288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  322 LRAHQRHRGESI------RRDLGvlgrgrrvHGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPG-------- 387
Cdd:PRK12467   368 AQAHQDLPFEQLvealqpERSLS--------HSPLFQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTAqfdlaldt 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  388 -AEADTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEELpLGETPVLLPGEEP--VRRDEPAPRV--TRTLPQLF 462
Cdd:PRK12467   440 yESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR-LGELPLLDAEERAreLVRWNAPATEyaPDCVHQLI 518

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  463 EARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPA 542
Cdd:PRK12467   519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  543 ERLALVMADAEPVAVVTDTAGSGRLP-ATDARVVVVDDArtVADLAGRAPHDLTDAdragaTGPYDTAYVIHTSGSTGRP 621
Cdd:PRK12467   599 DRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEP--ADLLCGYSGHNPEVA-----LDPDNLAYVIYTSGSTGQP 671

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVL 701
Cdd:PRK12467   672 KGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVL 751

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  702 NQTPSAFEQLvLADAATDRATGsLRYVVLGGEALVAERLRPWadRHGLDAPELVNMYGITETTVHVTFHRLvrADLEDPR 781
Cdd:PRK12467   752 KIVPSHLQAL-LQASRVALPRP-QRALVCGGEALQVDLLARV--RALGPGARLINHYGPTETTVGVSTYEL--SDEERDF 825

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  782 RRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGT 861
Cdd:PRK12467   826 GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGV 905

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  862 LVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVaGGAVVPRAAEDGLTQLVAYAVPAE-----EGGADPAGLRAHLAARL 936
Cdd:PRK12467   906 IEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV-REAVVLAQPGDAGLQLVAYLVPAAvadgaEHQATRDELKAQLRQVL 984

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  937 PAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSL 1015
Cdd:PRK12467   985 PDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTElEKRLAAIWADVLKV--ERVGLTDNFFELGGHSL 1062

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1016 LATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADAGrpLPALTASERPSLVPASFAQERMWFLSRMDGAAATYN 1095
Cdd:PRK12467  1063 LATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGA--QPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYH 1140

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1096 IPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTL---RPELHVVDCPDEERAAHVAAAMRRSF 1172
Cdd:PRK12467  1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLtleEPLLLAADKDEAQLKVYVEAEARQPF 1220

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1173 DLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApap 1251
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEhVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMD--- 1297

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1252 egPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNR 1331
Cdd:PRK12467  1298 --AGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHR 1375

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1332 WGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPA 1411
Cdd:PRK12467  1376 YSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLS 1455

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1412 RHPLFQVMLALQNN-ERAVLTLGEDRVPLRPAATGTAKFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGA 1490
Cdd:PRK12467  1456 HSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQASLTYATDLFEASTIERLAGH 1529

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1491 LRDLLTVVCADPEVRTGALPRADrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragAADRTEQ 1570
Cdd:PRK12467  1530 WLNLLQGLVADPERRLGELDLLD--------------------------------------------------EAERRQI 1559

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1571 VVSSLAPGTRVVAISGLPRTAEggldegalkdlpviDQVaagawrerlarlpgvreaevvleevpeelerrhvgrpraag 1650
Cdd:PRK12467  1560 LEGWNATHTGYPLARLVHQLIE--------------DQA----------------------------------------- 1584

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1651 gAAEPDAPSVerpasvpalsegpalpepsVSGwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRG 1730
Cdd:PRK12467  1585 -AATPEAVAL-------------------VFG------------------------EQELTYGELNRRANRLAHRLIALG 1620

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1731 LRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVP-----VSYATTSAAVSKLEGIWEMLDRpwiVTSAAGEPGLrEL 1805
Cdd:PRK12467  1621 VGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEyprerLAYMIEDSGIELLLTQSHLQAR---LPLPDGLRSL-VL 1696

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1806 AARREWSGLRLTTADALREEpedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWI 1885
Cdd:PRK12467  1697 DQEDDWLEGYSDSNPAVNLA----------PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFT 1766

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1886 PLDHVTGVVMFhLRDVYLGCRQIHAPtSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfqDRDWDLSPVRLVM 1965
Cdd:PRK12467  1767 SFAFDVSVWEL-FWPLINGARLVIAP-PGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD----EQVEHPLSLRRVV 1840

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1966 NAGEVVVASAARRFLHVLAPFGLpqdvmHPGWGMSETCSVVTDSvLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLP 2045
Cdd:PRK12467  1841 CGGEALEVEALRPWLERLPDTGL-----FNLYGPTETAVDVTHW-TCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVP 1914

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2046 EGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEA 2117
Cdd:PRK12467  1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEA 1994

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2118 CVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAP----GQDPAGALREIAGKVTREIgvSPAFLIP---VEAEAIPK 2190
Cdd:PRK12467  1995 RLREQGGV----REAVVIAQDGANGKQLVAYVVPTDPglvdDDEAQVALRAILKNHLKAS--LPEYMVPahlVFLARMPL 2068

                         2250
                   ....*....|.
gi 1573930569 2191 TEIGKIQRTKL 2201
Cdd:PRK12467  2069 TPNGKLDRKAL 2079
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 5-1327 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: 798.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    5 EDDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDG-DPDE 83
Cdd:COG1020     14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPvVAAP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   84 MPVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTAL 163
Cdd:COG1020     94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  164 AAGEE-PPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRAL 239
Cdd:COG1020    174 YAGAPlPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELpTDRPRPAVQSYrgARVSFRLPAELTAAL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  240 DEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDL 319
Cdd:COG1020    254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  320 RGLRAHQRHRGESIRRDLGVLGRGRrvHGPVVNIV-----PFSEDLTFGGHPSTSHHL-SGGAVDDLQISVRPgaEADTL 393
Cdd:COG1020    334 LAAYAHQDLPFERLVEELQPERDLS--RNPLFQVMfvlqnAPADELELPGLTLEPLELdSGTAKFDLTLTVVE--TGDGL 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  394 WLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEeLPLGETPVLLPGE-----EPVRRDEPAPRVTRTLPQLFEARVAE 468
Cdd:COG1020    410 RLTLEYNTDLFDAATIERMAGHLVTLLEALAADPD-QPLGDLPLLTAAErqqllAEWNATAAPYPADATLHELFEAQAAR 488

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  469 SPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:COG1020    489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTDTAGSGRLPATDARVVVVDDArtvadlagrAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPH 628
Cdd:COG1020    569 LEDAGARLVLTQSALAARLPELGVPVLALDAL---------ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  629 AHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAF 708
Cdd:COG1020    640 RALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLL 719

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  709 EQLVLADAATDRatgSLRYVVLGGEALVAERLRPWADRHGldAPELVNMYGITETTVHVTFHRLVRADLEDprRRGVIGR 788
Cdd:COG1020    720 RALLDAAPEALP---SLRLVLVGGEALPPELVRRWRARLP--GARLVNLYGPTETTVDSTYYEVTPPDADG--GSVPIGR 792

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:COG1020    793 PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA 872

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLL 948
Cdd:COG1020    873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLL 952

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  949 DALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERLVcgLFEEVLRLPADSVGTGGNFFDLGGHSLLATRLLARLRERT 1028
Cdd:COG1020    953 LPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEE--AALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1029 GTDVPISALFDTPTPAALAERLTAGADAGRPLPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDL 1108
Cdd:COG1020   1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1109 DALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELHVVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTG 1188
Cdd:COG1020   1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1189 DTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLAPAPEGPGRLERLTSFWRQAL 1268
Cdd:COG1020   1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270

                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 1269 DGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALAL 1327
Cdd:COG1020   1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1673-2208 0e+00

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: 732.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1673 PALPEPSVSGWAEALLRAAGR--PDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVAT 1750
Cdd:cd05906      1 PLHRPEGAPRTLLELLLRAAErgPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1751 LWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRD 1830
Cdd:cd05906     81 FWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1831 WYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHA 1910
Cdd:cd05906    161 LPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 PTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQ 1990
Cdd:cd05906    241 PTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1991 DVMHPGWGMSETCSVVTDSVlASEAPDHDEA--FVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNAR 2068
Cdd:cd05906    321 DAIRPAFGMTETCSGVIYSR-SFPTYDHSQAleFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2069 ANAESFTEDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAVRsDASAATDELAL 2148
Cdd:cd05906    400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVR-DPGAETEELAI 478

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2149 FlrLAPGQDPAGAL----REIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAG 2208
Cdd:cd05906    479 F--FVPEYDLQDALsetlRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 483-899 1.21e-150

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: 474.45  E-value: 1.21e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDT 561
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 AGSGRLPATDARVVVVDDARTVADLAGRAPhdltdADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEH 641
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAP-----PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFL-RLLDEEKVTVLNQTPSAFEQLVLADaatDR 720
Cdd:TIGR01733  156 YGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAAL---PP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  721 ATGSLRYVVLGGEALVAERLRPWADRHGldAPELVNMYGITETTVHVTFHRLVRADLEDPRRRGvIGRPLADLRVYVLDA 800
Cdd:TIGR01733  233 ALASLRLVILGGEALTPALVDRWRARGP--GARLINLYGPTETTVWSTATLVDPDDAPRESPVP-IGRPLANTRLYVLDD 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  801 AGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPF-GAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRI 879
Cdd:TIGR01733  310 DLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389

                          410       420
                   ....*....|....*....|
gi 1573930569  880 EPGEIEAVLTAHPAVAGGAV 899
Cdd:TIGR01733  390 ELGEIEAALLRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
462-875 7.29e-113

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 366.25  E-value: 7.29e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARVAESPGRTAVS-YAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGH 540
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  541 PAERLALVMADAEPVAVVTDTAGS--------GRLPATDARVVV-VDDARTVADLAGRAPHDLTDADRAGATGPYDTAYV 611
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVLdRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  612 IHTSGSTGRPKGVPVPHAHVVR----LFEASGEHFRFGADDVWTLFHSYAFDFSV-WELWGPLLHGGRLVVVPYEVSRSP 686
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVH 766
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 VTFHRLvraDLEDPRRRGVIGRPLADLRVYVLDAA-GRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgt 845
Cdd:pfam00501  318 VTTPLP---LDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------- 387

                          410       420       430
                   ....*....|....*....|....*....|
gi 1573930569  846 RMYRSGDLARWRPDGTLVHAGRADQQVKIR 875
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 2301-2705 1.87e-40

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 157.14  E-value: 1.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2301 RPGEAGDLAAVLERLEADGRTPDTVvhlAATEDA---EDGAAPGSDVSLLV-LAQALAGRTGGERPVdLLFVTAGAQAVT 2376
Cdd:cd08953     41 APAALASAFLALAYEAALLGLAAAE---AALLDAlsaLDPAAALQLLESLQrLLKAGLLAARASGRA-LLQVVTGLPGAL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2377 PEERPTASHAAAGALLKSLREELPWLRGVHLDLSGGSAG-DRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAPR 2455
Cdd:cd08953    117 GLDALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASaEALARELAAELAAPGAAEVRYRDGLRYVQTLEPLPLPAGA 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2456 TAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERhladagpassriEAFRRLRGLG-EVRY 2534
Cdd:cd08953    197 AASAPLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKA------------QTLAALEALGaRVLY 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2535 ETADVTDAAQVRAAVRRAADAWGvPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSS 2614
Cdd:cd08953    265 ISADVTDAAAVRRLLEKVRERYG-AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSS 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2615 VNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLA--WSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLAR 2692
Cdd:cd08953    344 VSAFFGGAGQADYAAANAFLDAFAAYLRQRGPQGRVLSinWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALEQAL 423

                          410
                   ....*....|...
gi 1573930569 2693 TLDLPHLLIGADR 2705
Cdd:cd08953    424 SSDLPQVLVSPGD 436
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 2479-2658 5.10e-25

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 104.49  E-value: 5.10e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  2479 EVAAHLLKEPGTRLLLIGRTGLPPEDTWErhladagpassrieAFRRLRGLG-EVRYETADVTDAAQVRAAVRRAADAWG 2557
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAA--------------LLAELEAAGaRVTVVACDVADRDALAAVLAAIPAVEG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  2558 vPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDL 2637
Cdd:smart00822   81 -PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDAL 159

                           170       180
                    ....*....|....*....|.
gi 1573930569  2638 ALRRRREGLPGQSLAWSMWRE 2658
Cdd:smart00822  160 AEYRRARGLPALSIAWGAWAE 180
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 2479-2658 1.39e-18

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 85.69  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2479 EVAAHLLKEPGTRLLLIGRTGLPPEDtwerhladagpASSRIeafRRLRGLG-EVRYETADVTDAAQVRAAVRRAADAwG 2557
Cdd:pfam08659   15 ELARWLAERGARHLVLLSRSAAPRPD-----------AQALI---AELEARGvEVVVVACDVSDPDAVAALLAEIKAE-G 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2558 VPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDL 2637
Cdd:pfam08659   80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                          170       180
                   ....*....|....*....|.
gi 1573930569 2638 ALRRRREGLPGQSLAWSMWRE 2658
Cdd:pfam08659  160 AEYRRSQGLPATSINWGPWAE 180
PRK12467 PRK12467
peptide synthase; Provisional
 2776-2839 1.38e-11

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 70.96  E-value: 1.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALA 2839
Cdd:PRK12467  3606 VEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2776-2845 3.62e-11

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: 61.41  E-value: 3.62e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2776 LESELAAVWCTVLG--RDRVGRDENFF-DLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:COG0236      6 LEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2778-2837 3.38e-10

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: 57.96  E-value: 3.38e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2778 SELAAVWCTVLGRD--RVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRA 2837
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2770-2845 2.24e-08

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: 53.41  E-value: 2.24e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569  2770 ADELRRLESELAAVWCTVLGR---DRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:smart00823    7 AERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 2249-2810 2.53e-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: 50.26  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2249 AGHRVLVLAGPAPHAHAVAEEVAGAVRDAGGLCTVVTEGPAPER---------------------NGAAAYRV------- 2300
Cdd:COG3321    789 DGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQlltalaqlwvagvpvdwsalyPGRGRRRVplptypf 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2301 -RPGEAGDLAAVLERLEADGRTPDTVVHLAATEDAEDGAAPGSDVSLLVLAQALAGRTGGERPVDLLFVTAGAQAVTPEE 2379
Cdd:COG3321    869 qREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2380 RPTASHAAAGALLKSLREELPWLRGVHLD-------LSGGSAGDRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDS 2452
Cdd:COG3321    949 AAAAAAALAAAEAGALLLLAAAAAAAAAAaaaaaaaAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALL 1028

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2453 APRTAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERHLADAGPASSRIEAFRRLRGLGEV 2532
Cdd:COG3321   1029 AAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLL 1108

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2533 RYETADVTDAAQVRAAVRRAADAWGVPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTF 2612
Cdd:COG3321   1109 LALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAA 1188

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2613 SSVNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLAWSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLAR 2692
Cdd:COG3321   1189 LAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAA 1268

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2693 TLDLPHLLIGADRTAPWVRSHVLAPVRQVRRTAARVVLDEGTDLGALYGAAARAAGPEGTFVLRSAGSSGRSEDTGGADE 2772
Cdd:COG3321   1269 AGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAA 1348

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1573930569 2773 LRRLESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLV 2810
Cdd:COG3321   1349 AAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2757-2844 9.30e-05

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: 48.52  E-value: 9.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2757 SAGSSGRSEDTGGAdELRRLESELAAVWCTVLGR--DRVGRDENFFDLGGNSLLLVAAQTAVNKALGCE--LGVVdlFSR 2832
Cdd:TIGR03443  831 AAVAKNRSASAADE-EFTETEREIRDLWLELLPNrpATISPDDSFFDLGGHSILATRMIFELRKKLNVElpLGLI--FKS 907

                           90
                   ....*....|..
gi 1573930569 2833 PTVRALARHLSQ 2844
Cdd:TIGR03443  908 PTIKGFAKEVDR 919
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 983-1052 1.80e-03

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: 39.54  E-value: 1.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569   983 ERLVCGLFEEVLRL-PADSVGTGGNFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAERLTA 1052
Cdd:smart00823   14 LDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 8-2201 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 911.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPD-EMPV 86
Cdd:PRK12467    49 RIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSlTIPL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   87 HRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:PRK12467   129 DDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EEPPPAGFE--SADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRALDE 241
Cdd:PRK12467   209 REPSLPALPiqYAD-YAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELpTDRPRPAVPSYrgARLRVDLPQALSAGLKA 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  242 AAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRG 321
Cdd:PRK12467   288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  322 LRAHQRHRGESI------RRDLGvlgrgrrvHGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPG-------- 387
Cdd:PRK12467   368 AQAHQDLPFEQLvealqpERSLS--------HSPLFQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTAqfdlaldt 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  388 -AEADTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEELpLGETPVLLPGEEP--VRRDEPAPRV--TRTLPQLF 462
Cdd:PRK12467   440 yESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR-LGELPLLDAEERAreLVRWNAPATEyaPDCVHQLI 518

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  463 EARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPA 542
Cdd:PRK12467   519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  543 ERLALVMADAEPVAVVTDTAGSGRLP-ATDARVVVVDDArtVADLAGRAPHDLTDAdragaTGPYDTAYVIHTSGSTGRP 621
Cdd:PRK12467   599 DRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEP--ADLLCGYSGHNPEVA-----LDPDNLAYVIYTSGSTGQP 671

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVL 701
Cdd:PRK12467   672 KGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVL 751

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  702 NQTPSAFEQLvLADAATDRATGsLRYVVLGGEALVAERLRPWadRHGLDAPELVNMYGITETTVHVTFHRLvrADLEDPR 781
Cdd:PRK12467   752 KIVPSHLQAL-LQASRVALPRP-QRALVCGGEALQVDLLARV--RALGPGARLINHYGPTETTVGVSTYEL--SDEERDF 825

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  782 RRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGT 861
Cdd:PRK12467   826 GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGV 905

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  862 LVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVaGGAVVPRAAEDGLTQLVAYAVPAE-----EGGADPAGLRAHLAARL 936
Cdd:PRK12467   906 IEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV-REAVVLAQPGDAGLQLVAYLVPAAvadgaEHQATRDELKAQLRQVL 984

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  937 PAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSL 1015
Cdd:PRK12467   985 PDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTElEKRLAAIWADVLKV--ERVGLTDNFFELGGHSL 1062

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1016 LATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADAGrpLPALTASERPSLVPASFAQERMWFLSRMDGAAATYN 1095
Cdd:PRK12467  1063 LATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGA--QPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYH 1140

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1096 IPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTL---RPELHVVDCPDEERAAHVAAAMRRSF 1172
Cdd:PRK12467  1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLtleEPLLLAADKDEAQLKVYVEAEARQPF 1220

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1173 DLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApap 1251
Cdd:PRK12467  1221 DLEQGPLLRVGLLRLAADEhVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMD--- 1297

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1252 egPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNR 1331
Cdd:PRK12467  1298 --AGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHR 1375

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1332 WGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPA 1411
Cdd:PRK12467  1376 YSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLS 1455

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1412 RHPLFQVMLALQNN-ERAVLTLGEDRVPLRPAATGTAKFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGA 1490
Cdd:PRK12467  1456 HSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYE------SSEGLQASLTYATDLFEASTIERLAGH 1529

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1491 LRDLLTVVCADPEVRTGALPRADrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragAADRTEQ 1570
Cdd:PRK12467  1530 WLNLLQGLVADPERRLGELDLLD--------------------------------------------------EAERRQI 1559

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1571 VVSSLAPGTRVVAISGLPRTAEggldegalkdlpviDQVaagawrerlarlpgvreaevvleevpeelerrhvgrpraag 1650
Cdd:PRK12467  1560 LEGWNATHTGYPLARLVHQLIE--------------DQA----------------------------------------- 1584

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1651 gAAEPDAPSVerpasvpalsegpalpepsVSGwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRG 1730
Cdd:PRK12467  1585 -AATPEAVAL-------------------VFG------------------------EQELTYGELNRRANRLAHRLIALG 1620

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1731 LRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVP-----VSYATTSAAVSKLEGIWEMLDRpwiVTSAAGEPGLrEL 1805
Cdd:PRK12467  1621 VGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEyprerLAYMIEDSGIELLLTQSHLQAR---LPLPDGLRSL-VL 1696

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1806 AARREWSGLRLTTADALREEpedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWI 1885
Cdd:PRK12467  1697 DQEDDWLEGYSDSNPAVNLA----------PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFT 1766

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1886 PLDHVTGVVMFhLRDVYLGCRQIHAPtSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfqDRDWDLSPVRLVM 1965
Cdd:PRK12467  1767 SFAFDVSVWEL-FWPLINGARLVIAP-PGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD----EQVEHPLSLRRVV 1840

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1966 NAGEVVVASAARRFLHVLAPFGLpqdvmHPGWGMSETCSVVTDSvLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLP 2045
Cdd:PRK12467  1841 CGGEALEVEALRPWLERLPDTGL-----FNLYGPTETAVDVTHW-TCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVP 1914

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2046 EGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEA 2117
Cdd:PRK12467  1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEA 1994

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2118 CVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAP----GQDPAGALREIAGKVTREIgvSPAFLIP---VEAEAIPK 2190
Cdd:PRK12467  1995 RLREQGGV----REAVVIAQDGANGKQLVAYVVPTDPglvdDDEAQVALRAILKNHLKAS--LPEYMVPahlVFLARMPL 2068

                         2250
                   ....*....|.
gi 1573930569 2191 TEIGKIQRTKL 2201
Cdd:PRK12467  2069 TPNGKLDRKAL 2079
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6-1122 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 854.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    6 DDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPDEMP 85
Cdd:PRK10252     5 SQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   86 VHRVDVSGEADPAAAAEEWIRRDLATPVDVAAG-PLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALA 164
Cdd:PRK10252    85 PEIIDLRTQPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  165 AGEEPPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLTDRTAPPRAP---FLRRTAVLSPAETRALDE 241
Cdd:PRK10252   165 RGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSAsadILRLKLEFTDGAFRQLAA 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  242 AAKGmgVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRG 321
Cdd:PRK10252   245 QASG--VQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKK 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  322 LRAHQRHRGESIRRDLGVLGRGRRVHGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPGaEADTLWLAFDAHP 401
Cdd:PRK10252   323 MRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPD-EHGGLSIEILANP 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  402 DLYEEDGLALFLERFLKVLRELRTCPeELPLGETPVLLPGE-EPVRR----DEPAPRVtrTLPQLFEARVAESPGRTAVS 476
Cdd:PRK10252   402 QRYDEATLIAHAERLKALIAQFAADP-ALLCGDVDILLPGEyAQLAQvnatAVEIPET--TLSALVAQQAAKTPDAPALA 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  477 YAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVA 556
Cdd:PRK10252   479 DARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  557 VVTDTAGSGRLPatdarvvvvdDARTVADLAGRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFE 636
Cdd:PRK10252   559 LITTADQLPRFA----------DVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  637 ASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLV--LA 714
Cdd:PRK10252   629 WMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVasLT 708

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  715 DAATDRATGSLRYVVLGGEALVAERLRPWadrHGLDAPELVNMYGITETTVHVTFHRLVRADLEDPRRRGV-IGRPLADL 793
Cdd:PRK10252   709 PEGARQSCASLRQVFCSGEALPADLCREW---QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVpIGYPVWNT 785

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  794 RVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRPDGTLVHAGRADQQVK 873
Cdd:PRK10252   786 GLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLK 864

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  874 IRGFRIEPGEIEAVLTAHPAVAGGAVVPR------AAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVL 947
Cdd:PRK10252   865 IRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQ 944

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  948 LDALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERLVCGLFEEVLRLPAdsVGTGGNFFDLGGHSLLATRLLARLRER 1027
Cdd:PRK10252   945 LDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDV--VDADADFFALGGHSLLAMKLAAQLSRQ 1022

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1028 TGTDVPISALFDTPTPAALAERLTAGADAGR-----PLPALTASERPSLV---PAS-FAQERMWFLSRMDGAAATYNIPL 1098
Cdd:PRK10252  1023 FARQVTPGQVMVASTVAKLATLLDAEEDESRrlgfgTILPLREGDGPTLFcfhPASgFAWQFSVLSRYLDPQWSIYGIQS 1102

                         1130      1140
                   ....*....|....*....|....
gi 1573930569 1099 PvALRHPLdldALRAALGDVADRH 1122
Cdd:PRK10252  1103 P-RPDGPM---QTATSLDEVCEAH 1122
PRK12316 PRK12316
peptide synthase; Provisional
 6-2203 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 818.43  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    6 DDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGpVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPD-EM 84
Cdd:PRK12316  1554 ADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQvEL 1632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   85 PVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSyklvARRLADTYTALA 164
Cdd:PRK12316  1633 PFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWS----NAQLLGEVLQRY 1708

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  165 AGEEPPPAGFESADRLAaeeaaYLGSDRHRRDRAYWTERLAGLPEPVRLTD--RTAPPRAPFLRRTAVLSPAETRALDEA 242
Cdd:PRK12316  1709 AGQPVAAPGGRYRDYIA-----WLQRQDAAASEAFWKEQLAALEEPTRLAQaaRTEDGQVGYGDHQQLLDPAQTRALAEF 1783

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  243 AKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRlgSAALrtPGTASDI------LPLRVAASADTPVGGFVRAVA 316
Cdd:PRK12316  1784 ARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGR--PAEL--PGIEQQIglfintLPVIAAPRPDQSVADWLQEVQ 1859

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  317 DDLRGLRAHQRHRGESIRRDLGVLGRGRRVHGPVVNIVPFSE--------DLTFG---GHPSTSHHLSggavddLQISVr 385
Cdd:PRK12316  1860 ALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEalkqgapaGLVFGrvsNHEQTNYPLT------LAVTL- 1932

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  386 pgAEADTLWLAFD-AHPDLYEEDGLALFLERFLKVLRElrtcPEELPLGETPVLLPGEEPV------RRDEPAPRVTRtL 458
Cdd:PRK12316  1933 --GETLSLQYSYDrGHFDAAAIERLDRHLLHLLEQMAE----DAQAALGELALLDAGERQRiladwdRTPEAYPRGPG-V 2005

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDP 538
Cdd:PRK12316  2006 HQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  539 GHPAERLALVMADAEPVAVVTDTAGSGRLP-ATDARVVVVDDARTVADLAGRAPhdltdadrAGATGPYDTAYVIHTSGS 617
Cdd:PRK12316  2086 NYPAERLAYMLEDSGAALLLTQRHLLERLPlPAGVARLPLDRDAEWADYPDTAP--------AVQLAGENLAYVIYTSGS 2157

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  618 TGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVsRSPREFLRLLDEEK 697
Cdd:PRK12316  2158 TGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMERHG 2236

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  698 VTVLNQTPSAFEQLVlADAATDRATGSLRYVVLGGEALVAERLRPWADrhGLDAPELVNMYGITETTVHVTFHRLVRADL 777
Cdd:PRK12316  2237 VTILDFPPVYLQQLA-EHAERDGRPPAVRVYCFGGEAVPAASLRLAWE--ALRPVYLFNGYGPTEAVVTPLLWKCRPQDP 2313

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  778 EDPRRrGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWR 857
Cdd:PRK12316  2314 CGAAY-VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYR 2392

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  858 PDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPAGLRAHLAARLP 937
Cdd:PRK12316  2393 ADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVPDDAAEDLLAELRAWLAARLP 2471

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  938 AYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSLL 1016
Cdd:PRK12316  2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGlEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLL 2549

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1017 ATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADAgrPLPALTASERPSLVPASFAQERMWFLSRMDGAAATYNI 1096
Cdd:PRK12316  2550 ATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS--RAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHL 2627

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1097 PLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPEL-HVVDCPDEERAAHVAAAMRRSFDLT 1175
Cdd:PRK12316  2628 PSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLeDCAGVADAAIRQRVAEEIQRPFDLA 2707

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1176 RDSALWAGVFG-TGDTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApapegP 1254
Cdd:PRK12316  2708 RGPLLRVRLLAlDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMD-----S 2782

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1255 GRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGA 1334
Cdd:PRK12316  2783 GEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSG 2862

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1335 GDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPARHP 1414
Cdd:PRK12316  2863 QSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSP 2942

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1415 LFQVMLALQNNERAVLTLGEDRVPLRPAATGTAKFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDL 1494
Cdd:PRK12316  2943 LFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWE------SAEGLGASLTYATDLFDARTVERLARHWQNL 3016

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1495 LTVVCADPEVRTGALPRADRPSPatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragaadrteqvvss 1574
Cdd:PRK12316  3017 LRGMVENPQRSVDELAMLDAEER--------------------------------------------------------- 3039

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1575 lapgtrvvaisglprtaeggldegalkdlpvidQVAAGAWRERLARLPgvreaevvleevpeelERRHVGRPRAAGGAAE 1654
Cdd:PRK12316  3040 ---------------------------------GQLLEAWNATAAEYP----------------LERGVHRLFEEQVERT 3070

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1655 PDApsverpasvPALSEGpalpepsvsgwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPG 1734
Cdd:PRK12316  3071 PDA---------VALAFG----------------------------------EQRLSYAELNRRANRLAHRLIERGVGPD 3107

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1735 DRVILQCDDTEDFVATLWGCVLGGFVAVPLTvPVSYATTSAAVSKLEGIWEMLDRPWIvtSAAGEPGLRELAARREWSGL 1814
Cdd:PRK12316  3108 VLVGVAVERSLEMVVGLLAILKAGGAYVPLD-PEYPEERLAYMLEDSGAQLLLSQSHL--RLPLAQGVQVLDLDRGDENY 3184

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1815 RLTTADALreepedrdwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVV 1894
Cdd:PRK12316  3185 AEANPAIR-----------TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE 3253

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1895 MFHLRDVYLGCRQIHAPTSWilEDPVRWPELADRHRVSVTWA-PNFAFGLLAEQAHRfqdrdwDLSPVRLVMNAGEVVVA 1973
Cdd:PRK12316  3254 ELFWPLMSGARVVLAGPEDW--RDPALLVELINSEGVDVLHAyPSMLQAFLEEEDAH------RCTSLKRIVCGGEALPA 3325

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1974 SAARRFLHVLAPFGLpqdvmhpgWGMSETcsvvTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQ 2053
Cdd:PRK12316  3326 DLQQQVFAGLPLYNL--------YGPTEA----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELY 3393

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2054 VRGTSVTHGYHDNARANAESFTEDGW------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV 2126
Cdd:PRK12316  3394 LGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVR 3473

                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 RSFTAAVAVRSDASAATDElalflrlapgqDPAGALREIAGKVTREigVSPAFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK12316  3474 EAVVLAVDGRQLVAYVVPE-----------DEAGDLREALKAHLKA--SLPEYMVPahlLFLERMPLTPNGKLDRKALPR 3540
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 5-1327 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: 798.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    5 EDDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDG-DPDE 83
Cdd:COG1020     14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPvVAAP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   84 MPVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTAL 163
Cdd:COG1020     94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  164 AAGEE-PPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRAL 239
Cdd:COG1020    174 YAGAPlPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELpTDRPRPAVQSYrgARVSFRLPAELTAAL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  240 DEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDL 319
Cdd:COG1020    254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  320 RGLRAHQRHRGESIRRDLGVLGRGRrvHGPVVNIV-----PFSEDLTFGGHPSTSHHL-SGGAVDDLQISVRPgaEADTL 393
Cdd:COG1020    334 LAAYAHQDLPFERLVEELQPERDLS--RNPLFQVMfvlqnAPADELELPGLTLEPLELdSGTAKFDLTLTVVE--TGDGL 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  394 WLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEeLPLGETPVLLPGE-----EPVRRDEPAPRVTRTLPQLFEARVAE 468
Cdd:COG1020    410 RLTLEYNTDLFDAATIERMAGHLVTLLEALAADPD-QPLGDLPLLTAAErqqllAEWNATAAPYPADATLHELFEAQAAR 488

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  469 SPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:COG1020    489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTDTAGSGRLPATDARVVVVDDArtvadlagrAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPH 628
Cdd:COG1020    569 LEDAGARLVLTQSALAARLPELGVPVLALDAL---------ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  629 AHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAF 708
Cdd:COG1020    640 RALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLL 719

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  709 EQLVLADAATDRatgSLRYVVLGGEALVAERLRPWADRHGldAPELVNMYGITETTVHVTFHRLVRADLEDprRRGVIGR 788
Cdd:COG1020    720 RALLDAAPEALP---SLRLVLVGGEALPPELVRRWRARLP--GARLVNLYGPTETTVDSTYYEVTPPDADG--GSVPIGR 792

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:COG1020    793 PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA 872

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLL 948
Cdd:COG1020    873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLL 952

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  949 DALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERLVcgLFEEVLRLPADSVGTGGNFFDLGGHSLLATRLLARLRERT 1028
Cdd:COG1020    953 LPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEE--AALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1029 GTDVPISALFDTPTPAALAERLTAGADAGRPLPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDL 1108
Cdd:COG1020   1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1109 DALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELHVVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTG 1188
Cdd:COG1020   1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1189 DTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLAPAPEGPGRLERLTSFWRQAL 1268
Cdd:COG1020   1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270

                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 1269 DGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALAL 1327
Cdd:COG1020   1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1673-2208 0e+00

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: 732.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1673 PALPEPSVSGWAEALLRAAGR--PDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVAT 1750
Cdd:cd05906      1 PLHRPEGAPRTLLELLLRAAErgPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1751 LWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRD 1830
Cdd:cd05906     81 FWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1831 WYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHA 1910
Cdd:cd05906    161 LPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 PTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQ 1990
Cdd:cd05906    241 PTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1991 DVMHPGWGMSETCSVVTDSVlASEAPDHDEA--FVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNAR 2068
Cdd:cd05906    321 DAIRPAFGMTETCSGVIYSR-SFPTYDHSQAleFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2069 ANAESFTEDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAVRsDASAATDELAL 2148
Cdd:cd05906    400 ANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVR-DPGAETEELAI 478

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2149 FlrLAPGQDPAGAL----REIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAG 2208
Cdd:cd05906    479 F--FVPEYDLQDALsetlRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
PRK05691 PRK05691
peptide synthase; Validated
 10-2125 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 708.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTpDGPRAVRDGDPDEMPVHRV 89
Cdd:PRK05691   677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYER-DGVALQRIDAQGEFALQRI 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   90 DVSGEADPAAAAEEW-IRRDLA-TPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGE 167
Cdd:PRK05691   756 DLSDLPEAEREARAAqIREEEArQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQ 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  168 E----PPPAGFesADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TD--RTAPPRAPFLRRTAVLSPAETRALD 240
Cdd:PRK05691   836 TaelaPLPLGY--AD-YGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELaTDhpRSARQAHSAARYSLRVDASLSEALR 912

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  241 EAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGL--ATMSRLGSAALrtPGTASDILPLRVAASADTPVGGFVRAVADD 318
Cdd:PRK05691   913 GLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVpnANRPRLETQGL--VGFFINTQVLRAQLDGRLPFTALLAQVRQA 990

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  319 LRGLRAHQRHRGESI--------------------RRDLGVLgrgRRVHGPVVNIVPF-SEDLTFgghpstshhlsggav 377
Cdd:PRK05691   991 TLGAQAHQDLPFEQLvealpqareqglfqvmfnhqQRDLSAL---RRLPGLLAEELPWhSREAKF--------------- 1052

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  378 dDLQISvrpgAEADT---LWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEeLPLGETPvLLPGEEPVRRDE----P 450
Cdd:PRK05691  1053 -DLQLH----SEEDRngrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQ-RALGDVQ-LLDAAERAQLAQwgqaP 1125

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  451 APRVTRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTG 530
Cdd:PRK05691  1126 CAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  531 AAYLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADragatgpyDTAY 610
Cdd:PRK05691  1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGD--------NLAY 1277

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  611 VIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFL 690
Cdd:PRK05691  1278 VIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIA 1357

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  691 RLLDEEKVTVLNQTPSAFEQLVLADAATDraTGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFH 770
Cdd:PRK05691  1358 ELVQQYGVTTLHFVPPLLQLFIDEPLAAA--CTSLRRLFSGGEALPAELRNRVLQR--LPQVQLHNRYGPTETAINVTHW 1433

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  771 RLVRADLEdprrRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRS 850
Cdd:PRK05691  1434 QCQAEDGE----RSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRT 1509

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  851 GDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPAGLRA 930
Cdd:PRK05691  1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGQEAEAERLKA 1588

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  931 HLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERlVCGLFEEVLRLPadSVGTGGNFFDL 1010
Cdd:PRK05691  1589 ALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQ-IAAIWREVLGLP--RVGLRDDFFAL 1665

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1011 GGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADAGR--PLPALTASERPSLVPASFAQERMWFLSRMD 1088
Cdd:PRK05691  1666 GGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGErnSQGAIARVDRSQPVPLSYSQQRMWFLWQME 1745

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1089 GAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELH-VVDCPDEERAAHVAA- 1166
Cdd:PRK05691  1746 PDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQdFSALPADARQQRLQQl 1825

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1167 ---AMRRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALW 1242
Cdd:PRK05691  1826 adsEAHQPFDLERGPLLRACLVKAAEREhYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVW 1905

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1243 QRRVLapapEGpGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLH 1322
Cdd:PRK05691  1906 QRQWL----ES-GERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMT 1980

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1323 GALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVE 1402
Cdd:PRK05691  1981 ATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVE 2060

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1403 EVNPRRHPARHPLFQVMLALQNNE----RAVLTLGEDRVPLRPAATgtaKFDLFVDVLERHGADGTAdgldlhVEYAADL 1478
Cdd:PRK05691  2061 ALQPPRSAAYNPLFQVMCNVQRWEfqqsRQLAGMTVEYLVNDARAT---KFDLNLEVTDLDGRLGCC------LTYSRDL 2131

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1479 YDPATAERFAGALRDLLTVVCADPEVRTGALPRAdrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvv 1558
Cdd:PRK05691  2132 FDEPRIARMAEHWQNLLEALLGDPQQRLAELPLL---------------------------------------------- 2165

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1559 pnragAADRTEQVVSSLApgtrvvaisglPRTAEGGLDEgALKDLpvidqvaagawrerlarlpgvreaevvleevpeel 1638
Cdd:PRK05691  2166 -----AAAEQQQLLDSLA-----------GEAGEARLDQ-TLHGL----------------------------------- 2193

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1639 errhvgrpRAAGGAAEPDAPSverpasvpalsegpalpepsvsgwaealLRAAGRpdgevvhvradgsetRRSYASLVPE 1718
Cdd:PRK05691  2194 --------FAAQAARTPQAPA----------------------------LTFAGQ---------------TLSYAELDAR 2222

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1719 ASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL--TVPVS---YATTSAAVSKLEGIWEMLDrpwiv 1793
Cdd:PRK05691  2223 ANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLdpEYPLErlhYMIEDSGIGLLLSDRALFE----- 2297

                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1794 tsAAGEpgLRELAARreWSgLRLTTAdALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMN 1873
Cdd:PRK05691  2298 --ALGE--LPAGVAR--WC-LEDDAA-ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369

                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1874 GLGSGDVSLNW--IPLDHVTGVVMFHLrdvYLGCRQI-HAPTSWILEDPVrwpELADRHRVSVT-WAPNFAFGL---LAE 1946
Cdd:PRK05691  2370 GMRADDCELHFysINFDAASERLLVPL---LCGARVVlRAQGQWGAEEIC---QLIREQQVSILgFTPSYGSQLaqwLAG 2443

                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1947 QAHRfqdrdwdlSPVRLVMNAGEVVVASAARRFLHVLAPfglpqDVMHPGWGMSETcsVVTDsvLASEAPD---HDEAFV 2023
Cdd:PRK05691  2444 QGEQ--------LPVRMCITGGEALTGEHLQRIRQAFAP-----QLFFNAYGPTET--VVMP--LACLAPEqleEGAASV 2506

                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2024 SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYI 2095
Cdd:PRK05691  2507 PIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEY 2586

                         2170      2180      2190
                   ....*....|....*....|....*....|
gi 1573930569 2096 TGRAKDVIIVNGVNHYSHEIEACVEELPSV 2125
Cdd:PRK05691  2587 VGRIDHQVKIRGFRIELGEIESRLLEHPAV 2616
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 470-964 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: 684.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd17643     81 ADSGPSLLLTD--------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHA 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:cd17643    117 NVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFY 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDAPELVNMYGITETTVHVTFHRLVRADLeDPRRRGVIGRP 789
Cdd:cd17643    197 QLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADL-PAAAASPIGRP 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  790 LADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:cd17643    276 LPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRAD 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLD 949
Cdd:cd17643    356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLD 435

                          490
                   ....*....|....*
gi 1573930569  950 ALPLTANGKLDTAAL 964
Cdd:cd17643    436 ALPLTVNGKLDRAAL 450
PRK12467 PRK12467
peptide synthase; Provisional
 10-1216 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 678.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDpDEMPVHRV 89
Cdd:PRK12467  1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPV-GSLTLEEP 1196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   90 DVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEEP 169
Cdd:PRK12467  1197 LLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSL 1276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  170 --PPAGFESADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPFL-RRTAV-LSPAETRALDEAAK 244
Cdd:PRK12467  1277 qlPALPIQYAD-YAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELpTDRPRPAVQSHRgARLAFeLPPALAEGLRALAR 1355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  245 GMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRGLRA 324
Cdd:PRK12467  1356 REGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQA 1435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  325 HQRHRGESI------RRDLGvlgrgrrvHGPVVNiVPFSEDLTFGGhpsTSHHLSGGAVDDLQISVRP---------GAE 389
Cdd:PRK12467  1436 HQDLPFEQLvealqpERSLS--------HSPLFQ-VMFNHQRDDHQ---AQAQLPGLSVESLSWESQTaqfdltldtYES 1503

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  390 ADTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEElPLGETPVLLPGE--------EPVRRDEPAprvTRTLPQL 461
Cdd:PRK12467  1504 SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPER-RLGELDLLDEAErrqilegwNATHTGYPL---ARLVHQL 1579

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP 541
Cdd:PRK12467  1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  542 AERLALVMADAEPVAVVTDTAGSGRLPATDA-RVVVVDDARtvADLAGRAphdltDADRAGATGPYDTAYVIHTSGSTGR 620
Cdd:PRK12467  1660 RERLAYMIEDSGIELLLTQSHLQARLPLPDGlRSLVLDQED--DWLEGYS-----DSNPAVNLAPQNLAYVIYTSGSTGR 1732

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  621 PKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTV 700
Cdd:PRK12467  1733 PKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTT 1812

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  701 LNQTPSAFEQLVLADAATDRATgSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFHRLVRADLEDp 780
Cdd:PRK12467  1813 LHFVPSMLQQLLQMDEQVEHPL-SLRRVVCGGEALEVEALRPWLER--LPDTGLFNLYGPTETAVDVTHWTCRRKDLEG- 1888

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  781 RRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDG 860
Cdd:PRK12467  1889 RDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADG 1968

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  861 TLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPAG--------LRAHL 932
Cdd:PRK12467  1969 VIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDDDEaqvalraiLKNHL 2047

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  933 AARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLPadSVGTGGNFFDLG 1011
Cdd:PRK12467  2048 KASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSElEQRLAAIWQDVLGLE--QVGLHDNFFELG 2125

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1012 GHSLLATRLLARLRErTGTDVPISALFDTPTPAALAerltAGADAGRPLPALTASERPSLVPASFAQeRMWFLSRMdGAA 1091
Cdd:PRK12467  2126 GDSIISIQVVSRARQ-AGIRFTPKDLFQHQTVQSLA----AVAQEGDGTVSIDQGPVTGDLPLLPIQ-QMFFADDI-PER 2198

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1092 ATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPEL---HVVDCPDEERAahVAAAM 1168
Cdd:PRK12467  2199 HHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRPLlwqVVVADKEELEA--LCEQA 2276

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 1169 RRSFDLTRDSALWAGVFGTGDTRT-LLLVLHHSAADGWSLRPLADDLGT 1216
Cdd:PRK12467  2277 QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRILLEDLQT 2325
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 470-964 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: 582.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraPHDLtdadragatgpydtAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd05930     81 EDSGAKLVLTD------------------------------PDDL--------------AYVIYTSGSTGKPKGVMVEHR 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:cd05930    117 GLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLR 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVlaDAATDRATGSLRYVVLGGEALVAERLRPWADRHglDAPELVNMYGITETTVHVTFHRLvraDLEDPRRRGV-IGR 788
Cdd:cd05930    197 LLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNLYGPTEATVDATYYRV---PPDDEEDGRVpIGR 269

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:cd05930    270 PIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRI 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLL 948
Cdd:cd05930    349 DDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVL 428

                          490
                   ....*....|....*.
gi 1573930569  949 DALPLTANGKLDTAAL 964
Cdd:cd05930    429 DALPLTPNGKVDRKAL 444
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1072-1502 1.21e-171

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: 535.85  E-value: 1.21e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELH 1151
Cdd:cd19540      2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWA 1230
Cdd:cd19540     82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEhVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1231 PPALQYADFALWQRRVLAPAPEGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLA 1310
Cdd:cd19540    162 PLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1311 DHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQAL 1390
Cdd:cd19540    242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1391 DHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRVPLRPAATGTAKFDLFVDVLERHGADGTADGLDL 1470
Cdd:cd19540    322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDADGAPAGLTG 401

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1573930569 1471 HVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19540    402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
PRK12316 PRK12316
peptide synthase; Provisional
 5-1372 3.48e-170

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 592.70  E-value: 3.48e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    5 EDDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRdgdPDEM 84
Cdd:PRK12316    46 SAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQV---PLDR 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   85 P--VHRVDVSGEADPAAAAE--EWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTY 160
Cdd:PRK12316   123 PleVEFEDCSGLPEAEQEARlrDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  161 TALAAGEEP--PPAGFESADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAP--PRAPFLRRTAVLSPAE 235
Cdd:PRK12316   203 SAYATGAEPglPALPIQYAD-YALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELpTDHPRPavPSYRGSRYEFSIDPAL 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  236 TRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAV 315
Cdd:PRK12316   282 AEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  316 ADDLRGLRAHQRHRGESIRRDLGVlgRGRRVHGPVVNIVPFSEDLTFG-GHPSTSHHLSGGAVD------DLQISVRPGA 388
Cdd:PRK12316   362 KDTVLGAQAHQDLPFERLVEALKV--ERSLSHSPLFQVMYNHQPLVADiEALDTVAGLEFGQLEwksrttQFDLTLDTYE 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  389 EADTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEElPLGETPVLLPGE--EPVRRDEPAPRVT---RTLPQLFE 463
Cdd:PRK12316   440 KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA-RVDELPMLDAEErgQLVEGWNATAAEYplqRGVHRLFE 518

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  464 ARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAE 543
Cdd:PRK12316   519 EQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE 598

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  544 RLALVMADAEPVAVVTDTAGSGRLPaTDARVVVVDDARTVADLAGRAphdltDADRAGATGPYDTAYVIHTSGSTGRPKG 623
Cdd:PRK12316   599 RLAYMLEDSGVQLLLSQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYS-----EENPGTELNPENLAYVIYTSGSTGKPKG 672

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  624 VPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQ 703
Cdd:PRK12316   673 AGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHF 752

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  704 TPSAFeQLVLADAATDRATgSLRYVVLGGEALvaerlrPWADRHGLDA----PELVNMYGITETTVHVTFHRLVRADLED 779
Cdd:PRK12316   753 VPSML-QAFLQDEDVASCT-SLRRIVCSGEAL------PADAQEQVFAklpqAGLYNLYGPTEAAIDVTHWTCVEEGGDS 824

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 PRrrgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGApGTRMYRSGDLARWRPD 859
Cdd:PRK12316   825 VP----IGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRAD 899

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  860 GTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVpraAEDGLtQLVAYAVPAEEGGADPAGLRAHLAARLPAY 939
Cdd:PRK12316   900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL---AVDGK-QLVGYVVLESEGGDWREALKAHLAASLPEY 975

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  940 MVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSlLAT 1018
Cdd:PRK12316   976 MVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNAlERTLAAIWQDVLGV--ERVGLDDNFFELGGDS-IVS 1052

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1019 RLLARLRERTGTDVPISALFDTPTPAALAERLTAGadagrplPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPL 1098
Cdd:PRK12316  1053 IQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAG-------QATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSL 1125

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1099 PVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPeLHVVDCPDEERAAHVAAAMRRSFDLTRDS 1178
Cdd:PRK12316  1126 LLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEV-LWQRQAASEEELLALCEEAQRSLDLEQGP 1204

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1179 ALWAGVFGTGD-TRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPdwappalQYADFALWQRRVLAPAPEGPGRL 1257
Cdd:PRK12316  1205 LLRALLVDMADgSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPA-------RTSSYQAWARRLHEHAGARAEEL 1277

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1258 ErltsFWRQALDGLPEESAPPPDRPRPAAPSGRggGVTVPLDAGTHRELLRLADHE-NASLFMVLHGALALLLNRWGAGD 1336
Cdd:PRK12316  1278 D----YWQAQLEDAPHELPCENPDGALENRHER--KLELRLDAERTRQLLQEAPAAyRTQVNDLLLTALARVTCRWSGQA 1351

                         1370      1380      1390      1400
                   ....*....|....*....|....*....|....*....|
gi 1573930569 1337 DIVVGTPVAGRTEPA----LDEVVGLLTNTLVLRADASGD 1372
Cdd:PRK12316  1352 SVLVQLEGHGREDLFedidLSRTVGWFTSLFPVRLTPAAD 1391
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 460-964 1.30e-167

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: 526.38  E-value: 1.30e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDltdadragatgPYDTAYVIHTSGSTG 619
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS-----------PDDLAYVMYTSGSTG 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPHAHVVRLFEASGeHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVT 699
Cdd:cd12117    150 RPKGVAVTHRGVVRLVKNTN-YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  700 VLNQTPSAFEQLVLADAAtdrATGSLRYVVLGGEALVAERLRPWADRHGldAPELVNMYGITETTVHVTFHRLVRADLED 779
Cdd:cd12117    229 VLWLTAALFNQLADEDPE---CFAGLRELLTGGEVVSPPHVRRVLAACP--GLRLVNGYGPTENTTFTTSHVVTELDEVA 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 PRRRgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRPD 859
Cdd:cd12117    304 GSIP--IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPD 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  860 GTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPaeEGGADPAGLRAHLAARLPAY 939
Cdd:cd12117    381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDAAELRAFLRERLPAY 458

                          490       500
                   ....*....|....*....|....*
gi 1573930569  940 MVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd12117    459 MVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 459-964 8.61e-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: 509.89  E-value: 8.61e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDP 538
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  539 GHPAERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDdartvADLAGRAPhdltdADRAGATGPYDTAYVIHTSGST 618
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGD-----EALAAPPA-----TPPLVPPRPDNLAYVIYTSGST 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  619 GRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKV 698
Cdd:cd17646    151 GRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGV 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  699 TVLNQTPSAFEQLVLADAATDRAtgSLRYVVLGGEALVAERLRPWADRhgLDApELVNMYGITETTVHVTFHRlVRADle 778
Cdd:cd17646    231 TTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLAL--PGA-ELHNLYGPTEAAIDVTHWP-VRGP-- 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 DPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRP 858
Cdd:cd17646    303 AETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRP 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEG-GADPAGLRAHLAARLP 937
Cdd:cd17646    382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAaGPDTAALRAHLAERLP 461

                          490       500
                   ....*....|....*....|....*..
gi 1573930569  938 AYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd17646    462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 470-964 1.21e-160

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: 506.06  E-value: 1.21e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDTAGSGRLPATDARVvvvddartvaDLAGRAPHdLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVL----------LLALAAAA-AAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHR 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPsAFE 709
Cdd:cd12116    150 NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATP-ATW 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADAATDRAtgSLRyVVLGGEALVAERLRPWADRHGldapELVNMYGITETTVHVTFHRLvradlEDPRRRGVIGRP 789
Cdd:cd12116    229 RMLLDAGWQGRA--GLT-ALCGGEALPPDLAARLLSRVG----SLWNLYGPTETTIWSTAARV-----TAAAGPIPIGRP 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  790 LADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:cd12116    297 LANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRAD 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRaAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLD 949
Cdd:cd12116    377 GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR-EDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLD 455

                          490
                   ....*....|....*
gi 1573930569  950 ALPLTANGKLDTAAL 964
Cdd:cd12116    456 ALPLTANGKLDRKAL 470
PRK12316 PRK12316
peptide synthase; Provisional
 10-1372 2.04e-160

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 561.12  E-value: 2.04e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRdgdPDEMPVHRV 89
Cdd:PRK12316  2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVI---LPNMSLRIV 2680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   90 DVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEEP 169
Cdd:PRK12316  2681 LEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQP 2760

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  170 P-PAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAETRALDEAAKG 245
Cdd:PRK12316  2761 TlPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELpLDRPRPALQSHrgARLDVALDVALSRELLALARR 2840

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  246 MGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRGLRAH 325
Cdd:PRK12316  2841 EGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAH 2920

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  326 QRHRGESIRRDLGvlGRGRRVHGPVVNIVPFSEDLTFGGHPSTSHHLSG----GAVDDLQISVRPGAEADTLWLAFDAHP 401
Cdd:PRK12316  2921 QDLPFEQLVEALQ--PERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESfawdGAATQFDLALDTWESAEGLGASLTYAT 2998

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  402 DLYEEDGLALFLERFLKVLRELRTCPE----ELPLGETPVLLPGEEPVRRDEPAPRVTRTLPQLFEARVAESPGRTAVSY 477
Cdd:PRK12316  2999 DLFDARTVERLARHWQNLLRGMVENPQrsvdELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAF 3078

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  478 AGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEpvAV 557
Cdd:PRK12316  3079 GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSG--AQ 3156

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  558 VTDTAGSGRLPATDARVVVVDDartvadlagRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEA 637
Cdd:PRK12316  3157 LLLSQSHLRLPLAQGVQVLDLD---------RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW 3227

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  638 SGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAA 717
Cdd:PRK12316  3228 MQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDA 3307

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  718 tdRATGSLRYVVLGGEALVAERLRPWadrhgLDAPELVNMYGITETTVHVTFHRLVradlEDPRRRGVIGRPLADLRVYV 797
Cdd:PRK12316  3308 --HRCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEATITVTHWQCV----EEGKDAVPIGRPIANRACYI 3376

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  798 LDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGF 877
Cdd:PRK12316  3377 LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGF 3455

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  878 RIEPGEIEAVLTAHPAVAGGAVVPRAAEdgltQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANG 957
Cdd:PRK12316  3456 RIELGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNG 3531

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  958 KLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLPadSVGTGGNFFDLGGHSLLATRLLARLRErTGTDVPISA 1036
Cdd:PRK12316  3532 KLDRKALPRPDAALLQQDYVAPVNElERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKD 3608

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1037 LFDTPTPAALAE--RLTAGADAGR-----PLPALTASERPslVPASFAQERMWFLSrmdgaaatynipLPVALRHPLDLD 1109
Cdd:PRK12316  3609 LFQHQTIQGLARvaRVGGGVAVDQgpvsgETLLLPIQQQF--FEEPVPERHHWNQS------------LLLKPREALDAA 3674

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1110 ALRAALGDVADRHESLRTVFGEEDGAIHQRVLP---PGTLRPELHVVDCPDEERAAHVAAamrRSFDLTRDSALWAGV-- 1184
Cdd:PRK12316  3675 ALEAALQALVEHHDALRLRFVEDAGGWTAEHLPvelGGALLWRAELDDAEELERLGEEAQ---RSLDLADGPLLRALLat 3751

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1185 FGTGDTRtLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRrvlapAPEGPGRLERLTSFW 1264
Cdd:PRK12316  3752 LADGSQR-LLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQ-----EHARGEALKAELAYW 3825

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1265 RQALDGLPEESAPPPDRPRPAAPSGRggGVTVPLDAGTHRELLRLADHE-NASLFMVLHGALALLLNRWGAGDDIVVGTP 1343
Cdd:PRK12316  3826 QEQLQGVSSELPCDHPQGALQNRHAA--SVQTRLDRELTRRLLQQAPAAyRTQVNDLLLTALARVVCRWTGEASALVQLE 3903

                         1370      1380      1390
                   ....*....|....*....|....*....|...
gi 1573930569 1344 VAGRTE----PALDEVVGLLTNTLVLRADASGD 1372
Cdd:PRK12316  3904 GHGREDlfadIDLSRTVGWFTSLFPVRLSPVED 3936
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 470-965 4.04e-158

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: 497.16  E-value: 4.04e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd17652     81 ADARPALLLTT--------------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHR 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAfe 709
Cdd:cd17652    117 GLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAA-- 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 qlvlADAATDRATGSLRYVVLGGEALVAERLRPWADRHgldapELVNMYGITETTVHVTFHRLVRADLEDPrrrgvIGRP 789
Cdd:cd17652    195 ----LAALPPDDLPDLRTLVVAGEACPAELVDRWAPGR-----RMINAYGPTETTVCATMAGPLPGGGVPP-----IGRP 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  790 LADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:cd17652    261 VPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRAD 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLD 949
Cdd:cd17652    341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLD 420

                          490
                   ....*....|....*.
gi 1573930569  950 ALPLTANGKLDTAALP 965
Cdd:cd17652    421 ALPLTPNGKLDRRALP 436
PRK12316 PRK12316
peptide synthase; Provisional
 2-1052 3.09e-157

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 550.72  E-value: 3.09e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    2 SGNEDDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGpVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDP 81
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVVHK 4174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   82 D-EMPVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTY 160
Cdd:PRK12316  4175 QvSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  161 TalaaGEEPPPAGFESADRLAaeeaaYLGSDRHRRDRAYWTERLAGLPEPVRLTD-------RTAPPRAPFLRrtaVLSP 233
Cdd:PRK12316  4255 S----GRPPAQPGGRYRDYIA-----WLQRQDAAASEAFWREQLAALDEPTRLAQaiaradlRSANGYGEHVR---ELDA 4322

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  234 AETRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRlgsaALRTPGTASDI------LPLRVAASADTP 307
Cdd:PRK12316  4323 TATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGR----PAELPGIEGQIglfintLPVIATPRAQQS 4398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  308 VGGFVRAVADDLRGLRAHQRHRGESIRRDLGVLGRGRRVHGPVVNIVPFSEDLTFGghpsTSHHLSGGAVDDLQISVRPG 387
Cdd:PRK12316  4399 VVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQG----APGGLRFGEVTNHEQTNYPL 4474

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  388 AEA----DTLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEeLPLGETPVLLPGEEPV------RRDEPAPRvTRT 457
Cdd:PRK12316  4475 TLAvglgETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQ-RRLGELQLLEKAEQQRivalwnRTDAGYPA-TRC 4552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:PRK12316  4553 VHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLD 4632

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTDTAGSGRLPATD-ARVVVVDDARtvaDLAGRAphdltDADRAGATGPYDTAYVIHTSG 616
Cdd:PRK12316  4633 PEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDgLASLALDRDE---DWEGFP-----AHDPAVRLHPDNLAYVIYTSG 4704

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSrSPREFLRLLDEE 696
Cdd:PRK12316  4705 STGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEH 4783

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  697 KVTVLNQTPSAFEQLvLADAATDRATGSLRYVVLGGEALVAERLRPWAdrHGLDAPELVNMYGITETTVHVTfHRLVRAD 776
Cdd:PRK12316  4784 RVTVLVFPPVYLQQL-AEHAERDGEPPSLRVYCFGGEAVAQASYDLAW--RALKPVYLFNGYGPTETTVTVL-LWKARDG 4859

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  777 LEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARW 856
Cdd:PRK12316  4860 DACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARY 4939

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  857 RPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVpraAEDGLT--QLVAYAVPAEEGGADP--------A 926
Cdd:PRK12316  4940 RADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI---AQEGAVgkQLVGYVVPQDPALADAdeaqaelrD 5016

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  927 GLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLPadSVGTGG 1005
Cdd:PRK12316  5017 ELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSElEQQVAAIWAEVLQLE--RVGLDD 5094

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*..
gi 1573930569 1006 NFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAERLTA 1052
Cdd:PRK12316  5095 NFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAA 5141
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 462-965 1.06e-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: 495.33  E-value: 1.06e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP 541
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  542 AERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADlagraphdlTDADRAGATGPYDTAYVIHTSGSTGRP 621
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAG---------ADAEPDPALDADDLAYVIYTSGSTGRP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVL 701
Cdd:cd17651    152 KGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  702 NQTPSAFEQLVLADAATDRATGSLRYVVLGGEALV-AERLRPWADRHGldAPELVNMYGITETTVhVTFHRLvRADLEDP 780
Cdd:cd17651    232 FLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLP--GLRLHNHYGPTETHV-VTALSL-PGDPAAW 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  781 RRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRPDG 860
Cdd:cd17651    308 PAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDG 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  861 TLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYM 940
Cdd:cd17651    387 ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYM 466

                          490       500
                   ....*....|....*....|....*
gi 1573930569  941 VPAACVLLDALPLTANGKLDTAALP 965
Cdd:cd17651    467 VPSAFVLLDALPLTPNGKLDRRALP 491
PRK12467 PRK12467
peptide synthase; Provisional
 6-1257 1.41e-151

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 532.04  E-value: 1.41e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    6 DDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGpVDTALFETALRRTVREADTFALRFLDTPDGPRAVR-DGDPDEM 84
Cdd:PRK12467  2644 EDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQvVYKQARL 2722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   85 PVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTala 164
Cdd:PRK12467  2723 PFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF--- 2799

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  165 aGEEPPPAGFESADRLAaeeaaYLGSDRHRRDRAYWTERLAGLPEPVRL----TDRTAPPRAPFLRRTAVLSPAETRALD 240
Cdd:PRK12467  2800 -GQPPPAREGRYRDYIA-----WLQAQDAEASEAFWKEQLAALEEPTRLaralYPAPAEAVAGHGAHYLHLDATQTRQLI 2873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  241 EAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRlgSAALR----TPGTASDILPLRVAASADTPVGGFVRAVA 316
Cdd:PRK12467  2874 EFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR--PAQLRgaeqQLGLFINTLPVIASPRAEQTVSDWLQQVQ 2951

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  317 DDLRGLRAHQRHRGESIRRDLGVLGRGRRVHGPVVNIVPFSEDLTFGGhPSTshhLSGGAVDDLQISVRPGAEA----DT 392
Cdd:PRK12467  2952 AQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGA-PSG---LRFGAVSSREQTNYPLTLAvglgDT 3027

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  393 LWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEElPLGETPVLLPGE-----EPVRRDEPAPRVTRTLPQLFEARVA 467
Cdd:PRK12467  3028 LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAA-RLGELPTLAAHErrqvlHAWNATAAAYPSERLVHQLIEAQVA 3106

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  468 ESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLAL 547
Cdd:PRK12467  3107 RTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  548 VMADAEPVAVVTDTAGSGRLPA-TDARVVVVDDArtvaDLAGRAPHDLTDAdragaTGPYDTAYVIHTSGSTGRPKGVPV 626
Cdd:PRK12467  3187 MIEDSGVKLLLTQAHLLEQLPApAGDTALTLDRL----DLNGYSENNPSTR-----VMGENLAYVIYTSGSTGKPKGVGV 3257

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  627 PHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVsRSPREFLRLLDEEKVTVLNQTPS 706
Cdd:PRK12467  3258 RHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPA 3336

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  707 AFEQLvlADAATDRATGSLRYVVLGGEALVAERLRpwADRHGLDAPELVNMYGITETTVHVTfHRLVRADLEDPRRRGVI 786
Cdd:PRK12467  3337 YLQQF--AEDAGGADCASLDIYVFGGEAVPPAAFE--QVKRKLKPRGLTNGYGPTEAVVTVT-LWKCGGDAVCEAPYAPI 3411

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  787 GRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAG 866
Cdd:PRK12467  3412 GRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLG 3491

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  867 RADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACV 946
Cdd:PRK12467  3492 RIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLL 3570

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  947 LLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERLVCGLFEEVLRLPadSVGTGGNFFDLGGHSLLATRLLARLRE 1026
Cdd:PRK12467  3571 VLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVE--QVGVTDNFFELGGDSLLALQVLSRIRQ 3648

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1027 RTGTDVPISALFDTPTPAALAERLTAGADAGRPLpaltaserpslvpasfaqermwflsrmdgaaatyniplpvalrhpL 1106
Cdd:PRK12467  3649 SLGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLL---------------------------------------------L 3683

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1107 DLDALRAALGDVADRHESLRTVFGEEdgAIhQRVLPpgtlrpelhvvdcpdeeraahvaaamrrsfdltrdsalwagvfg 1186
Cdd:PRK12467  3684 DLNRLETGFPALFCRHEGLGTVFDYE--PL-AVILE-------------------------------------------- 3716

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 1187 tGDTRTLLLVLHHSAADGWSlrpladdlgtayaarragaAPDWAPPALQYADFALWQRrvlapaPEGPGRL 1257
Cdd:PRK12467  3717 -GDRHVLGLTCRHLLDDGWQ-------------------DTSLQAMAVQYADYILWQQ------AKGPYGL 3761
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 483-899 1.21e-150

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: 474.45  E-value: 1.21e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDT 561
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 AGSGRLPATDARVVVVDDARTVADLAGRAPhdltdADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEH 641
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAP-----PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFL-RLLDEEKVTVLNQTPSAFEQLVLADaatDR 720
Cdd:TIGR01733  156 YGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAAL---PP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  721 ATGSLRYVVLGGEALVAERLRPWADRHGldAPELVNMYGITETTVHVTFHRLVRADLEDPRRRGvIGRPLADLRVYVLDA 800
Cdd:TIGR01733  233 ALASLRLVILGGEALTPALVDRWRARGP--GARLINLYGPTETTVWSTATLVDPDDAPRESPVP-IGRPLANTRLYVLDD 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  801 AGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPF-GAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRI 879
Cdd:TIGR01733  310 DLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389

                          410       420
                   ....*....|....*....|
gi 1573930569  880 EPGEIEAVLTAHPAVAGGAV 899
Cdd:TIGR01733  390 ELGEIEAALLRHPGVREAVV 409
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1072-1502 4.51e-150

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: 474.06  E-value: 4.51e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELH 1151
Cdd:cd19538      2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGD-TRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWA 1230
Cdd:cd19538     82 IKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGEnEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1231 PPALQYADFALWQRRVLAPAPEGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLA 1310
Cdd:cd19538    162 PLPVQYADYALWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1311 DHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQAL 1390
Cdd:cd19538    242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1391 DHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRVPLRPAATGTAKFDLFVDVLERHgADGTADGLDL 1470
Cdd:cd19538    322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQY-NDGTPNGIEG 400

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1573930569 1471 HVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19538    401 FIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 460-968 1.14e-145

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: 463.72  E-value: 1.14e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDtaGSGRLPATDARVVVVDDARTVAdlagrapHDlTDADRAGATGPYDTAYVIHTSGSTG 619
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQ--SHLQPPIAFIGLIDLLDEDTIY-------HE-ESENLEPVSKSDDLAYVIYTSGSTG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPHAHVVRLFEA------SGEHFRFGaddvwtLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLL 693
Cdd:cd17655    151 KPKGVMIEHRGVVNLVEWankviyQGEHLRVA------LFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYI 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSafeQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGlDAPELVNMYGITETTVHVTFHRLV 773
Cdd:cd17655    225 RQNRITIIDLTPA---HLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFG-TNPTITNAYGPTETTVDASIYQYE 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  774 RADLEDPRRRgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgAPGTRMYRSGDL 853
Cdd:cd17655    301 PETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDL 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPAGLRAHLA 933
Cdd:cd17655    378 ARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQLREFLA 455

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAALPAPD 968
Cdd:cd17655    456 RELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 470-965 3.12e-141

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: 449.13  E-value: 3.12e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEpvavvtdtagsgrlpatdARVVVVDDARTVAdlagraphdltdadragatgpydtaYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd17649     81 EDSG------------------AGLLLTHHPRQLA-------------------------YVIYTSGSTGTPKGVAVSHG 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:cd17649    118 PLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQ 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVL-ADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapeLVNMYGITETTVHVTFHrLVRADLEDPRRRGVIGR 788
Cdd:cd17649    198 QLAEeADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVR----LFNAYGPTEATVTPLVW-KCEAGAARAGASMPIGR 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:cd17649    273 PLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRV 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAeDGLTQLVAYAVP--AEEGGADPAGLRAHLAARLPAYMVPAACV 946
Cdd:cd17649    353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQLVAYVVLraAAAQPELRAQLRTALRASLPDYMVPAHLV 431

                          490
                   ....*....|....*....
gi 1573930569  947 LLDALPLTANGKLDTAALP 965
Cdd:cd17649    432 FLARLPLTPNGKLDRKALP 450
PRK05691 PRK05691
peptide synthase; Validated
 7-1515 2.19e-139

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 492.38  E-value: 2.19e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    7 DRR---PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFlDTPDGPRAVRDGDPDE 83
Cdd:PRK05691  1724 DRSqpvPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTF-PSVDGVPVQQVAEDSG 1802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   84 MPVHRVDVSGEADPAAAA--EEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYT 161
Cdd:PRK05691  1803 LRMDWQDFSALPADARQQrlQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYE 1882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  162 ALAAGEEPP--PAGFESADrLAAEEAAYLGSDRHRRDRAYWTERLaGLPEPVRL--TDRTAPP----RAPFLRRTavLSP 233
Cdd:PRK05691  1883 AFLDDRESPlePLPVQYLD-YSVWQRQWLESGERQRQLDYWKAQL-GNEHPLLElpADRPRPPvqshRGELYRFD--LSP 1958

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  234 ---AETRALDeAAKGMGVARTdlLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGG 310
Cdd:PRK05691  1959 elaARVRAFN-AQRGLTLFMT--MTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSE 2035

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  311 FVRAVADDLRGLRAHQ----RHRGESIRRDLGVlgrgrrVHGPVVNIVPFSEDLTFgghpSTSHHLSGGAVD-------- 378
Cdd:PRK05691  2036 LLEQVRQTVIEGQSHQdlpfDHLVEALQPPRSA------AYNPLFQVMCNVQRWEF----QQSRQLAGMTVEylvndara 2105

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  379 ---DLQISVrpgAEAD-TLWLAFDAHPDLYEEDGLALFLERFLKVLRELRTCPEElPLGETPVLLPGEEPVRRDEPAP-- 452
Cdd:PRK05691  2106 tkfDLNLEV---TDLDgRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQ-RLAELPLLAAAEQQQLLDSLAGea 2181

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  453 ---RVTRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKT 529
Cdd:PRK05691  2182 geaRLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  530 GAAYLPLDPGHPAERLALVMADAEPVAVVTDTA---GSGRLPATDARVVVVDDARTVADLAGRAPHDLTdadragatGPY 606
Cdd:PRK05691  2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRAlfeALGELPAGVARWCLEDDAAALAAYSDAPLPFLS--------LPQ 2333

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRlVVVPYEVSRSP 686
Cdd:PRK05691  2334 HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGAR-VVLRAQGQWGA 2412

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLDEEKVTVLNQTPSAFEQLVlADAATDRATGSLRYVVLGGEALVAERLRpwADRHGLDAPELVNMYGITETTVh 766
Cdd:PRK05691  2413 EEICQLIREQQVSILGFTPSYGSQLA-QWLAGQGEQLPVRMCITGGEALTGEHLQ--RIRQAFAPQLFFNAYGPTETVV- 2488

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 VTFHRLVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTR 846
Cdd:PRK05691  2489 MPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGR 2568

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  847 MYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPA 926
Cdd:PRK05691  2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYLVSAVAGQDDEA 2647

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  927 ------GLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE-ERLVCGLFEEVLRLpaD 999
Cdd:PRK05691  2648 qaalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSElEQQLAQIWREVLNV--E 2725

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1000 SVGTGGNFFDLGGHSLLATRLLARLRERtGTDVPISALFDTPTPAALAERLTAGAdagrplpALTASERPSLVPASFAQE 1079
Cdd:PRK05691  2726 RVGLGDNFFELGGDSILSIQVVSRARQL-GIHFSPRDLFQHQTVQTLAAVATHSE-------AAQAEQGPLQGASGLTPI 2797

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1080 RMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPgTLRPELHVVDCPDEE 1159
Cdd:PRK05691  2798 QHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAV-TAQELLWQVTVADFA 2876

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1160 RAAHVAAAMRRSFDLTRDSALWAG-VFGTGDTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPdwAPPALQYAd 1238
Cdd:PRK05691  2877 ECAALFADAQRSLDLQQGPLLRALlVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEP--ALPAKTSA- 2953

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1239 FALWQRRVLAPApeGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRggGVTVPLDAGTHRELLRLADHE-NASL 1317
Cdd:PRK05691  2954 FRDWAARLQAYA--GSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQ--TVSVRLDAERTRQLLQQAPAAyRTQV 3029

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1318 FMVLHGALALLLNRWGAGDDIVVGTPVAGRtEPALDEV-----VGLLTNT--LVLRADASGDPTFRELLARVRAfDVQAL 1390
Cdd:PRK05691  3030 NDLLLTALARVLCRWSGQPSVLVQLEGHGR-EALFDDIdltrsVGWFTSAypLRLTPAPGDDAARGESIKAIKE-QLRAV 3107

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1391 DHQDLPFDRLveevnprRHPARHPLFQVMLALQNNERAVLTLGE------DRVPLRPA-ATGTAKFDLFVDVLERHGADG 1463
Cdd:PRK05691  3108 PHKGLGYGVL-------RYLADAAVREAMAALPQAPITFNYLGQfdqsfaSDALFRPLdEPAGPAHDPDAPLPNELSVDG 3180

                         1530      1540      1550      1560      1570
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 1464 TADG--LDLHVEYAADLYDPATAERFAGA-LRDLLTVVCADPEVRTGALPRADRP 1515
Cdd:PRK05691  3181 QVYGgeLVLRWTYSAERYDEQTIAELAEAyLAELQALIAHCLADGAGGLTPSDFP 3235
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1072-1502 1.96e-136

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: 434.48  E-value: 1.96e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrpELH 1151
Cdd:cd19531      2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPL--PLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVDC---PDEERAA----HVAAAMRRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRA 1223
Cdd:cd19531     80 VVDLsglPEAEREAeaqrLAREEARRPFDLARGPLLRATLLRLGEDEhVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1224 GAAPDWAPPALQYADFALWQRRVLAPapegpGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTH 1303
Cdd:cd19531    160 GRPSPLPPLPIQYADYAVWQREWLQG-----EVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELT 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1304 RELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVR 1383
Cdd:cd19531    235 AALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVR 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1384 AFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRVPLRPAATGTAKFDLFVDVLErhgadg 1463
Cdd:cd19531    315 ETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTE------ 388

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1573930569 1464 TADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19531    389 TDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 458-964 3.85e-135

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: 431.74  E-value: 3.85e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGS 617
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTD--------------------------------------------PDDLAYVIYTSGS 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  618 TGRPKGVPVPHAHVVRLFEASGEHFrfGADDVWTLFH--SYAFDFSVWELWGPLLHGGRlvVVPYEVSRSPREFLRLLDe 695
Cdd:cd12115    117 TGRPKGVAIEHRNAAAFLQWAAAAF--SAEELAGVLAstSICFDLSVFELFGPLATGGK--VVLADNVLALPDLPAAAE- 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  696 ekVTVLNQTPSAFEQLVLADAATdratGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFHRLVRA 775
Cdd:cd12115    192 --VTLINTVPSAAAELLRHDALP----ASVRVVNLAGEPLPRDLVQRLYAR--LQVERVVNLYGPSEDTTYSTVAPVPPG 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  776 DLEDPRrrgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLAR 855
Cdd:cd12115    264 ASGEVS----IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVR 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  856 WRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAAR 935
Cdd:cd12115    339 WRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTR 418

                          490       500
                   ....*....|....*....|....*....
gi 1573930569  936 LPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd12115    419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 457-965 4.12e-132

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: 423.77  E-value: 4.12e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL 536
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraPHDLtdadragatgpydtAYVIHTSG 616
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ------------------------------PENL--------------AYVIYTSG 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEE 696
Cdd:cd17644    117 STGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQW 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  697 KVTVLNQTPSAFEQLVLAdAATDRATG--SLRYVVLGGEALVAERLRPWADRHGlDAPELVNMYGITETTVHVTFHRLvR 774
Cdd:cd17644    197 QLTVLSLPPAYWHLLVLE-LLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVG-NFIQLINVYGPTEATIAATVCRL-T 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  775 ADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPF-GAPGTRMYRSGDL 853
Cdd:cd17644    274 QLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDL 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLA 933
Cdd:cd17644    354 ARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLK 433

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAALP 965
Cdd:cd17644    434 AKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 8-427 1.10e-130

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: 417.54  E-value: 1.10e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDgDPDEMPVH 87
Cdd:cd19533      1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWID-PYTPVPIR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   88 RVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGE 167
Cdd:cd19533     80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  168 EPPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLTDRTAPPRAPFLRRTAVLSPAETRALDEAAKGMG 247
Cdd:cd19533    160 PAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAAEAHG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  248 VARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRGLRAHQR 327
Cdd:cd19533    240 ASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQR 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  328 HRGESIRRDLGVLGRGRRVHGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPGAEADTLWLAFDAHPDLYEED 407
Cdd:cd19533    320 YRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDRDDESGLRIDFDANPALYSGE 399

                          410       420
                   ....*....|....*....|
gi 1573930569  408 GLALFLERFLKVLRELRTCP 427
Cdd:cd19533    400 DLARHQERLLRLLEEAAADP 419
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 470-964 9.09e-123

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: 397.41  E-value: 9.09e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDTAGsgrlpatDARVVVVDDARTVADLAGRAPHDLTDADRAgatgPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd12114     81 ADAGARLVLTDGPD-------AQLDVAVFDVLILDLDALAAPAPPPPVDVA----PDDLAYVIFTSGSTGTPKGVMISHR 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:cd12114    150 AALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLE 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFHRLVRADledPRRRGV-IGR 788
Cdd:cd12114    230 MLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRAL--APDARLISLGGATEASIWSIYHPIDEVP---PDWRSIpYGR 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPfgaPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:cd12114    305 PLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRR 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRaAEDGLTQLVAYAVPAEEG-GADPAGLRAHLAARLPAYMVPAACVL 947
Cdd:cd12114    382 DGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIA 460

                          490
                   ....*....|....*..
gi 1573930569  948 LDALPLTANGKLDTAAL 964
Cdd:cd12114    461 LEALPLTANGKVDRAAL 477
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 466-964 3.19e-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: 394.69  E-value: 3.19e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  466 VAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERL 545
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  546 ALVMADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVP 625
Cdd:cd05945     81 REILDAAKPALLIAD--------------------------------------------GDDNAYIIFTSGSTGRPKGVQ 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  626 VPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTP 705
Cdd:cd05945    117 ISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTP 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 SAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRhgldAPE--LVNMYGITETTVHVTFHRLVRADLED---- 779
Cdd:cd05945    197 SFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQR----FPDarIYNTYGPTEATVAVTYIEVTPEVLDGydrl 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 PrrrgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFlpdpFGAPGTRMYRSGDLARWRPD 859
Cdd:cd05945    273 P-----IGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEAD 343

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  860 GTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGA-DPAGLRAHLAARLPA 938
Cdd:cd05945    344 GLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgLTKAIKAELAERLPP 423

                          490       500
                   ....*....|....*....|....*.
gi 1573930569  939 YMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05945    424 YMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 470-965 2.62e-121

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: 392.15  E-value: 2.62e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAG-PGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADaepvavvtdtagsgrlpaTDARVVVvddartvadlagraphdltdadragaTGPYDTAYVIHTSGSTGRPKGVPVPH 628
Cdd:cd17648     81 LED------------------TGARVVI--------------------------TNSTDLAYAIYTSGTTGKPKGVLVEH 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  629 AHVVRLFEASGEHFrFGA---DDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTP 705
Cdd:cd17648    117 GSVVNLRTSLSERY-FGRdngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTP 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 SAFEQLVLAdaatdRATgSLRYVVLGGEALVAERLRpwADRHGLDAPeLVNMYGITETTVHvtfhRLVRADLEDPRRRGV 785
Cdd:cd17648    196 SVLQQYDLA-----RLP-HLKRVDAAGEEFTAPVFE--KLRSRFAGL-IINAYGPTETTVT----NHKRFFPGDQRFDKS 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  786 IGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPG-------TRMYRSGDLARWRP 858
Cdd:cd17648    263 LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLP 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPR-----AAEDGLTQLVAYAVPaEEGGADPAGLRAHLA 933
Cdd:cd17648    343 SGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedasqAQSRIQKYLVGYYLP-EPGHVPESDLLSFLR 421

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAALP 965
Cdd:cd17648    422 AKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 458-964 7.33e-120

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: 389.21  E-value: 7.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADaepvavvtdtagsgrlpaTDARVVVVDDartvadlagraphdltdadragatgPYDTAYVIHTSGS 617
Cdd:cd05918     81 PSHPLQRLQEILQD------------------TGAKVVLTSS-------------------------PSDAAYVIFTSGS 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  618 TGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVvpyevsrsPREFLRL----- 692
Cdd:cd05918    118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--------PSEEDRLndlag 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 -LDEEKVTVLNQTPSAFEQLVLADAAtdratgSLRYVVLGGEALVAERLRPWADRhgldaPELVNMYGITETTVHVTFHR 771
Cdd:cd05918    190 fINRLRVTWAFLTPSVARLLDPEDVP------SLRTLVLGGEALTQSDVDTWADR-----VRLINAYGPAECTIAATVSP 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  772 LVRAdlEDPRrrgVIGRPLAdLRVYVLDAA--GRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPF------GAP 843
Cdd:cd05918    259 VVPS--TDPR---NIGRPLG-ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGR 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  844 GTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV---PRAAEDGLTQLVAYAVPAEE 920
Cdd:cd05918    333 GRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvKPKDGSSSPQLVAFVVLDGS 412

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  921 GGADPAG-----------------LRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05918    413 SSGSGDGdslflepsdefralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 470-964 5.46e-119

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: 385.28  E-value: 5.46e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd17650     81 EDSGAKLLLTQ--------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHR 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTL-FHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAF 708
Cdd:cd17650    117 NVAHAAHAWRREYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALI 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  709 EQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGlDAPELVNMYGITETTVHVTFHRLVRADLEDPRRRGvIGR 788
Cdd:cd17650    197 RPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFG-QGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVP-IGR 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:cd17650    275 PLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRV 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPAGLRAHLAARLPAYMVPAACVLL 948
Cdd:cd17650    354 DHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAT--LNTAELRAFLAKELPSYMIPSYYVQL 431

                          490
                   ....*....|....*.
gi 1573930569  949 DALPLTANGKLDTAAL 964
Cdd:cd17650    432 DALPLTPNGKVDRRAL 447
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 458-966 5.58e-119

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: 385.32  E-value: 5.58e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTdtagsgrlpatdarvvvvddartvadlagraphdltdadragatgpydtAYVIHTSGS 617
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-------------------------------------------------ALILYTSGT 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  618 TGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFdfsVWELWGPLLHGGRLVVVPyevSRSPREFLRLL 693
Cdd:COG0318    112 TGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLP---RFDPERVLELI 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVHVTfhrlV 773
Cdd:COG0318    186 ERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVT----V 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  774 RADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFlPDPFgapgtrmYRSGDL 853
Cdd:COG0318    259 NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDL 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLA 933
Cdd:COG0318    331 GRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLR 410

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAALPA 966
Cdd:COG0318    411 ERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
AMP-binding pfam00501
AMP-binding enzyme;
462-875 7.29e-113

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 366.25  E-value: 7.29e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARVAESPGRTAVS-YAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGH 540
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  541 PAERLALVMADAEPVAVVTDTAGS--------GRLPATDARVVV-VDDARTVADLAGRAPHDLTDADRAGATGPYDTAYV 611
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVLdRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  612 IHTSGSTGRPKGVPVPHAHVVR----LFEASGEHFRFGADDVWTLFHSYAFDFSV-WELWGPLLHGGRLVVVPYEVSRSP 686
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVH 766
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 VTFHRLvraDLEDPRRRGVIGRPLADLRVYVLDAA-GRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgt 845
Cdd:pfam00501  318 VTTPLP---LDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------- 387

                          410       420       430
                   ....*....|....*....|....*....|
gi 1573930569  846 RMYRSGDLARWRPDGTLVHAGRADQQVKIR 875
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 460-964 5.62e-110

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: 358.55  E-value: 5.62e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAgsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTG 619
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTDS------------------------------------------PDDLAYIIFTSGSTG 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVvpyevSRSPREFLRLLDEekVT 699
Cdd:cd17653    119 IPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL-----ADPSDPFAHVART--VD 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  700 VLNQTPSAFEQLVLADAAtdratgSLRYVVLGGEALVAERLRPWADRhgldaPELVNMYGITETTVHVTFHRLvradleD 779
Cdd:cd17653    192 ALMSTPSILSTLSPQDFP------NLKTIFLGGEAVPPSLLDRWSPG-----RRLYNAYGPTECTISSTMTEL------L 254

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 PRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGaPGTRMYRSGDLARWRPD 859
Cdd:cd17653    255 PGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTED 333

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  860 GTLVHAGRADQQVKIRGFRIEPGEIEA-VLTAHPAVAGGAVVprAAEDgltQLVAYAVPAeegGADPAGLRAHLAARLPA 938
Cdd:cd17653    334 GGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI--VVNG---RLVAFVTPE---TVDVDGLRSELAKHLPS 405

                          490       500
                   ....*....|....*....|....*.
gi 1573930569  939 YMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd17653    406 YAVPDRIIALDSFPLTANGKVDRKAL 431
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 460-965 3.56e-109

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: 356.48  E-value: 3.56e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd17645      2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDtagsgrlpatdarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTG 619
Cdd:cd17645     82 YPGERIAYMLADSSAKILLTN--------------------------------------------PDDLAYVIYTSGSTG 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVT 699
Cdd:cd17645    118 LPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  700 VLNQTPSAFEQLVLADaatdraTGSLRYVVLGGEALVAERLRPWadrhgldapELVNMYGITETTVHVTfhrlvRADLED 779
Cdd:cd17645    198 ISFLPTGAAEQFMQLD------NQSLRVLLTGGDKLKKIERKGY---------KLVNNYGPTENTVVAT-----SFEIDK 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 PRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPD 859
Cdd:cd17645    258 PYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPD 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  860 GTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPAGLRAHLAARLPAY 939
Cdd:cd17645    337 GNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEE--IPHEELREWLKNDLPDY 414

                          490       500
                   ....*....|....*....|....*.
gi 1573930569  940 MVPAACVLLDALPLTANGKLDTAALP 965
Cdd:cd17645    415 MIPTYFVHLKALPLTANGKVDRKALP 440
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1055-2529 2.63e-107

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: 377.27  E-value: 2.63e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1055 DAGRPLPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDG 1134
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1135 AIHQRVLPPGTLRPELHVVD-----CPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTRTLLLV-LHHSAADGWSLR 1208
Cdd:COG1020     81 RPVQVIQPVVAAPLPVVVLLvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLaLHHIISDGLSDG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1209 PLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLAPapegpGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPS 1288
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQG-----EELARQLAYWRQQLAGLPPLLELPTDRPRPAVQS 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1289 GRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRAD 1368
Cdd:COG1020    236 YRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVD 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1369 ASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRVPLRPAATGTAK 1448
Cdd:COG1020    316 LSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAK 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1449 FDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADPEVRTGALPRAdrpspatadttaraga 1528
Cdd:COG1020    396 FDLTLTVVE------TGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLL---------------- 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1529 ltravlevpgvgdavvlpgPDGEPATVYVVPNRAGAADRTEQVVSSLapgtrvvaisglprtaeggldegalkdlpVIDQ 1608
Cdd:COG1020    454 -------------------TAAERQQLLAEWNATAAPYPADATLHEL-----------------------------FEAQ 485

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1609 VaagawrerlarlpgvreaevvleevpeelerrhvgrpraaggAAEPDApsverpasvPALSEGpalpepsvsgwaeall 1688
Cdd:COG1020    486 A------------------------------------------ARTPDA---------VAVVFG---------------- 498

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 raagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL--TV 1766
Cdd:COG1020    499 ------------------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLdpAY 560

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1767 PVsyattsaavsklEGIWEMLDR---PWIVTSAAGEPGLRELAARRewsgLRLTTAdALREEPEDRDWYEARPDDLVLML 1843
Cdd:COG1020    561 PA------------ERLAYMLEDagaRLVLTQSALAARLPELGVPV----LALDAL-ALAAEPATNPPVPVTPDDLAYVI 623

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1844 MTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVmfhlrDVYL----GCRqIHAPTSWILEDP 1919
Cdd:COG1020    624 YTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVW-----EIFGallsGAT-LVLAPPEARRDP 697

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1920 VRWPELADRHRVSVTWAPNFAFGLLAEQAHRfqdrdwDLSPVRLVMNAGEVVVASAARRFLHVlapfgLPQDVMHPGWGM 1999
Cdd:COG1020    698 AALAELLARHRVTVLNLTPSLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGP 766

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2000 SETCSVVTDSVLasEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW 2079
Cdd:COG1020    767 TETTVDSTYYEV--TPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF 844

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2080 FD-------TGDLA-FLRDGELYITGRAKDVIIVNGvnhysH-----EIEACVEELPSVVRsftAAVAVRSDASAATdEL 2146
Cdd:COG1020    845 GFpgarlyrTGDLArWLPDGNLEFLGRADDQVKIRG-----FrielgEIEAALLQHPGVRE---AVVVAREDAPGDK-RL 915

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2147 ALFLRLAPGQDPAGALREIAGKVTREIGVSPAFLipVEAEAIPKTEIGKIQRTKLRKSFEAGEFDGAVRETQLLLGTAAT 2226
Cdd:COG1020    916 VAYVVPEAGAAAAAALLRLALALLLPPYMVPAAV--VLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAAL 993

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2227 VPDWFLHPLWRPAENLHAATLPAGHRVLVLAG------------PAPHAHAVAEEVAGAVRDAGGLCTVVTEGPAPERNG 2294
Cdd:COG1020    994 ALLLLLVVVVGDDDFFFFGGGLGLLLLLALARaarlllllllllLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP 1073

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2295 AAAYRVRPGEAGDLAAVLERLEADGRTPDTVVHLAATEDAEDGAAPGSDVSLLVLAQALAGRTGGERPVDLLFVTAGAQA 2374
Cdd:COG1020   1074 PLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAAL 1153

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2375 VTPEERPTASHAAAGALLKSLREELPWLRGVHLDLSGGSAGDRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAP 2454
Cdd:COG1020   1154 LALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLA 1233

                         1450      1460      1470      1480      1490      1500      1510
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2455 RTAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERHLADAGPASSRIEAFRRLRGL 2529
Cdd:COG1020   1234 LALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLA 1308
PRK05691 PRK05691
peptide synthase; Validated
 6-1048 1.10e-106

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 384.91  E-value: 1.10e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    6 DDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVreADTFALRFLDTPDGPRAVRD--GDPDE 83
Cdd:PRK05691  3255 EDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVV--ARHEALRASFSWNAGETMLQviHKPGR 3332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   84 MPVHRVDVSGEADPAAAA--EEWIRRDLATPVDVAAGPLFSHALLTLAPDRFiWFLRA-HHILLDGYSYKLVARRLADTY 160
Cdd:PRK05691  3333 TPIDYLDWRGLPEDGQEQrlQALHKQEREAGFDLLNQPPFHLRLIRVDEARY-WFMMSnHHILIDAWCRSLLMNDFFEIY 3411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  161 TALAAGEE---PPPAGFEsadrlaaEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLtdrtaPPRAPFLRRTA-------- 229
Cdd:PRK05691  3412 TALGEGREaqlPVPPRYR-------DYIGWLQRQDLAQARQWWQDNLRGFERPTPI-----PSDRPFLREHAgdsggmvv 3479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  230 -----VLSPAETRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGS--AALRTPGTASDILPLRVAa 302
Cdd:PRK05691  3480 gdcytRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVQ- 3558

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  303 sadTPVGGFVRAVADDLRGLRAHQRHRGEsirrdlgvlgrgrRVHGPVVNI-----VP-----FSEDLTFGGHP------ 366
Cdd:PRK05691  3559 ---LPAAGQRCSVRQWLQGLLDSNMELRE-------------YEYLPLVAIqecseLPkgqplFDSLFVFENAPvevsvl 3622

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  367 STSHHL-----SGGAVDDLQISV--RPGAEADtLWLAFDAHpdLYEEDGLALFLERFLKVLREL----RTCPEELPL--- 432
Cdd:PRK05691  3623 DRAQSLnassdSGRTHTNFPLTAvcYPGDDLG-LHLSYDQR--YFDAPTVERLLGEFKRLLLALvqgfHGDLSELPLlge 3699

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  433 GETPVLLPGEEPVRRDEPaprVTRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALA 512
Cdd:PRK05691  3700 QERDFLLDGCNRSERDYP---LEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALL 3776

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  513 LPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLalvmadaepvavvTDTAGSGRLPATDARVVVVDDARTVADLAGRAPH 592
Cdd:PRK05691  3777 AERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRL-------------QRIIELSRTPVLVCSAACREQARALLDELGCANR 3843

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  593 ------------DLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDF 660
Cdd:PRK05691  3844 prllvweevqagEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDI 3923

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  661 SVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAAtdrATGSLRYVVLGGEALVAERL 740
Cdd:PRK05691  3924 SVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQ---ALDGLRWMLPTGEAMPPELA 4000

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  741 RPWADRHgldaPE--LVNMYGITETTVHVTFHRLvraDLEDPRRRGV-IGRPLADLRVYVLDAAGRPVPPGATGEMYVSG 817
Cdd:PRK05691  4001 RQWLQRY----PQigLVNAYGPAECSDDVAFFRV---DLASTRGSYLpIGSPTDNNRLYLLDEALELVPLGAVGELCVAG 4073

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  818 PGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGG 897
Cdd:PRK05691  4074 TGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA 4153

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  898 AVVPRAAEDGlTQLVAYAVPAEEGGADPAGL---RAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTG 974
Cdd:PRK05691  4154 AVAVQEGVNG-KHLVGYLVPHQTVLAQGALLeriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQS 4232

                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  975 GAPPATPE--ERLVCGLFEEVLRlpADSVGTGGNFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAE 1048
Cdd:PRK05691  4233 QAYLAPRNelEQTLATIWADVLK--VERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAE 4306
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 469-965 2.70e-105

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: 347.15  E-value: 2.70e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  469 SPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTDTAGSGRLPATDARVVVVDDartvadlagraphDLTDADRAGATGPY---DTAYVIHTSGSTGRPKGVP 625
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDP-------------SISQEDTSNIDYINnsdDLLYIIYTSGTTGKPKGVQ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  626 VPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNqTP 705
Cdd:cd17656    148 LEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 SAFEQLV--LADAATDRATGsLRYVVLGGEAL-VAERLRPWADRHGLdapELVNMYGITETTVHVTFhrlvRADLEDPRR 782
Cdd:cd17656    227 VAFLKFIfsEREFINRFPTC-VKHIITAGEQLvITNEFKEMLHEHNV---HLHNHYGPSETHVVTTY----TINPEAEIP 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  783 R-GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPDGT 861
Cdd:cd17656    299 ElPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGN 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  862 LVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPAGLRAHLAARLPAYMV 941
Cdd:cd17656    378 IEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE--LNISQLREYLAKQLPEYMI 455

                          490       500
                   ....*....|....*....|....
gi 1573930569  942 PAACVLLDALPLTANGKLDTAALP 965
Cdd:cd17656    456 PSFFVPLDQLPLTPNGKVDRKALP 479
PRK05691 PRK05691
peptide synthase; Validated
 457-2201 2.03e-100

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 364.49  E-value: 2.03e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGET------LSYAELNAEANRLARLLVEQgAGPGRFVALALPRGPRLVPALLAVLKTG 530
Cdd:PRK05691    10 TLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  531 AAYLPLDPG-----HPAERLALVMADAEPVAVVTDTAGSGRLPATDArvVVVDDARTVADLAGRAPhDLTDADRAGATGP 605
Cdd:PRK05691    89 VIAVPAYPPesarrHHQERLLSIIADAEPRLLLTVADLRDSLLQMEE--LAAANAPELLCVDTLDP-ALAEAWQEPALQP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  606 YDTAYVIHTSGSTGRPKGVPVPHAHVV--RLFEASGEHFRFGADDV---W-TLFHSYAFdfsVWELWGPLLHGGRLVVVP 679
Cdd:PRK05691   166 DDIAFLQYTSGSTALPKGVQVSHGNLVanEQLIRHGFGIDLNPDDVivsWlPLYHDMGL---IGGLLQPIFSGVPCVLMS 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  680 --YEVSRsPREFLRLLDEEKVTVLNQTPSAFEQLV--LADAATDRATGS-LRYVVLGGEALVAERLRPWADRH---GLDA 751
Cdd:PRK05691   243 paYFLER-PLRWLEAISEYGGTISGGPDFAYRLCSerVSESALERLDLSrWRVAYSGSEPIRQDSLERFAEKFaacGFDP 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  752 PELVNMYGITETTVHVTFHR------LVRADLE-------DPRRRGVI---GRPLADLRVYVLDAA-GRPVPPGATGEMY 814
Cdd:PRK05691   322 DSFFASYGLAEATLFVSGGRrgqgipALELDAEalarnraEPGTGSVLmscGRSQPGHAVLIVDPQsLEVLGDNRVGEIW 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  815 VSGPGVAPGYLNRPELTEERFLPdpfgAPGTRMYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAH-PA 893
Cdd:PRK05691   402 ASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREvEV 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  894 VAGGAVVPRAAEDG----------LTQLVAYAVPAEeggadpAGLRAHLAARLPAYM-VPAACVLLD--ALPLTANGKLD 960
Cdd:PRK05691   477 VRKGRVAAFAVNHQgeegigiaaeISRSVQKILPPQ------ALIKSIRQAVAEACQeAPSVVLLLNpgALPKTSSGKLQ 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  961 TAA---------------LPAPDFGGGTGGAPPATPEERLVCGLFEEVLRlpADSVGTGGNFFDLGGHSLLATRLLARLR 1025
Cdd:PRK05691   551 RSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLK--VEQVAADDHFFLLGGNSIAATQVVARLR 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1026 ERTGTDVPISALFDTPTPAALAERLTAG-ADAGRPLPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRH 1104
Cdd:PRK05691   629 DELGIDLNLRQLFEAPTLAAFSAAVARQlAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRG 708

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1105 PLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrpELHVVDC---PDEERAAHVA----AAMRRSFDLTRD 1177
Cdd:PRK05691   709 ELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEF--ALQRIDLsdlPEAEREARAAqireEEARQPFDLEKG 786

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1178 SALWAGVFGTGDTRTLLLV-LHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApapegPGR 1256
Cdd:PRK05691   787 PLLRVTLVRLDDEEHQLLVtLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLA-----QGE 861

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1257 LERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGD 1336
Cdd:PRK05691   862 AARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQG 941

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1337 DIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRhpaRHPLF 1416
Cdd:PRK05691   942 DIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR---EQGLF 1018

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1417 QVMLALQNNERAVLTlgedRVP-----LRPAATGTAKFDlfvdvLERHGADGTADGLDLHVEYAADLYDPATAERFAGAL 1491
Cdd:PRK05691  1019 QVMFNHQQRDLSALR----RLPgllaeELPWHSREAKFD-----LQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHF 1089

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1492 RDLLTVVCADPEVrtgalpradrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragaadrteqv 1571
Cdd:PRK05691  1090 LALLEQVCEDPQR------------------------------------------------------------------- 1102

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1572 vsslapgtrvvaisglprtaeggldegALKDLPVIDQvaagAWRERLArlpgvreaevvleevpeelerrhvgrpraagg 1651
Cdd:PRK05691  1103 ---------------------------ALGDVQLLDA----AERAQLA-------------------------------- 1119

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1652 aaepdapsverpasvpALSEGPALPEPSvsgWAEALLRAAGRPDGEVVHVRADGSETrrSYASLVPEASRVLAGLRRRGL 1731
Cdd:PRK05691  1120 ----------------QWGQAPCAPAQA---WLPELLNEQARQTPERIALVWDGGSL--DYAELHAQANRLAHYLRDKGV 1178

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1732 RPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVP-----VSYATTSAAVSKLEGIWEMLDRpwiVTSAAGEpglrela 1806
Cdd:PRK05691  1179 GPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDypaerLAYMLADSGVELLLTQSHLLER---LPQAEGV------- 1248

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1807 arrewSGLRLTTADaLREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIP 1886
Cdd:PRK05691  1249 -----SAIALDSLH-LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAP 1322

                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1887 LDHVTGVVMFHLrDVYLGCRQIHAPTSWiLEDPVRWPELADRHRVSVTwapNFAFGLLaeQAHRFQDRDWDLSPVRLVMN 1966
Cdd:PRK05691  1323 ISFDVSVWECFW-PLITGCRLVLAGPGE-HRDPQRIAELVQQYGVTTL---HFVPPLL--QLFIDEPLAAACTSLRRLFS 1395

                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1967 AGEVVVASAARRFLHVlapfgLPQDVMHPGWGMSETCSVVTDSVLASEapdhDEAFVSCGLPYPGFAMRVVDDQDALLPE 2046
Cdd:PRK05691  1396 GGEALPAELRNRVLQR-----LPQVQLHNRYGPTETAINVTHWQCQAE----DGERSPIGRPLGNVLCRVLDAELNLLPP 1466

                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2047 GDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEAC 2118
Cdd:PRK05691  1467 GVAGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRArWNADGALEYLGRLDQQVKLRGFRVEPEEIQAR 1546

                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2119 VEELPSVVRsftAAVAVRSDASAAtdELALFLRLAPGQD-PAGALREIAGKVTREIGVsPAFLIPVeaEAIPKTEIGKIQ 2197
Cdd:PRK05691  1547 LLAQPGVAQ---AAVLVREGAAGA--QLVGYYTGEAGQEaEAERLKAALAAELPEYMV-PAQLIRL--DQMPLGPSGKLD 1618


                   ....
gi 1573930569 2198 RTKL 2201
Cdd:PRK05691  1619 RRAL 1622
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 1689-2207 1.04e-97

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: 327.66  E-value: 1.04e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPD-GEVVHVRADGSETRR-SYASLVPEASRVLAGLRRRGlRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTV 1766
Cdd:cd05931      2 RAAARPDrPAYTFLDDEGGREETlTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1767 PVSYATtsaaVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRDW--YEARPDDLVLMLM 1844
Cdd:cd05931     81 PTPGRH----AERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWppPSPDPDDIAYLQY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1845 TSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWILEDPVRWPE 1924
Cdd:cd05931    157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLR 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1925 LADRHRVSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSETCS 2004
Cdd:cd05931    237 LISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATL 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2005 VVT--------------------DSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQD-ALLPEGDVGRLQVRGTSVTHGY 2063
Cdd:cd05931    317 FVSggppgtgpvvlrvdrdalagRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGY 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2064 HDNARANAESF------TEDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRS 2137
Cdd:cd05931    397 WGRPEATAETFgalaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALR--PGCVAAFS 474

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2138 DASAATDELALFLRLAPGQ---DPAGALREIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:cd05931    475 VPDDGEERLVVVAEVERGAdpaDLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1068-1502 1.21e-91

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: 305.94  E-value: 1.21e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1068 RPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLR 1147
Cdd:cd19546      1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1148 PELHVVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDT-RTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAA 1226
Cdd:cd19546     81 PELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTeHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1227 PDWAPPALQYADFALWQRRVLAPAPEGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHREL 1306
Cdd:cd19546    161 PERAPLPLQFADYALWERELLAGEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1307 LRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRT-EPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAF 1385
Cdd:cd19546    241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1386 DVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNER------AVLTLGEDRVPLRPAATGtakFDLFVDVLERH 1459
Cdd:cd19546    321 VREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNdpwdapELPGLRTSPVPLGTEAME---LDLSLALTERR 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1573930569 1460 GADGTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19546    398 NDDGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 1698-2210 3.77e-91

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: 306.72  E-value: 3.77e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1698 VVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPltvpVSYATTSAAV 1777
Cdd:cd05908      4 IIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVP----VSIGSNEEHK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1778 SKLEGIWEMLDRPWIVTSaagepglrelaarrewsglrlttadalrEEPEDRDwyearPDDLVLMLMTSGSTGLPKAVRL 1857
Cdd:cd05908     80 LKLNKVWNTLKNPYLITE----------------------------EEVLCEL-----ADELAFIQFSSGSTGDPKGVML 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1858 THRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWILEDPVRWPELADRHRVSVTWAP 1937
Cdd:cd05908    127 THENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSP 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1938 NFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSETCSVVTDSVLASE--A 2015
Cdd:cd05908    207 NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPKAQSPfkT 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2016 PDHDEAFVSCGLPYP---------------GFAM-----RVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFT 2075
Cdd:cd05908    287 ITLGRRHVTHGEPEPevdkkdsecltfvevGKPIdetdiRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFT 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2076 EDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAVrSDASAATDELALFLRLAPG 2155
Cdd:cd05908    367 DDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGV-NNSNTRNEEIFCFIEHRKS 445

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 2156 QDPAGAL-REIAGKVTREIGVSPAFLIPVeaEAIPKTEIGKIQRTKLRKSFEAGEF 2210
Cdd:cd05908    446 EDDFYPLgKKIKKHLNKRGGWQINEVLPI--RRIPKTTSGKVKRYELAQRYQSGEF 499
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1684-2212 4.10e-91

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: 304.81  E-value: 4.10e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAGR-PDGEVVHVRadgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:COG0318      2 ADLLRRAAARhPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 PltVPVSYattsaavsklegiwemldrpwivtsaagepGLRELAARrewsgLRLTTADALreepedrdwyearpddLVLM 1842
Cdd:COG0318     78 P--LNPRL------------------------------TAEELAYI-----LEDSGARAL----------------VTAL 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1843 LM-TSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTswilEDPVR 1921
Cdd:COG0318    105 ILyTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR----FDPER 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1922 WPELADRHRVSV-TWAPNFAFGLLAEQahrfQDRDWDLSPVRLVMNAGEVVVASAARRFLHVlapFGLPqdvMHPGWGMS 2000
Cdd:COG0318    181 VLELIERERVTVlFGVPTMLARLLRHP----EFARYDLSSLRLVVSGGAPLPPELLERFEER---FGVR---IVEGYGLT 250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2001 ETCSVVTdsvlASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWF 2080
Cdd:COG0318    251 ETSPVVT----VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWL 325

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2081 DTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASaaTDELALFLRLAPGQDP- 2158
Cdd:COG0318    326 RTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEA--AVVGVPDEKW--GERVVAFVVLRPGAELd 401

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2159 AGALRE-IAGKVtreigvsPAFLIPVE---AEAIPKTEIGKIQRTKLRKSFEAGEFDG 2212
Cdd:COG0318    402 AEELRAfLRERL-------ARYKVPRRvefVDELPRTASGKIDRRALRERYAAGALEA 452
PRK12467 PRK12467
peptide synthase; Provisional
 1060-2203 2.63e-83

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 307.86  E-value: 2.63e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1060 LPALTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQR 1139
Cdd:PRK12467    38 LPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQV 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1140 VLPPgtLRPELHVVDCPDEERA-------AHVAAAMRRSFDLTRDSALWAGVFG-TGDTRTLLLVLHHSAADGWSLRPLA 1211
Cdd:PRK12467   118 IDAS--LSLTIPLDDLANEQGRaresqieAYINEEVARPFDLANGPLLRVRLLRlADDEHVLVVTLHHIISDGWSMRVLV 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1212 DDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLApapegPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRG 1291
Cdd:PRK12467   196 EELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLE-----AGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRG 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1292 GGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASG 1371
Cdd:PRK12467   271 ARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDP 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1372 DPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQN-----NERAVLTLGEDRVPLRPAATGT 1446
Cdd:PRK12467   351 QASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNtatggRDREGAQLPGLTVEELSWARHT 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1447 AKFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADPEVRTGALPRAdrpspatadttara 1526
Cdd:PRK12467   431 AQFDLALDTYE------SAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLL-------------- 490

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1527 galtravlevpgvgdavvlpgpDGEPATVYVVPNRAGAADRTEQVVSSLapgtrvvaisglprtaeggldegalkdlpvi 1606
Cdd:PRK12467   491 ----------------------DAEERARELVRWNAPATEYAPDCVHQL------------------------------- 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1607 dqvaagaWRERLARLPGVreaevvleevpeelerrhvgrpraaggaaepdapsverpasvPALSEGpalpepsvsgwaea 1686
Cdd:PRK12467   518 -------IEAQARQHPER------------------------------------------PALVFG-------------- 534

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1687 llraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL-- 1764
Cdd:PRK12467   535 --------------------EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLdp 594

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 TVPVsyattsaavsklEGIWEMLDrpwivtsaagEPGLRELAARREWSGlRLTTADALREEP--EDRDWYEAR------- 1835
Cdd:PRK12467   595 EYPQ------------DRLAYMLD----------DSGVRLLLTQSHLLA-QLPVPAGLRSLCldEPADLLCGYsghnpev 651

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 ---PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMF-----HLRDVYLGCRQ 1907
Cdd:PRK12467   652 aldPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELfgalaSGATLHLLPPD 731

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 IHaptswilEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRdwdlsPVRLVMNAGEVVVASAARRFLHVlapfg 1987
Cdd:PRK12467   732 CA-------RDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-----PQRALVCGGEALQVDLLARVRAL----- 794

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1988 LPQDVMHPGWGMSETCSVVTDSVLASEAPDHDEAFVscGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNA 2067
Cdd:PRK12467   795 GPGARLINHYGPTETTVGVSTYELSDEERDFGNVPI--GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRP 872

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2068 RANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAVRSDA 2139
Cdd:PRK12467   873 ALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL 952

                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2140 SaatdelaLFLRLAPGQDPAGALREIAGKVTREI--GVSPAFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK12467   953 Q-------LVAYLVPAAVADGAEHQATRDELKAQlrQVLPDYMVPahlLLLDSLPLTPNGKLDRKALPK 1014
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1071-1502 2.39e-81

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: 275.80  E-value: 2.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1071 LVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIH-QRVLPPGTLRPE 1149
Cdd:cd19539      1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPrQEILPPGPAPLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1150 LHVVDCPDEERAAHVAAAMRRS----FDLTRDSALWAGVFGTGDTRT-LLLVLHHSAADGWSLRPLADDLGTAYAARRAG 1224
Cdd:cd19539     81 VRDLSDPDSDRERRLEELLREResrgFDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1225 AAPDWAPPALQYADFALWQRRVLApAPegpgRLERLTSFWRQALDGLpeESAPPPDRPRPAAPSGRGGGVTV-PLDAGTH 1303
Cdd:cd19539    161 PAAPLPELRQQYKEYAAWQREALA-AP----RAAELLDFWRRRLRGA--EPTALPTDRPRPAGFPYPGADLRfELDAELV 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1304 RELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVR 1383
Cdd:cd19539    234 AALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1384 AFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQN---NERAVLTLGEDRVPLRPaaTGTAKFDLFVDVLErhg 1460
Cdd:cd19539    314 KALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNapaGELELAGGLSYTEGSDI--PDGAKFDLNLTVTE--- 388

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1573930569 1461 adgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19539    389 ---EGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 607-960 8.47e-81

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: 270.70  E-value: 8.47e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPyevSRSP 686
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVH 766
Cdd:cd04433     78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTETGGT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 VTFhrlVRADlEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFlpdpfgapGTR 846
Cdd:cd04433    155 VAT---GPPD-DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDG 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  847 MYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPA 926
Cdd:cd04433    223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE 302

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1573930569  927 GLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd04433    303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
PRK12316 PRK12316
peptide synthase; Provisional
 1059-2201 2.04e-80

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 298.41  E-value: 2.04e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1059 PLPALTASERPSlvPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQ 1138
Cdd:PRK12316    39 PIPAGVSSAERD--RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLA 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1139 RVLPPGTLrpELHVVDC---PDEERAAHVAAAMRRS----FDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPL 1210
Cdd:PRK12316   117 QVPLDRPL--EVEFEDCsglPEAEQEARLRDEAQREslqpFDLCEGPLLRVRLLRLGEEEhVLLLTLHHIVSDGWSMNVL 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1211 ADDLGTAYAARRAGAAPDWAPPALQYADFALWQRRVLAPapegpGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGR 1290
Cdd:PRK12316   195 IEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEA-----GEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYR 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1291 GGGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADAS 1370
Cdd:PRK12316   270 GSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFD 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1371 GDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQN---NERAVLTLGEDRVPLRPAATGTA 1447
Cdd:PRK12316   350 GRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPlvaDIEALDTVAGLEFGQLEWKSRTT 429

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1448 KFDLFVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADPEVRTGALPRADrpspatadttarag 1527
Cdd:PRK12316   430 QFDLTLDTYE------KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLD-------------- 489

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1528 altravlevpgvgdavvlpgpdgepatvyvvpnragAADRTEQVvsslapgtrvvaiSGLPRTAEGGLDEGALKDLpvid 1607
Cdd:PRK12316   490 ------------------------------------AEERGQLV-------------EGWNATAAEYPLQRGVHRL---- 516

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1608 qvaagaWRERLARLPGVreaevvleevpeelerrhvgrpraaggaaepdapsverpasvPALSEGpalpepsvsgwaeal 1687
Cdd:PRK12316   517 ------FEEQVERTPEA------------------------------------------PALAFG--------------- 533

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1688 lraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvP 1767
Cdd:PRK12316   534 -------------------EETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD-P 593

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1768 VSYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLrlttaDALREEPEDRdwyEARPDDLVLMLMTSG 1847
Cdd:PRK12316   594 EYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWL-----EGYSEENPGT---ELNPENLAYVIYTSG 665

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1848 STGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLrDVYLGCRQIHAPTSwILEDPVRWPELAD 1927
Cdd:PRK12316   666 STGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAPG-DHRDPAKLVELIN 743

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1928 RHRVSVTwapNFAFGLLaeQAHRFQDRDWDLSPVRLVMNAGEVVVASAarrflhVLAPFG-LPQDVMHPGWGMSETCSVV 2006
Cdd:PRK12316   744 REGVDTL---HFVPSML--QAFLQDEDVASCTSLRRIVCSGEALPADA------QEQVFAkLPQAGLYNLYGPTEAAIDV 812

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2007 TDSVLASEAPDHdeafVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFD----- 2081
Cdd:PRK12316   813 THWTCVEEGGDS----VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAgermy 888

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2082 -TGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSvvrsftaavaVRSDASAATDELALFLRLAPgQDPA 2159
Cdd:PRK12316   889 rTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW----------VREAAVLAVDGKQLVGYVVL-ESEG 957

                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2160 GALREIAGKVTREigVSPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:PRK12316   958 GDWREALKAHLAA--SLPEYMVPaqwLALERLPLTPNGKLDRKAL 1000
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
461-959 5.16e-79

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 273.91  E-value: 5.16e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  461 LFEARVAESPGRTAVSYAGE-----TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:COG0365     14 CLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDTAGSGR------LPATDA---------RVVVVDDARTVADLAGraPHDLTDA-DR 599
Cdd:COG0365     94 VFPGFGAEALADRIEDAEAKVLITADGGLRGgkvidlKEKVDEaleelpsleHVIVVGRTGADVPMEG--DLDWDELlAA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  600 AGATGPY------DTAYVIHTSGSTGRPKGVPvpHAHVVRLFEASGE---HFRFGADDV--------WTLFHSYAfdfsv 662
Cdd:COG0365    172 ASAEFEPeptdadDPLFILYTSGTTGKPKGVV--HTHGGYLVHAATTakyVLDLKPGDVfwctadigWATGHSYI----- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  663 weLWGPLLHGGRLVVvpYE---VSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLAD--AATDRATGSLRYVVLGGEALVA 737
Cdd:COG0365    245 --VYGPLLNGATVVL--YEgrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdePLKKYDLSSLRLLGSAGEPLNP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  738 ERLRPWADRHGLdapELVNMYGITETTVHVTFHRLVradleDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSG 817
Cdd:COG0365    321 EVWEWWYEAVGV---PIVDGWGQTETGGIFISNLPG-----LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  818 --PGVAPGYLNRPELTEERFLPDPFGapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVA 895
Cdd:COG0365    393 pwPGMFRGYWNDPERYRETYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  896 GGAVVPRAAEDGLTQLVAYAVPAEEGGADPA---GLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:COG0365    468 EAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1072-1505 6.93e-79

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: 269.59  E-value: 6.93e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFG-EEDGAIHQRVLPpgtLRP-E 1149
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILE---ERPfE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1150 LHVVDCPDEERAA---HVAAAMRR----SFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAAR 1221
Cdd:pfam00668   82 LEIIDISDLSESEeeeAIEAFIQRdlqsPFDLEKGPLFRAGLFRIAENRhHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1222 RAGAAPDwAPPALQYADFALWQRRVLAPApegpgRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAG 1301
Cdd:pfam00668  162 LKGEPLP-LPPKTPYKDYAEWLQQYLQSE-----DYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDED 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1302 THRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLAR 1381
Cdd:pfam00668  236 TEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1382 VRAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQN----------NERAVLTLGedrvpLRPAATGTAKFDL 1451
Cdd:pfam00668  316 VQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNylgqdsqeeeFQLSELDLS-----VSSVIEEEAKYDL 390

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 1452 FVDVLERHGadgtadGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADPEVR 1505
Cdd:pfam00668  391 SLTASERGG------GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
468-964 2.01e-76

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 264.45  E-value: 2.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  468 ESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLAL 547
Cdd:PRK04813    14 TQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEM 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  548 VMADAEPvAVVTDTAGsgrLPATDARVVVVddarTVADLAgRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVP 627
Cdd:PRK04813    94 IIEVAKP-SLIIATEE---LPLEILGIPVI----TLDELK-DIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQIS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  628 HAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSa 707
Cdd:PRK04813   165 HDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPS- 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  708 FEQLVLADAATDRAT-GSLRYVVLGGEAL---VAERLR---PWAdrhgldapELVNMYGITETTVHVTFHRLVRADLED- 779
Cdd:PRK04813   244 FADMCLLDPSFNEEHlPNLTHFLFCGEELphkTAKKLLerfPSA--------TIYNTYGPTEATVAVTSIEITDEMLDQy 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  780 ---PrrrgvIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFlpdpFGAPGTRMYRSGDLARW 856
Cdd:PRK04813   316 krlP-----IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYL 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  857 rPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGL----RAHL 932
Cdd:PRK04813   387 -EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELtkaiKKEL 465

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1573930569  933 AARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK04813   466 KERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 200-1080 3.92e-74

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: 274.63  E-value: 3.92e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  200 WTERLAGLPEPVRLTDRTAPPRAPFLRRTavlspaETRALDEAAKGMGVARTD--LLVAAVAAFLHRMTGADDLVLGLAT 277
Cdd:TIGR03443    2 WSERLDNPTLSVLPHDYLRPANNRLVEAT------YSLQLPSAEVTAGGGSTPfiILLAAFAALVYRLTGDEDIVLGTSS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  278 MSRLGSAALRTPGTASDILPLRVAASADTpvggFVRAVADD---LRGLRAHQRHRGESIRRDlgVLGRGRRVHGPvvniv 354
Cdd:TIGR03443   76 NKSGRPFVLRLNITPELSFLQLYAKVSEE----EKEGASDIgvpFDELSEHIQAAKKLERTP--PLFRLAFQDAP----- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  355 pfsedltfgghPSTSHHLSGGAVDDLQISVRPGAEADTLWLAFDAHpdLYEEDGLALFLERFLKVLRELRTCPEElPLGE 434
Cdd:TIGR03443  145 -----------DNQQTTYSTGSTTDLTVFLTPSSPELELSIYYNSL--LFSSDRITIVADQLAQLLSAASSNPDE-PIGK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  435 TPVLLPGEepvRRDEPAPrvTRTL---------PQLFEARVAESPGRTAV---------SYAGETLSYAELNAEANRLAR 496
Cdd:TIGR03443  211 VSLITPSQ---KSLLPDP--TKDLdwsgfrgaiHDIFADNAEKHPDRTCVvetpsfldpSSKTRSFTYKQINEASNILAH 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  497 LLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVA-VVTDTAGS----------- 564
Cdd:TIGR03443  286 YLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRAlIVIEKAGTldqlvrdyidk 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  565 -----GRLPAtdarVVVVDDARTVAdlaGRAPHDLTD---------ADRAGAT-GPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:TIGR03443  366 elelrTEIPA----LALQDDGSLVG---GSLEGGETDvlapyqalkDTPTGVVvGPDSNPTLSFTSGSEGIPKGVLGRHF 438

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPsAFE 709
Cdd:TIGR03443  439 SLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTP-AMG 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADAATdrATGSLRYVVLGGEALVAE---RLRPWADRhgldaPELVNMYGITETTVHVTFHRlVRADLEDP----RR 782
Cdd:TIGR03443  518 QLLSAQATT--PIPSLHHAFFVGDILTKRdclRLQTLAEN-----VCIVNMYGTTETQRAVSYFE-IPSRSSDStflkNL 589

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  783 RGVI--GRPLADLRVYVLDAAGRPVP--PGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGT------------- 845
Cdd:TIGR03443  590 KDVMpaGKGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkper 669

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  846 --------RMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVP 917
Cdd:TIGR03443  670 efwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVP 749

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  918 AEEG-------GADPA---------GL----------RAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGG 971
Cdd:TIGR03443  750 QDKSdeleefkSEVDDeessdpvvkGLikyrklikdiREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQ 829

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  972 GTGGAPPATPE---------ERLVCGLFEEVLRLPADSVGTGGNFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPT 1042
Cdd:TIGR03443  830 LAAVAKNRSASaadeeftetEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909

                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 1043 PAALA---ERLTAG---ADAG--------RPLPALTASERPSLV---PASFAQER 1080
Cdd:TIGR03443  910 IKGFAkevDRLKKGeelADEGdseieeeeTVLELDYAKDAKTLVdslPKSYPSRK 964
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 458-964 1.22e-71

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: 249.02  E-value: 1.22e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAepvavvtdtagsgrlpatDARVVVVDDARTVAdLAGRAPHDLTDADRAGatgpyDTAYVIHTSGS 617
Cdd:cd05936     81 PLYTPRELEHILNDS------------------GAKALIVAVSFTDL-LAAGAPLGERVALTPE-----DVAVLQYTSGT 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  618 TGRPKGVPVPHAHVVRLFEASGEHF--RFGADDVWT----LFHSYAFDFSvweLWGPLLHGGRLVVVPyevSRSPREFLR 691
Cdd:cd05936    137 TGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLaalpLFHVFGLTVA---LLLPLALGATIVLIP---RFRPIGVLK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  692 LLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETTVHVTFHR 771
Cdd:cd05936    211 EIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP---IVEGYGLTETSPVVAVNP 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  772 lvradLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmyRSG 851
Cdd:cd05936    288 -----LDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTG 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  852 DLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDgltqLVAYAVPAEEGGADPAG 927
Cdd:cd05936    355 DIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvpdPYSGEA----VKAFVVLKEGASLTEEE 430

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1573930569  928 LRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05936    431 IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 1689-2206 1.52e-71

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 251.45  E-value: 1.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGevVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPV 1768
Cdd:PRK07768    11 NARTSPRG--MVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 SYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARrewsGLR-LTTADALREEPEDRdwYEARPDDLVLMLMTSG 1847
Cdd:PRK07768    89 PRTDLAVWAEDTLRVIGMIGAKAVVVGEPFLAAAPVLEEK----GIRvLTVADLLAADPIDP--VETGEDDLALMQLTSG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1848 STGLPKAVRLTHRNVLTRAAA-TEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWILEDPVRWPELA 1926
Cdd:PRK07768   163 STGSPKAVQITHGNLYANAEAmFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1927 DRHRVSVTWAPNFAFGLLAEQAHRFQDR-DWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSET--- 2002
Cdd:PRK07768   243 SKYRGTMTAAPNFAYALLARRLRRQAKPgAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEAtla 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2003 -------CSVVTDSVLASE----------APDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHD 2065
Cdd:PRK07768   323 vsfspcgAGLVVDEVDADLlaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLT 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2066 NARANAESfTEDGWFDTGDLAFLRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAATD 2144
Cdd:PRK07768   403 MDGFIPAQ-DADGWLDTGDLGYLTEeGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG--NAVAVRLDAGHSRE 479

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2145 ELALFLRLAPGQDPAGALR---EIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFE 2206
Cdd:PRK07768   480 GFAVAVESNAFEDPAEVRRirhQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELVT 544
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1838-2197 2.93e-70

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: 240.26  E-value: 2.93e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVtGVVMFHLRDVYLGCRQIHAPTSwile 1917
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKF---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1918 DPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfQDRDWDLSPVRLVMNAGEVVVASAARRFLhvlapfGLPQDVMHPGW 1997
Cdd:cd04433     76 DPEAALELIEREKVTILLGVPTLLARLLKAP---ESAGYDLSSLRALVSGGAPLPPELLERFE------EAPGIKLVNGY 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1998 GMSETCSVVTdsvlASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAEsFTED 2077
Cdd:cd04433    147 GLTETGGTVA----TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDED 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2078 GWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASaATDELALFLRLAPGQ 2156
Cdd:cd04433    222 GWYRTGDLGRLDeDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPDPE-WGERVVAVVVLRPGA 297

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1573930569 2157 DPagALREIAGKVTREIG--VSPAFLIPVeaEAIPKTEIGKIQ 2197
Cdd:cd04433    298 DL--DAEELRAHVRERLApyKVPRRVVFV--DALPRTASGKID 336
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 457-960 6.86e-69

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 242.78  E-value: 6.86e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL 536
Cdd:PRK06187     7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMADAEPVAVVTDTAGS-------GRLPATDARVVVVDDARTVADLAGRAPHDLTDA----DRAGATGP 605
Cdd:PRK06187    87 NIRLKPEEIAYILNDAEDRVVLVDSEFVpllaailPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAasdtFDFPDIDE 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  606 YDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAfdfsvwelWG----PLLHGGRLVV 677
Cdd:PRK06187   167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHA--------WGlpylALMAGAKQVI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  678 VPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNM 757
Cdd:PRK06187   239 PR---RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGID---LVQG 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  758 YGITETTVHVTFHRLVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPP--GATGEMYVSGPGVAPGYLNRPELTEERF 835
Cdd:PRK06187   313 YGMTETSPVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  836 LPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEdgltQL 911
Cdd:PRK06187   393 DGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvpdEKWGE----RP 460

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569  912 VAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:PRK06187   461 VAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 465-960 2.28e-68

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: 238.66  E-value: 2.28e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPghpaer 544
Cdd:cd17631      4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF------ 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  545 lalvmadaepvavvtdtagsgRLPATDARVVVVD-DARTVADlagraphdltdadragatgpyDTAYVIHTSGSTGRPKG 623
Cdd:cd17631     78 ---------------------RLTPPEVAYILADsGAKVLFD---------------------DLALLMYTSGTTGRPKG 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  624 VPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAFDFsvweLWGP-LLHGGRLVVVPyevSRSPREFLRLLDEEKV 698
Cdd:cd17631    116 AMLTHRNLLWNAVNALAALDLGPDDVLLvvapLFHIGGLGV----FTLPtLLRGGTVVILR---KFDPETVLDLIERHRV 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  699 TVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHgldaPELVNMYGITETTVHVTFhrLVRADLE 778
Cdd:cd17631    189 TSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARG----VKFVQGYGMTETSPGVTF--LSPEDHR 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 dpRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmyRSGDLARWRP 858
Cdd:cd17631    263 --RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDE 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPA 938
Cdd:cd17631    333 DGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLAR 412

                          490       500
                   ....*....|....*....|..
gi 1573930569  939 YMVPAACVLLDALPLTANGKLD 960
Cdd:cd17631    413 YKIPKSVEFVDALPRNATGKIL 434
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1073-1502 1.33e-67

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: 236.15  E-value: 1.33e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPgTLRPELHV 1152
Cdd:cd19066      3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDK-TVRFRIEI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1153 VD-----CPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTRTLLLVL-HHSAADGWSLRPLADDLgTAYAARRAGAA 1226
Cdd:cd19066     82 IDlrnlaDPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAiHHIIVDGGSFQILFEDI-SSVYDAAERQK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1227 PDWAPPALQYADFALWQRRVLapapeGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHREL 1306
Cdd:cd19066    161 PTLPPPVGSYADYAAWLEKQL-----ESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1307 LRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFD 1386
Cdd:cd19066    236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1387 VQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLG---EDRVPLRPaaTGTAKFDLfvdVLErhGADG 1463
Cdd:cd19066    316 REAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGgfiFTTPVYTS--SEGTVFDL---DLE--ASED 388

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1573930569 1464 TADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19066    389 PDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
AMP-binding pfam00501
AMP-binding enzyme;
1689-2105 1.96e-64

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 226.42  E-value: 1.96e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGEVVhvrADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP----- 1763
Cdd:pfam00501    4 QAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPlnprl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 ----LTVPVSYATTSAAVSKLEGIWEMLDRpwiVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRDWYEARPDDL 1839
Cdd:pfam00501   81 paeeLAYILEDSGAKVLITDDALKLEELLE---ALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1840 VLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMN----GLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRqIHAPTSWI 1915
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT-VVLPPGFP 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 LEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPfglpqdVMHP 1995
Cdd:pfam00501  237 ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP---KRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALVN 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1996 GWGMSETCSVVTDSVLAseaPDHDEAFVSCGLPYPGFAMRVVDDQD-ALLPEGDVGRLQVRGTSVTHGYHDNARANAESF 2074
Cdd:pfam00501  308 GYGLTETTGVVTTPLPL---DEDLRSLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF 384

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1573930569 2075 TEDGWFDTGDLA-FLRDGELYITGRAKDVIIV 2105
Cdd:pfam00501  385 DEDGWYRTGDLGrRDEDGYLEIVGRKKDQIKL 416
PRK09192 PRK09192
fatty acyl-AMP ligase;
1712-2210 3.04e-64

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 231.05  E-value: 3.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1712 YASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWEMLDRPW 1791
Cdd:PRK09192    52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIAQLRGMLASAQPAA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1792 IVTSAAGEPGLRELAARREwSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATeA 1871
Cdd:PRK09192   132 IITPDELLPWVNEATHGNP-LLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI-S 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1872 MNGL--GSGDVSLNWIPLDHVTGVVMFHLRDV-------YLgcrqihaPTSWILEDPVRWPELADRHRVSVTWAPNFAFG 1942
Cdd:PRK09192   210 HDGLkvRPGDRCVSWLPFYHDMGLVGFLLTPVatqlsvdYL-------PTRDFARRPLQWLDLISRNRGTISYSPPFGYE 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1943 LLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSET----------CSVVTDSV-- 2010
Cdd:PRK09192   283 LCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEAtlavsfsplgSGIVVEEVdr 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2011 ---------LASEAPDHD-EAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNaRANAESFTEDGWF 2080
Cdd:PRK09192   363 drleyqgkaVAPGAETRRvRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWL 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2081 DTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSvVRSFTAAVAVRSDASAATDELALFLRLAPGQDPAG 2160
Cdd:PRK09192   442 DTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPE-LRSGDAAAFSIAQENGEKIVLLVQCRISDEERRGQ 520

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2161 ALREIAGKVTREIGVSpAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAGEF 2210
Cdd:PRK09192   521 LIHALAALVRSEFGVE-AAVELVPPHSLPRTSSGKLSRAKAKKRYLSGAF 569
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 470-964 9.02e-64

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: 227.64  E-value: 9.02e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:cd05959     18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTD-------TAGSGRLPATDARVVVVDDARTVADLAGRA--PHDLTDADRAGATGPYDTAYVIHTSGSTGR 620
Cdd:cd05959     98 EDSRARVVVVSgelapvlAAALTKSEHTLVVLIVSGGAGPEAGALLLAelVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  621 PKGVPVPHA---HVVRLFEASGEHFRfgADDVW----TLFHSYAFDFSvweLWGPLLHGGRLVVVPYEVSrsPREFLRLL 693
Cdd:cd05959    178 PKGVVHLHAdiyWTAELYARNVLGIR--EDDVCfsaaKLFFAYGLGNS---LTFPLSVGATTVLMPERPT--PAAVFKRI 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETtVHVTFhrlv 773
Cdd:cd05959    251 RRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD---ILDGIGSTEM-LHIFL---- 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  774 rADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgtrMYRSGDL 853
Cdd:cd05959    323 -SNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE--------WTRTGDK 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPA---EEGGADPAGLRA 930
Cdd:cd05959    394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyEDSEALEEELKE 473

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569  931 HLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05959    474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 10-443 3.25e-63

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: 224.13  E-value: 3.25e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDG-PRAVRDgDPDEMPVHR 88
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGePVQVIL-EERPFELEI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   89 VDVSGEADPAAAAE--EWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:pfam00668   85 IDISDLSESEEEEAieAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EEPPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLTDRTAPPRAPFL---RRTAVLSPAETRALDEAA 243
Cdd:pfam00668  165 EPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFkgdRLSFTLDEDTEELLRKLA 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  244 KGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRGLR 323
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  324 AHQRHRGESIRRDLGVLGRGRR--VHGPVVNIVPF------SEDLTF-GGHPSTSHHLSGGAVDDLQISVRPgaEADTLW 394
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRhpLFDPMFSFQNYlgqdsqEEEFQLsELDLSVSSVIEEEAKYDLSLTASE--RGGGLT 402

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569  395 LAFDAHPDLYEEDGLALFLERFLKVLRELRTCPeELPLGEtPVLLPGEE 443
Cdd:pfam00668  403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHP-SQPLSE-LDLLSDAE 449
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1704-2197 2.21e-62

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: 222.86  E-value: 2.21e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1704 DGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL-------TVPVSYATTSA 1775
Cdd:cd05911      4 DADTGKElTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAAnpiytadELAHQLKISKP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1776 -----AVSKLEGIWEMLDRPW-----IVTSAAGEPGLRELaarrEWSGLRLTTADALREEPEdrdwyEARPDDLVLMLMT 1845
Cdd:cd05911     84 kviftDPDGLEKVKEAAKELGpkdkiIVLDDKPDGVLSIE----DLLSPTLGEEDEDLPPPL-----KDGKDDTAAILYS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1846 SGSTGLPKAVRLTHRNVLTRAAATEAMNGL--GSGDVSLNWIPLDHVTGVVMFHLRdVYLGCRQIhaptswILE--DPVR 1921
Cdd:cd05911    155 SGTTGLPKGVCLSHRNLIANLSQVQTFLYGndGSNDVILGFLPLYHIYGLFTTLAS-LLNGATVI------IMPkfDSEL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1922 WPELADRHRVSVTWAPNFAFGLLAEQAhrfQDRDWDLSPVRLVMNAGevvvASAARRFLHVLAPFGLPQDVMHpGWGMSE 2001
Cdd:cd05911    228 FLDLIEKYKITFLYLVPPIAAALAKSP---LLDKYDLSSLRVILSGG----APLSKELQELLAKRFPNATIKQ-GYGMTE 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2002 TCSVVTdsvlasEAPDHDEAFVSCGLPYPGFAMRVVDDQ-DALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWF 2080
Cdd:cd05911    300 TGGILT------VNPDGDDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2081 DTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAatDELAL-FLRLAPG-QD 2157
Cdd:cd05911    374 HTGDIGYFDeDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD---AAVIGIPDEVS--GELPRaYVVRKPGeKL 448

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2158 PAGALRE-IAGKVTR----EIGVSpaFLipveaEAIPKTEIGKIQ 2197
Cdd:cd05911    449 TEKEVKDyVAKKVASykqlRGGVV--FV-----DEIPKSASGKIL 486
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 483-965 4.38e-61

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: 217.16  E-value: 4.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTA 562
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDPA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  563 gsgrlpatdarvvvvddartvadlagraphdltdadragatgpydtaYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHF 642
Cdd:cd05934     85 -----------------------------------------------SILYTSGTTGPPKGVVITHANLTFAGYYSARRF 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  643 RFGADDVW----TLFHSYAfdfSVWELWGPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAAT 718
Cdd:cd05934    118 GLGEDDVYltvlPLFHINA---QAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  719 DRATGSLRyVVLGGEALvAERLRPWADRHGLdapELVNMYGITETTVHVTfhrlvrADLEDPRRRGVIGRPLADLRVYVL 798
Cdd:cd05934    192 DDRAHRLR-AAYGAPNP-PELHEEFEERFGV---RLLEGYGMTETIVGVI------GPRDEPRRPGSIGRPAPGYEVRIV 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  799 DAAGRPVPPGATGEMYV---SGPGVAPGYLNRPELTEERFlpdpfgAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIR 875
Cdd:cd05934    261 DDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRR 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  876 GFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTA 955
Cdd:cd05934    333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412

                          490
                   ....*....|
gi 1573930569  956 NGKLDTAALP 965
Cdd:cd05934    413 TEKVAKAQLR 422
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1684-2209 6.33e-61

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 219.67  E-value: 6.33e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAG-RPDGEVVhvRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:PRK06187     9 GRILRHGARkHPDKEAV--YFDGRRT--TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 PLTV-----PVSYATTSAA----------VSKLEGIWEMLD--RPWIVTSAAGEPGLRELAARREwsglrlttaDALREE 1825
Cdd:PRK06187    85 PINIrlkpeEIAYILNDAEdrvvlvdsefVPLLAAILPQLPtvRTVIVEGDGPAAPLAPEVGEYE---------ELLAAA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1826 PEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRdVYLGC 1905
Cdd:PRK06187   156 SDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1906 RQI---HAPTSWILedpvrwpELADRHRVSVTWA-PNFAFGLLAEQAHRFQdrdwDLSPVRLVMNAGEVVVASAARRFLH 1981
Cdd:PRK06187   235 KQViprRFDPENLL-------DLIETERVTFFFAvPTIWQMLLKAPRAYFV----DFSSLRLVIYGGAALPPALLREFKE 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1982 VlapFGLpqDVMHpGWGMSETCSVVTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLP--EGDVGRLQVRGTSV 2059
Cdd:PRK06187   304 K---FGI--DLVQ-GYGMTETSPVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWL 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2060 THGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAVRSD 2138
Cdd:PRK06187   378 MQGYWNRPEATAETI-DGGWLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAV-----AEVAVIGV 451

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2139 ASAATDE--LAlFLRLAPGQDP-AGALRE-IAGKVTReigvspaFLIPVE---AEAIPKTEIGKIQRTKLRKSFEAGE 2209
Cdd:PRK06187   452 PDEKWGErpVA-VVVLKPGATLdAKELRAfLRGRLAK-------FKLPKRiafVDELPRTSVGKILKRVLREQYAEGK 521
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 456-964 2.23e-59

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 214.77  E-value: 2.23e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:PRK07656     5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVV-------TDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDL----TDADRAGATG 604
Cdd:PRK07656    85 LNTRYTADEAAYILARGDAKALFvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFlaagDPAERAPEVD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  605 PYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHsyAFDFSVwELWGPLLHGGRLVVVPy 680
Cdd:PRK07656   165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylaANPFFH--VFGYKA-GVNAPLMRGATILPLP- 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  681 evSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGI 760
Cdd:PRK07656   241 --VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESE--LGVDIVLTGYGL 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  761 TETTVHVTFHRlvradLEDPRRR--GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPD 838
Cdd:PRK07656   317 SEASGVTTFNR-----LDDDRKTvaGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  839 PFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGltqlVAY 914
Cdd:PRK07656   392 GW-------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgvpdERLGEVG----KAY 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569  915 AVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK07656   461 VVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 456-964 6.31e-59

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: 214.24  E-value: 6.31e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:COG1021     25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVF 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDTAGSG------------RLPaTDARVVVVDDARTVADLAgraphDLTDADRAG-- 601
Cdd:COG1021    105 ALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyralarelqaEVP-SLRHVLVVGDAGEFTSLD-----ALLAAPADLse 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  602 -ATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW--TLFHSYAFDFSVWELWGPLLHGGRLVVV 678
Cdd:COG1021    179 pRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYlaALPAAHNFPLSSPGVLGVLYAGGTVVLA 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  679 PyevSRSPREFLRLLDEEKVTVLNQTPSAFeQLVLADAATDRAT-GSLRYVVLGGEAL---VAERLRPwadrhGLDApEL 754
Cdd:COG1021    259 P---DPSPDTAFPLIERERVTVTALVPPLA-LLWLDAAERSRYDlSSLRVLQVGGAKLspeLARRVRP-----ALGC-TL 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  755 VNMYGITETTVHVTfhrlvraDLEDPR--RRGVIGRPL-ADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELT 831
Cdd:COG1021    329 QQVFGMAEGLVNYT-------RLDDPEevILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHN 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  832 EERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVkIR-GFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQ 910
Cdd:COG1021    402 ARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGER 473

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  911 LVAYAVPAEEgGADPAGLRAHLAAR-LPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:COG1021    474 SCAFVVPRGE-PLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 481-964 2.92e-58

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: 209.64  E-value: 2.92e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:cd17654     16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 tagsgrlpatdarvvvvddartvaDLAGRAPHDLTDADRAGAT-GPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASG 639
Cdd:cd17654     96 ------------------------KELDNAPLSFTPEHRHFNIrTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFR 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  640 EHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEE-KVTVLNQTPSAFEQL--VLADA 716
Cdd:cd17654    152 SLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFRRFgsQSIKS 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  717 ATDRATGSLRYVVLGGEALVAER-LRPWadRHGLDAPELVNMYGITETTVHVTFHRLVRADLEDPrrrgvIGRPLADLRV 795
Cdd:cd17654    232 TVLSATSSLRVLALGGEPFPSLViLSSW--RGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQ-----LGSPLLGTVI 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  796 YVLDAAGRPVppgaTGEmyVSGPGVAPGYlnrpelteerFLPDPFGAPGTRMYRSGDLARwRPDGTLVHAGRADQQVKIR 875
Cdd:cd17654    305 EVRDQNGSEG----TGQ--VFLGGLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRR 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  876 GFRIEPGEIEAVLTAHPAVAGGAVvprAAEDgLTQLVAYAVPAEEGGADPAGLRAHLaarLPAYMVPAACVLLDALPLTA 955
Cdd:cd17654    368 GKRINLDLIQQVIESCLGVESCAV---TLSD-QQRLIAFIVGESSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTS 440


                   ....*....
gi 1573930569  956 NGKLDTAAL 964
Cdd:cd17654    441 HGKVDKSEL 449
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 479-959 1.53e-57

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: 208.61  E-value: 1.53e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  479 GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVV 558
Cdd:cd05911      8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  559 TDTAG------SGRLPATDARVVVVDDAR--------TVADLAGRAPHDLTDADRAGATgpyDTAYVIHTSGSTGRPKGV 624
Cdd:cd05911     88 TDPDGlekvkeAAKELGPKDKIIVLDDKPdgvlsiedLLSPTLGEEDEDLPPPLKDGKD---DTAAILYSSGTTGLPKGV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  625 PVPHAHVVRLFEASGEHFR--FGADDVW----TLFHSYAFDFSVWELwgplLHGGRLVVVPyevSRSPREFLRLLDEEKV 698
Cdd:cd05911    165 CLSHRNLIANLSQVQTFLYgnDGSNDVIlgflPLYHIYGLFTTLASL----LNGATVIIMP---KFDSELFLDLIEKYKI 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  699 TVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAL---VAERLRPwadrhGLDAPELVNMYGITETTVHVTfhrlvrA 775
Cdd:cd05911    238 TFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLskeLQELLAK-----RFPNATIKQGYGMTETGGILT------V 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  776 DLEDPRRRGVIGRPLADLRVYVLDAAGRP-VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLA 854
Cdd:cd05911    307 NPDGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIG 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  855 RWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQL-VAYAVPAEEGGADPAGLRAHLA 933
Cdd:cd05911    380 YFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS-GELpRAYVVRKPGEKLTEKEVKDYVA 458

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569  934 ARLPAYM-----VpaacVLLDALPLTANGKL 959
Cdd:cd05911    459 KKVASYKqlrggV----VFVDEIPKSASGKI 485
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 9-423 5.30e-57

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: 205.34  E-value: 5.30e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    9 RPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPDEMPVHR 88
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   89 VDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEE 168
Cdd:cd19066     82 IDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKP 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  169 PPPAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLT---DRTAPPRAPFLRRTAVLSPAETRALDEAAKG 245
Cdd:cd19066    162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPkakRPSQVASYEVLTLEFFLRSEETKRLREVARE 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  246 MGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDLRGLRAH 325
Cdd:cd19066    242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  326 QRHRGESIRRDLGV---LGRGRRVhGPVVNIV--PFSEDLTFGGHPSTS-HHLSGGAVDDLQISVRPGAEADTLwLAFDA 399
Cdd:cd19066    322 QRVPFIELVRHLGVvpeAPKHPLF-EPVFTFKnnQQQLGKTGGFIFTTPvYTSSEGTVFDLDLEASEDPDGDLL-LRLEY 399

                          410       420
                   ....*....|....*....|....
gi 1573930569  400 HPDLYEEDGLALFLERFLKVLREL 423
Cdd:cd19066    400 SRGVYDERTIDRFAERYMTALRQL 423
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 466-967 8.12e-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: 207.76  E-value: 8.12e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  466 VAESPgrTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERL 545
Cdd:cd17647      7 VVETP--SLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  546 ALVMADAEPVAVVTdtagsgrlpATDARVVVvddartvadlagraphdltdadragatGPYDTAYVIHTSGSTGRPKGVP 625
Cdd:cd17647     85 NIYLGVAKPRGLIV---------IRAAGVVV---------------------------GPDSNPTLSFTSGSEGIPKGVL 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  626 VPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTP 705
Cdd:cd17647    129 GRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTP 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 sAFEQLVLADAATdrATGSLRYVVLGGEALVAE---RLRPWADRHgldapELVNMYGITETTVHVTFHRlVRADLEDP-- 780
Cdd:cd17647    209 -AMGQLLTAQATT--PFPKLHHAFFVGDILTKRdclRLQTLAENV-----RIVNMYGTTETQRAVSYFE-VPSRSSDPtf 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  781 --RRRGVI--GRPLADLRVYVLDAAGRP--VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPG---------- 844
Cdd:cd17647    280 lkNLKDVMpaGRGMLNVQLLVVNRNDRTqiCGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnn 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  845 -----------TRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVA 913
Cdd:cd17647    360 epwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVS 439

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  914 YAVP---------------AEEGGADPA------------GLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPA 966
Cdd:cd17647    440 YIVPrfdkpddesfaqedvPKEVSTDPIvkgligyrklikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQF 519


                   .
gi 1573930569  967 P 967
Cdd:cd17647    520 P 520
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 472-964 1.23e-56

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: 204.62  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  472 RTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG-HPAErLALVMA 550
Cdd:cd05919      1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDD-YAYIAR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  551 DAEpvavvtdtagsgrlpatdARVVVVDDArtvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPHAH 630
Cdd:cd05919     80 DCE------------------ARLVVTSAD--------------------------DIAYLLYSSGTTGPPKGVMHAHRD 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  631 VVRLFEASG-EHFRFGADDVW----TLFHSYAFDFSvweLWGPLLHGGRLVVVPyeVSRSPREFLRLLDEEKVTVLNQTP 705
Cdd:cd05919    116 PLLFADAMArEALGLTPGDRVfssaKMFFGYGLGNS---LWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVP 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 SAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDAPElvnmyGITETTVHVTFhrlvRADLEDPRRRGV 785
Cdd:cd05919    191 TFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILD-----GIGATEVGHIF----LSNRPGAWRLGS 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  786 IGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHA 865
Cdd:cd05919    262 TGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDADGWYTHA 333

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  866 GRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPAG-----LRAHLAARLPAYM 940
Cdd:cd05919    334 GRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP--AAPQEslardIHRHLLERLSAHK 411

                          490       500
                   ....*....|....*....|....
gi 1573930569  941 VPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05919    412 VPRRIAFVDELPRTATGKLQRFKL 435
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 474-960 9.11e-56

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: 203.70  E-value: 9.11e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  474 AVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAE 553
Cdd:cd05926      7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  554 PVAVVTDtaGSGRLPATDARVVVVDDARTVADLAGR------------APHDLTDADRAGATGPYDTAYVIHTSGSTGRP 621
Cdd:cd05926     87 SKLVLTP--KGELGPASRAASKLGLAILELALDVGVlirapsaeslsnLLADKKNAKSEGVPLPDDLALILHTSGTTGRP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHSYAFdfsVWELWGPLLHGGRLVVVPyevSRSPREFLRLLDEEK 697
Cdd:cd05926    165 KGVPLTHRNLAASATNITNTYKLTPDDrtlvVMPLFHVHGL---VASLLSTLAAGGSVVLPP---RFSASTFWPDVRDYN 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  698 VTVLNQTPSaFEQLVLADAATD--RATGSLRYVVLGGEALVAERLRPWADRHGldAPeLVNMYGITETTVHVTFHRLVra 775
Cdd:cd05926    239 ATWYTAVPT-IHQILLNRPEPNpeSPPPKLRFIRSCSASLPPAVLEALEATFG--AP-VLEAYGMTEAAHQMTSNPLP-- 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  776 dlEDPRRRGVIGRPlADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLAR 855
Cdd:cd05926    313 --PGPRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGY 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  856 WRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVpRAAEDGLTQLVAYAVPAEEGG-ADPAGLRAHLAA 934
Cdd:cd05926    383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAF-GVPDEKYGEEVAAAVVLREGAsVTEEELRAFCRK 461

                          490       500
                   ....*....|....*....|....*.
gi 1573930569  935 RLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd05926    462 HLAAFKVPKKVYFVDELPKTATGKIQ 487
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 491-964 4.72e-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.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 200.36  E-value: 4.72e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  491 ANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAA----YLPLDPGHPAERLALVMADAEPVAVVTDTAGSGR 566
Cdd:cd05922      3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  567 LpatDARVVVVDDARTVADLagraphDLTDADRAGATG----PYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHF 642
Cdd:cd05922     83 L---RDALPASPDPGTVLDA------DGIRAARASAPAhevsHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  643 RFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPyeVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAAtDRAT 722
Cdd:cd05922    154 GITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFD-PAKL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  723 GSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFhrlVRADLEDpRRRGVIGRPLADLRVYVLDAAG 802
Cdd:cd05922    231 PSLRYLTQAGGRLPQETIARLREL--LPGAQVYVMYGQTEATRRMTY---LPPERIL-EKPGSIGLAIPGGEFEILDDDG 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  803 RPVPPGATGEMYVSGPGVAPGYLNRPElteerFLPDPfGAPGTRMYrSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPG 882
Cdd:cd05922    305 TPTPPGEPGEIVHRGPNVMKGYWNDPP-----YRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  883 EIEAVLTAHPAVAGGAVVprAAEDGLTQLVAYAVPAEEGgADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTA 962
Cdd:cd05922    378 EIEAAARSIGLIIEAAAV--GLPDPLGEKLALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454


                   ..
gi 1573930569  963 AL 964
Cdd:cd05922    455 AL 456
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1687-2198 1.50e-54

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: 198.22  E-value: 1.50e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1687 LLRAAGRpDGEVVHVRADGseTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtv 1766
Cdd:cd17631      1 LRRRARR-HPDRTALVFGG--RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1767 pvsyattsaavsklegiwemldrPWIVTSAagepglrELAARREWSGLRLTTadalreepedrdwyearpDDLVLMLMTS 1846
Cdd:cd17631     76 -----------------------NFRLTPP-------EVAYILADSGAKVLF------------------DDLALLMYTS 107

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1847 GSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIhaptswILE--DPVRWPE 1924
Cdd:cd17631    108 GTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVV------ILRkfDPETVLD 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1925 LADRHRVSVTWAPNFAFGLLAeQAHRFQDRdwDLSPVRLVMNAGevvvASAARRFLHVLAPFGLpqdVMHPGWGMSETCS 2004
Cdd:cd17631    182 LIERHRVTSFFLVPTMIQALL-QHPRFATT--DLSSLRAVIYGG----APMPERLLRALQARGV---KFVQGYGMTETSP 251

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2005 VVTdsVLASEapDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGD 2084
Cdd:cd17631    252 GVT--FLSPE--DHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGD 326

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2085 LAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS-------------FTAAVAVRSDASAATDELALFL 2150
Cdd:cd17631    327 LGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVavigvpdekwgeaVVAVVVPRPGAELDEDELIAHC 406

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 2151 RlapgqdpagalREIAG-KVTREIGVspaflipveAEAIPKTEIGKIQR 2198
Cdd:cd17631    407 R-----------ERLARyKIPKSVEF---------VDALPRNATGKILK 435
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1072-1502 3.51e-54

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: 196.91  E-value: 3.51e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVF--GEEDGAIHQRVLPPGTLRpe 1149
Cdd:cd19532      2 EPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLR-- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1150 LHVVDCPDEERAAHVAAAMR-RSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGtayaarRAGAAP 1227
Cdd:cd19532     80 LEHVQISDEAEVEEEFERLKnHVYDLESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRDLE------RAYNGQ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1228 DWAPPALQYADFALWQRRVLAPapegpGRLERLTSFWRQALDGLPEesapppdrprpaapsgrgggvTVPL--------- 1298
Cdd:cd19532    154 PLLPPPLQYLDFAARQRQDYES-----GALDEDLAYWKSEFSTLPE---------------------PLPLlpfakvksr 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1299 ----DAGTHRELLRLaDHENAS---------------LFMVlhgALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLL 1359
Cdd:cd19532    208 ppltRYDTHTAERRL-DAALAArikeasrklrvtpfhFYLA---ALQVLLARLLDVDDICIGIADANRTDEDFMETIGFF 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1360 TNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRVPL 1439
Cdd:cd19532    284 LNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEG 363

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 1440 RPAATGTAKFDLFVDVLERHGADGTadgLDLHVEyaADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19532    364 EEFEDARTPYDLSLDIIDNPDGDCL---LTLKVQ--SSLYSEEDAELLLDSYVNLLEAFARDP 421
PRK05691 PRK05691
peptide synthase; Validated
 1684-2280 4.18e-54

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 211.57  E-value: 4.18e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALL-RAAGRPDGEVVHVRADGSETRR--SYASLVPEASRVLAGLRRRGlRPGDRVILQCDDTEDFVATLWGCVLGGFV 1760
Cdd:PRK05691    12 VQALQrRAAQTPDRLALRFLADDPGEGVvlSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1761 AVPLTVPVSyaTTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRdWYEA--RPDD 1838
Cdd:PRK05691    91 AVPAYPPES--ARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEA-WQEPalQPDD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1839 LVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNG--LGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWIL 1916
Cdd:PRK05691   168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYFL 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1917 EDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPG 1996
Cdd:PRK05691   248 ERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFFAS 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETCSVVTDSV---------LASEA-------PDHDEAFVSCGLPYPGFAMRVVDDQD-ALLPEGDVGRLQVRGTSV 2059
Cdd:PRK05691   328 YGLAEATLFVSGGRrgqgipaleLDAEAlarnraePGTGSVLMSCGRSQPGHAVLIVDPQSlEVLGDNRVGEIWASGPSI 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2060 THGYHDNARANAESFTE-DG--WFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS-FTAAVAV 2135
Cdd:PRK05691   408 AHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgRVAAFAV 487

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2136 RSDASAATDELALFLR----LAPGQDPAGALREIAGKVTREigvSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAGEFD 2211
Cdd:PRK05691   488 NHQGEEGIGIAAEISRsvqkILPPQALIKSIRQAVAEACQE---APSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLD 564

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2212 GAVR---ETQLLLGTAATVPDWF---LHPLWRpaENLHAATLPAGHRVLVLAGPAphahAVAEEVAGAVRDAGGL 2280
Cdd:PRK05691   565 SYALfpaLQAVEAAQTAASGDELqarIAAIWC--EQLKVEQVAADDHFFLLGGNS----IAATQVVARLRDELGI 633
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1684-2202 4.50e-54

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: 198.17  E-value: 4.50e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAGR-PDGEVVhvraDGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:cd05936      2 ADLLEEAARRfPDKTAL----IFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 PLTvpvsyattsaavsklegiwemldrpWIVTSaagepglRELAARREWSGLR-----LTTADALREEPEDRDWYEARPD 1837
Cdd:cd05936     78 PLN-------------------------PLYTP-------RELEHILNDSGAKalivaVSFTDLLAAGAPLGERVALTPE 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEA-MNGLGSG-DVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSwi 1915
Cdd:cd05936    126 DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAwLEDLLEGdDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRF-- 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 leDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHrfqDRDWDLSPVRLVMNAGEVVVASAARRFLHVlapFGLPqdvMHP 1995
Cdd:cd05936    204 --RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE---FKKRDFSSLRLCISGGAPLPVEVAERFEEL---TGVP---IVE 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1996 GWGMSETCSVVTDSvlaseaPDHDEAFV-SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESF 2074
Cdd:cd05936    273 GYGLTETSPVVAVN------PLDGPRKPgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2075 TeDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSV----------------VRSFtaaVAVRS 2137
Cdd:cd05936    347 V-DGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVaeaavvgvpdpysgeaVKAF---VVLKE 422

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 2138 DASAATDELALFLRlapgqdpagalREIAG-KVTREIGVspaflipveAEAIPKTEIGKIQRTKLR 2202
Cdd:cd05936    423 GASLTEEEIIAFCR-----------EQLAGyKVPRQVEF---------RDELPKSAVGKILRRELR 468
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 1732-2211 1.59e-53

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 200.35  E-value: 1.59e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1732 RPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPvsyattsaavsKLEGIWEMLD------RPWIV-TSAAGEPGLRE 1804
Cdd:PRK12476    90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAP-----------ELPGHAERLDtalrdaEPTVVlTTTAAAEAVEG 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1805 LAARRewSGLRLTTADALREEP----EDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA-TEAMNGLGSGD 1879
Cdd:PRK12476   159 FLRNL--PRLRRPRVIAIDAIPdsagESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQmILSIDLLDRNT 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1880 VSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWIlEDPVRW-PELAD--RHRVSVTWAPNFAFGLLAEQAHRFQDRDW 1956
Cdd:PRK12476   237 HGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFV-RRPQRWiKALSEgsRTGRVVTAAPNFAYEWAAQRGLPAEGDDI 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1957 DLSPVRLVmNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSETCSVVTDSVLASE-------------------APD 2017
Cdd:PRK12476   316 DLSNVVLI-IGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEpsvvyldreqlgagravrvAAD 394

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2018 HDEAF--VSCGLPYPG-FAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESF------------------TE 2076
Cdd:PRK12476   395 APNAVahVSCGQVARSqWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDD 474

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2077 DGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEEL-PSVVRSFTAAVAVRSDASaatDELALFLRLAPG 2155
Cdd:PRK12476   475 GTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRGYVTAFTVPAEDN---ERLVIVAERAAG 551

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2156 ---QDPAGALREIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAGEFD 2211
Cdd:PRK12476   552 tsrADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLG 610
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 456-964 1.60e-53

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: 196.78  E-value: 1.60e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:cd05920     15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVtdtaGSGRLPATDARvvvvDDARTVAdlagraphdltdadragATGPyDTAYVIHTS 615
Cdd:cd05920     95 ALPSHRRSELSAFCAHAEAVAYI----VPDRHAGFDHR----ALARELA-----------------ESIP-EVALFLLSG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  616 GSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDF--SVWELWGPLLHGGRLVVVPyevSRSPREFLRLL 693
Cdd:cd05920    149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFplACPGVLGTLLAGGRVVLAP---DPSPDAAFPLI 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGG---EALVAERLRPWADrhgldaPELVNMYGITETTVHVTfh 770
Cdd:cd05920    226 EREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGarlSPALARRVPPVLG------CTLQQVFGMAEGLLNYT-- 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  771 rlvRADLEDPRRRGVIGRPL-ADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYR 849
Cdd:cd05920    298 ---RLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YR 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  850 SGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEgGADPAGLR 929
Cdd:cd05920    368 TGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDP-PPSAAQLR 446

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1573930569  930 AHLAAR-LPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05920    447 RFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1683-2203 2.75e-53

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 198.41  E-value: 2.75e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1683 WAEALL--RAAGRPDGE-VVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGF 1759
Cdd:COG0365     10 IAYNCLdrHAEGRGDKVaLIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1760 VAVPLTV---PVSYAT-----------TSAAV----------SKLEGIWEMLDRPWIVTSAAGEPGLRELAARREWsglr 1815
Cdd:COG0365     90 VHSPVFPgfgAEALADriedaeakvliTADGGlrggkvidlkEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDW---- 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1816 lttADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTrAAATEAMN--GLGSGDV-----SLNWIPld 1888
Cdd:COG0365    166 ---DELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLV-HAATTAKYvlDLKPGDVfwctaDIGWAT-- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1889 HVTGVVMFHLrdvYLGCRQIHAPTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRdWDLSPVRLVMNAG 1968
Cdd:COG0365    240 GHSYIVYGPL---LNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKK-YDLSSLRLLGSAG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1969 EVVVASAARRFLHVlapFGLPqdvMHPGWGMSETCSVVtdsvlASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGD 2048
Cdd:COG0365    316 EPLNPEVWEWWYEA---VGVP---IVDGWGQTETGGIF-----ISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2049 VGRLQVRG--TSVTHGYHDNARANAESF--TEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELP 2123
Cdd:COG0365    385 EGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2124 SVVRSftAAVAVRsdasaatDEL-----ALFLRLAPGQDPAGALR-EIAGKVTREIGvspAFLIP---VEAEAIPKTEIG 2194
Cdd:COG0365    465 AVAEA--AVVGVP-------DEIrgqvvKAFVVLKPGVEPSDELAkELQAHVREELG---PYAYPreiEFVDELPKTRSG 532


                   ....*....
gi 1573930569 2195 KIQRTKLRK 2203
Cdd:COG0365    533 KIMRRLLRK 541
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 482-964 3.61e-53

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: 194.09  E-value: 3.61e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALvmadaepvavvtdt 561
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEY-------------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 agsgRLPATDARVVVVDDArtvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPH----AHVVRL--- 634
Cdd:cd05972     67 ----RLEAAGAKAIVTDAE--------------------------DPALIYFTSGTTGLPKGVLHTHsyplGHIPTAayw 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  635 --FEASGEHFRFgADDVWTLFHSYAFdfsvwelWGPLLHGgrLVVVPYEVSR-SPREFLRLLDEEKVTVLNQTPSAFEQL 711
Cdd:cd05972    117 lgLRPDDIHWNI-ADPGWAKGAWSSF-------FGPWLLG--ATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYRML 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  712 VLADAATdRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETTVHVTFHRLVradledPRRRGVIGRPLA 791
Cdd:cd05972    187 IKQDLSS-YKFSHLRLVVSAGEPLNPEVIEWWRAATGLP---IRDGYGQTETGLTVGNFPDM------PVKPGSMGRPTP 256

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  792 DLRVYVLDAAGRPVPPGATGEMYV--SGPGVAPGYLNRPELTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:cd05972    257 GYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRAD 328

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRaAEDGLTQLV-AYAVPAEEGGADPA---GLRAHLAARLPAYMVPAAC 945
Cdd:cd05972    329 DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGS-PDPVRGEVVkAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREI 407

                          490
                   ....*....|....*....
gi 1573930569  946 VLLDALPLTANGKLDTAAL 964
Cdd:cd05972    408 EFVEELPKTISGKIRRVEL 426
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 472-964 7.53e-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: 193.66  E-value: 7.53e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  472 RTAVSYAGETLSYAELNAEANRLARLLVEQGA-GPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMA 550
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  551 DAEPVAVVtdtagsgrlpatdarvvvvddartvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPHAH 630
Cdd:cd05941     82 DSEPSLVL------------------------------------------------DPALILYTSGTTGRPKGVVLTHAN 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  631 VVRLFEASGEHFRFGADDVWT----LFHSYAFdfsVWELWGPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPS 706
Cdd:cd05941    114 LAANVRALVDAWRWTEDDVLLhvlpLHHVHGL---VNALLCPLFAGASVEFLP---KFDPKEVAISRLMPSITVFMGVPT 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  707 AFEQLVLADAATDR--------ATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTfhrlvrADLE 778
Cdd:cd05941    188 IYTRLLQYYEAHFTdpqfaraaAAERLRLMVSGSAALPVPTLEEWEAITGH---TLLERYGMTEIGMALS------NPLD 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 DPRRRGVIGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWR 857
Cdd:cd05941    259 GERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVD 331

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  858 PDGTLVHAGR-ADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGA-DPAGLRAHLAAR 935
Cdd:cd05941    332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAAlSLEELKEWAKQR 411

                          490       500
                   ....*....|....*....|....*....
gi 1573930569  936 LPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05941    412 LAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 457-958 1.34e-51

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 193.68  E-value: 1.34e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL 536
Cdd:PRK05605    33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMAD-AEPVAVVTDTAGS--GRLPATDA--RVVVVD-------------------DARTVADLAGRAP- 591
Cdd:PRK05605   113 NPLYTAHELEHPFEDhGARVAIVWDKVAPtvERLRRTTPleTIVSVNmiaampllqrlalrlpipaLRKARAALTGPAPg 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  592 ----HDLTDADRAG--------ATGPYDTAYVIHTSGSTGRPKGVPVPHAHVvRLFEASGEHFRFGADD-------VWTL 652
Cdd:PRK05605   193 tvpwETLVDAAIGGdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLTHRNL-FANAAQGKAWVPGLGDgpervlaALPM 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  653 FHSY------AFDFSVwelwgpllhGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLR 726
Cdd:PRK05605   272 FHAYgltlclTLAVSI---------GGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVR 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  727 YVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVHVtfhrlVRADLEDPRRRGVIGRPLADLRVYVLDA--AGRP 804
Cdd:PRK05605   340 NAFSGAMALPVSTVELWEKLTG---GLLVEGYGLTETSPII-----VGNPMSDDRRPGYVGVPFPDTEVRIVDPedPDET 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  805 VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEI 884
Cdd:PRK05605   412 MPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  885 EAVLTAHPAVAGGAVVPRAAEDGLTQLVAyAVPAEEGGA-DPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:PRK05605   484 EEVLREHPGVEDAAVVGLPREDGSEEVVA-AVVLEPGAAlDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1707-2202 2.82e-51

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: 188.27  E-value: 2.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyattsaavsklegiwem 1786
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPIN--------------------- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1787 ldrpwivTSAAGEpglrELAARREWSGLRLTTADalreepedrdwyearpddLVLMLMTSGSTGLPKAVRLTHRNVLTRA 1866
Cdd:cd05934     60 -------TALRGD----ELAYIIDHSGAQLVVVD------------------PASILYTSGTTGPPKGVVITHANLTFAG 110

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1867 AATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGC-----RQIHAPTSWileDPVRwpeladRHRVSVTWAPNFAF 1941
Cdd:cd05934    111 YYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGAtlvllPRFSASRFW---SDVR------RYGATVTNYLGAML 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1942 GLLAEQAHRFQDRDwdlSPVRLVMNAGevVVASAARRFlhvLAPFGLPqdvMHPGWGMSETCSVVTDsvlaseAPDHDEA 2021
Cdd:cd05934    182 SYLLAQPPSPDDRA---HRLRAAYGAP--NPPELHEEF---EERFGVR---LLEGYGMTETIVGVIG------PRDEPRR 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2022 FVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVR---GTSVTHGYHDNARANAESFtEDGWFDTGDLAFLR-DGELYITG 2097
Cdd:cd05934    245 PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDaDGFFYFVD 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2098 RAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAatDELALFLRLAPGQ--DPAGALREIAGKVtreigv 2175
Cdd:cd05934    324 RKKDMIRRRGENISSAEVERAILRHPAVREA--AVVAVPDEVGE--DEVKAVVVLRPGEtlDPEELFAFCEGQL------ 393

                          490       500       510
                   ....*....|....*....|....*....|
gi 1573930569 2176 sPAFLIP--VE-AEAIPKTEIGKIQRTKLR 2202
Cdd:cd05934    394 -AYFKVPryIRfVDDLPKTPTEKVAKAQLR 422
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 465-959 5.37e-51

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: 191.30  E-value: 5.37e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVSYA------GETLSYAELNAEANRLARLLVEQGAgPGRFVALALPRGPRLVPALLAVLKTGA----AYL 534
Cdd:cd05931      2 RAAARPDRPAYTFLddeggrEETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PlDPGHPAERLALVMADAEPVAVVTDTAGSGRLPAT-DARVVVVDDARTVADLAgraPHDLTDADRAGATGPYDTAYVIH 613
Cdd:cd05931     81 P-TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFaASRPAAGTPRLLVVDLL---PDTSAADWPPPSPDPDDIAYLQY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  614 TSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAFDFSvweLWGPLLHGGRLVVV-PYEVSRSPRE 688
Cdd:cd05931    157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG---LLTPLYSGGPSVLMsPAAFLRRPLR 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  689 FLRLLDEEKVTVlnqTPS---AFEQLVLADAATDRAT---GSLRYVVLGGEALVAERLRPWADR---HGLDAPELVNMYG 759
Cdd:cd05931    234 WLRLISRYRATI---SAApnfAYDLCVRRVRDEDLEGldlSSWRVALNGAEPVRPATLRRFAEAfapFGFRPEAFRPSYG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHVTF---------HRLVRADLEDPRRRGVI-----------GRPLADLRVYVLDAAG-RPVPPGATGEMYVSGP 818
Cdd:cd05931    311 LAEATLFVSGgppgtgpvvLRVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGP 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  819 GVAPGYLNRPELTEERFLPDPfGAPGTRMYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEA-VLTAHPAVAGG 897
Cdd:cd05931    391 SVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALRPG 468

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  898 AVVPRA--AEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAY--MVPAACVLL--DALPLTANGKL 959
Cdd:cd05931    469 CVAAFSvpDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVrpGSIPRTSSGKI 536
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 466-959 5.61e-50

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: 188.94  E-value: 5.61e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  466 VAESPGRTAVSYAGE------TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd17634     63 LRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAG--SGRL-------------PATDARVVVVDDaRTVADLAGRAPHDL---------T 595
Cdd:cd17634    143 FAPEAVAGRIIDSSSRLLITADGGvrAGRSvplkknvddalnpNVTSVEHVIVLK-RTGSDIDWQEGRDLwwrdliakaS 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRAGATGPYDTAYVIHTSGSTGRPKGVPVPH-AHVVRLFEASGEHFRFGADDVWTLFHSYAFDFS-VWELWGPLLHGG 673
Cdd:cd17634    222 PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTgGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGA 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  674 rlVVVPYE---VSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLAD----AATDRAtgSLRyvVLGGealVAERLRP---- 742
Cdd:cd17634    302 --TTLLYEgvpNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaiEGTDRS--SLR--ILGS---VGEPINPeaye 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  743 WADRH-GLDAPELVNMYGITETTVHVTFHRLVRadleDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYV--SGPG 819
Cdd:cd17634    373 WYWKKiGKEKCPVVDTWWQTETGGFMITPLPGA----IELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVItdPWPG 448

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  820 VAPGYLNRPELTEERFLPDPFGapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAV 899
Cdd:cd17634    449 QTRTLFGDHERFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  900 VPRAAEDGLTQLVAYAVpAEEGGADPAGLRAHLAARLPAYM----VPAACVLLDALPLTANGKL 959
Cdd:cd17634    524 VGIPHAIKGQAPYAYVV-LNHGVEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 472-964 6.72e-50

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: 184.99  E-value: 6.72e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  472 RTAVSYAGETLSYAELNAEANRLARLLV-EQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMA 550
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  551 DAEPVavvtdtagsgrlpatdarVVVVDDARTVADlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPHAH 630
Cdd:cd05958     81 KARIT------------------VALCAHALTASD---------------------DICILAFTSGTTGAPKATMHFHRD 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  631 VVRLFEASGEH-FRFGADDVWT----LFHSYAFDFSvweLWGPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTP 705
Cdd:cd05958    122 PLASADRYAVNvLRLREDDRFVgsppLAFTFGLGGV---LLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAP 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  706 SAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETtvhvtFHRLVRADlEDPRRRGV 785
Cdd:cd05958    196 TAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP---IIDGIGSTEM-----FHIFISAR-PGDARPGA 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  786 IGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPgvaPGYLNRPELTEERFLPDPFGAPGTRMYRSgdlarwrPDGTLVHA 865
Cdd:cd05958    267 TGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRD-------PDGYFRHQ 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  866 GRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRA---HLAARLPAYMVP 942
Cdd:cd05958    337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAPYKYP 416

                          490       500
                   ....*....|....*....|..
gi 1573930569  943 AACVLLDALPLTANGKLDTAAL 964
Cdd:cd05958    417 RAIEFVTELPRTATGKLQRFAL 438
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 466-916 7.21e-50

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: 186.67  E-value: 7.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  466 VAESPGRTAV--SYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDP-GHPA 542
Cdd:cd05904     15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPlSTPA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  543 ErLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGA-TGPYDTAYVIHTSGSTGRP 621
Cdd:cd05904     95 E-IAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvIKQDDVAALLYSSGTTGRS 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEA--SGEHFRFGADDVW----TLFHSYAFdfsVWELWGPLLHGGRLVVVPyevSRSPREFLRLLDE 695
Cdd:cd05904    174 KGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFlcvlPMFHIYGL---SSFALGLLRLGATVVVMP---RFDLEELLAAIER 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  696 EKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETT--VHVTFhrlv 773
Cdd:cd05904    248 YKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAK--FPNVDLGQGYGMTESTgvVAMCF---- 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  774 rADLEDPRRRGVIGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGD 852
Cdd:cd05904    322 -APEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGD 393

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  853 LARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAV 916
Cdd:cd05904    394 LCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV 457
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1709-2203 1.52e-49

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: 183.74  E-value: 1.52e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1709 RRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPltVPVSYATTSAAvsklegiwemld 1788
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNP--ILPFFREHELA------------ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1789 rpWIVTSAAGepglRELAARREWSGLRlttadalreepedrdwYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA 1868
Cdd:cd05903     67 --FILRRAKA----KVFVVPERFRQFD----------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQ 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 TEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQiHAPTSWileDPVRWPELADRHRVSVTW-APNFAFGLLaeQ 1947
Cdd:cd05903    125 YAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV-VLQDIW---DPDKALALMREHGVTFMMgATPFLTDLL--N 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1948 AHRFQDRdwDLSPVRLVMNAGEVVVASAARRFLHVLAPFglpqdvMHPGWGMSETCSVVTdsvlASEAPDHDEAFVSCGL 2027
Cdd:cd05903    199 AVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK------VCSAYGSTECPGAVT----SITPAPEDRRLYTDGR 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2028 PYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVN 2106
Cdd:cd05903    267 PLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLdEDGYLRITGRSKDIIIRG 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2107 GVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAAtDELALFLRLAPGQDPagALREIAGKVTREiGVSpAFLIP---V 2183
Cdd:cd05903    346 GENIPVLEVEDLLLGHPGVI---EAAVVALPDERLG-ERACAVVVTKSGALL--TFDELVAYLDRQ-GVA-KQYWPerlV 417

                          490       500
                   ....*....|....*....|
gi 1573930569 2184 EAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05903    418 HVDDLPRTPSGKVQKFRLRE 437
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1073-1502 3.15e-49

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: 182.40  E-value: 3.15e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVF-GEEDGAIHQRVLPPGTLRpeLH 1151
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVLKDRKLP--WR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVD---CPDEERAAHVAAAM----RRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRA 1223
Cdd:cd19543     81 ELDlshLSEAEQEAELEALAeedrERGFDLARAPLMRLTLIRLGDDRyRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1224 GAAPDwAPPALQYADFALW-QRRVLAPApegpgrlerlTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGT 1302
Cdd:cd19543    161 GQPPS-LPPVRPYRDYIAWlQRQDKEAA----------EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAEL 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1303 HRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRtEPALDEV---VGLLTNTLVLRADASGDPTFRELL 1379
Cdd:cd19543    230 TARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPGIetmVGLFINTLPVRVRLDPDQTVLELL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1380 ARVRAFDVQALDHQDLPFDRLveevnPRRHPARHPLFQVMLALQNNER-AVLTLGEDRVPLRpaatgtakfdlFVDVler 1458
Cdd:cd19543    309 KDLQAQQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENYPVdESLEEEQDEDGLR-----------ITDV--- 369

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 1459 HGADGT----------ADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19543    370 SAEEQTnypltvvaipGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 457-967 1.83e-48

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 182.88  E-value: 1.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL 536
Cdd:PRK06188    13 TYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMADAE-------PVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRA----PHDLTDADRagatgP 605
Cdd:PRK06188    93 HPLGSLDDHAYVLEDAGistlivdPAPFVERALALLARVPSLKHVLTLGPVPDGVDLLAAAakfgPAPLVAAAL-----P 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  606 YDTAYVIHTSGSTGRPKGVPVPH---AHVVRLFEASGE---HFRFGAddVWTLFHSYAFDFSVwelwgPLLHGGRLVVVP 679
Cdd:PRK06188   168 PDIAGLAYTGGTTGKPKGVMGTHrsiATMAQIQLAEWEwpaDPRFLM--CTPLSHAGGAFFLP-----TLLRGGTVIVLA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  680 yevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYG 759
Cdd:PRK06188   241 ---KFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFG---PIFAQYYG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHVTFHRLVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDp 839
Cdd:PRK06188   315 QTEAPMVITYLRKRDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG- 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  840 fgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAV--VPraaEDGLTQLV-AYAV 916
Cdd:PRK06188   394 -------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVigVP---DEKWGEAVtAVVV 463

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  917 PAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAP 967
Cdd:PRK06188   464 LRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 1732-2217 2.56e-48

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 184.93  E-value: 2.56e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1732 RPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPvsyaTTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLREL-----A 1806
Cdd:PRK07769    77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDP----AEPGHVGRLHAVLDDCTPSAILTTTDSAEGVRKFfrarpA 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1807 ARREwsglRLTTADALreePED--RDWYEARP--DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSL 1882
Cdd:PRK07769   153 KERP----RVIAVDAV---PDEvgATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGV 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1883 NWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWIlEDPVRW-PELA---DRHRVSVTWAPNFAFGLLAEQA-HRFQDRDWD 1957
Cdd:PRK07769   226 SWLPFFHDMGLITVLLPALLGHYITFMSPAAFV-RRPGRWiRELArkpGGTGGTFSAAPNFAFEHAAARGlPKDGEPPLD 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1958 LSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSETCSVVTDSVLASEAP----DHDE------------- 2020
Cdd:PRK07769   305 LSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPTviyvDRDElnagrfvevpada 384

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2021 ----AFVSCG-LPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESF----------------TEDG- 2078
Cdd:PRK07769   385 pnavAQVSAGkVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAl 464

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2079 WFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS-FTAAVAV-----------------RSDAS 2140
Cdd:PRK07769   465 WVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTgYVAAFSVpanqlpqvvfddshaglKFDPE 544

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2141 AATDELALFLRLAPG---QDPAGALREIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAGEFDGAVRET 2217
Cdd:PRK07769   545 DTSEQLVIVAERAPGahkLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQP 624
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 461-958 6.70e-48

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 180.84  E-value: 6.70e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  461 LFEARVAESPGRTAV---SYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:PRK07514     5 LFDALRAAFADRDAPfieTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTDTAGSGRLPATDAR-----VVVVDDART--VADLAGRAPHDLTDADRagatGPYDTAY 610
Cdd:PRK07514    85 TAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAagaphVETLDADGTgsLLEAAAAAPDDFETVPR----GADDLAA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  611 VIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVwtLFHSYAFdFSVWELW----GPLLHGGRLVVVPyevSRSP 686
Cdd:PRK07514   161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDV--LIHALPI-FHTHGLFvatnVALLAGASMIFLP---KFDP 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLdeEKVTVLNQTPSAFEQLvLADAATDR-ATGSLRYVVLGGEALVAERLRPWADRHGLDAPElvnMYGITETTV 765
Cdd:PRK07514   235 DAVLALM--PRATVMMGVPTFYTRL-LQEPRLTReAAAHMRLFISGSAPLLAETHREFQERTGHAILE---RYGMTETNM 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  766 hvtfhrLVRADLEDPRRRGVIGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapg 844
Cdd:PRK07514   309 ------NTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---- 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  845 trmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGAD 924
Cdd:PRK07514   379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD 455

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569  925 PAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:PRK07514   456 EAAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 482-959 8.90e-48

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: 178.48  E-value: 8.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPldpghpaerlaLVMADAEPvavvtdt 561
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQP-----------LFTAFGPK------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 AGSGRLPATDARVVVVDDARTvadlagrapHDLTDadragatgpyDTAYVIHTSGSTGRPKGVPVPhahvVRLFEASGEH 641
Cdd:cd05973     63 AIEHRLRTSGARLVVTDAANR---------HKLDS----------DPFVMMFTSGTTGLPKGVPVP----LRALAAFGAY 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFG------------ADDVWTLFHSYAfdfsvweLWGPLLHGGRLVVvpYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:cd05973    120 LRDAvdlrpedsfwnaADPGWAYGLYYA-------ITGPLALGHPTIL--LEGGFSVESTWRVIERLGVTNLAGSPTAYR 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADA-ATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTFHRlvraDLEDPRRRGVIGR 788
Cdd:cd05973    191 LLMAAGAeVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGV---PIHDHYGQTELGMVLANHH----ALEHPVHAGSAGR 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEmyvsgpgVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRA 868
Cdd:cd05973    264 AMPGWRVAVLDDDGDELGPGEPGR-------LAIDIANSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRA 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRaAEDGLTQLV-AYAVPAEEGGADPA---GLRAHLAARLPAYMVPAA 944
Cdd:cd05973    337 DDVITMSGYRIGPFDVESALIEHPAVAEAAVIGV-PDPERTEVVkAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRT 415

                          490
                   ....*....|....*
gi 1573930569  945 CVLLDALPLTANGKL 959
Cdd:cd05973    416 IHFVDELPKTPSGKI 430
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 480-959 3.41e-47

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: 176.85  E-value: 3.41e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVT 559
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  560 DtagsgrlpatdarvvvvddartvadlagraphdltdadragatGPYDTAYVIHTSGSTGRPKGVPvpHAHVVRLFEASG 639
Cdd:cd05971     85 D-------------------------------------------GSDDPALIIYTSGTTGPPKGAL--HAHRVLLGHLPG 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  640 -----EHFRFGADDVWTLfHSYAFDFSVWELWGPLLHGGrLVVVPYEVSR-SPREFLRLLDEEKVTVLNQTPSAFEQLVL 713
Cdd:cd05971    120 vqfpfNLFPRDGDLYWTP-ADWAWIGGLLDVLLPSLYFG-VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTALKMMRQ 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  714 ADAATDRATGSLRYVVLGGEALVAERLRpWADRH-GLDAPELvnmYGITETTvhvtfhrLVRADLED--PRRRGVIGRPL 790
Cdd:cd05971    198 QGEQLKHAQVKLRAIATGGESLGEELLG-WAREQfGVEVNEF---YGQTECN-------LVIGNCSAlfPIKPGSMGKPI 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  791 ADLRVYVLDAAGRPVPPGATGEMYVSGPG-VA-PGYLNRPELTEERFLPDPFgapgtrmyRSGDLARWRPDGTLVHAGRA 868
Cdd:cd05971    267 PGHRVAIVDDNGTPLPPGEVGEIAVELPDpVAfLGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRD 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  869 DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAE-EGGAD--PAGLRAHLAARLPAYMVPAAC 945
Cdd:cd05971    339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPgETPSDalAREIQELVKTRLAAHEYPREI 418

                          490
                   ....*....|....
gi 1573930569  946 VLLDALPLTANGKL 959
Cdd:cd05971    419 EFVNELPRTATGKI 432
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 1726-2211 1.04e-46

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 178.98  E-value: 1.04e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1726 LRRRGlRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVP---VSYATTSAAVSKLEgiwemldrPWIV--TSAAGEP 1800
Cdd:PRK05850    52 LRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPqggAHDERVSAVLRDTS--------PSVVltTSAVVDD 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1801 GLRELAARREWSGLRLTTADALREEPEDRdwYEARPDDL---VLMLMTSGSTGLPKAVRLTHRNVLTRA--------AAT 1869
Cdd:PRK05850   123 VTEYVAPQPGQSAPPVIEVDLLDLDSPRG--SDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmsdyfGDT 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1870 EAMNGLGSGDVSlnWIPLDHVTGVVMFHLRDVYLGCRQI-HAPTSWiLEDPVRWPELADRHRVSVTWAPNFAFGLlaeQA 1948
Cdd:PRK05850   201 GGVPPPDTTVVS--WLPFYHDMGLVLGVCAPILGGCPAVlTSPVAF-LQRPARWMQLLASNPHAFSAAPNFAFEL---AV 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1949 HRFQDRD---WDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSE-TCSVVT--------------DSV 2010
Cdd:PRK05850   275 RKTSDDDmagLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEaTVYVATrepgqppesvrfdyEKL 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2011 LASEA----PDHDEAFVSCGLPYPGfAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESF----------T 2075
Cdd:PRK05850   355 SAGHAkrceTGGGTPLVSYGSPRSP-TVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgT 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2076 EDG-WFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEElpsVVRSFTAAVAVRSDasaATDELALFLRLAP 2154
Cdd:PRK05850   434 PEGpWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQE---ITGGRVAAISVPDD---GTEKLVAIIELKK 507

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2155 GQDPAGALREIAGKVTREI--------GVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAGEFD 2211
Cdd:PRK05850   508 RGDSDEEAMDRLRTVKREVtsaiskshGLSVADLVLVAPGSIPITTSGKIRRAACVEQYRQDEFT 572
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 457-960 1.47e-46

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 177.77  E-value: 1.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL 536
Cdd:PRK07798     4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDAR------VVVVDDARTVADLAGRAPHD--LT--DADRAGATGPY 606
Cdd:PRK07798    84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRlpklrtLVVVEDGSGNDLLPGAVDYEdaLAagSPERDFGERSP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVvrlFEASGEHFRFG----ADDVWTLFHSYAFDF-SVWELWGPLLHG--------- 672
Cdd:PRK07798   164 DDLYLLYTGGTTGMPKGVMWRQEDI---FRVLLGGRDFAtgepIEDEEELAKRAAAGPgMRRFPAPPLMHGagqwaafaa 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  673 ---GRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLA--DAATDRATGSLRYVVLGGEAL---VAERLRPWa 744
Cdd:PRK07798   241 lfsGQTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMARPLLDalEARGPYDLSSLFAIASGGALFspsVKEALLEL- 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  745 drhgLDAPELVNMYGITETTVHvTFHRLVRADLEDPRRRGVIGRpladlRVYVLDAAGRPVPPGATGEMYVSGPGVAP-G 823
Cdd:PRK07798   320 ----LPNVVLTDSIGSSETGFG-GSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGHIPlG 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  824 YLNRPELTEERFlpdpFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRA 903
Cdd:PRK07798   390 YYKDPEKTAETF----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  904 AEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:PRK07798   466 DERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 468-964 1.81e-46

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 178.31  E-value: 1.81e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  468 ESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLAL 547
Cdd:PRK06178    45 ERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSY 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  548 VMADAEPVAVVT---------------------DTAGSGRLPATDARVV--VVDDARTVADLAGR---APHDLTDADRAG 601
Cdd:PRK06178   125 ELNDAGAEVLLAldqlapvveqvraetslrhviVTSLADVLPAEPTLPLpdSLRAPRLAAAGAIDllpALRACTAPVPLP 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  602 ATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEAS-GEHFRFGADDVwtlFHSYAFDFsvW---ELWG---PLLHGGR 674
Cdd:PRK06178   205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAyAVAVVGGEDSV---FLSFLPEF--WiagENFGllfPLFSGAT 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVVpyevSR-SPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYV--VLGGEALVAERLRPWADRHGLDA 751
Cdd:PRK06178   280 LVLL----ARwDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVrvVSFVKKLNPDYRQRWRALTGSVL 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  752 PELVnmYGITETTVHVTFHRLVRADLEDPRRRGV-IGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPGVAPGYLNRPE 829
Cdd:PRK06178   356 AEAA--WGMTETHTCDTFTAGFQDDDFDLLSQPVfVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPE 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  830 LTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLT 909
Cdd:PRK06178   434 ATAEALRDG--------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQ 505

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  910 QLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAAcVLLDALPLTANGKLDTAAL 964
Cdd:PRK06178   506 VPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDL 559
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 458-967 1.87e-46

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 175.56  E-value: 1.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPG-RTAVSYAGETLSYAELNAEANRLArllvEQGAGPGRFVALALPRgPRLVPALLAVLKTGAAYLPL 536
Cdd:PRK07787     1 LASLNPAAVAAAADiADAVRIGGRVLSRSDLAGAATAVA----ERVAGARRVAVLATPT-LATVLAVVGALIAGVPVVPV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  537 DPGHPAERLALVMADAEPVAVVtdtagsGRLPATDARVVVVDdartvADLAGRAPHDLTDADragatgPYDTAYVIHTSG 616
Cdd:PRK07787    76 PPDSGVAERRHILADSGAQAWL------GPAPDDPAGLPHVP-----VRLHARSWHRYPEPD------PDAPALIVYTSG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAFdfsVWELWGPLLHGGRLVVVpyeVSRSPREFLRL 692
Cdd:PRK07787   139 TTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVhglpLFHVHGL---VLGVLGPLRIGNRFVHT---GRPTPEAYAQA 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 LDEeKVTVLNQTPSAFEQLVlADAATDRATGSLRYVVLGGEAL---VAERLRpwadrhGLDAPELVNMYGITETTVHVTf 769
Cdd:PRK07787   213 LSE-GGTLYFGVPTVWSRIA-ADPEAARALRGARLLVSGSAALpvpVFDRLA------ALTGHRPVERYGMTETLITLS- 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  770 hrlVRADLEdpRRRGVIGRPLADLRVYVLDAAGRPVP--PGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrm 847
Cdd:PRK07787   284 ---TRADGE--RRPGWVGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW------- 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  848 YRSGDLARWRPDGTLVHAGR-ADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEggADPA 926
Cdd:PRK07787   352 FRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAAD 429

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1573930569  927 GLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAP 967
Cdd:PRK07787   430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1845-2208 2.60e-46

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 176.88  E-value: 2.60e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1845 TSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSG-DVSLNWIPLDHVTGVVmFHLRDVYLGCRQIHAPTSWILEDPVRWP 1923
Cdd:PRK05851   160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWL 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1924 ELADRHRVSVTWAPNFAFGLLAEQAHRFqdRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQDVMHPGWGMSE-T 2002
Cdd:PRK05851   239 SWLSDSRATLTAAPNFAYNLIGKYARRV--SDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAEsT 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2003 CSVVT----DSVLASEAPDHDEAFVS----CGLPYPGFAMRVV-DDQDALLPEGDVGRLQVRGTSVTHGYhdnarANAES 2073
Cdd:PRK05851   317 CAVTVpvpgIGLRVDEVTTDDGSGARrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGY-----LGQAP 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2074 FTEDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAATDELALFLRLA 2153
Cdd:PRK05851   392 IDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREG--AVVAVGTGEGSARPGLVIAAEFR 469

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2154 pGQDPAGALREIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEAG 2208
Cdd:PRK05851   470 -GPDEAGARSEVVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRRLAVKRSLEAA 523
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1074-1318 5.16e-46

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 167.14  E-value: 5.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1074 ASFAQERMWFlsrMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrpELHVV 1153
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADL--PLEVV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1154 DC-------PDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLGTAYAARRAGA 1225
Cdd:COG4908     76 DLsalpepeREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEhVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1226 APDWAPPALQYADFALWQRRVLApapegPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHRE 1305
Cdd:COG4908    156 PPPLPELPIQYADYAAWQRAWLQ-----SEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEA 230

                          250
                   ....*....|...
gi 1573930569 1306 LLRLADHENASLF 1318
Cdd:COG4908    231 LKALAKAHGATVN 243
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 482-968 7.01e-46

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: 173.07  E-value: 7.01e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLdpghpaerLALVMADAepvavVTDt 561
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL--------FSAFGPEA-----IRD- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 agsgRLPATDARVVVvddarTVADLAGRaphdltdadragaTGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEH 641
Cdd:cd05969     67 ----RLENSEAKVLI-----TTEELYER-------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYV 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGADDV--------WTLFHSYAfdfsvweLWGPLLHGGRLVVvpYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVL 713
Cdd:cd05969    125 LDLHPDDIywctadpgWVTGTVYG-------IWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  714 ADAATDRA--TGSLRYVVLGGEALVAERLRpWADRhGLDAPeLVNMYGITETTVHVTFHRLVRadledPRRRGVIGRPLA 791
Cdd:cd05969    196 EGDELARKydLSSLRFIHSVGEPLNPEAIR-WGME-VFGVP-IHDTWWQTETGSIMIANYPCM-----PIKPGSMGKPLP 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  792 DLRVYVLDAAGRPVPPGATGEMYVSG--PGVAPGYLNRPELTEERFLpdpfgapgTRMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:cd05969    268 GVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRAD 339

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLTQLVAYAVPAEEGGADPAG-----LRAHLAARLPAYMVPAA 944
Cdd:cd05969    340 DIIKTSGHRVGPFEVESALMEHPAVAEAGVI--GKPDPLRGEIIKAFISLKEGFEPSDelkeeIINFVRQKLGAHVAPRE 417

                          490       500
                   ....*....|....*....|....
gi 1573930569  945 CVLLDALPLTANGKLDTAALPAPD 968
Cdd:cd05969    418 IEFVDNLPKTRSGKIMRRVLKAKE 441
PRK12316 PRK12316
peptide synthase; Provisional
 1040-2203 1.01e-44

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 180.54  E-value: 1.01e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1040 TPTPAALAERLTAGADaGRPLPAltaSERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRhPLDLDALRAALGDVA 1119
Cdd:PRK12316  4075 TPSDFPLAGLDQARLD-ALPLPL---GEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQ-GLDVERFRAAWQAAL 4149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1120 DRHESLRTVFGEEDG------AIHQRVLPPGTlrpELHVVDCPDEERA--AHVAAAMRRSFDLTRDSALWAGVFGTGDTR 1191
Cdd:PRK12316  4150 DRHDVLRSGFVWQGElgrplqVVHKQVSLPFA---ELDWRGRADLQAAldALAAAERERGFDLQRAPLLRLVLVRTAEGR 4226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1192 T-LLLVLHHSAADGWSLRPLADDLGTAYAARRAgaapdwAPPALQYADFALWQRRVLAPAPEgpgrlerltSFWRQALDG 1270
Cdd:PRK12316  4227 HhLIYTNHHILMDGWSNSQLLGEVLERYSGRPP------AQPGGRYRDYIAWLQRQDAAASE---------AFWREQLAA 4291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1271 LPEESAPPPDRPRPAAPSGRGGGVTVP-LDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTE 1349
Cdd:PRK12316  4292 LDEPTRLAQAIARADLRSANGYGEHVReLDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPA 4371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1350 --PALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFdrlvEEVNPRRHPARHPLFQVMLALQN--- 1424
Cdd:PRK12316  4372 elPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPL----YEIQRWAGQGGEALFDSLLVFENypv 4447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1425 ----NERAVLTLGEDRVPLRpaATGTAKFDLFVDVlerhgadgtADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCA 1500
Cdd:PRK12316  4448 sealQQGAPGGLRFGEVTNH--EQTNYPLTLAVGL---------GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAE 4516

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1501 DPEVRTGALPRADrpspatADTTARAGALtravlevpgvgdavvlpgpdgepatvyvvpnragaADRTEqvvsslapgtr 1580
Cdd:PRK12316  4517 DPQRRLGELQLLE------KAEQQRIVAL-----------------------------------WNRTD----------- 4544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1581 vvaiSGLPRTaeggldegalkdlPVIDQVAAgawrERLARlpgvreaevvleevpeelerrhvgrpraaggaaEPDAPSV 1660
Cdd:PRK12316  4545 ----AGYPAT-------------RCVHQLVA----ERARM---------------------------------TPDAVAV 4570

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1661 ERpasvpalsegpalpepsvsgwaeallraagrpdgevvhvradgSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQ 1740
Cdd:PRK12316  4571 VF-------------------------------------------DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIA 4607

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1741 CDDTEDFVATLWGCVLGGFVAVPLTvPVSYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARR--EWSGLRltt 1818
Cdd:PRK12316  4608 MERSAEMMVGLLAVLKAGGAYVPLD-PEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRdeDWEGFP--- 4683

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1819 adalREEPEDRdwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHL 1898
Cdd:PRK12316  4684 ----AHDPAVR----LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYH 4755

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1899 RDVYLGCRQIHAPTSWileDPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfqDRDWDLSPVRLVMNAGEVVVASAARR 1978
Cdd:PRK12316  4756 PLINGASVVIRDDSLW---DPERLYAEIHEHRVTVLVFPPVYLQQLAEHA----ERDGEPPSLRVYCFGGEAVAQASYDL 4828

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1979 FLHVLAPFGLpqdvmHPGWGMSETcsvvTDSVLASEAPDHDE---AFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVR 2055
Cdd:PRK12316  4829 AWRALKPVYL-----FNGYGPTET----TVTVLLWKARDGDAcgaAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLG 4899

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2056 GTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVR 2127
Cdd:PRK12316  4900 GEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4979

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2128 SFTAAVavrsdASAATDELALFL-----RLAPGQDPAGALREIAGKVTReiGVSPAFLIPVE---AEAIPKTEIGKIQRT 2199
Cdd:PRK12316  4980 AVVIAQ-----EGAVGKQLVGYVvpqdpALADADEAQAELRDELKAALR--ERLPEYMVPAHlvfLARMPLTPNGKLDRK 5052


                   ....
gi 1573930569 2200 KLRK 2203
Cdd:PRK12316  5053 ALPQ 5056
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1689-2107 1.40e-44

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 173.36  E-value: 1.40e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvpv 1768
Cdd:COG1022     20 RAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI---- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 sYATTSAA---------------VSKLEgiweMLDRpwiVTSAAGE-PGLRE---LAARREWSGLRLTTADALRE---EP 1826
Cdd:COG1022     96 -YPTSSAEevayilndsgakvlfVEDQE----QLDK---LLEVRDElPSLRHivvLDPRGLRDDPRLLSLDELLAlgrEV 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1827 EDRDWYEAR-----PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTG-VVMFHLrd 1900
Cdd:COG1022    168 ADPAELEARraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFErTVSYYA-- 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1901 VYLGCRQIHAP-TSWILED------------PvR-WPELADRHRVSVTWAP-------NFAFGlLAEQAHRFQDRDWDLS 1959
Cdd:COG1022    246 LAAGATVAFAEsPDTLAEDlrevkptfmlavP-RvWEKVYAGIQAKAEEAGglkrklfRWALA-VGRRYARARLAGKSPS 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1960 PV-RLVMNAGEVVVASAAR----------------------RFLHVLapfGLPqdvMHPGWGMSETCSVVTDSvlaseaP 2016
Cdd:COG1022    324 LLlRLKHALADKLVFSKLRealggrlrfavsggaalgpelaRFFRAL---GIP---VLEGYGLTETSPVITVN------R 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2017 DHDEAFVSCGLPYPGFAMRVVDDqdallpegdvGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYI 2095
Cdd:COG1022    392 PGDNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDeDGFLRI 461

                          490
                   ....*....|..
gi 1573930569 2096 TGRAKDVIIVNG 2107
Cdd:COG1022    462 TGRKKDLIVTSG 473
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1690-2202 3.03e-44

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 171.00  E-value: 3.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDG-EVVHVRADGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL--- 1764
Cdd:PRK13295    34 VASCPDKtAVTAVRLGTGAPRRfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 ------------------TVPVSYA--TTSAAVSKLEGIWEMLdRPWIVTSAAGEPGLRELAARREWSGLRLTTADALRE 1824
Cdd:PRK13295   114 frerelsfmlkhaeskvlVVPKTFRgfDHAAMARRLRPELPAL-RHVVVVGGDGADSFEALLITPAWEQEPDAPAILARL 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1825 EPedrdwyeaRPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLG 1904
Cdd:PRK13295   193 RP--------GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLG 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1905 CRQIHAPTsWileDPVRWPELADRHRVSVTWApnfAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLa 1984
Cdd:PRK13295   265 ATAVLQDI-W---DPARAAELIRTEGVTFTMA---STPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL- 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1985 pfGLpqdVMHPGWGMSEtCSVVTDSVLasEAPDhDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYH 2064
Cdd:PRK13295   337 --GA---KIVSAWGMTE-NGAVTLTKL--DDPD-ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYL 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2065 DNARANAESFteDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAVRSDASAAT 2143
Cdd:PRK13295   408 KRPQLNGTDA--DGWFDTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAI-----AQVAIVAYPDERL 480

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2144 DELAL-FLRLAPGQ--DPAGALREI-AGKVTREIgvSPAFLIPVEAeaIPKTEIGKIQRTKLR 2202
Cdd:PRK13295   481 GERACaFVVPRPGQslDFEEMVEFLkAQKVAKQY--IPERLVVRDA--LPRTPSGKIQKFRLR 539
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1690-2203 4.95e-44

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: 169.73  E-value: 4.95e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVS 1769
Cdd:cd12119      6 ARLHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLF 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1770 -----Y-------------ATTSAAVSKLEGIWEMLDRPWIVTSAAGEPglrELAARREWSglrltTADALREEPEDRDW 1831
Cdd:cd12119     86 peqiaYiinhaedrvvfvdRDFLPLLEAIAPRLPTVEHVVVMTDDAAMP---EPAGVGVLA-----YEELLAAESPEYDW 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHR-NVL-TRAAATEAMNGLGSGDVSLNWIPLDHVTG------VVMFHLRDVYL 1903
Cdd:cd12119    158 PDFDENTAAAICYTSGTTGNPKGVVYSHRsLVLhAMAALLTDGLGLSESDVVLPVVPMFHVNAwglpyaAAMVGAKLVLP 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1904 GCRqihaptswilEDPVRWPELADRHRVSVTWA-PNFAFGLLAEQAhrfqDRDWDLSPVRLVMNAGEVVVASAARRF--L 1980
Cdd:cd12119    238 GPY----------LDPASLAELIEREGVTFAAGvPTVWQGLLDHLE----ANGRDLSSLRRVVIGGSAVPRSLIEAFeeR 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1981 HVlapfglpqDVMHpGWGMSETCSVVTDSVLASEAP--DHDEAF---VSCGLPYPGFAMRVVDDQDALLPEGD--VGRLQ 2053
Cdd:cd12119    304 GV--------RVIH-AWGMTETSPLGTVARPPSEHSnlSEDEQLalrAKQGRPVPGVELRIVDDDGRELPWDGkaVGELQ 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2054 VRGTSVTHGYHdNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAA 2132
Cdd:cd12119    375 VRGPWVTKSYY-KNDEESEALTEDGWLRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEA--AV 451

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2133 VAVRSDasaATDELAL-FLRLAPGQDP-AGALRE-IAGKVTReigvspaFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd12119    452 IGVPHP---KWGERPLaVVVLKEGATVtAEELLEfLADKVAK-------WWLPddvVFVDEIPKTSTGKIDKKALRE 518
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 482-959 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 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTdt 561
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 agsgrlpatdarvvvvddartvadlagraphdLTDADragatgpyDTAYVIHTSGSTGRPKGVPvpHAHVVRLFEASGEH 641
Cdd:cd05935     80 --------------------------------GSELD--------DLALIPYTSGTTGLPKGCM--HTHFSAAANALQSA 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGAD--DVWT----LFHSYAFDFSvweLWGPLLHGGRLVVVpyevSRSPREFLR-LLDEEKVTVLNQTPSAFEQLVLA 714
Cdd:cd05935    118 VWTGLTpsDVILaclpLFHVTGFVGS---LNTAVYVGGTYVLM----ARWDRETALeLIEKYKVTFWTNIPTMLVDLLAT 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  715 DAATDRATGSLRYVVLGGEAL---VAERLRpwaDRHGLDapeLVNMYGITETTVHVTFHRLVRADLEdprrrgVIGRPLA 791
Cdd:cd05935    191 PEFKTRDLSSLKVLTGGGAPMppaVAEKLL---KLTGLR---FVEGYGLTETMSQTHTNPPLRPKLQ------CLGIP*F 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  792 DLRVYVLDA-AGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPfgapGTRMYRSGDLARWRPDGTLVHAGRADQ 870
Cdd:cd05935    259 GVDARVIDIeTGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKR 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  871 QVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAV--PAEEGGADPAGLRAHLAARLPAYMVPAACVLL 948
Cdd:cd05935    335 MINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAYKYPREVEFV 414

                          490
                   ....*....|.
gi 1573930569  949 DALPLTANGKL 959
Cdd:cd05935    415 DELPRSASGKI 425
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 450-957 4.13e-43

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 167.61  E-value: 4.13e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  450 PAPRVTR--TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVL 527
Cdd:PRK06164     2 PHDAAPRadTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  528 KTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTAGSG-------------RLPATDARVVVVDDARTVADLAGRAPHDL 594
Cdd:PRK06164    82 RLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGidfaailaavppdALPPLRAIAVVDDAADATPAPAPGARVQL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  595 TD-ADRAGATG-------PYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELW 666
Cdd:PRK06164   162 FAlPDPAPPAAageraadPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  667 GPLLHGGRLVVVP-YEVSRSprefLRLLDEEKVTVLNQTPSAFEQLvLADAATDRATGSLRYVVLGGEALVAERLRPWAD 745
Cdd:PRK06164   242 GALAGGAPLVCEPvFDAART----ARALRRHRVTHTFGNDEMLRRI-LDTAGERADFPSARLFGFASFAPALGELAALAR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  746 RHGLdapELVNMYGITETTVHVTFHRlvrADLEDPRRRGVIGRPL-ADLRVYVLDAA-GRPVPPGATGEMYVSGPGVAPG 823
Cdd:PRK06164   317 ARGV---PLTGLYGSSEVQALVALQP---ATDPVSVRIEGGGRPAsPEARVRARDPQdGALLPDGESGEIEIRAPSLMRG 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  824 YLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPrA 903
Cdd:PRK06164   391 YLDNPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-A 462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  904 AEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANG 957
Cdd:PRK06164   463 TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1703-2203 1.02e-42

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: 165.18  E-value: 1.02e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1703 ADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL------------------ 1764
Cdd:cd05926      8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLnpaykkaefefyladlgs 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 ---TVPvSYATTSAAVSKLEGIWEMLDrpwivtsAAGEPGLRELAARREWSGLRLTTADALREEPEdrdwyeARPDDLVL 1841
Cdd:cd05926     88 klvLTP-KGELGPASRAASKLGLAILE-------LALDVGVLIRAPSAESLSNLLADKKNAKSEGV------PLPDDLAL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1842 MLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSwileDPVR 1921
Cdd:cd05926    154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRF----SAST 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1922 -WPELADrhrVSVTW---APNFAFGLLAEQAHRFQDRdwdLSPVRLVMNAGevvvASAARRFLHVL-APFGLPqdvMHPG 1996
Cdd:cd05926    230 fWPDVRD---YNATWytaVPTIHQILLNRPEPNPESP---PPKLRFIRSCS----ASLPPAVLEALeATFGAP---VLEA 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETCSVVTDSVLaseaPDHDEAFVSCGLPYpGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTE 2076
Cdd:cd05926    297 YGMTEAAHQMTSNPL----PPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFK 371

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2077 DGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSV--VRSF-----------TAAVAVRSDASAA 2142
Cdd:cd05926    372 DGWFRTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVleAVAFgvpdekygeevAAAVVLREGASVT 451

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2143 TDELALFLRlapgqdpagalREIAG-KVTREIgvspaflipVEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05926    452 EEELRAFCR-----------KHLAAfKVPKKV---------YFVDELPKTATGKIQRRKVAE 493
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 11-248 1.05e-42

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 157.51  E-value: 1.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   11 LSGAQEGLWFahrLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPDeMPVHRVD 90
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDAD-LPLEVVD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   91 VSGEADPAAAAEE--WIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEE 168
Cdd:COG4908     77 LSALPEPEREAELeeLVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  169 PP-PAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPFL--RRTAVLSPAETRALDEAAK 244
Cdd:COG4908    157 PPlPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELpTDRPRPAVQTFRgaTLSFTLPAELTEALKALAK 236


                   ....
gi 1573930569  245 GMGV 248
Cdd:COG4908    237 AHGA 240
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 470-959 2.08e-42

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 165.52  E-value: 2.08e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:PRK08314    24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTD---------------------TAGSGRLPAtDARVVVVDDARTVADLAGRAP---HDLTDADRAGAT- 603
Cdd:PRK08314   104 VTDSGARVAIVGselapkvapavgnlrlrhvivAQYSDYLPA-EPEIAVPAWLRAEPPLQALAPggvVAWKEALAAGLAp 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 -----GPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAFDFSvweLWGPLLHGGR 674
Cdd:PRK08314   183 pphtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLavlpLFHVTGMVHS---MNAPIYAGAT 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVVPyevsRSPREF-LRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAL---VAERLRpwaDRHGLD 750
Cdd:PRK08314   260 VVLMP----RWDREAaARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMpeaVAERLK---ELTGLD 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  751 apeLVNMYGITETTVHVTFHRLVRAdledprRRGVIGRPLADLRVYVLDAA-GRPVPPGATGEMYVSGPGVAPGYLNRPE 829
Cdd:PRK08314   333 ---YVEGYGLTETMAQTHSNPPDRP------KLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPE 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  830 LTEERFLPdpfgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLT 909
Cdd:PRK08314   404 ATAEAFIE----IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI--ATPDPRR 477

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  910 QLVAYAV----PAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK08314   478 GETVKAVvvlrPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 481-959 2.50e-42

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: 162.55  E-value: 2.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 TAGSGRLPATDarvvvvddartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGE 640
Cdd:cd05903     81 ERFRQFDPAAM---------------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  641 HFRFGADDV-WT---LFHSYAFdfsVWELWGPLLHGGRLVVvpyEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADA 716
Cdd:cd05903    128 RLGLGPGDVfLVaspMAHQTGF---VYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVE 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  717 ATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTvhvtfHRLVRADLEDPRRRGVI-GRPLADLRV 795
Cdd:cd05903    202 EAGEPLSRLRTFVCGGATVPRSLARRAAELLGA---KVCSAYGSTECP-----GAVTSITPAPEDRRLYTdGRPLPGVEI 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  796 YVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTeERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRAdQQVKIR 875
Cdd:cd05903    274 KVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGW-------FRTGDLARLDEDGYLRITGRS-KDIIIR 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  876 -GFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLTQLVAYAVPAEEGGADP--AGLRAHL-AARLPAYMVPAACVLLDAL 951
Cdd:cd05903    345 gGENIPVLEVEDLLLGHPGVIEAAVV--ALPDERLGERACAVVVTKSGALLtfDELVAYLdRQGVAKQYWPERLVHVDDL 422


                   ....*...
gi 1573930569  952 PLTANGKL 959
Cdd:cd05903    423 PRTPSGKV 430
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1685-2203 2.89e-42

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 164.31  E-value: 2.89e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGR-PDGEVVHvraDGSEtRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP 1763
Cdd:PRK07656     9 ELLARAARRfGDKEAYV---FGDQ-RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 L-----TVPVSY------ATTSAAVSKLEGIWE-------MLDRPWIVTSAAGEPGLRELAARREWsglrLTTADALREE 1825
Cdd:PRK07656    85 LntrytADEAAYilargdAKALFVLGLFLGVDYsattrlpALEHVVICETEEDDPHTEKMKTFTDF----LAAGDPAERA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1826 PEdrdwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVtgvvmFHLRDVYLGC 1905
Cdd:PRK07656   161 PE------VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHV-----FGYKAGVNAP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1906 rQIHAPTSWILE--DPVRWPELADRHRVSVTWAP----NFafgLLAEQAHRfqdrDWDLSPVRLVMNAGEVVVASAARRF 1979
Cdd:PRK07656   230 -LMRGATILPLPvfDPDEVFRLIETERITVLPGPptmyNS---LLQHPDRS----AEDLSSLRLAVTGAASMPVALLERF 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1980 LHVLapfglPQDVMHPGWGMSETCSVVTDSvlaseaPDHDEAFV---SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRG 2056
Cdd:PRK07656   302 ESEL-----GVDIVLTGYGLSEASGVTTFN------RLDDDRKTvagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2057 TSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFT----- 2130
Cdd:PRK07656   371 PNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVigvpd 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2131 --------AAVAVRSDASAATDELALFLRlapgqdpagalREIAG-KVTREIgvspAFLipveaEAIPKTEIGKIQRTKL 2201
Cdd:PRK07656   451 erlgevgkAYVVLKPGAELTEEELIAYCR-----------EHLAKyKVPRSI----EFL-----DELPKNATGKVLKRAL 510


                   ..
gi 1573930569 2202 RK 2203
Cdd:PRK07656   511 RE 512
PRK07529 PRK07529
AMP-binding domain protein; Validated
 441-964 4.27e-42

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 166.28  E-value: 4.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  441 GEEPVRRDEPAPRVTRTLP----QLFEARVAESPGRTAVSY--------AGETLSYAELNAEANRLARLLVEQGAGPGRF 508
Cdd:PRK07529     6 TLADIEAIEAVPLAARDLPastyELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  509 VALALPRGPRLVPALLAVLKTGAAYlP----LDPGHPAE-----------------------RLALVMADAEPVAVVTDT 561
Cdd:PRK07529    86 VAFLLPNLPETHFALWGGEAAGIAN-PinplLEPEQIAEllraagakvlvtlgpfpgtdiwqKVAEVLAALPELRTVVEV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 AGSGRLPAT----------DARVVVVDDARTVAdlagRAPHDLTDADRagATGPYDTAYVIHTSGSTGRPKGVPVPHAHV 631
Cdd:PRK07529   165 DLARYLPGPkrlavplirrKAHARILDFDAELA----RQPGDRLFSGR--PIGPDDVAAYFHTGGTTGMPKLAQHTHGNE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  632 VRLFEASGEHFRFGADDV----WTLFHSYAfdfSVWELWGPLLHGGRLVVVPYEVSRSP---REFLRLLDEEKVTVLNQT 704
Cdd:PRK07529   239 VANAWLGALLLGLGPGDTvfcgLPLFHVNA---LLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  705 PSAFEqlVLADAATDRA-TGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTfhrlvRADLEDPRRR 783
Cdd:PRK07529   316 PTVYA--ALLQVPVDGHdISSLRYALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEATCVSS-----VNPPDGERRI 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  784 GVIGRPL--ADLRVYVLDAAG---RPVPPGATGEMYVSGPGVAPGYL----NRPELTEERFLpdpfgapgtrmyRSGDLA 854
Cdd:PRK07529   386 GSVGLRLpyQRVRVVILDDAGrylRDCAVDEVGVLCIAGPNVFSGYLeaahNKGLWLEDGWL------------NTGDLG 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  855 RWRPDGTLVHAGRAdQQVKIR-GFRIEPGEIEAVLTAHPAVAGGAVVPR----AAEdgltqL-VAYAVPAEEGGADPAGL 928
Cdd:PRK07529   454 RIDADGYFWLTGRA-KDLIIRgGHNIDPAAIEEALLRHPAVALAAAVGRpdahAGE-----LpVAYVQLKPGASATEAEL 527

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1573930569  929 RAHLAARLP---AymVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK07529   528 LAFARDHIAeraA--VPKHVRILDALPKTAVGKIFKPAL 564
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 444-964 9.78e-42

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: 163.22  E-value: 9.78e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  444 PVRRDEPAPRvtrTLPQLFEARVAESPGRTAVSY----AGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRL 519
Cdd:cd05906      1 PLHRPEGAPR---TLLELLLRAAERGPTKGITYIdadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  520 VPALLAVLKTGAAYLPLDPGH----PAERLalvmadaEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLT 595
Cdd:cd05906     78 IPAFWACVLAGFVPAPLTVPPtydePNARL-------RKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIE 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRAGA------TGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVwTLfhsyafdfsvweLWGPL 669
Cdd:cd05906    151 ELLDTAAdhdlpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV-FL------------NWVPL 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  670 LHGGRLV---------------VVPYEVSRSPREFLRLLDEEKVTVlNQTPSAFEQLVLADAATDRAT----GSLRYVVL 730
Cdd:cd05906    218 DHVGGLVelhlravylgcqqvhVPTEEILADPLRWLDLIDRYRVTI-TWAPNFAFALLNDLLEEIEDGtwdlSSLRYLVN 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  731 GGEALVA---ERLRPWADRHGLDAPELVNMYGITETTVHVTFHRLVRADLEDPRRRGV-IGRPLADLRVYVLDAAGRPVP 806
Cdd:cd05906    297 AGEAVVAktiRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVsLGRPIPGVSMRIVDDEGQLLP 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  807 PGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLArWRPDGTLVHAGRADQQVKIRGFRIEPGEIEA 886
Cdd:cd05906    377 EGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  887 VLTAHPAVAGG---AVVPRAAEDGLTQLVAYAVPAEEGGADPAGL----RAHLAARL---PAYMVPAAcvlLDALPLTAN 956
Cdd:cd05906    449 AVEEVPGVEPSftaAFAVRDPGAETEELAIFFVPEYDLQDALSETlraiRSVVSREVgvsPAYLIPLP---KEEIPKTSL 525


                   ....*...
gi 1573930569  957 GKLDTAAL 964
Cdd:cd05906    526 GKIQRSKL 533
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 456-959 1.62e-41

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: 161.52  E-value: 1.62e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAY 533
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  534 LPLDPGHPAERLALVMADAEPVAVVTdtaGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDTAYVIH 613
Cdd:cd05923     81 ALINPRLKAAELAELIERGEMTAAVI---AVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  614 TSGSTGRPKGVPVPHAHVVR--LFEASGEHFRFGADDV----WTLFHSYAFdFSVweLWGPLLHGGRLVVVPYEvsrSPR 687
Cdd:cd05923    158 TSGTTGLPKGAVIPQRAAESrvLFMSTQAGLRHGRHNVvlglMPLYHVIGF-FAV--LVAALALDGTYVVVEEF---DPA 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  688 EFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAL---VAERLrpwadrHGLDAPELVNMYGITETt 764
Cdd:cd05923    232 DALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMpdaVLERV------NQHLPGEKVNIYGTTEA- 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  765 VHVTFHRLVRAdledprrrGVIGRPLADLRVYVLDAAGRPV---PPGATGEMYVSGPGVAP--GYLNRPELTEERfLPDp 839
Cdd:cd05923    305 MNSLYMRDART--------GTEMRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAAftGYLNQPEATAKK-LQD- 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  840 fgapgtRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDgLTQLVAYAVPAE 919
Cdd:cd05923    375 ------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADER-WGQSVTACVVPR 447

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1573930569  920 EGGADPAGLRAH-LAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:cd05923    448 EGTLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKV 488
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 456-959 2.10e-41

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 162.53  E-value: 2.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAV------SYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKT 529
Cdd:PRK13295    24 RTINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  530 GAAYLPLDPGHPAERLALVMADAEPVAVVT-------DTAGSGR-----LPATDaRVVVV--DDARTVADLAGRAPHDLT 595
Cdd:PRK13295   104 GAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfDHAAMARrlrpeLPALR-HVVVVggDGADSFEALLITPAWEQE 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRAGAT----GPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFdfsVWELWG 667
Cdd:PRK13295   183 PDAPAILArlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIlmasPMAHQTGF---MYGLMM 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  668 PLLHGGRLVvvpYEVSRSPREFLRLLDEEKVT-VLNQTPSAFEqLVLADAATDRATGSLRYVVLGGEAL---VAERLRpw 743
Cdd:PRK13295   260 PVMLGATAV---LQDIWDPARAAELIRTEGVTfTMASTPFLTD-LTRAVKESGRPVSSLRTFLCAGAPIpgaLVERAR-- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  744 adrHGLDApELVNMYGITETTVhVTFHRLvraDLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPG 823
Cdd:PRK13295   334 ---AALGA-KIVSAWGMTENGA-VTLTKL---DDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGG 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  824 YLNRPELTEErflpdpfGAPGtrMYRSGDLARWRPDGTLVHAGRAdQQVKIRGFR-IEPGEIEAVLTAHPAVAGGAVV-- 900
Cdd:PRK13295   406 YLKRPQLNGT-------DADG--WFDTGDLARIDADGYIRISGRS-KDVIIRGGEnIPVVEIEALLYRHPAIAQVAIVay 475

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  901 --PRAAEdgltQLVAYAVPAEEGGADPAGLRAHL-AARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK13295   476 pdERLGE----RACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1072-1501 2.14e-41

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: 159.73  E-value: 2.14e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTL---RP 1148
Cdd:cd20483      2 RPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFhliVI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1149 ELHVVDCPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTR-TLLLVLHHSAADGWSLRPLADDLgTAYAARRAGAAP 1227
Cdd:cd20483     82 DLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEfALVLASHHIAWDRGSSKSIFEQF-TALYDALRAGRD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1228 DW--APPALQYADFALWQRRVLAPApegpgRLERLTSFWRQALDGLPEESAPP--PDRPRPAAPSGRGGGVTVPLDAGTH 1303
Cdd:cd20483    161 LAtvPPPPVQYIDFTLWHNALLQSP-----LVQPLLDFWKEKLEGIPDASKLLpfAKAERPPVKDYERSTVEATLDKELL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1304 RELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVR 1383
Cdd:cd20483    236 ARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1384 AFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNNEravltlgedrvPLRPAATGTAKF------------DL 1451
Cdd:cd20483    316 TTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHG-----------KFPEYDTGDFKFtdydhydiptacDI 384

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1452 FVDVLErhGADGtadGLDLHVEYAADLYDPATAERFAGALRDLLTVVCAD 1501
Cdd:cd20483    385 ALEAEE--DPDG---GLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1689-2207 2.53e-41

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: 161.85  E-value: 2.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAG----RPDGEVVHVRAD---------GSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCV 1755
Cdd:COG1021     17 REAGywrgETLGDLLRRRAErhpdriavvDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALF 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1756 LGGfvAVPLTVPVS--------YATTSAAVSklegiwemldrpWIVTSAAGEPGLRELAA--RREWSGLR---------- 1815
Cdd:COG1021     97 RAG--AIPVFALPAhrraeishFAEQSEAVA------------YIIPDRHRGFDYRALARelQAEVPSLRhvlvvgdage 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1816 LTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHR----NVLTRAAATeamnGLGSGDVSLNWIPLDH-- 1889
Cdd:COG1021    163 FTSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAEIC----GLDADTVYLAALPAAHnf 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1890 ------VTGVvmfhlrdVYLGCRQIHAPTSwileDPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfQDRDWDLSPVRL 1963
Cdd:COG1021    239 plsspgVLGV-------LYAGGTVVLAPDP----SPDTAFPLIERERVTVTALVPPLALLWLDAA---ERSRYDLSSLRV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1964 VMNAGEVVVASAARRflhVLAPFGL-PQDVmhpgWGMSETCSVVTDsvlaseaPDHDEAFV--SCGLPY-PGFAMRVVDD 2039
Cdd:COG1021    305 LQVGGAKLSPELARR---VRPALGCtLQQV----FGMAEGLVNYTR-------LDDPEEVIltTQGRPIsPDDEVRIVDE 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2040 QDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEAC 2118
Cdd:COG1021    371 DGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRAKDQINRGGEKIAAEEVENL 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2119 VEELPSVVRSftAAVAV-------RSDAsaatdelalFLRLAPGQDPAGALReiagKVTREIGVSpAFLIP--VE-AEAI 2188
Cdd:COG1021    451 LLAHPAVHDA--AVVAMpdeylgeRSCA---------FVVPRGEPLTLAELR----RFLRERGLA-AFKLPdrLEfVDAL 514

                          570
                   ....*....|....*....
gi 1573930569 2189 PKTEIGKIQRTKLRKSFEA 2207
Cdd:COG1021    515 PLTAVGKIDKKALRAALAA 533
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 446-964 3.17e-41

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 161.85  E-value: 3.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  446 RRDEPAPRVTRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLA 525
Cdd:PRK06155    11 RAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLG 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  526 VLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDA------RVVVVDDARTVADLAGRAPHDLTDADR 599
Cdd:PRK06155    91 CAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPgdlplpAVWLLDAPASVSVPAGWSTAPLPPLDA 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  600 ---AGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFDfsvwELWGPLLHG 672
Cdd:PRK06155   171 papAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLyttlPLFHTNALN----AFFQALLAG 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  673 GRLVVVP-YEVSRspreFLRLLDEEKVTVlNQTPSAFEQLVLADAATDRATGSLRYVVLGGeALVAERLRPWADRHGLDa 751
Cdd:PRK06155   247 ATYVLEPrFSASG----FWPAVRRHGATV-TYLLGAMVSILLSQPARESDRAHRVRVALGP-GVPAALHAAFRERFGVD- 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  752 peLVNMYGITETTVhvtfhrlVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYV--SGPGV-APGYLNRP 828
Cdd:PRK06155   320 --LLDGYGSTETNF-------VIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLraDEPFAfATGYFGMP 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  829 ELTEErflpdpfgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGL 908
Cdd:PRK06155   391 EKTVE--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGE 462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  909 TQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK06155   463 DEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 470-964 1.20e-40

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: 159.72  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGE----TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERL 545
Cdd:cd12119     10 GDREIVSRTHEgevhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQI 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  546 ALVMADAEPVAVVTD-------TAGSGRLPaTDARVVVVDDArtvADLAGRAPHDLTDADR--AGATGPYD-------TA 609
Cdd:cd12119     90 AYIINHAEDRVVFVDrdflpllEAIAPRLP-TVEHVVVMTDD---AAMPEPAGVGVLAYEEllAAESPEYDwpdfdenTA 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  610 YVI-HTSGSTGRPKGV------PVPHAHVVRLFEASGehfrFGADDVWT----LFHSYAfdfsvwelWG-P---LLHGGR 674
Cdd:cd12119    166 AAIcYTSGTTGNPKGVvyshrsLVLHAMAALLTDGLG----LSESDVVLpvvpMFHVNA--------WGlPyaaAMVGAK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVvPyEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAlVAERLRPWADRHGLDapeL 754
Cdd:cd12119    234 LVL-P-GPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSA-VPRSLIEAFEERGVR---V 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  755 VNMYGITETTVHVTFHRL---VRADLEDPR--RRGVIGRPLADLRVYVLDAAGRPVP--PGATGEMYVSGPGVAPGYLNR 827
Cdd:cd12119    308 IHAWGMTETSPLGTVARPpseHSNLSEDEQlaLRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKN 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  828 PELTEErFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDG 907
Cdd:cd12119    388 DEESEA-LTEDGW-------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKW 459

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  908 LTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd12119    460 GERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 462-964 1.32e-40

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 158.82  E-value: 1.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARVaeSPGR-TAVSYA-GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:PRK09088     3 FHARL--QPQRlAAVDLAlGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAgsgrLPATDARVVVVDDARTVADLAGRAPHDLTDADRAgatgpydtAYVIHTSGSTG 619
Cdd:PRK09088    81 LSASELDALLQDAEPRLLLGDDA----VAAGRTDVEDLAAFIASADALEPADTPSIPPERV--------SLILFTSGTSG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPH------AHVVRLFEASGEHFRFGADDvwTLFHSYAFDFSVWELwgpLLHGGRLVVVP-YEVSRSprefLRL 692
Cdd:PRK09088   149 QPKGVMLSErnlqqtAHNFGVLGRVDAHSSFLCDA--PMFHIIGLITSVRPV---LAVGGSILVSNgFEPKRT----LGR 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 LDEEKVTVLN-----QTPSAFEQLVLADAAtdrATGSLRYVVLGGEALVAERLRPWADrhglDAPELVNMYGITET-TVh 766
Cdd:PRK09088   220 LGDPALGITHyfcvpQMAQAFRAQPGFDAA---ALRHLTALFTGGAPHAAEDILGWLD----DGIPMVDGFGMSEAgTV- 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 vtFHRLVRADLEDpRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtr 846
Cdd:PRK09088   292 --FGMSVDCDVIR-AKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------ 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  847 mYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGltqlVAYAVPAEEGG 922
Cdd:PRK09088   363 -FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgmadAQWGEVG----YLAIVPADGAP 437

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1573930569  923 ADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK09088   438 LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 2301-2705 1.87e-40

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 157.14  E-value: 1.87e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2301 RPGEAGDLAAVLERLEADGRTPDTVvhlAATEDA---EDGAAPGSDVSLLV-LAQALAGRTGGERPVdLLFVTAGAQAVT 2376
Cdd:cd08953     41 APAALASAFLALAYEAALLGLAAAE---AALLDAlsaLDPAAALQLLESLQrLLKAGLLAARASGRA-LLQVVTGLPGAL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2377 PEERPTASHAAAGALLKSLREELPWLRGVHLDLSGGSAG-DRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAPR 2455
Cdd:cd08953    117 GLDALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDAGEASaEALARELAAELAAPGAAEVRYRDGLRYVQTLEPLPLPAGA 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2456 TAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERhladagpassriEAFRRLRGLG-EVRY 2534
Cdd:cd08953    197 AASAPLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKA------------QTLAALEALGaRVLY 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2535 ETADVTDAAQVRAAVRRAADAWGvPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSS 2614
Cdd:cd08953    265 ISADVTDAAAVRRLLEKVRERYG-AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSS 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2615 VNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLA--WSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLAR 2692
Cdd:cd08953    344 VSAFFGGAGQADYAAANAFLDAFAAYLRQRGPQGRVLSinWPAWREGGMAADLGARELLARAGLLPIEPEEGLQALEQAL 423

                          410
                   ....*....|...
gi 1573930569 2693 TLDLPHLLIGADR 2705
Cdd:cd08953    424 SSDLPQVLVSPGD 436
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 1711-2125 6.34e-40

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: 155.83  E-value: 6.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvpvsYATTSAAvsklegiwemlDRP 1790
Cdd:cd05907      7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI-----YPTSSAE-----------QIA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTSAAgepglrelaarrewsglrlttADALREEPedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05907     71 YILNDSE---------------------AKALFVED---------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALA 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAP-TSWILED------------PVRWPELADR-HRVSVTWA 1936
Cdd:cd05907    121 ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASsAETLLDDlsevrptvflavPRVWEKVYAAiKVKAVPGL 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1937 PNFAFGLLAeqahrfqdrdwdLSPVRLVMNAGevvvASAARRFLHVLAPFGLPqdvMHPGWGMSETCSVVTDSvlaseaP 2016
Cdd:cd05907    201 KRKLFDLAV------------GGRLRFAASGG----APLPAELLHFFRALGIP---VYEGYGLTETSAVVTLN------P 255

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2017 DHDEAFVSCGLPYPGFAMRVVDDqdallpegdvGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYI 2095
Cdd:cd05907    256 PGDNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGeIDEDGFLHI 325

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1573930569 2096 TGRAKDVIIV-NGVNHYSHEIEACVEELPSV 2125
Cdd:cd05907    326 TGRKKDLIITsGGKNISPEPIENALKASPLI 356
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
447-895 1.05e-39

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 158.34  E-value: 1.05e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  447 RDEPAPRVTRTLPQLFEARVAESPGRTAVSY----AGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPA 522
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  523 LLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTAG--------SGRLPATDaRVVVVDD--------ARTVADL 586
Cdd:COG1022     82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqldkllevRDELPSLR-HIVVLDPrglrddprLLSLDEL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  587 --AGRAPHDLTDAD-RAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLF----HSYAFD 659
Cdd:COG1022    161 laLGREVADPAELEaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplaHVFERT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  660 FSVWelwgpLLHGGrlVVVPYevSRSPREFLRLLDEEKVTVL-------------------------------------- 701
Cdd:COG1022    241 VSYY-----ALAAG--ATVAF--AESPDTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkrklfrwalavgrr 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  702 -------NQTPSAFEQLVLADAatDR--------ATGS-LRYVVLGGEALvAERLrpwaDR--HGLDAPeLVNMYGITET 763
Cdd:COG1022    312 yararlaGKSPSLLLRLKHALA--DKlvfsklreALGGrLRFAVSGGAAL-GPEL----ARffRALGIP-VLEGYGLTET 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  764 TVHVTFHRLVRadledpRRRGVIGRPLADLRVYVldaagrpvppGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgap 843
Cdd:COG1022    384 SPVITVNRPGD------NRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW--- 444

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  844 gtrmYRSGDLARWRPDGTLVHAGRADQQVKIR-GFRIEPGEIEAVLTAHPAVA 895
Cdd:COG1022    445 ----LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIE 493
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 479-960 2.01e-39

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: 155.57  E-value: 2.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  479 GETLSYAELNAEANRLARLLvEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVV 558
Cdd:cd05909      5 GTSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  559 T-----DTAGSGRLP--ATDARVVVVDDAR---TVAD-----LAGRAPHDLTDAdRAGATG--PYDTAYVIHTSGSTGRP 621
Cdd:cd05909     84 TskqfiEKLKLHHLFdvEYDARIVYLEDLRakiSKADkckafLAGKFPPKWLLR-IFGVAPvqPDDPAVILFTSGSEGLP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFDFSvweLWGPLLHGGRLVVVPyevsrSP---REFLRLLD 694
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVfgalPFFHSFGLTGC---LWLPLLSGIKVVFHP-----NPldyKKIPELIY 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  695 EEKVTVLNQTPSAFEQlvLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTFHRlvr 774
Cdd:cd05909    235 DKKATILLGTPTFLRG--YARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGI---RILEGYGTTECSPVISVNT--- 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  775 adLEDPRRRGVIGRPLADLRVYVLDAAGR-PVPPGATGEMYVSGPGVAPGYLNRPELTEErflpdpfgAPGTRMYRSGDL 853
Cdd:cd05909    307 --PQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSF--------AFGDGWYDTGDI 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPrAAEDGL--TQLVAYAVPAEeggADPAGLRAH 931
Cdd:cd05909    377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVV-SVPDGRkgEKIVLLTTTTD---TDPSSLNDI 452

                          490       500       510
                   ....*....|....*....|....*....|
gi 1573930569  932 L-AARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd05909    453 LkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 481-959 6.81e-39

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: 156.32  E-value: 6.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:cd05967     82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTA 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 TAG-------------------SGRLPAT-------DARVVVVDDARTV---ADLAGRAPHDLTDADragATgpyDTAYV 611
Cdd:cd05967    162 SCGiepgkvvpykplldkalelSGHKPHHvlvlnrpQVPADLTKPGRDLdwsELLAKAEPVDCVPVA---AT---DPLYI 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  612 IHTSGSTGRPKGVPVPHA-HVVRLFEA--------SGEHFrFGADDV-WTLFHSYAfdfsvweLWGPLLHG-------GR 674
Cdd:cd05967    236 LYTSGTTGKPKGVVRDNGgHAVALNWSmrniygikPGDVW-WAASDVgWVVGHSYI-------VYGPLLHGattvlyeGK 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVVPyevsrSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRAT----GSLRYVVLGGEALVAERLRpWADRHgLD 750
Cdd:cd05967    308 PVGTP-----DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIKkydlSSLRTLFLAGERLDPPTLE-WAENT-LG 380

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  751 APeLVNMYGITETTVHVTFHRLVRADLedPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPgVAPGYLNRPEL 830
Cdd:cd05967    381 VP-VIDHWWQTETGWPITANPVGLEPL--PIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWK 456

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  831 TEERFLPDPFGA-PGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLT 909
Cdd:cd05967    457 NDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV--GVRDELK 532

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  910 QLV--AYAVPAEEGGADPA----GLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:cd05967    533 GQVplGLVVLKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
457-959 8.52e-39

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 154.91  E-value: 8.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVS-YAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:PRK06087    24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDT------------AGSGRLPATDaRVVVVDDAR------TVADLAGRAPhDLTDA 597
Cdd:PRK06087   104 LLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLPQLQ-QIVGVDKLApatsslSLSQIIADYE-PLTTA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  598 DRAGATgpyDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFDFSVWelwGPLLHGG 673
Cdd:PRK06087   182 ITTHGD---ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFmmpaPLGHATGFLHGVT---APFLIGA 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  674 RLVVvpyEVSRSPREFLRLLDEEKVT-VLNQTPSAFEQLVLADAATDRATgSLRYVVLGGeALVAERLRPWADRHGLdap 752
Cdd:PRK06087   256 RSVL---LDIFTPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPADLS-ALRFFLCGG-TTIPKKVARECQQRGI--- 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  753 ELVNMYGITETTVHVtfhrLVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTe 832
Cdd:PRK06087   328 KLLSVYGSTESSPHA----VVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELT- 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  833 ERFLPDpfgapgTRMYRSGDLARWRPDGTLVHAGRaDQQVKIRGFR-IEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQL 911
Cdd:PRK06087   403 ARALDE------EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERS 475

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569  912 VAYAVP-AEEGGADPAGLRAHLA-ARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK06087   476 CAYVVLkAPHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKI 525
PRK12316 PRK12316
peptide synthase; Provisional
 1040-2203 1.22e-38

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 160.51  E-value: 1.22e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1040 TPTPAALAERLTAGADAgrpLPaLTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHpLDLDALRAALGDVA 1119
Cdd:PRK12316  1529 TPSDFPLAGLSQAQLDA---LP-LPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATV 1603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1120 DRHESLRTVFGEEDG------AIHQRVLPPGTLRPELHVVDcPDEERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTR-T 1192
Cdd:PRK12316  1604 DRHEILRSGFLWQDGleqplqVIHKQVELPFAELDWRGRED-LGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRhH 1682

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1193 LLLVLHHSAADGWSLRPLaddLGTAYAARRAGAAPDwapPALQYADFALWQRRVLAPAPEgpgrlerltSFWRQALDGLP 1272
Cdd:PRK12316  1683 LIYTNHHILMDGWSNAQL---LGEVLQRYAGQPVAA---PGGRYRDYIAWLQRQDAAASE---------AFWKEQLAALE 1747

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1273 EESAPPPDRPRPAAPSGRGGGVtVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTE--P 1350
Cdd:PRK12316  1748 EPTRLAQAARTEDGQVGYGDHQ-QLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelP 1826

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1351 ALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLP---------------FDRLVEEVNprrhparhpl 1415
Cdd:PRK12316  1827 GIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPlydiqrwagqggealFDSLLVFEN---------- 1896

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1416 FQVMLALQNNERAVLTLGedrvplRPAATGTAKFDLFVDVlerhgadGTADGLDLHVEYAADLYDPATAERFAGALRDLL 1495
Cdd:PRK12316  1897 YPVAEALKQGAPAGLVFG------RVSNHEQTNYPLTLAV-------TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLL 1963

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1496 TVVCADPEVRTGALPRADrpspatadttaragaltravlevpgvgdavvlpgpdgepatvyvvpnragaadrteqvvssl 1575
Cdd:PRK12316  1964 EQMAEDAQAALGELALLD-------------------------------------------------------------- 1981

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1576 aPGTRVVAISGLPRTaegglDEGALKDLPVIDQVAAGAwrerlarlpgvreaevvleevpeelerrhvgrpraaggAAEP 1655
Cdd:PRK12316  1982 -AGERQRILADWDRT-----PEAYPRGPGVHQRIAEQA--------------------------------------ARAP 2017

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1656 DAPSVerpasvpalsegpalpepsVSGwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPGD 1735
Cdd:PRK12316  2018 EAIAV-------------------VFG------------------------DQHLSYAELDSRANRLAHRLRARGVGPEV 2054

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1736 RVILQCDDTEDFVATLWGCVLGGFVAVPLTvpVSYATtsaavsklEGIWEMLDRPWIVTSAAGEPGLRELAARREWSGLR 1815
Cdd:PRK12316  2055 RVAIAAERSFELVVALLAVLKAGGAYVPLD--PNYPA--------ERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLP 2124

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1816 LTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDhVTGVVM 1895
Cdd:PRK12316  2125 LDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFS-FDGAHE 2203

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1896 FHLRDVYLGCRQIHAPTSwiLEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHrfqdRDWDLSPVRLVMNAGEVVVASA 1975
Cdd:PRK12316  2204 QWFHPLLNGARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE----RDGRPPAVRVYCFGGEAVPAAS 2277

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1976 ARRFLHVLAPFGLPQdvmhpGWGMSETcsVVTDSVLASEAPD-HDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQV 2054
Cdd:PRK12316  2278 LRLAWEALRPVYLFN-----GYGPTEA--VVTPLLWKCRPQDpCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYL 2350

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2055 RGTSVTHGYHDNARANAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVv 2126
Cdd:PRK12316  2351 GGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV- 2429

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 rsfTAAVAVRSDASAATDELALFLRLAPGQDPAGALREIAGkvtreiGVSPAFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK12316  2430 ---REAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLA------ARLPAYMVPahwVVLERLPLNPNGKLDRKALPK 2500
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
465-959 1.53e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 152.42  E-value: 1.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAER 544
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  545 LALVMADAEPVAVVTDtagsgrlPATDARVVVVDDAR--TVADLAGRAPHDLTDADRAgatgpyDTAYVIHTSGSTGRPK 622
Cdd:PRK03640    91 LLWQLDDAEVKCLITD-------DDFEAKLIPGISVKfaELMNGPKEEAEIQEEFDLD------EVATIMYTSGTTGKPK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  623 GVPVPHA-HvvrLFEASGEHFRFG--ADDVW----TLFHSYAFdfSVweLWGPLLHGGRLVVVP-YEVSRSprefLRLLD 694
Cdd:PRK03640   158 GVIQTYGnH---WWSAVGSALNLGltEDDCWlaavPIFHISGL--SI--LMRSVIYGMRVVLVEkFDAEKI----NKLLQ 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  695 EEKVTVLNQTPSAFEQLvLADAATDRATGSLRYVVLGG----EALVAErlrpwADRHGLdaPeLVNMYGITETTVHVtfh 770
Cdd:PRK03640   227 TGGVTIISVVSTMLQRL-LERLGEGTYPSSFRCMLLGGgpapKPLLEQ-----CKEKGI--P-VYQSYGMTETASQI--- 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  771 rlVRADLEDPRRR-GVIGRPLADLRVYVLDAaGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmyR 849
Cdd:PRK03640   295 --VTLSPEDALTKlGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------K 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  850 SGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLTQLVAYAVPAEEGGADPAGLR 929
Cdd:PRK03640   364 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV--GVPDDKWGQVPVAFVVKSGEVTEEELR 441

                          490       500       510
                   ....*....|....*....|....*....|
gi 1573930569  930 AHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK03640   442 HFCEEKLAKYKVPKRFYFVEELPRNASGKL 471
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1683-2202 2.00e-38

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: 152.91  E-value: 2.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1683 WAEALLRAAGRPDGEVVhvraDGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:cd05959      7 TLVDLNLNEGRGDKTAF----IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 P---LTVP---VSYATTSAA-VSKLEGiwEMLDRpwiVTSAAG--EPGLREL--AARREWSGLRLTTADALREEPEDRDW 1831
Cdd:cd05959     83 PvntLLTPddyAYYLEDSRArVVVVSG--ELAPV---LAAALTksEHTLVVLivSGGAGPEAGALLLAELVAAEAEQLKP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHRNvLTRAAATEAMNGLG--SGDVSLNWIPLDHVTGV---VMFHL----RDVY 1902
Cdd:cd05959    158 AATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYARNVLGirEDDVCFSAAKLFFAYGLgnsLTFPLsvgaTTVL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1903 LGCRqihaPTswiledPVRWPELADRHRVSVTWA-PNFAFGLLAeqAHRFQDRDwdLSPVRLVMNAGEVVVASAARRFLh 1981
Cdd:cd05959    237 MPER----PT------PAAVFKRIRRYRPTVFFGvPTLYAAMLA--APNLPSRD--LSSLRLCVSAGEALPAEVGERWK- 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1982 vlAPFGLpqDVMHpGWGMSETCSVvtdsvLASEAPdHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTH 2061
Cdd:cd05959    302 --ARFGL--DILD-GIGSTEMLHI-----FLSNRP-GRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSAT 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2062 GYHDNARANAESFtEDGWFDTGDlAFLR--DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDA 2139
Cdd:cd05959    371 MYWNNRDKTRDTF-QGEWTRTGD-KYVRddDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGVEDE 445

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2140 SAATDELAlFLRLAPGQDPAGAL-REIAGKVTREIgvsPAFLIP---VEAEAIPKTEIGKIQRTKLR 2202
Cdd:cd05959    446 DGLTKPKA-FVVLRPGYEDSEALeEELKEFVKDRL---APYKYPrwiVFVDELPKTATGKIQRFKLR 508
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1073-1502 2.01e-38

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: 150.93  E-value: 2.01e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrpELHV 1152
Cdd:cd20484      3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPL--SFQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1153 VDCPD---EERAAHVAAAMRRSFDLTRDSALWAGVFGTGDTRT-LLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPD 1228
Cdd:cd20484     81 EDISSlkeSEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1229 WAPPALQYADFALWQRRVLApAPEGpgrlERLTSFWRQALDG------LPEESAPppdrprPAAPSGRGGGVTVPLDAGT 1302
Cdd:cd20484    161 LASSPASYYDFVAWEQDMLA-GAEG----EEHRAYWKQQLSGtlpileLPADRPR------SSAPSFEGQTYTRRLPSEL 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1303 HRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARV 1382
Cdd:cd20484    230 SNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKL 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1383 RAFDVQALDHQDLPFDRLVEEVNPRRHPARHPLFQVMLALQNneraVLTLGEDRVPLRPAATGTA-----------KFDL 1451
Cdd:cd20484    310 QLTVLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQN----FLQSTSLQQFLAEYQDVLSiefvegihqegEYEL 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 1452 FVDVLErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd20484    386 VLEVYE------QEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 8-423 2.64e-38

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: 150.61  E-value: 2.64e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADtfALRFLDTPDGPRAVRDG--DPDEMP 85
Cdd:cd19539      1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHE--ALRTLLVRDDGGVPRQEilPPGPAP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   86 VHRVDVSGEADPAAAAEEWIRRDLA-TPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALA 164
Cdd:cd19539     79 LEVRDLSDPDSDRERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  165 AGEEPP-PAGFESADRLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRLTDRTAPPRAPflRRTAVLS---PAETR-AL 239
Cdd:cd19539    159 KGPAAPlPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRPAGFP--YPGADLRfelDAELVaAL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  240 DEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAVADDL 319
Cdd:cd19539    237 RELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  320 RGLRAHQRHRGESIRRDLGVL---GRGRRVHG--PVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPGAEADTLW 394
Cdd:cd19539    317 VDAQRHQELPFQQLVAELPVDrdaGRHPLVQIvfQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGS 396

                          410       420
                   ....*....|....*....|....*....
gi 1573930569  395 LAFDAhpDLYEEDGLALFLERFLKVLREL 423
Cdd:cd19539    397 LGYAT--SLFDEETIQGFLADYLQVLRQL 423
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
463-964 3.67e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 151.94  E-value: 3.67e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  463 EARVAESPGRTAVSYAGETLSYAELNAEANRLARLLV-EQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP 541
Cdd:PRK06839     9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  542 AERLALVMADAEpVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDTAYvihTSGSTGRP 621
Cdd:PRK06839    89 ENELIFQLKDSG-TTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIICY---TSGTTGKP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVvrLFEASGEHFRFG--ADDV----WTLFHSYA---FDFSVWelwgplLHGGRlVVVPYEVSrsPREFLRL 692
Cdd:PRK06839   165 KGAVLTQENM--FWNALNNTFAIDltMHDRsivlLPLFHIGGiglFAFPTL------FAGGV-IIVPRKFE--PTKALSM 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 LDEEKVTVLNQTPSAFEQLVladAATDRATGSL---RYVVLGGEALVAERLRPWADRhGLdapELVNMYGITETTVhvTF 769
Cdd:PRK06839   234 IEKHKVTVVMGVPTIHQALI---NCSKFETTNLqsvRWFYNGGAPCPEELMREFIDR-GF---LFGQGFGMTETSP--TV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  770 HRLVRadlEDPRRR-GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEErflpdpfgAPGTRMY 848
Cdd:PRK06839   305 FMLSE---EDARRKvGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWL 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  849 RSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGL 928
Cdd:PRK06839   374 CTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDV 453

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1573930569  929 RAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK06839   454 IEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 10-326 4.68e-38

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: 149.81  E-value: 4.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVR--EAdtfaLR--FLDTPDGPRAVRDgDPDEMP 85
Cdd:cd19531      3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVArhEA----LRttFVEVDGEPVQVIL-PPLPLP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   86 VHRVDVSGEADPAAAA--EEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTAL 163
Cdd:cd19531     78 LPVVDLSGLPEAEREAeaQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  164 AAGEEP--PPAGFESADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPVRL-TDRTAPPRAPFL--RRTAVLSPAETRA 238
Cdd:cd19531    158 LAGRPSplPPLPIQYAD-YAVWQREWLQGEVLERQLAYWREQLAGAPPVLELpTDRPRPAVQSFRgaRVRFTLPAELTAA 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  239 LDEAAKGMGVarTD--LLVAAVAAFLHRMTGADDLVLGLATmsrlgsaALRT-PGTASDI------LPLRVAASADTPVG 309
Cdd:cd19531    237 LRALARREGA--TLfmTLLAAFQVLLHRYSGQDDIVVGTPV-------AGRNrAELEGLIgffvntLVLRTDLSGDPTFR 307

                          330
                   ....*....|....*..
gi 1573930569  310 GFVRAVADDLRGLRAHQ 326
Cdd:cd19531    308 ELLARVRETALEAYAHQ 324
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1711-2203 7.70e-38

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: 149.02  E-value: 7.70e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyattsaavsklegiwEMLdrp 1790
Cdd:cd05972      2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLT-------------------TLL--- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 wivtsaagepGLRELAARREWSGLRLTTADAlreepedrdwyearpDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05972     60 ----------GPKDIEYRLEAAGAKAIVTDA---------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLN-----WI---------PLDHVTGVVMFHLRDVylgcrqihaptswileDPVRWPELADRHRVSVTWA 1936
Cdd:cd05972    115 YWLGLRPDDIHWNiadpgWAkgawssffgPWLLGATVFVYEGPRF----------------DAERILELLERYGVTSFCG 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1937 PNFAFGLLAEQ-AHRFqdrdwDLSPVRLVMNAGEVVVASAARRFlhvLAPFGLPqdvMHPGWGMSETCSVVTDSVLASEA 2015
Cdd:cd05972    179 PPTAYRMLIKQdLSSY-----KFSHLRLVVSAGEPLNPEVIEWW---RAATGLP---IRDGYGQTETGLTVGNFPDMPVK 247

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2016 PDhdeafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVR--GTSVTHGYHDNARANAESFTEDgWFDTGDLA-FLRDGE 2092
Cdd:cd05972    248 PG------SMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAyRDEDGY 320

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2093 LYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVA----VRSDASAAtdelalFLRLAPGQDPAGAL-REIAG 2167
Cdd:cd05972    321 FWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE--AAVVGspdpVRGEVVKA------FVVLTSGYEPSEELaEELQG 392

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1573930569 2168 KVTREIGvspAFLIPVEAE---AIPKTEIGKIQRTKLRK 2203
Cdd:cd05972    393 HVKKVLA---PYKYPREIEfveELPKTISGKIRRVELRD 428
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1711-2125 1.41e-37

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: 147.80  E-value: 1.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLR-RRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyatTSAAVSKLEGIWEMLDR 1789
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLD-------PAYPAERLAFILEDAGA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1790 PWIVTSAAGEPGLRELA-ARREWSGLRLTTADALREEPEDRDwyEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA 1868
Cdd:TIGR01733   74 RLLLTDSALASRLAGLVlPVILLDPLELAALDDAPAPPPPDA--PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 TEAMNGLGSGDVSLNWIPLDHVTGVV-MFhlRDVYLGCRQIHAPTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQ 1947
Cdd:TIGR01733  152 LARRYGLDPDDRVLQFASLSFDASVEeIF--GALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1948 AHRfqdrdwDLSPVRLVMNAGEVVVASAARRFLHVLapfglPQDVMHPGWGMSETCsVVTDSVLASEAPDHDEAFVSCGL 2027
Cdd:TIGR01733  230 LPP------ALASLRLVILGGEALTPALVDRWRARG-----PGARLINLYGPTETT-VWSTATLVDPDDAPRESPVPIGR 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2028 PYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG--------WFDTGDLAFLR-DGELYITGR 2098
Cdd:TIGR01733  298 PLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLpDGNLEFLGR 377

                          410       420
                   ....*....|....*....|....*..
gi 1573930569 2099 AKDVIIVNGVNHYSHEIEACVEELPSV 2125
Cdd:TIGR01733  378 IDDQVKIRGYRIELGEIEAALLRHPGV 404
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
477-966 1.93e-37

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 152.88  E-value: 1.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  477 YAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVA 556
Cdd:PRK06060    26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  557 VVTdtagSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGAtgpydtAYVIHTSGSTGRPKGVPVPHAHVVRLFE 636
Cdd:PRK06060   106 VVT----SDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDAL------AYATYTSGTTGPPKAAIHRHADPLTFVD 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  637 A-SGEHFRFGADDVW----TLFHSYAFDFSVWelwGPLLHGGRLVVVPYEVSRSPREFLRLLDEEkvTVLNQTPSAFEQL 711
Cdd:PRK06060   176 AmCRKALRLTPEDTGlcsaRMYFAYGLGNSVW---FPLATGGSAVINSAPVTPEAAAILSARFGP--SVLYGVPNFFARV 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  712 VlaDAATDRATGSLRYVVLGGEAL---VAERLRPWADrhGLDApelvnMYGITETTVHVTFhrlvRADLEDPRRRGVIGR 788
Cdd:PRK06060   251 I--DSCSPDSFRSLRCVVSAGEALelgLAERLMEFFG--GIPI-----LDGIGSTEVGQTF----VSNRVDEWRLGTLGR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 PLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPE--LTEERFLpdpfgapGTRmyrsgDLARWRPDGTLVHAG 866
Cdd:PRK06060   318 VLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL-------DTR-----DRVCIDSDGWVTYRC 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  867 RADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLR---AHLAARLPAYMVPA 943
Cdd:PRK06060   386 RADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPH 465

                          490       500
                   ....*....|....*....|...
gi 1573930569  944 ACVLLDALPLTANGKLDTAALPA 966
Cdd:PRK06060   466 RFAVVDRLPRTPNGKLVRGALRK 488
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1690-2201 2.16e-37

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: 148.55  E-value: 2.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVhvraDGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvs 1769
Cdd:cd05945      1 AAANPDRPAV----VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD---- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1770 yatTSAAVSKLEGIwemldrpwivtSAAGEPGLrelaarrewsglrlttadalreepedrdwYEARPDDLVLMLMTSGST 1849
Cdd:cd05945     73 ---ASSPAERIREI-----------LDAAKPAL-----------------------------LIADGDDNAYIIFTSGST 109

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1850 GLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDhvtgvvmFHLRDVYLGCRQIHAPTSWIL-----EDPVRWPE 1924
Cdd:cd05945    110 GRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS-------FDLSVMDLYPALASGATLVPVprdatADPKQLFR 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1925 LADRHRVSVtW--APNFAFGLLAEQAhRFQDRdwdLSPVRLVMNAGEVVVASAARRFLHVLapfglPQDVMHPGWGMSET 2002
Cdd:cd05945    183 FLAEHGITV-WvsTPSFAAMCLLSPT-FTPES---LPSLRHFLFCGEVLPHKTARALQQRF-----PDARIYNTYGPTEA 252

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2003 CSVVTDSVLaSEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTED---GW 2079
Cdd:cd05945    253 TVAVTYIEV-TPEVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRA 331

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2080 FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAPGqDP 2158
Cdd:cd05945    332 YRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV----KEAVVVPKYKGEKVTELIAFVVPKPG-AE 406

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569 2159 AGALREIAGKVTREIgvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd05945    407 AGLTKAIKAELAERL---PPYMIPrrfVYLDELPLNANGKIDRKAL 449
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 605-958 4.43e-37

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: 144.73  E-value: 4.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  605 PYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----LFHSYAfdfSVWELWGPLLHGGRLVVVpy 680
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCipvpLFHCFG---SVLGVLACLTHGATMVFP-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  681 EVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRpwADRHGLDAPELVNMYGI 760
Cdd:cd05917     76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMK--RVIEVMNMKDVTIAYGM 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  761 TETTVHVTFHRlvrADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPP-GATGEMYVSGPGVAPGYLNRPELTEERFLPDp 839
Cdd:cd05917    154 TETSPVSTQTR---TDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  840 fgapgtRMYRSGDLARWRPDGTLVHAGRAdQQVKIRGFR-IEPGEIEAVLTAHPAVAGGAVV----PRAAEdgltQLVAY 914
Cdd:cd05917    230 ------GWLHTGDLAVMDEDGYCRIVGRI-KDMIIRGGEnIYPREIEEFLHTHPKVSDVQVVgvpdERYGE----EVCAW 298

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1573930569  915 AVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:cd05917    299 IRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1836-2202 7.89e-37

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: 143.96  E-value: 7.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSWi 1915
Cdd:cd05917      1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSF- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 leDPVrwPELADRHRVSVTwapnFAFGL----LAEQAHRFQDRdWDLSPVRLVMNAGEVVVASAARRflhVLAPFGLPQd 1991
Cdd:cd05917     80 --DPL--AVLEAIEKEKCT----ALHGVptmfIAELEHPDFDK-FDLSSLRTGIMAGAPCPPELMKR---VIEVMNMKD- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1992 vMHPGWGMSETCSVVTDSVLASEApdhDEAFVSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARAN 2070
Cdd:cd05917    147 -VTIAYGMTETSPVSTQTRTDDSI---EKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKT 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2071 AESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAatDELALF 2149
Cdd:cd05917    223 AEAIDGDGWLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDV--QVVGVPDERYG--EEVCAW 298

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 2150 LRLAPGQDPAGA-LRE-IAGKVTR-EIgvsPAFLIPVeaEAIPKTEIGKIQRTKLR 2202
Cdd:cd05917    299 IRLKEGAELTEEdIKAyCKGKIAHyKV---PRYVFFV--DEFPLTVSGKIQKFKLR 349
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1684-2211 8.56e-37

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 148.16  E-value: 8.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAGR-PDGEVVHVRadgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVav 1762
Cdd:PRK08316    14 GDILRRSARRyPDKTALVFG----DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV-- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 plTVPVSYATTSAAVSKLEGIWEmldrpwiVTSAAGEPGLRELAARREWSGLRLTTADALREEPED--------RDWYEA 1834
Cdd:PRK08316    88 --HVPVNFMLTGEELAYILDHSG-------ARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREapggwldfADWAEA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RP----------DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLG 1904
Cdd:PRK08316   159 GSvaepdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1905 CrqihapTSWILE--DPVRWPELADRHRVSVTWA-PNFAFGLLaeQAHRFQDRDwdLSPVR------LVMnAGEVVVASA 1975
Cdd:PRK08316   239 A------TNVILDapDPELILRTIEAERITSFFApPTVWISLL--RHPDFDTRD--LSSLRkgyygaSIM-PVEVLKELR 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1976 ARrflhvlapfgLPQDVMHPGWGMSETCSVVTdsVLASEapDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVR 2055
Cdd:PRK08316   308 ER----------LPGLRFYNCYGQTEIAPLAT--VLGPE--EHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2056 GTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSV--------- 2125
Cdd:PRK08316   374 SPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVaevaviglp 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2126 ----VRSFTAAVAVRSDASAATDELALFLR--LAPgqdpagalreiagkvtreigvspaFLIP---VEAEAIPKTEIGKI 2196
Cdd:PRK08316   453 dpkwIEAVTAVVVPKAGATVTEDELIAHCRarLAG------------------------FKVPkrvIFVDELPRNPSGKI 508

                          570
                   ....*....|....*
gi 1573930569 2197 QRTKLRKSFEAGEFD 2211
Cdd:PRK08316   509 LKRELRERYAGAFTD 523
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 2328-2703 9.58e-37

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 144.45  E-value: 9.58e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2328 LAATEDAEDGAAPGSDVSLLVLAQALA-----GRTGGERPVDLLFVTAGAQAVTPEERPTASHAAAGALLKSLREELPWL 2402
Cdd:cd05274      9 AGALSLLAVAPACGAADAVLALAALLAlvaalLAAYASTGPPLWLVTRGAEAVSADDVAALAQAALWGLLRVLALEHPEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2403 RGVHLDLSGGSAGDRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAPRTAPAPAPADGFHLVSGGLGGVGSEVAA 2482
Cdd:cd05274     89 WGGLVDLDAADAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALELAAAPGGLDGTYLITGGLGGLGLLVAR 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2483 HLLKEPGTRLLLIGRTGLPPEDTWerhladagpassrieAFRRLRGLG-EVRYETADVTDAAQVRAAVRRAADawGVPLV 2561
Cdd:cd05274    169 WLAARGARHLVLLSRRGPAPRAAA---------------RAALLRAGGaRVSVVRCDVTDPAALAALLAELAA--GGPLA 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2562 SVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDLALRR 2641
Cdd:cd05274    232 GVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQR 311

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2642 RREGLPGQSLAWSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLARTLDLPHLLIGA 2703
Cdd:cd05274    312 RRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQAVVAS 373
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 470-959 1.00e-36

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 148.27  E-value: 1.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:PRK07470    21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDTAGSGRLPAtdARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDTAYVIH--------TSGSTGRP 621
Cdd:PRK07470   101 EASGARAMICHADFPEHAAA--VRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHddpcwfffTSGTTGRP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHA--------HVVRLFEASGEHfrfgaddvwtlfhsyafDFSVweLWGPLLHG-----------GRLVVVPYEV 682
Cdd:PRK07470   179 KAAVLTHGqmafvitnHLADLMPGTTEQ-----------------DASL--VVAPLSHGagihqlcqvarGAATVLLPSE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  683 SRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGealvAERLRpwADR-HGLDA--PELVNMYG 759
Cdd:PRK07470   240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG----APMYR--ADQkRALAKlgKVLVQYFG 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHVTFHRLVRADLED-PRRR-GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLP 837
Cdd:PRK07470   314 LGEVTGNITVLPPALHDAEDgPDARiGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRD 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  838 DPFgapgtrmyRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGltqlVA 913
Cdd:PRK07470   394 GWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLgvpdPVWGEVG----VA 461

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569  914 YAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK07470   462 VCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 453-959 1.13e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 148.54  E-value: 1.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  453 RVTRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALaLPRGPR-LVPALLAVLKTGA 531
Cdd:PRK07788    46 RRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRgFVLALYAAGKVGA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  532 AYLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRL---PATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDT 608
Cdd:PRK07788   125 RIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLsalPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPK 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  609 A-----YVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTL----FHSYAFdfSVWELwgPLLHGGRLVVvp 679
Cdd:PRK07788   205 PpkpggIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLpapmFHATGW--AHLTL--AMALGSTVVL-- 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  680 yevSR--SPREFLRLLDEEKVTVLNQTPSAFEQLV--LADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPELV 755
Cdd:PRK07788   279 ---RRrfDPEATLEDIAKHKATALVVVPVMLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFG---PVLY 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  756 NMYGITETTVHVTfhrlvrADLEDPRRR-GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLN-RPELTEE 833
Cdd:PRK07788   353 NLYGSTEVAFATI------ATPEDLAEApGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIID 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  834 RFLpdpfgapgtrmyRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVA 913
Cdd:PRK07788   427 GLL------------SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRA 494

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569  914 YAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK07788   495 FVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1707-2201 1.27e-36

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: 146.13  E-value: 1.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL--TVPVSYattsaavskLEGIw 1784
Cdd:cd05930     10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLdpSYPAER---------LAYI- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1785 emldrpwivtsaagepgLRELAARrewsgLRLTTadalreepedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLT 1864
Cdd:cd05930     80 -----------------LEDSGAK-----LVLTD-----------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVN 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1865 RAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHlrdVYL--GCRQIHAPTSWILeDPVRWPELADRHRVSVTWAPNFAFG 1942
Cdd:cd05930    121 LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF---GALlaGATLVVLPEEVRK-DPEALADLLAEEGITVLHLTPSLLR 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1943 LLAEQAhrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVlapfgLPQDVMHPGWGMSETCSVVTDSVLASEAPDHDEaf 2022
Cdd:cd05930    197 LLLQEL-----ELAALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTEATVDATYYRVPPDDEEDGR-- 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2023 VSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFD------TGDLA-FLRDGELYI 2095
Cdd:cd05930    265 VPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVrWLPDGNLEF 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2096 TGRAKDVIIVNGvnhysH-----EIEACVEELPSVVRsftAAVAVRSDAsAATDELALFLRLAPGQDP-AGALREIAGKV 2169
Cdd:cd05930    345 LGRIDDQVKIRG-----YrielgEIEAALLAHPGVRE---AAVVAREDG-DGEKRLVAYVVPDEGGELdEEELRAHLAER 415

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1573930569 2170 TreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd05930    416 L------PDYMVPsafVVLDALPLTPNGKVDRKAL 444
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 607-964 2.23e-36

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: 143.00  E-value: 2.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV----WTLFHSYAfdfSVWELWGPLLHGGRLVVVPYEV 682
Cdd:cd05944      3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVllcgLPLFHVNG---SVVTLLTPLASGAHVVLAGPAG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  683 SRSP---REFLRLLDEEKVTVLNQTPSAFEqlVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYG 759
Cdd:cd05944     80 YRNPglfDNFWKLVERYRITSLSTVPTVYA--ALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL---PVVEGYG 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHVTfhrlvRADLEDPRRRGVIGRPL--ADLRVYVLDAAG---RPVPPGATGEMYVSGPGVAPGYLNrpeltEER 834
Cdd:cd05944    155 LTEATCLVA-----VNPPDGPKRPGSVGLRLpyARVRIKVLDGVGrllRDCAPDEVGEICVAGPGVFGGYLY-----TEG 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  835 FLpDPFGAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAY 914
Cdd:cd05944    225 NK-NAFVADG--WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAY 301

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  915 AVPAEEGGADPAGLRAHLAARLPAY-MVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05944    302 VQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 448-959 6.37e-36

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 145.46  E-value: 6.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  448 DEPAPRVTR-TLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVAlALPRGPRLVPAL-LA 525
Cdd:PRK08316     2 MERSTRARRqTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVA-ALGHNSDAYALLwLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  526 VLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGP 605
Cdd:PRK08316    81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  606 Y----------DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV----WTLFHSYAFDFsvweLWGPLLH 671
Cdd:PRK08316   161 VaepdveladdDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIplhaLPLYHCAQLDV----FLGPYLY 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 -GGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRhgLD 750
Cdd:PRK08316   237 vGATNVILD---APDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRER--LP 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  751 APELVNMYGITETTvhvTFHRLVRADlEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPEL 830
Cdd:PRK08316   312 GLRFYNCYGQTEIA---PLATVLGPE-EHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEK 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  831 TEERFLPDPFgapgtrmyRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEd 906
Cdd:PRK08316   388 TAEAFRGGWF--------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIglpdPKWIE- 458

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  907 gltQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK08316   459 ---AVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 481-936 1.04e-35

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: 143.50  E-value: 1.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEpvavvtd 560
Cdd:cd05907      5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSE------- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 tagsgrlpatdARVVVVDDartvadlagraphdltdadragatgPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGE 640
Cdd:cd05907     78 -----------AKALFVED-------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAE 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  641 HFRFGADDVWTLF----HSYAfdfSVWELWGPLLHGGRLVVVPyevsrSPREFLRLLDEEKVTVLNQTPSAFEQLVLADA 716
Cdd:cd05907    122 RLPATEGDRHLSFlplaHVFE---RRAGLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIK 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  717 ATD-----------RATGSLRYVVLGGEALVAERLRPWadrHGLDAPeLVNMYGITETTVHVTFHRLVRadledpRRRGV 785
Cdd:cd05907    194 VKAvpglkrklfdlAVGGRLRFAASGGAPLPAELLHFF---RALGIP-VYEGYGLTETSAVVTLNPPGD------NRIGT 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  786 IGRPLADLRVYVldaagrpvppGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHA 865
Cdd:cd05907    264 VGKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHIT 326

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  866 GRA-DQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV--------------PRAAEDGLTQLVAYAVPAEEGGADPAgLRA 930
Cdd:cd05907    327 GRKkDLIITSGGKNISPEPIENALKASPLISQAVVIgdgrpflvalivpdPEALEAWAEEHGIAYTDVAELAANPA-VRA 405


                   ....*.
gi 1573930569  931 HLAARL 936
Cdd:cd05907    406 EIEAAV 411
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 462-958 1.17e-35

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 145.81  E-value: 1.17e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEA--RVAESP--GRTAVSYAG----ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAY 533
Cdd:PRK04319    46 YEAidRHADGGrkDKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  534 LPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATD----ARVVVVDDARTVAD-------LAGRAPHDLTdadrAGA 602
Cdd:PRK04319   126 GPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDlpslKHVLLVGEDVEEGPgtldfnaLMEQASDEFD----IEW 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  603 TGPYDTAYVIHTSGSTGRPKGvpVPHAHvvrlfEASGEHFRFG-------ADDV--------WTLFHSYAfdfsvweLWG 667
Cdd:PRK04319   202 TDREDGAILHYTSGSTGKPKG--VLHVH-----NAMLQHYQTGkyvldlhEDDVywctadpgWVTGTSYG-------IFA 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  668 PLLHGGRLVVvpYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLA--DAATDRATGSLRYVVLGGEALVAERLRpWAD 745
Cdd:PRK04319   268 PWLNGATNVI--DGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAgdDLVKKYDLSSLRHILSVGEPLNPEVVR-WGM 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  746 RhGLDAPELVNmYGITETTVHV-----TFhrlvradledPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYV-SG-P 818
Cdd:PRK04319   345 K-VFGLPIHDN-WWMTETGGIMianypAM----------DIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwP 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  819 GVAPGYLNRPELTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGA 898
Cdd:PRK04319   413 SMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  899 VV----PRAAE---------DGLTqlvayavPAEEGGADpagLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:PRK04319   485 VIgkpdPVRGEiikafvalrPGYE-------PSEELKEE---IRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 10-326 1.47e-35

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: 142.34  E-value: 1.47e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDG-PRAVRDGDPdEMPVHR 88
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGePLQVVLKDR-KLPWRE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   89 VDVSGEADPAAAAE--EWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:cd19543     82 LDLSHLSEAEQEAEleALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EE---PPPAGFEsadrlaaEEAAYLgsDRHRRD--RAYWTERLAGLPEPVRL-TDRTAPPRAPFLRRTAV--LSPAETRA 238
Cdd:cd19543    162 QPpslPPVRPYR-------DYIAWL--QRQDKEaaEAYWREYLAGFEEPTPLpKELPADADGSYEPGEVSfeLSAELTAR 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  239 LDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGlATMSrlgsaalrtpGTASDI-------------LPLRVAASAD 305
Cdd:cd19543    233 LQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFG-TTVS----------GRPAELpgietmvglfintLPVRVRLDPD 301

                          330       340
                   ....*....|....*....|.
gi 1573930569  306 TPVGGFVRAVADDLRGLRAHQ 326
Cdd:cd19543    302 QTVLELLKDLQAQQLELREHE 322
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1073-1502 2.01e-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: 141.29  E-value: 2.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMwfLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEE--DGAIHQRVLPpgTLRPEL 1150
Cdd:cd19542      3 PCTPMQEGM--LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLK--SLDPPI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1151 HVVDCPDEEraahVAAAMRRSFDltrDSALWAGVF-------GTGDTRTLLLVLHHSAADGWSLRPLADDL-----GTAY 1218
Cdd:cd19542     79 EEVETDEDS----LDALTRDLLD---DPTLFGQPPhrltlleTSSGEVYLVLRISHALYDGVSLPIILRDLaaaynGQLL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1219 aarragaapdwaPPALQYADFAlwQRRVLAPAPEGpgrlerlTSFWRQALDGLPEESAPPPDrprpaapSGRGGGVTVPL 1298
Cdd:cd19542    152 ------------PPAPPFSDYI--SYLQSQSQEES-------LQYWRKYLQGASPCAFPSLS-------PKRPAERSLSS 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1299 DAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRT--EPALDEVVGLLTNTLVLRADASGDPTFR 1376
Cdd:cd19542    204 TRRSLAKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVL 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1377 ELLARVRAFDVQALDHQDLPFDRLVEEVNPRRHparHPLFQVMLALQN-NERAVLTLGEDRVPLRPAATGTAKFDLFVDV 1455
Cdd:cd19542    284 DLLRQLQQQYLRSLPHQHLSLREIQRALGLWPS---GTLFNTLVSYQNfEASPESELSGSSVFELSAAEDPTEYPVAVEV 360

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1573930569 1456 LErhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19542    361 EP------SGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 1701-2203 3.28e-35

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: 141.66  E-value: 3.28e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1701 VRADGSetRRSYASLVPEASRVLAGLRRRG-LRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvPVSYattsaavsk 1779
Cdd:cd05941      5 IVDDGD--SITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPL--NPSY--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1780 legiwemldrpwivtsaagepGLRELAARREWSGLRLTTADALreepedrdwyearpddlvlMLMTSGSTGLPKAVRLTH 1859
Cdd:cd05941     72 ---------------------PLAELEYVITDSEPSLVLDPAL-------------------ILYTSGTTGRPKGVVLTH 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1860 RNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSwileDPVRWPELADRHRVSVTWA-PN 1938
Cdd:cd05941    112 ANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKF----DPKEVAISRLMPSITVFMGvPT 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1939 FAFGLLAEQAHRFQDRDWDLS----PVRLVMNAgevvvaSAArrflhvlapfgLPQDVMHPgW------------GMSET 2002
Cdd:cd05941    188 IYTRLLQYYEAHFTDPQFARAaaaeRLRLMVSG------SAA-----------LPVPTLEE-WeaitghtlleryGMTEI 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2003 csvvtdsVLASEAPDHDEAFV-SCGLPYPGFAMRVVDDQDA-LLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWF 2080
Cdd:cd05941    250 -------GMALSNPLDGERRPgTVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWF 322

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2081 DTGDLAFLR-DGELYITGRAKDVII-VNGVNHYSHEIEACVEELPSVVRS-------------FTAAVAVRSDASAAT-D 2144
Cdd:cd05941    323 KTGDLGVVDeDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECavigvpdpdwgerVVAVVVLRAGAAALSlE 402

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 2145 ELALFL--RLAPGQDPagalreiagkvTREIGVspaflipveaEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05941    403 ELKEWAkqRLAPYKRP-----------RRLILV----------DELPRNAMGKVNKKELRK 442
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1073-1496 4.03e-35

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: 140.97  E-value: 4.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrpELHV 1152
Cdd:cd19533      3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPV--PIRH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1153 VDC---PDEERAAH--VAAAMRRSFDLTRDSALWAGVFGTGDTRTLLLV-LHHSAADGWSLRPLADDLGTAYAARRAGAa 1226
Cdd:cd19533     81 IDLsgdPDPEGAAQqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTALLKGR- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1227 pdwAPPALQYADFALWQRRVLAPApeGPGRLERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGggvTVPLDAGTHREL 1306
Cdd:cd19533    160 ---PAPPAPFGSFLDLVEEEQAYR--QSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRR---TAELPPELTRTL 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1307 LRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFD 1386
Cdd:cd19533    232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1387 VQALDHQDLPFDRLVEEVnpRRHPARHPLFQVMLALQNNERAvLTLGEDRVPLRPAATGTAKfDLFVDVLERhgadGTAD 1466
Cdd:cd19533    312 RSLLRHQRYRYEDLRRDL--GLTGELHPLFGPTVNYMPFDYG-LDFGGVVGLTHNLSSGPTN-DLSIFVYDR----DDES 383

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1573930569 1467 GLDLHVEYAADLYDPATA----ERFAGALRDLLT 1496
Cdd:cd19533    384 GLRIDFDANPALYSGEDLarhqERLLRLLEEAAA 417
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 1686-2205 7.68e-35

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 141.94  E-value: 7.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1686 ALLRAAGRPDGEVVHVRADGSetRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLT 1765
Cdd:PRK07514     7 DALRAAFADRDAPFIETPDGL--RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1766 VpvsyATTSAAVSKLEGIWEmldrP-WIVTSAAGEPGLRELAARR----------EWSGlrlTTADALREEPEDRDWYEA 1834
Cdd:PRK07514    85 T----AYTLAELDYFIGDAE----PaLVVCDPANFAWLSKIAAAAgaphvetldaDGTG---SLLEAAAAAPDDFETVPR 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGvvMFHLRDVYL--GCRQIHAP- 1911
Cdd:PRK07514   154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHG--LFVATNVALlaGASMIFLPk 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1912 -------------TSW---------ILEDPVRWPELADRHRVSVTW-APnfafgLLAEQAHRFQDRdwdlspvrlvmnAG 1968
Cdd:PRK07514   232 fdpdavlalmpraTVMmgvptfytrLLQEPRLTREAAAHMRLFISGsAP-----LLAETHREFQER------------TG 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1969 EVVVasaaRRFlhvlapfglpqdvmhpgwGMSETCsvvtdsVLASEAPDHDEAFVSCGLPYPGFAMRVVD-DQDALLPEG 2047
Cdd:PRK07514   295 HAIL----ERY------------------GMTETN------MNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPG 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2048 DVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV 2126
Cdd:PRK07514   347 EIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVV 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 RS---------F----TAAVAVRSDASAatdelalflrlapgqDPAGALREIAGKVTReigvspaFLIP---VEAEAIPK 2190
Cdd:PRK07514   427 ESavigvphpdFgegvTAVVVPKPGAAL---------------DEAAILAALKGRLAR-------FKQPkrvFFVDELPR 484

                          570
                   ....*....|....*
gi 1573930569 2191 TEIGKIQRTKLRKSF 2205
Cdd:PRK07514   485 NTMGKVQKNLLREQY 499
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 607-964 9.01e-35

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: 137.46  E-value: 9.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFH--SYAFdfsvweLWGPLLHGGRLVVVPY 680
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWllslPLYHvgGLAI------LVRSLLAGAELVLLER 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  681 EvsrspREFLRLLDEEKVTVLNQTPSAFEQLvLADAATDRATGSLRYVVLGGEALVAERLRPWADRHgldaPELVNMYGI 760
Cdd:cd17630     75 N-----QALAEDLAPPGVTHVSLVPTQLQRL-LDSGQGPAALKSLRAVLLGGAPIPPELLERAADRG----IPLYTTYGM 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  761 TETTVHVTFHRLvradleDPRRRGVIGRPLADLRVYVLDaagrpvppgaTGEMYVSGPGVAPGYLNRPelteerfLPDPF 840
Cdd:cd17630    145 TETASQVATKRP------DGFGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQ-------LVPEF 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  841 GAPGTrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPaeE 920
Cdd:cd17630    202 NEDGW--FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG--R 277

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1573930569  921 GGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd17630    278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1684-2202 9.91e-35

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 142.60  E-value: 9.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAGR-PDGEVVHVRADGseTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:PRK12583    21 GDAFDATVARfPDREALVVRHQA--LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 PLTVPVSYATTSAAVSKLEGIW-------------EMLDR--PWIVTSAAGE------PGLRELA--ARREWSGLrlTTA 1819
Cdd:PRK12583    99 NINPAYRASELEYALGQSGVRWvicadafktsdyhAMLQEllPGLAEGQPGAlacerlPELRGVVslAPAPPPGF--LAW 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1820 DALREEPE---DRDWYEA----RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTG 1892
Cdd:PRK12583   177 HELQARGEtvsREALAERqaslDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFG 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1893 VVMFHLRDVYLGCRQIHAPTSWileDPVRWPELADRHRVSVTWAPNFAFglLAEQAHRfQDRDWDLSPVRLVMNAGEVVV 1972
Cdd:PRK12583   257 MVLANLGCMTVGACLVYPNEAF---DPLATLQAVEEERCTALYGVPTMF--IAELDHP-QRGNFDLSSLRTGIMAGAPCP 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1973 ASAARRflhVLAPFGLPQDVMhpGWGMSETCSVvtdSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRL 2052
Cdd:PRK12583   331 IEVMRR---VMDEMHMAEVQI--AYGMTETSPV---SLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2053 QVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftA 2131
Cdd:PRK12583   403 CTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAV-----A 477

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2132 AVAVRS-DASAATDELALFLRLAPGQDPA-GALREIAG------KVTREIGVSPAFlipveaeaiPKTEIGKIQRTKLR 2202
Cdd:PRK12583   478 DVQVFGvPDEKYGEEIVAWVRLHPGHAASeEELREFCKariahfKVPRYFRFVDEF---------PMTVTGKVQKFRMR 547
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 469-964 1.49e-34

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 140.68  E-value: 1.49e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  469 SPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRfVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:PRK07638    14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAgatgPYdtaYVIHTSGSTGRPKGVPVPH 628
Cdd:PRK07638    93 LAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNA----PF---YMGFTSGSTGKPKAFLRAQ 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  629 AHVVRLFEASGEHFRFGADD----VWTLFHSYafdFsvweLWGPL--LHGGRLVVVpyEVSRSPREFLRLLDEEKVTVLN 702
Cdd:PRK07638   166 QSWLHSFDCNVHDFHMKREDsvliAGTLVHSL---F----LYGAIstLYVGQTVHL--MRKFIPNQVLDKLETENISVMY 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  703 QTPSAFEQLVLADAATDRatgSLRYVVLGG--EALVAERLR---PWADRHgldapelvNMYGITETTVhVTFhrLVRADL 777
Cdd:PRK07638   237 TVPTMLESLYKENRVIEN---KMKIISSGAkwEAEAKEKIKnifPYAKLY--------EFYGASELSF-VTA--LVDEES 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  778 EdpRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEErflPDPFGAPGTRmyrsgDLARWR 857
Cdd:PRK07638   303 E--RRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---LNADGWMTVR-----DVGYED 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  858 PDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAvpaeEGGADPAGLRAHLAARLP 937
Cdd:PRK07638   373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLS 448

                          490       500
                   ....*....|....*....|....*..
gi 1573930569  938 AYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK07638   449 SFKIPKEWHFVDEIPYTNSGKIARMEA 475
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1703-2202 3.37e-34

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: 138.75  E-value: 3.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1703 ADGSETRRSyasLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV---PLTVPVSYAttsaavsk 1779
Cdd:cd05919      7 ADRSVTYGQ---LHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDDYA-------- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1780 legiwemldrpwivtsaagepglreLAARRewSGLRLTTADAlreepedrdwyearpDDLVLMLMTSGSTGLPKAVRLTH 1859
Cdd:cd05919     76 -------------------------YIARD--CEARLVVTSA---------------DDIAYLLYSSGTTGPPKGVMHAH 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1860 RNVLT--RAAATEAMnGLGSGDVSLNWIPLDHVTGV---VMFHLrdvYLGCRQIHAPTSwilEDPVRWPELADRHRVSVT 1934
Cdd:cd05919    114 RDPLLfaDAMAREAL-GLTPGDRVFSSAKMFFGYGLgnsLWFPL---AVGASAVLNPGW---PTAERVLATLARFRPTVL 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1935 W-APNFAFGLLAEQAHRFQDrdwdLSPVRLVMNAGEVVVASAARRFLhvlAPFGLPqdvMHPGWGMSETCSVvtdsvLAS 2013
Cdd:cd05919    187 YgVPTFYANLLDSCAGSPDA----LRSLRLCVSAGEALPRGLGERWM---EHFGGP---ILDGIGATEVGHI-----FLS 251

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2014 EAPDHDEAfVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHdNARANAESFTEDGWFDTGDL-AFLRDGE 2092
Cdd:cd05919    252 NRPGAWRL-GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYW-NNPEKSRATFNGGWYRTGDKfCRDADGW 329

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2093 LYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAATdeLALFLRLAPGQDPAGAL-REIAGKVTR 2171
Cdd:cd05919    330 YTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEA--AVVAVPESTGLSR--LTAFVVLKSPAAPQESLaRDIHRHLLE 405

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569 2172 EIgvsPAFLIP---VEAEAIPKTEIGKIQRTKLR 2202
Cdd:cd05919    406 RL---SAHKVPrriAFVDELPRTATGKLQRFKLR 436
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 475-959 6.54e-34

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 139.27  E-value: 6.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  475 VSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEP 554
Cdd:PRK08276     5 MAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  555 VAVVTDT---------AGSGRLPATDARVV--VVDDARTVADLAGRAPHDLTDADRAGAtgpyDTAYvihTSGSTGRPKG 623
Cdd:PRK08276    85 KVLIVSAaladtaaelAAELPAGVPLLLVVagPVPGFRSYEEALAAQPDTPIADETAGA----DMLY---SSGTTGRPKG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  624 V--PVPHAHV-------VRLFeasGEHFRFGADDVW----TLFHSYAFDFSVWELwgplLHGGRLVVVPyevSRSPREFL 690
Cdd:PRK08276   158 IkrPLPGLDPdeapgmmLALL---GFGMYGGPDSVYlspaPLYHTAPLRFGMSAL----ALGGTVVVME---KFDAEEAL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  691 RLLDEEKVTVLNQTPSAFEQLV-LADAATDR-ATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVhVT 768
Cdd:PRK08276   228 ALIERYRVTHSQLVPTMFVRMLkLPEEVRARyDVSSLRVAIHAAAPCPVEVKRAMIDWWG---PIIHEYYASSEGGG-VT 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  769 FhrlvrADLED-PRRRGVIGRPLaDLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgtRM 847
Cdd:PRK08276   304 V-----ITSEDwLAHPGSVGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPH-------GW 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  848 YRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAG 927
Cdd:PRK08276   371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAL 450

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1573930569  928 ---LRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK08276   451 aaeLIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1707-2202 9.64e-34

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: 138.25  E-value: 9.64e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVpvSYATtsaavsklEGIWEM 1786
Cdd:cd17651     18 GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP--AYPA--------ERLAFM 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1787 LDRPWIVTSAAGEPGLRELAARREWsGLRLTTADALREEPEDRDwYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRA 1866
Cdd:cd17651     88 LADAGPVLVLTHPALAGELAVELVA-VTLLDQPGAAAGADAEPD-PALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1867 AATEAMNGLGSGDVSLNWIPLdhvTGVVMFHLRDVYLGC-RQIHAPTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLA 1945
Cdd:cd17651    166 AWQARASSLGPGARTLQFAGL---GFDVSVQEIFSTLCAgATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALA 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1946 EQAHRFQDRDWDLspvRLVMNAGE-VVVASAARRFLHvlapfGLPQDVMHPGWGMSETcSVVTDSVLASEAPDHDEAfVS 2024
Cdd:cd17651    243 EHGRPLGVRLAAL---RYLLTGGEqLVLTEDLREFCA-----GLPGLRLHNHYGPTET-HVVTALSLPGDPAAWPAP-PP 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2025 CGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW------FDTGDLA-FLRDGELYITG 2097
Cdd:cd17651    313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLArWLPDGELEFLG 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2098 RAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDAsAATDELALFLRLAPGQDP-AGALREIAGKVTreigvs 2176
Cdd:cd17651    393 RADDQVKIRGFRIELGEIEAALARHPGVRE---AVVLAREDR-PGEKRLVAYVVGDPEAPVdAAELRAALATHL------ 462

                          490       500
                   ....*....|....*....|....*....
gi 1573930569 2177 PAFLIP---VEAEAIPKTEIGKIQRTKLR 2202
Cdd:cd17651    463 PEYMVPsafVLLDALPLTPNGKLDRRALP 491
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1711-2201 1.39e-33

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: 136.45  E-value: 1.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyattsaavsklegiwemldrP 1790
Cdd:cd05935      3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPIN------------------------P 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTsaagepglRELAARREWSGLRLTTAdalreepedrdwyEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05935     59 MLKE--------RELEYILNDSGAKVAVV-------------GSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSA 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGcRQIHAPTSWileDPVRWPELADRHRVSVTWA-PNFAFGLLAEQah 1949
Cdd:cd05935    118 VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG-GTYVLMARW---DRETALELIEKYKVTFWTNiPTMLVDLLATP-- 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1950 RFQDRDWdlSPVRLVMNAGEVVVASAARRFLHVLAPFGLpqdvmhPGWGMSETCSVVTDSvlaseaPDHDEAFVSCGLPY 2029
Cdd:cd05935    192 EFKTRDL--SSLKVLTGGGAPMPPAVAEKLLKLTGLRFV------EGYGLTETMSQTHTN------PPLRPKLQCLGIP* 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2030 PGFAMRVVDDQD-ALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG---WFDTGDLAFL-RDGELYITGRAKDVII 2104
Cdd:cd05935    258 FGVDARVIDIETgRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMdEEGYFFFVDRVKRMIN 337

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2105 VNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAAtDELALFLRLAPgqdpagalrEIAGKVTRE------IGVSPA 2178
Cdd:cd05935    338 VSGFKVWPAEVEAKLYKHPAI*E---VCVISVPDERVG-EEVKAFIVLRP---------EYRGKVTEEdiiewaREQMAA 404

                          490       500
                   ....*....|....*....|....*.
gi 1573930569 2179 FLIPVEAE---AIPKTEIGKIQRTKL 2201
Cdd:cd05935    405 YKYPREVEfvdELPRSASGKILWRLL 430
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 462-959 1.62e-33

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 137.71  E-value: 1.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  462 FEARvaESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP 541
Cdd:PRK06145    10 FHAR--RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  542 AERLALVMADAEPVAVVTDTAGSGrLPATDARVVVVDDARTVADLAGRAPHDltDADRAGATGPYDTAYVIHTSGSTGRP 621
Cdd:PRK06145    88 ADEVAYILGDAGAKLLLVDEEFDA-IVALETPKIVIDAAAQADSRRLAQGGL--EIPPQAAVAPTDLVRLMYTSGTTDRP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVvrlFEASGEH---FRFGADD----VWTLFHSYAFDF-SVWELWgpllHGGRLVVvpyEVSRSPREFLRLL 693
Cdd:PRK06145   165 KGVMHSYGNL---HWKSIDHviaLGLTASErllvVGPLYHVGAFDLpGIAVLW----VGGTLRI---HREFDPEAVLAAI 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSAFEQlVLADAATDR-ATGSLRYVVLGGEALVAERLRPWADRhgLDAPELVNMYGITETTVHVTFHRL 772
Cdd:PRK06145   235 ERHRLTCAWMAPVMLSR-VLTVPDRDRfDLDSLAWCIGGGEKTPESRIRDFTRV--FTRARYIDAYGLTETCSGDTLMEA 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  773 VRaDLEdprRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmyRSGD 852
Cdd:PRK06145   312 GR-EIE---KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGD 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  853 LARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEdgltQLVAYAVPAEEGGADPAGL 928
Cdd:PRK06145   380 VGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgvhdDRWGE----RITAVVVLNPGATLTLEAL 455

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569  929 RAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK06145   456 DRHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
458-964 1.71e-33

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 138.48  E-value: 1.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  458 LPQLFEARVAESPGRTAVSYAGE--TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:PRK05852    18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDAR---VVVVDDARTVADLAGRAPH-DLTDADRAGATGP----YD 607
Cdd:PRK05852    98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRwwpLTVNVGGDSGPSGGTLSVHlDAATEPTPATSTPeglrPD 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  608 TAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHSYAFdfsVWELWGPLLHGGRlVVVPYEVS 683
Cdd:PRK05852   178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDatvaVMPLYHGHGL---IAALLATLASGGA-VLLPARGR 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  684 RSPREFLRLLDEEKVTVLNQTPsAFEQLVLADAATD---RATGSLRYVVLGGEALVAERLRPWADRHGldAPeLVNMYGI 760
Cdd:PRK05852   254 FSAHTFWDDIKAVGATWYTAVP-TIHQILLERAATEpsgRKPAALRFIRSCSAPLTAETAQALQTEFA--AP-VVCAFGM 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  761 TETTVHVTFHRLVRADL-EDPRRR-GVIGRPLAdLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPD 838
Cdd:PRK05852   330 TEATHQVTTTQIEGIGQtENPVVStGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  839 PFgapgtrmyRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPA 918
Cdd:PRK05852   409 WL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPR 480

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569  919 EEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK05852   481 ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 427-942 2.17e-33

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 139.24  E-value: 2.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  427 PEELPlgETPVLLPGEEPVRRDEPAPRvtRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPG 506
Cdd:PRK08279    12 PRRLP--DLPGILRGLKRTALITPDSK--RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  507 RFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLA---------LVMADAEPVAVVTDTAGSGRLP-----ATDA 572
Cdd:PRK08279    88 DVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAhslnlvdakHLIVGEELVEAFEEARADLARPprlwvAGGD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  573 RVVVVDDARTVADLAGRAPhDLTDADRAGATGPyDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW-- 650
Cdd:PRK08279   168 TLDDPEGYEDLAAAAAGAP-TTNPASRSGVTAK-DTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLyc 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  651 --TLFHSYAFDFSvwelWGPLLHGGRLVVVPYEVSRSprEFLRLLDEEKVTV-----------LNQTPSafeqlvladaA 717
Cdd:PRK08279   246 clPLYHNTGGTVA----WSSVLAAGATLALRRKFSAS--RFWDDVRRYRATAfqyigelcrylLNQPPK----------P 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  718 TDRATgSLRYVVlgGEALVAERLRPWADRHGLdaPELVNMYGITETTV------------------HVTFHRLVRADLE- 778
Cdd:PRK08279   310 TDRDH-RLRLMI--GNGLRPDIWDEFQQRFGI--PRILEFYAASEGNVgfinvfnfdgtvgrvplwLAHPYAIVKYDVDt 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 -DPRRrgvigrpladlrvyvlDAAGR--PVPPGATGEMY--VSGPGVAPGYlNRPELTEERFLPDPFgAPGTRMYRSGDL 853
Cdd:PRK08279   385 gEPVR----------------DADGRciKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVF-KKGDAWFNTGDL 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  854 ARWRPDGtlvHAGRADqqvkiR-G--FR-----IEPGEIEAVLTAHPAVAGGAV----VPRAaeDGLTQLVAyAVPAEEG 921
Cdd:PRK08279   447 MRDDGFG---HAQFVD-----RlGdtFRwkgenVATTEVENALSGFPGVEEAVVygveVPGT--DGRAGMAA-IVLADGA 515

                          570       580
                   ....*....|....*....|.
gi 1573930569  922 GADPAGLRAHLAARLPAYMVP 942
Cdd:PRK08279   516 EFDLAALAAHLYERLPAYAVP 536
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1680-2138 3.89e-33

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 136.53  E-value: 3.89e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1680 VSGWAEAllRAAGRPDgevvHVRADGSETRRSYASLVPEASRVLAGLRRR-GLRPGDRVILQCDDTEDFVATLWGCVLGG 1758
Cdd:PRK06839     4 IAYWIEK--RAYLHPD----RIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1759 FVAVPLTVPVsyaTTSAAVSKLE--GIWEMLDRPWIVTSAAGEPGLRELAARREWSGLrlttADALREEPEDRDwyEARP 1836
Cdd:PRK06839    78 CIAVPLNIRL---TENELIFQLKdsGTTVLFVEKTFQNMALSMQKVSYVQRVISITSL----KEIEDRKIDNFV--EKNE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIhAPTSWil 1916
Cdd:PRK06839   149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII-VPRKF-- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1917 eDPVRWPELADRHRVSVTWA-PNFAFGLLaeQAHRFQDRdwDLSPVRLVMNAGEVVVASAARRFLHVLAPFGlpqdvmhP 1995
Cdd:PRK06839   226 -EPTKALSMIEKHKVTVVMGvPTIHQALI--NCSKFETT--NLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------Q 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1996 GWGMSETCSVVTdsVLASEapDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFt 2075
Cdd:PRK06839   294 GFGMTETSPTVF--MLSEE--DARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI- 368

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2076 EDGWFDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSD 2138
Cdd:PRK06839   369 QDGWLCTGDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE---VAVVGRQH 429
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 1687-2211 4.30e-33

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 137.09  E-value: 4.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1687 LLRAAGR--PDgEVVHVRADGSETRRSYASLVpeaSRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP- 1763
Cdd:PRK07470    12 FLRQAARrfPD-RIALVWGDRSWTWREIDARV---DALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPt 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 ---LTVP-VSYATTS----------------AAVSKLEgiwemLDRPWIVTSAAGEPGLRELAARREWSGLRLTTADALR 1823
Cdd:PRK07470    88 nfrQTPDeVAYLAEAsgaramichadfpehaAAVRAAS-----PDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1824 EEPEdrdWYearpddlvlmLMTSGSTGLPKAVRLTHRN---VLTRAAAtEAMNGLGSGDVSLNWIPLDHVTGVvmfH-LR 1899
Cdd:PRK07470   163 DDPC---WF----------FFTSGTTGRPKAAVLTHGQmafVITNHLA-DLMPGTTEQDASLVVAPLSHGAGI---HqLC 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1900 DVYLGCRQIhAPTSWILEDPVRWpELADRHRVSVTWAPNFAFGLLAEqaHRFQDRdWDLSPVRLVMNAGEVVVASAARRF 1979
Cdd:PRK07470   226 QVARGAATV-LLPSERFDPAEVW-ALVERHRVTNLFTVPTILKMLVE--HPAVDR-YDHSSLRYVIYAGAPMYRADQKRA 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1980 LHVLAPfglpqdVMHPGWGMSET--CSVVTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGT 2057
Cdd:PRK07470   301 LAKLGK------VLVQYFGLGEVtgNITVLPPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2058 SVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrSFTAAVAVr 2136
Cdd:PRK07470   375 AVFAGYYNNPEANAKAF-RDGWFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAV--SEVAVLGV- 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2137 SDASAATDELALFLRLAPGQDPAGALRE-IAGKVTReigvspaFLIP---VEAEAIPKTEIGKIQRTKLRKSFEA-GEFD 2211
Cdd:PRK07470   451 PDPVWGEVGVAVCVARDGAPVDEAELLAwLDGKVAR-------YKLPkrfFFWDALPKSGYGKITKKMVREELEErGLLD 523
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1676-2202 4.63e-33

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 137.20  E-value: 4.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1676 PEPSVSGWAEALLRAAGRPDGEVVHVRADGseTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCV 1755
Cdd:PRK06155    15 PLPPSERTLPAMLARQAERYPDRPLLVFGG--TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1756 LGGFVAVPLT------------------VPVSYATTSAAVSKLEGIWEMLDRPWIVTSAAgepglrELAARREWSGLRLT 1817
Cdd:PRK06155    93 WLGAIAVPINtalrgpqlehilrnsgarLLVVEAALLAALEAADPGDLPLPAVWLLDAPA------SVSVPAGWSTAPLP 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1818 TADALreepedRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFh 1897
Cdd:PRK06155   167 PLDAP------APAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAF- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1898 LRDVYLGCRQIHAPTswiLEDPVRWPELAdRHRVSVTWAPNFAFGLLAEQAHRFQDRDwdlSPVRLVMNAGevVVASAAR 1977
Cdd:PRK06155   240 FQALLAGATYVLEPR---FSASGFWPAVR-RHGATVTYLLGAMVSILLSQPARESDRA---HRVRVALGPG--VPAALHA 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1978 RFlhvLAPFGLPqdvMHPGWGMSETCSVVTDSvLASEAPDhdeafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGT 2057
Cdd:PRK06155   311 AF---RERFGVD---LLDGYGSTETNFVIAVT-HGSQRPG------SMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2058 ---SVTHGYHDNARANAESFtEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrSFTAAV 2133
Cdd:PRK06155   378 epfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDaDGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV--AAAAVF 454

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2134 AVRSDasAATDELALFLRLAPGQ--DPAGALREIAGKVtreigvsPAFLIP--VE-AEAIPKTEIGKIQRTKLR 2202
Cdd:PRK06155   455 PVPSE--LGEDEVMAAVVLRDGTalEPVALVRHCEPRL-------AYFAVPryVEfVAALPKTENGKVQKFVLR 519
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 456-960 7.86e-33

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 135.97  E-value: 7.86e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSY---AGET--LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTG 530
Cdd:PRK08008     7 QHLRQMWDDLADVYGHKTALIFessGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  531 AAYLPLDPGHPAERLALVMADAEPVAVVTDTAgsgRLPATDArvvVVDDART------VADLAGRAPHDLTDADRAGATG 604
Cdd:PRK08008    87 AIMVPINARLLREESAWILQNSQASLLVTSAQ---FYPMYRQ---IQQEDATplrhicLTRVALPADDGVSSFTQLKAQQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  605 PY-----------DTAYVIHTSGSTGRPKGVPVPHAHVvrLFEA--SGEHFRFGADDVW-TLFHSYAFDFSVWELWGPLL 670
Cdd:PRK08008   161 PAtlcyapplstdDTAEILFTSGTTSRPKGVVITHYNL--RFAGyySAWQCALRDDDVYlTVMPAFHIDCQCTAAMAAFS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  671 HGGRLVVV-PYevsrSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLrPWADRHGL 749
Cdd:PRK08008   239 AGATFVLLeKY----SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKD-AFEERFGV 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  750 dapELVNMYGITETTVHVTFHRlvradLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSG-PG--VAPGYLN 826
Cdd:PRK08008   314 ---RLLTSYGMTETIVGIIGDR-----PGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYL 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  827 RPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAV--VPRAA 904
Cdd:PRK08008   386 DPKATAKVLEADGW-------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgIKDSI 458

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  905 EDgltQLV-AYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:PRK08008   459 RD---EAIkAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 452-959 8.16e-33

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 136.83  E-value: 8.16e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  452 PRVTRTLPQLFEARVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKT 529
Cdd:PRK12583    14 PLLTQTIGDAFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARI 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  530 GAAYLPLDPGHPAERLA----------LVMADAEP--------VAVVTDTAGSGRLPATDAR------VVVVDDART--- 582
Cdd:PRK12583    94 GAILVNINPAYRASELEyalgqsgvrwVICADAFKtsdyhamlQELLPGLAEGQPGALACERlpelrgVVSLAPAPPpgf 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  583 --VADLAGRA----PHDLtdADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWT----L 652
Cdd:PRK12583   174 laWHELQARGetvsREAL--AERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvpvpL 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  653 FHSYAFDFSVWelwGPLLHGGRLVVvPYEvSRSPREFLRLLDEEKVTVLNQTPSAF-EQLVLADAATDRATgSLRYVVLG 731
Cdd:PRK12583   252 YHCFGMVLANL---GCMTVGACLVY-PNE-AFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLS-SLRTGIMA 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  732 GEALVAERLRPWADRhgLDAPELVNMYGITETTvHVTFHRLVRADLEdpRRRGVIGRPLADLRVYVLDAAGRPVPPGATG 811
Cdd:PRK12583   326 GAPCPIEVMRRVMDE--MHMAEVQIAYGMTETS-PVSLQTTAADDLE--RRVETVGRTQPHLEVKVVDPDGATVPRGEIG 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  812 EMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrMYrSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAH 891
Cdd:PRK12583   401 ELCTRGYSVMKGYWNNPEATAESIDEDGW------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTH 473

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  892 PAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK12583   474 PAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
pimA TIGR03205
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ...
 1816-2202 9.19e-33

dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.


Pssm-ID: 132249 [Multi-domain]  Cd Length: 541  Bit Score: 136.24  E-value: 9.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1816 LTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNvLTRAAATEAMNGLGS----GDVS--LNWIPLDH 1889
Cdd:TIGR03205  171 VTYADFVKGAAAPAEWPAVTPDDVALLQYTGGTTGLPKGAMLTHGN-LTSAVSIYDVWGKPSratrGDVErvICVLPLFH 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1890 VTGVVMFHLRDVYLGcRQIHAPTSWILEDPVRwpELADRHRVSVTWAPNFAFGLLAEQAhrFQDRDwdLSPVRLVMNAGE 1969
Cdd:TIGR03205  250 IYALTVILLRSLRRG-DLISLHQRFDVAAVFR--DIEEKRATVFPGVPTMWIALANDPS--LEKRD--LSSLATIGSGGA 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1970 VVVASAARRFLHVLapfGLPqdvMHPGWGMSETCSVVTDSVLasEAPDHDEafvSCGLPYPGFAMRVV--DDQDALLPEG 2047
Cdd:TIGR03205  323 PLPVEVANFFERKT---GLK---LKSGWGMTETCSPGTGHPP--EGPDKPG---SIGLMLPGIELDVVslDDPTKVLPPG 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2048 DVGRLQVRGTSVTHGYHDNARANAESFTeDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV 2126
Cdd:TIGR03205  392 EVGELRIRGPNVTRGYWNRPEESAEAFV-GDRFLTGDIGYMdTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQ 470

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 RSFTAAVA--VRSDASAAtdelalFLRLAPGQDP--AGALRE-IAGKVTR-EIGVSPAFLipveaEAIPKTEIGKIQRTK 2200
Cdd:TIGR03205  471 EVIVIGIPdqYRGEAAKA------FVKLRPGAKPfsLDELRAfLAGKLGKhELPVAVEFV-----DELPRTPVGKLSRHE 539


                   ..
gi 1573930569 2201 LR 2202
Cdd:TIGR03205  540 LR 541
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1711-2209 1.28e-32

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 136.28  E-value: 1.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV---PL---------------TVPVSYAT 1772
Cdd:PRK05605    59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLytahelehpfedhgaRVAIVWDK 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1773 TSAAVSKLEGIWEmLDRPWIVTSAAGEPGLRELAARrewsgLRLTTADALREE-----PEDRDW---------------- 1831
Cdd:PRK05605   139 VAPTVERLRRTTP-LETIVSVNMIAAMPLLQRLALR-----LPIPALRKARAAltgpaPGTVPWetlvdaaiggdgsdvs 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 -YEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEA-MNGLGSGD-VSLNWIPLDHVTGVVMFHLRDVYLGCRQI 1908
Cdd:PRK05605   213 hPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwVPGLGDGPeRVLAALPMFHAYGLTLCLTLAVSIGGELV 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 HAPTswiledpVRWPELAD---RHRVsvTWAPNFA--FGLLAEQAhrfQDRDWDLSPVRlvmNAgeVVVASAarrflhvl 1983
Cdd:PRK05605   293 LLPA-------PDIDLILDamkKHPP--TWLPGVPplYEKIAEAA---EERGVDLSGVR---NA--FSGAMA-------- 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1984 apfgLPQDVMHP-----------GWGMSETCSVVTDSVLAseaPDHDEAFVscGLPYPGFAMRVVD--DQDALLPEGDVG 2050
Cdd:PRK05605   348 ----LPVSTVELwekltggllveGYGLTETSPIIVGNPMS---DDRRPGYV--GVPFPDTEVRIVDpeDPDETMPDGEEG 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2051 RLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSf 2129
Cdd:PRK05605   419 ELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMeEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA- 496

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2130 tAAVAV-RSDASaatDELALFLRLAPGQ--DPAGaLRE------IAGKVTREIgvspaflipVEAEAIPKTEIGKIQRTK 2200
Cdd:PRK05605   497 -AVVGLpREDGS---EEVVAAVVLEPGAalDPEG-LRAycrehlTRYKVPRRF---------YHVDELPRDQLGKVRRRE 562


                   ....*....
gi 1573930569 2201 LRKSFEAGE 2209
Cdd:PRK05605   563 VREELLEKL 571
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 457-966 1.56e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 135.54  E-value: 1.56e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESpgRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRF-VALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:PRK13388     4 TIAQLLRDRAGDD--TIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATD---ARVVVVDDARtVADLAGRAPhdltDADRAGATGPYDTAYVI 612
Cdd:PRK13388    82 LNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDlpgVRVLDVDTPA-YAELVAAAG----ALTPHREVDAMDPFMLI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  613 HTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV----WTLFHSYAfdfsVWELWGPLLHGGRLVVVPYEVSRSprE 688
Cdd:PRK13388   157 FTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVcyvsMPLFHSNA----VMAGWAPAVASGAAVALPAKFSAS--G 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  689 FLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRyVVLGGEAlVAERLRPWADRHGLdapELVNMYGITETTVHVT 768
Cdd:PRK13388   231 FLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLR-VAFGNEA-SPRDIAEFSRRFGC---QVEDGYGSSEGAVIVV 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  769 fhrlvradLEDPRRRGVIGRPLADLRVY-----------VLDAAGRPV-PPGATGEMYVS-GPGVAPGYLNRPELTEERF 835
Cdd:PRK13388   306 --------REPGTPPGSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVNTaGAGFFEGYYNNPEATAERM 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  836 lpdpfgAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYA 915
Cdd:PRK13388   378 ------RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAAL 449

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  916 VPAEEGGADPAGLRAHLAAR--LPAYMVPAACVLLDALPLTANGKLDTAALPA 966
Cdd:PRK13388   450 VLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 1703-2201 2.03e-32

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: 134.67  E-value: 2.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1703 ADGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDF-VATLWGCVLGGFVAvpltvPVSYATTSAAVSKL 1780
Cdd:cd05904     25 IDAATGRAlTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFpVAFLAVLSLGAVVT-----TANPLSTPAEIAKQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1781 EGiwemLDRP-WIVTSAAGEPGLRELAAR-----REWSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKA 1854
Cdd:cd05904    100 VK----DSGAkLAFTTAELAEKLASLALPvvlldSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKG 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1855 VRLTHRNVLTRAAATEAMNGLGS--GDVSLNWIPLDHVTGVVMFHLRDVYLGCrQIHAPTSWILEDPVrwpELADRHRVS 1932
Cdd:cd05904    176 VMLTHRNLIAMVAQFVAGEGSNSdsEDVFLCVLPMFHIYGLSSFALGLLRLGA-TVVVMPRFDLEELL---AAIERYKVT 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1933 VTW-APNFafgLLAEQAHRFQDrDWDLSPVRLVMNA----GEVVVASAARRFLHVlapfglpqDVMHpGWGMSETCSVVT 2007
Cdd:cd05904    252 HLPvVPPI---VLALVKSPIVD-KYDLSSLRQIMSGaaplGKELIEAFRAKFPNV--------DLGQ-GYGMTESTGVVA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2008 DSVLASEAPDHdeaFVSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA 2086
Cdd:cd05904    319 MCFAPEKDRAK---YGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLC 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2087 FL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAATDELALFLRlAPGQDPAGAlrEI 2165
Cdd:cd05904    396 YIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEIL---DAAVIPYPDEEAGEVPMAFVVR-KPGSSLTED--EI 469

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1573930569 2166 AGKVTREigVSP-------AFLipveaEAIPKTEIGKIQRTKL 2201
Cdd:cd05904    470 MDFVAKQ--VAPykkvrkvAFV-----DAIPKSPSGKILRKEL 505
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 460-959 2.57e-32

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: 136.08  E-value: 2.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEARVAESPGRTAVSYAGE-----TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYL 534
Cdd:cd05968     65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PLDPGHPAERLALVMADAEPVAVVTD--TAGSGRL--------------PATDARVVV----VDDARTVADLAGRAPHDL 594
Cdd:cd05968    145 PIFSGFGKEAAATRLQDAEAKALITAdgFTRRGREvnlkeeadkacaqcPTVEKVVVVrhlgNDFTPAKGRDLSYDEEKE 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  595 TDADRAGATGPYDTAYVIHTSGSTGRPKGvpVPHAHVVRLFEAS---GEHFRFGADDVWTLFHSYAFDFSVWELWGPLLH 671
Cdd:cd05968    225 TAGDGAERTESEDPLMIIYTSGTTGKPKG--TVHVHAGFPLKAAqdmYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 GGRLVVvpYEVS---RSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLG--GEALVAERLRPWADR 746
Cdd:cd05968    303 GATMVL--YDGApdhPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGstGEPWNPEPWNWLFET 380

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  747 HGLDAPELVNMYGITETTVHVTFHRLVRadledPRRRGVIGRPLADLRVYVLDAAGRPVPPgATGEMYVSGP--GVAPGY 824
Cdd:cd05968    381 VGKGRNPIINYSGGTEISGGILGNVLIK-----PIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPwpGMTRGF 454

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  825 LNrpelTEERFLpDPFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAA 904
Cdd:cd05968    455 WR----DEDRYL-ETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPH 529

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569  905 EDGLTQLVAYAVpAEEGGADPAGLRAHLAARLPAYM----VPAACVLLDALPLTANGKL 959
Cdd:cd05968    530 PVKGEAIVCFVV-LKPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKV 587
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 465-959 3.03e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 134.43  E-value: 3.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPA 542
Cdd:PRK13391     6 HAQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  543 ERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVdDARTVADLAGRAP--HDLTDADRAGATGPYDT----AYVIHTSG 616
Cdd:PRK13391    86 AEAAYIVDDSGARALITSAAKLDVARALLKQCPGV-RHRLVLDGDGELEgfVGYAEAVAGLPATPIADeslgTDMLYSSG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGV--PVPHAHVVR---LFEASGEHFRFGADDVW----TLFHS--YAFDFSVWELwgpllhGGRLVVVPYevsRS 685
Cdd:PRK13391   165 TTGRPKGIkrPLPEQPPDTplpLTAFLQRLWGFRSDMVYlspaPLYHSapQRAVMLVIRL------GGTVIVMEH---FD 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  686 PREFLRLLDEEKVTVLNQTPSAFEQ-LVLADAATDRATGSLRYVVLGGEA----LVAERLRPWAdrhgldAPELVNMYGI 760
Cdd:PRK13391   236 AEQYLALIEEYGVTHTQLVPTMFSRmLKLPEEVRDKYDLSSLEVAIHAAApcppQVKEQMIDWW------GPIIHEYYAA 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  761 TEtTVHVTFhrlVRADlEDPRRRGVIGRPL-ADLRvyVLDAAGRPVPPGATGEMYVSGpGVAPGYLNRPELTEERFLPDP 839
Cdd:PRK13391   310 TE-GLGFTA---CDSE-EWLAHPGTVGRAMfGDLH--ILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  840 fgapgtRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAE 919
Cdd:PRK13391   382 ------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD 455

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1573930569  920 EGGADPA---GLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK13391   456 GVDPGPAlaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 1818-2198 3.12e-32

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: 133.34  E-value: 3.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1818 TADALR---EEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVV 1894
Cdd:cd05914     67 TADEVHhilNHSEAKAIFVSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLT 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1895 MFHLRDVYLGcrqihAPTSWILEDPVRWPELADRHRVSvtwaPNFAFGLLAEQAHRF----QDRDwDLSPVRLVMNAGEV 1970
Cdd:cd05914    147 FTLLLPLLNG-----AHVVFLDKIPSAKIIALAFAQVT----PTLGVPVPLVIEKIFkmdiIPKL-TLKKFKFKLAKKIN 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1971 V--VASAARRFLH----------VLAPFGLPQDVMH----------PGWGMSETCSVVtdsvlaSEAPDHDEAFVSCGLP 2028
Cdd:cd05914    217 NrkIRKLAFKKVHeafggnikefVIGGAKINPDVEEflrtigfpytIGYGMTETAPII------SYSPPNRIRLGSAGKV 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2029 YPGFAMRVvddqDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYITGRAKDVIIV-N 2106
Cdd:cd05914    291 IDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGkIDAEGYLYIRGRKKEMIVLsS 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2107 GVNHYSHEIEACVEELPSVVRSFTAAVAVRSDASAATDELALFLRLAPGQDPAGALR-EIAGKVTREIgvsPAFL----I 2181
Cdd:cd05914    367 GKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKwEVRDKVNQKV---PNYKkiskV 443

                          410
                   ....*....|....*..
gi 1573930569 2182 PVEAEAIPKTEIGKIQR 2198
Cdd:cd05914    444 KIVKEEFEKTPKGKIKR 460
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 1836-2202 9.32e-32

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 133.74  E-value: 9.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNG--LGSG-DVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPT 1912
Cdd:PRK05677   206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnLNEGcEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 SWILEDPVRwpELAdRHRVSVTWAPNFAFGLLAeqaHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLapfGLPqdv 1992
Cdd:PRK05677   286 PRDLPAMVK--ELG-KWKFSGFVGLNTLFVALC---NNEAFRKLDFSALKLTLSGGMALQLATAERWKEVT---GCA--- 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 MHPGWGMSETCSVVTDSvlaseaPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAE 2072
Cdd:PRK05677   354 ICEGYGMTETSPVVSVN------PSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2073 SFTEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRSDASAATDELALFLR 2151
Cdd:PRK05677   428 ILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ--CAAIGVPDEKSGEAIKVFVVVK 505

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2152 LAPGQDPAGALREIAGKVTreigvspAFLIPVEAE---AIPKTEIGKIQRTKLR 2202
Cdd:PRK05677   506 PGETLTKEQVMEHMRANLT-------GYKVPKAVEfrdELPTTNVGKILRRELR 552
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 481-959 1.44e-31

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: 130.16  E-value: 1.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEpvaVVTD 560
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD---VKLD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 tagsgrlpatdarvvvvddartvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVP---H-AHVVrlfe 636
Cdd:cd05912     78 ----------------------------------------------DIATIMYTSGTTGKPKGVQQTfgnHwWSAI---- 107

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  637 ASGEHFRFGADDVW----TLFHSYAFdfSVweLWGPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLV 712
Cdd:cd05912    108 GSALNLGLTEDDNWlcalPLFHISGL--SI--LMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLL 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  713 LADAATDRAtgSLRYVVLGGEALVAERLRPWADRhglDAPeLVNMYGITETtvhvtFHRLVRADLED-PRRRGVIGRPLA 791
Cdd:cd05912    181 EILGEGYPN--NLRCILLGGGPAPKPLLEQCKEK---GIP-VYQSYGMTET-----CSQIVTLSPEDaLNKIGSAGKPLF 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  792 DLRVYVLDAAGrpvPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmyRSGDLARWRPDGTLVHAGRADQQ 871
Cdd:cd05912    250 PVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDL 318

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  872 VKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDAL 951
Cdd:cd05912    319 IISGGENIYPAEIEEVLLSHPAIKEAGVV--GIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDEL 396


                   ....*...
gi 1573930569  952 PLTANGKL 959
Cdd:cd05912    397 PRTASGKL 404
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1683-2204 2.80e-31

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 131.79  E-value: 2.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1683 WAEALL------RAAGRPDGEVVhvrADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVL 1756
Cdd:PRK06087    20 WGDASLadywqqTARAMPDKIAV---VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLK 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1757 GGFVAVPLTVPVSYATTSAAVSKLEGiwEMLDRPWIVTSAAGEPGLRELAAR-REWSGLRL-------TTADALREEPED 1828
Cdd:PRK06087    97 VGAVSVPLLPSWREAELVWVLNKCQA--KMFFAPTLFKQTRPVDLILPLQNQlPQLQQIVGvdklapaTSSLSLSQIIAD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1829 RDWYEARP----DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGvvMFH--LRDVY 1902
Cdd:PRK06087   175 YEPLTTAItthgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATG--FLHgvTAPFL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1903 LGCR----QIHAPTSWIledpvrwpELADRHRVsvTW---APNFAFGLLAEqahrFQDRDWDLSPVRLVMNAGEVVvasa 1975
Cdd:PRK06087   253 IGARsvllDIFTPDACL--------ALLEQQRC--TCmlgATPFIYDLLNL----LEKQPADLSALRFFLCGGTTI---- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1976 arrflhvlapfglPQDVMHPGWGMS-ETCSVV--TDSVLASEAPDHD--EAFVSC-GLPYPGFAMRVVDDQDALLPEGDV 2049
Cdd:PRK06087   315 -------------PKKVARECQQRGiKLLSVYgsTESSPHAVVNLDDplSRFMHTdGYAAAGVEIKVVDEARKTLPPGCE 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2050 GRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV-- 2126
Cdd:PRK06087   382 GEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHda 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 ------------RSFTAAVAVRSDASAATDELALFLRlapgqdpagalreiagkvTREIgvsPAFLIP---VEAEAIPKT 2191
Cdd:PRK06087   462 cvvampderlgeRSCAYVVLKAPHHSLTLEEVVAFFS------------------RKRV---AKYKYPehiVVIDKLPRT 520

                          570
                   ....*....|...
gi 1573930569 2192 EIGKIQRTKLRKS 2204
Cdd:PRK06087   521 ASGKIQKFLLRKD 533
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1711-2207 3.00e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 132.09  E-value: 3.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvPVSYA---------TTSAAVSKLE 1781
Cdd:PRK06178    60 TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS-PLFREhelsyelndAGAEVLLALD 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1782 GIWEMLD--------RPWIVTSAA----GEPGLRE----LAARREWSGlrltTAD---ALREEPEDRDWYEARPDDLVLM 1842
Cdd:PRK06178   139 QLAPVVEqvraetslRHVIVTSLAdvlpAEPTLPLpdslRAPRLAAAG----AIDllpALRACTAPVPLPPPALDALAAL 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1843 LMTSGSTGLPKAVRLTHRN-VLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHApTSWileDPVR 1921
Cdd:PRK06178   215 NYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLL-ARW---DAVA 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1922 WPELADRHRVSVTwapnfafGLLAEQAHRFQD----RDWDLSPVRLVMNAGEVVVASAA-RRFLHVLAPFGLpqdvMHPG 1996
Cdd:PRK06178   291 FMAAVERYRVTRT-------VMLVDNAVELMDhprfAEYDLSSLRQVRVVSFVKKLNPDyRQRWRALTGSVL----AEAA 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSET--CSVVTdsvLASEAPDHDEAF--VSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANA 2071
Cdd:PRK06178   360 WGMTEThtCDTFT---AGFQDDDFDLLSqpVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATA 436

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2072 ESFtEDGWFDTGDL-AFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftaAVAVRSDASAATDELAlFL 2150
Cdd:PRK06178   437 EAL-RDGWLHTGDIgKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGS---AVVGRPDPDKGQVPVA-FV 511

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2151 RLAPGQD-PAGALREIAGKVTREIGVSPAFLIpveaEAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:PRK06178   512 QLKPGADlTAAALQAWCRENMAVYKVPEIRIV----DALPMTATGKVRKQDLQALAEE 565
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 482-959 3.08e-31

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 131.36  E-value: 3.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDT 561
Cdd:PRK12406    12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 ----AGSGRLPAtDARVVVVDDARTVADLAGRAPHDLTDadRAGATG---------PYDT------AYVIHTSGSTGRPK 622
Cdd:PRK12406    92 dllhGLASALPA-GVTVLSVPTPPEIAAAYRISPALLTP--PAGAIDwegwlaqqePYDGppvpqpQSMIYTSGTTGHPK 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  623 GV----PVP-HAHVVRLFEASGEHFRFGADDVWT--LFHS--YAFDFSVWELwgpllhGGRLVVVPyevSRSPREFLRLL 693
Cdd:PRK12406   169 GVrraaPTPeQAAAAEQMRALIYGLKPGIRALLTgpLYHSapNAYGLRAGRL------GGVLVLQP---RFDPEELLQLI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  694 DEEKVTVLNQTPSAFEQLVLADAATDRA--TGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVhVTFHr 771
Cdd:PRK12406   240 ERHRITHMHMVPTMFIRLLKLPEEVRAKydVSSLRHVIHAAAPCPADVKRAMIEWWG---PVIYEYYGSTESGA-VTFA- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  772 lvraDLEDP-RRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAP-GYLNRPeltEERFLPDPFGapgtrMYR 849
Cdd:PRK12406   315 ----TSEDAlSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP---EKRAEIDRGG-----FIT 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  850 SGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLR 929
Cdd:PRK12406   383 SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIR 462

                          490       500       510
                   ....*....|....*....|....*....|
gi 1573930569  930 AHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK12406   463 AQLKARLAGYKVPKHIEIMAELPREDSGKI 492
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1689-2201 3.75e-31

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: 130.40  E-value: 3.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGEVVhVRADGSETrrsYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGcVL---GGFVAVPLT 1765
Cdd:cd12117      6 QAARTPDAVAV-VYGDRSLT---YAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLA-VLkagAAYVPLDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1766 VPVSyattsaavsKLEGIWEMLDRPWIVTSAAGEPGLRELAARrewsglrLTTADALREEPEDRDWYEARPDDLVLMLMT 1845
Cdd:cd12117     81 LPAE---------RLAFMLADAGAKVLLTDRSLAGRAGGLEVA-------VVIDEALDAGPAGNPAVPVSPDDLAYVMYT 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1846 SGSTGLPKAVRLTHRNVLTRAAATEAMnGLGSGDVSLN-------------WIPLDHvtgvvmfhlrdvylGCRQIHAPT 1912
Cdd:cd12117    145 SGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQtsplafdastfeiWGALLN--------------GARLVLAPK 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 SWILeDPVRWPELADRHRVSVTWAPNFAFGLLAEQahrfqDRDWdLSPVRLVMNAGEVVVASAARRFLHVLAPfglpqDV 1992
Cdd:cd12117    210 GTLL-DPDALGALIAEEGVTVLWLTAALFNQLADE-----DPEC-FAGLRELLTGGEVVSPPHVRRVLAACPG-----LR 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 MHPGWGMSETCSVVTDSVLASEAPDHDEafVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAE 2072
Cdd:cd12117    278 LVNGYGPTENTTFTTSHVVTELDEVAGS--IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAE 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2073 SFTEDGWFD------TGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATdE 2145
Cdd:cd12117    356 RFVADPFGPgerlyrTGDLArWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVRE---AVVVVREDAGGDK-R 431

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2146 LALFLRLAPGQDPAgALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd12117    432 LVAYVVAEGALDAA-ELRAFLRERL------PAYMVPaafVVLDELPLTANGKVDRRAL 483
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 1711-2202 5.61e-31

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: 129.16  E-value: 5.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRV-ILQCDDTEDFVATLwGCVLGGFVAVPLTvpvsyattsaavsklegiwemldr 1789
Cdd:cd05969      2 TFAQLKVLSARFANVLKSLGVGKGDRVfVLSPRSPELYFSML-GIGKIGAVICPLF------------------------ 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1790 pwivtSAAGEPGLRElaaRREWSGLR-LTTADALREEPEdrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA 1868
Cdd:cd05969     57 -----SAFGPEAIRD---RLENSEAKvLITTEELYERTD--------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFT 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 TEAMNGLGSGDVSlnWIPLDH--VTGVVmFHLRDVYLgcrqiHAPTSWILE---DPVRWPELADRHRVSVTWAPNFAFGL 1943
Cdd:cd05969    121 GKYVLDLHPDDIY--WCTADPgwVTGTV-YGIWAPWL-----NGVTNVVYEgrfDAESWYGIIERVKVTVWYTAPTAIRM 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1944 L----AEQAhrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVlapFGLPqdvMHPGWGMSETCSVVTdsvlaSEAPDHD 2019
Cdd:cd05969    193 LmkegDELA-----RKYDLSSLRFIHSVGEPLNPEAIRWGMEV---FGVP---IHDTWWQTETGSIMI-----ANYPCMP 256

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2020 EAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRG--TSVTHGY-HDNARANaESFTeDGWFDTGDLAFL-RDGELYI 2095
Cdd:cd05969    257 IKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIwNDEERYK-NSFI-DGWYLTGDLAYRdEDGYFWF 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2096 TGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELAlFLRLAPGQDPAGALR-EIAGKVTREIG 2174
Cdd:cd05969    335 VGRADDIIKTSGHRVGPFEVESALMEHPAVAE---AGVIGKPDPLRGEIIKA-FISLKEGFEPSDELKeEIINFVRQKLG 410

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569 2175 vspAFLIPVEAE---AIPKTEIGKIQRTKLR 2202
Cdd:cd05969    411 ---AHVAPREIEfvdNLPKTRSGKIMRRVLK 438
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 456-960 7.38e-31

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 133.90  E-value: 7.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYA-GETLSYAELNAEANRLARLLvEQGAGPGRFVALALPrgPRLVPAL--LAVLKTGAA 532
Cdd:PRK08633   615 PPLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLL-KRELKDEENVGILLP--PSVAGALanLALLLAGKV 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  533 YLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPA--------TDARVVVVDDART--------VADLAGR-APHDLT 595
Cdd:PRK08633   692 PVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNkgfdlelpENVKVIYLEDLKAkiskvdklTALLAARlLPARLL 771

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV----WTLFHSyaFDFSVwELWGPLLH 671
Cdd:PRK08633   772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVilssLPFFHS--FGLTV-TLWLPLLE 848

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 GGRLVVVPyevsrSPREFL---RLLDEEKVTVLNQTPSAFeqlvLADAATDRAT----GSLRYVVLGgealvAERLRP-- 742
Cdd:PRK08633   849 GIKVVYHP-----DPTDALgiaKLVAKHRATILLGTPTFL----RLYLRNKKLHplmfASLRLVVAG-----AEKLKPev 914

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  743 ---WADRHGLDAPElvnMYGITETT----VHVTFHRLVRADLEDPRRRGVIGRPLADLRVYVLDA-AGRPVPPGATGEMY 814
Cdd:PRK08633   915 adaFEEKFGIRILE---GYGATETSpvasVNLPDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDPeTFEELPPGEDGLIL 991

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  815 VSGPGVAPGYLNRPELTEErFLPDpfgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLtaHPAV 894
Cdd:PRK08633   992 IGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKAL 1065

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  895 AGGAVVpraaedgltqLVAYAVPAEEGG-----------ADPAGLRAHLAA-RLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:PRK08633  1066 GGEEVV----------FAVTAVPDEKKGeklvvlhtcgaEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLD 1133
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 467-964 9.76e-31

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: 129.03  E-value: 9.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  467 AESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP---AE 543
Cdd:cd05929      3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPraeAC 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  544 RLALVMADAEPVAVVTDTAGSGRLPATDArvvvvddartvadLAGRAPHDLTDADRAGAtgpydtaYVIHTSGSTGRPKG 623
Cdd:cd05929     83 AIIEIKAAALVCGLFTGGGALDGLEDYEA-------------AEGGSPETPIEDEAAGW-------KMLYSGGTTGRPKG 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  624 VPVPHAHVVR----LFEASGEhFRFGADDVW----TLFHSYAFDFSVwelwGPLLHGGRLVVVPyevSRSPREFLRLLDE 695
Cdd:cd05929    143 IKRGLPGGPPdndtLMAAALG-FGPGADSVYlspaPLYHAAPFRWSM----TALFMGGTLVLME---KFDPEEFLRLIER 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  696 EKVTVLNQTPSAFEQLV-LADAATDRA-TGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETtVHVTFhrlV 773
Cdd:cd05929    215 YRVTFAQFVPTMFVRLLkLPEAVRNAYdLSSLKRVIHAAAPCPPWVKEQWIDWGG---PIIWEYYGGTEG-QGLTI---I 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  774 RAD--LEDPrrrGVIGRPLADlRVYVLDAAGRPVPPGATGEMYVSGPGvAPGYLNRPELTEERFLPDPFgapgtrmyRS- 850
Cdd:cd05929    288 NGEewLTHP---GSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGW--------STl 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  851 GDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPA---G 927
Cdd:cd05929    355 GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaeE 434

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1573930569  928 LRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05929    435 LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1687-2201 1.18e-30

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: 128.98  E-value: 1.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1687 LLRAAGRPDGEVVHVRADgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGfvAVPltv 1766
Cdd:cd05920     20 LLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVP--- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1767 pvsyattsaavsklegIWEMldrpwivtsaagePGLRelaaRREWSGL-RLTTADAL----REEPED-----RDWYEARP 1836
Cdd:cd05920     93 ----------------VLAL-------------PSHR----RSELSAFcAHAEAVAYivpdRHAGFDhralaRELAESIP 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DdLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDH--------VTGVVMFhlrdvylGCRQI 1908
Cdd:cd05920    140 E-VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplacpgVLGTLLA-------GGRVV 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 HAPTSwileDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPfGL 1988
Cdd:cd05920    212 LAPDP----SPDAAFPLIEREGVTVTALVPALVSLWLDAAAS---RRADLSSLRLLQVGGARLSPALARRVPPVLGC-TL 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1989 PQdvmhpGWGMSEtcsvvtdSVLASEAPD--HDEAFVSCGLPY-PGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHD 2065
Cdd:cd05920    284 QQ-----VFGMAE-------GLLNYTRLDdpDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYR 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2066 NARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATD 2144
Cdd:cd05920    352 APEHNARAFTPDGFYRTGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAV----HDAAVVAMPDELLGE 427

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2145 ELALFLRLAPGQDPAGALReiagKVTREIGVSpAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd05920    428 RSCAFVVLRDPPPSAAQLR----RFLRERGLA-AYKLPdriEFVDSLPLTAVGKIDKKAL 482
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1697-2201 2.02e-30

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: 127.42  E-value: 2.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1697 EVVHVRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyattsaa 1776
Cdd:cd17643      2 EAVAVVDEDRRL--TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPID----------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1777 vsklegiwemldrpwivtsaAGEPGLReLAARREWSGLRLTTADalreepedrdwyearPDDLVLMLMTSGSTGLPKAVR 1856
Cdd:cd17643     69 --------------------PAYPVER-IAFILADSGPSLLLTD---------------PDDLAYVIYTSGSTGRPKGVV 112

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1857 LTHRNVLTRAAATEAMNGLGSGDVslnwipldhvtgVVMFHLRDVYLGCRQIHAPTS----------WILEDPVRWPELA 1926
Cdd:cd17643    113 VSHANVLALFAATQRWFGFNEDDV------------WTLFHSYAFDFSVWEIWGALLhggrlvvvpyEVARSPEDFARLL 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1927 DRHRVSVTWAPNFAFGLLAEQAHRFQDrdwDLSPVRLVMNAGEVVVASAARRFLhvlAPFGLPQDVMHPGWGMSETCSVV 2006
Cdd:cd17643    181 RDEGVTVLNQTPSAFYQLVEAADRDGR---DPLALRYVIFGGEALEAAMLRPWA---GRFGLDRPQLVNMYGITETTVHV 254

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2007 TDSVL-ASEAPDHDEAFVscGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW------ 2079
Cdd:cd17643    255 TFRPLdAADLPAAAASPI--GRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsr 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2080 -FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAATDELALFLRLAPGQD 2157
Cdd:cd17643    333 mYRTGDLArRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVR---DAAVIVREDEPGDTRLVAYVVADDGAAA 409

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1573930569 2158 PAGALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd17643    410 DIAELRALLKELL------PDYMVParyVPLDALPLTVNGKLDRAAL 450
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 611-960 2.92e-30

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: 124.30  E-value: 2.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  611 VIHTSGSTGRPKGVPVPHAHVVrlfeASGEHF----RFGADDVW----TLFHSYAFDFSVwelwgPLLH-GGRLVVVPye 681
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLI----AANLQLihamGLTEADVYlnmlPLFHIAGLNLAL-----ATFHaGGANVVME-- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  682 vSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVlggealvaerlrpwadrhGLDAPELVN----- 756
Cdd:cd17637     74 -KFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL------------------GLDAPETIQrfeet 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  757 -------MYGITETTVHVTFHRLVRadledprRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPE 829
Cdd:cd17637    135 tgatfwsLYGQTETSGLVTLSPYRE-------RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPE 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  830 LTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQ--VKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRA 903
Cdd:cd17637    208 LTAYTFRNG--------WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIgvpdPKW 279

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  904 AEdgltQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd17637    280 GE----GIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 470-959 3.38e-30

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 128.81  E-value: 3.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAV--SYAGETLSYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLA 546
Cdd:PLN02574    53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  547 LVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAP--HDLTDADRAGATGP----YDTAYVIHTSGSTGR 620
Cdd:PLN02574   133 KRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPkfYELIKEDFDFVPKPvikqDDVAAIMYSSGTTGA 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  621 PKGVPVPHAHVVRL------FEASgEHFRFGADDVW----TLFHSYAFDFSVWELwgplLHGGRLVVVPYEVSRSprEFL 690
Cdd:PLN02574   213 SKGVVLTHRNLIAMvelfvrFEAS-QYEYPGSDNVYlaalPMFHIYGLSLFVVGL----LSLGSTIVVMRRFDAS--DMV 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  691 RLLDEEKVTVLNQTPSAFEQLV-LADAATDRATGSLRYVVLGGEALVAERLRPWADrhGLDAPELVNMYGITETTVHVTf 769
Cdd:PLN02574   286 KVIDRFKVTHFPVVPPILMALTkKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQ--TLPHVDFIQGYGMTESTAVGT- 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  770 hrlvRA-DLEDPRRRGVIGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrm 847
Cdd:PLN02574   363 ----RGfNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW------- 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  848 YRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAG 927
Cdd:PLN02574   432 LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1573930569  928 LRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PLN02574   512 VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKI 543
PLN02246 PLN02246
4-coumarate--CoA ligase
 1711-2208 3.99e-30

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 128.17  E-value: 3.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFV---AVPLTVPVSYAT-TSAAVSKLegiwem 1786
Cdd:PLN02246    52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttANPFYTPAEIAKqAKASGAKL------ 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1787 ldrpwIVTSAAGEPGLRELAARRewsGLRLTTADALRE-----------EPEDRDWYEARPDDLVLMLMTSGSTGLPKAV 1855
Cdd:PLN02246   126 -----IITQSCYVDKLKGLAEDD---GVTVVTIDDPPEgclhfseltqaDENELPEVEISPDDVVALPYSSGTTGLPKGV 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1856 RLTHRNVLTRAAAT---EAMN-GLGSGDVSLNWIPLDHVtgvvmFHLRDVYL-GCRQIHAptswILEDP----VRWPELA 1926
Cdd:PLN02246   198 MLTHKGLVTSVAQQvdgENPNlYFHSDDVILCVLPMFHI-----YSLNSVLLcGLRVGAA----ILIMPkfeiGALLELI 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1927 DRHRVSVtwAPnFAFGLLAEQAHRFQDRDWDLSPVRLVMnagevvvaSAArrflhvlAPFG----------LPQDVMHPG 1996
Cdd:PLN02246   269 QRHKVTI--AP-FVPPIVLAIAKSPVVEKYDLSSIRMVL--------SGA-------APLGkeledafrakLPNAVLGQG 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETCSVVTDSVLASEAPdhdeaFV----SCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANA 2071
Cdd:PLN02246   331 YGMTEAGPVLAMCLAFAKEP-----FPvksgSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATA 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2072 ESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAATDELALFL 2150
Cdd:PLN02246   406 NTIDKDGWLHTGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIA---DAAVVPMKDEVAGEVPVAFVV 482

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2151 RLAPGQDPAGALRE-IAGKVTREIGVSPAFLIpveaEAIPKTEIGKIQRTKLRKSFEAG 2208
Cdd:PLN02246   483 RSNGSEITEDEIKQfVAKQVVFYKRIHKVFFV----DSIPKAPSGKILRKDLRAKLAAG 537
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 8-315 4.12e-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. 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: 126.22  E-value: 4.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADtfALR---FLDTPDGPRAVrdgdPDEM 84
Cdd:cd20483      1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHE--VLRtayFEGDDFGEQQV----LDDP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   85 PVH--RVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTA 162
Cdd:cd20483     75 SFHliVIDLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  163 LAAGE-----EPPPAGFesADRLAAEEAaYLGSDRHRRDRAYWTERLAGLPEPVRL-----TDRtaPPRAPFLRRT--AV 230
Cdd:cd20483    155 LRAGRdlatvPPPPVQY--IDFTLWHNA-LLQSPLVQPLLDFWKEKLEGIPDASKLlpfakAER--PPVKDYERSTveAT 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  231 LSPAETRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGG 310
Cdd:cd20483    230 LDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDD 309


                   ....*
gi 1573930569  311 FVRAV 315
Cdd:cd20483    310 LLEST 314
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 470-959 1.25e-29

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 126.82  E-value: 1.25e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPG-RFVALALPRgPRLVPALLAVLKTGAAYLPLDPGHPAERLALV 548
Cdd:PRK07786    31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGdRVLILMLNR-TEFVESVLAANMLGAIAVPVNFRLTPPEIAFL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  549 MADAEPVAVVTDT-----AGSGRLPATDARVVVVDDARTVADLAGRapHDL---TDADRAGATGPYDT-AYVIHTSGSTG 619
Cdd:PRK07786   110 VSDCGAHVVVTEAalapvATAVRDIVPLLSTVVVAGGSSDDSVLGY--EDLlaeAGPAHAPVDIPNDSpALIMYTSGTTG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  620 RPKGVPVPHAHVVRlfEASGEHFRFGAD---DVW----TLFHSYAFDfSVwelwGPLLHGGRLVVVPYEVSRSPREFLRL 692
Cdd:PRK07786   188 RPKGAVLTHANLTG--QAMTCLRTNGADinsDVGfvgvPLFHIAGIG-SM----LPGLLLGAPTVIYPLGAFDPGQLLDV 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 LDEEKVTVLNQTPSAFeQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADrhGLDAPELVNMYGITETTvHVTfhrl 772
Cdd:PRK07786   261 LEAEKVTGIFLVPAQW-QAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAA--TFPEAQILAAFGQTEMS-PVT---- 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  773 VRADLEDP-RRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFlpdpfgAPGtrMYRSG 851
Cdd:PRK07786   333 CMLLGEDAiRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--WFHSG 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  852 DLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGA-DPAGLRA 930
Cdd:PRK07786   405 DLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAlTLEDLAE 484

                          490       500
                   ....*....|....*....|....*....
gi 1573930569  931 HLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK07786   485 FLTDRLARYKHPKALEIVDALPRNPAGKV 513
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 607-960 1.34e-29

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: 122.41  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPH-------AHVVRL--------FEASGEHFRFGaddvwTLFHSYAFdfsvwelwgpLLH 671
Cdd:cd17636      1 DPVLAIYTAAFSGRPNGALLSHqallaqaLVLAVLqaidegtvFLNSGPLFHIG-----TLMFTLAT----------FHA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 GGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVL--GGEALVAERLRPWADRHGL 749
Cdd:cd17636     66 GGTNVFVR---RVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPGG 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  750 dapelvnmYGITETTVHVTFHRLVRADLedprrrGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPE 829
Cdd:cd17636    143 --------YGQTEVMGLATFAALGGGAI------GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPE 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  830 LTEERFlpdpfgapGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLT 909
Cdd:cd17636    209 VNARRT--------RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ 280

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  910 QLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd17636    281 SVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 2325-2689 1.56e-29

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 123.16  E-value: 1.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2325 VVHLAATeDAEDGAAPGSDVSLLVLAQALA-----GRTGGERPVDLLFVTAGAQAVTPE-ERPTASHAAAGALLKSLREE 2398
Cdd:cd08955     11 VVHLWSL-DAPREEPADAASQELGCASALHlvqalSKAGLRRAPRLWLVTRGAQSVLADgEPVSPAQAPLWGLGRVIALE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2399 LPWLRGVHLDLSGGSAGDRAAAVLAEAAGFP-ADTEVARREGLRYVRRLAPLPDSAPRTAPAPAPADGFhlvsgglGGVG 2477
Cdd:cd08955     90 HPELRCGLVDLDPEATAAEEAEALLAELLAAdAEDQVALRGGARYVARLVRAPARPLRPDATYLITGGL-------GGLG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2478 SEVAAHLLKEPGTRLLLIGRTGLPPEdtwerhladagpassRIEAFRRLRGLG-EVRYETADVTDAAQVRAAVRRAADAW 2556
Cdd:cd08955    163 LLVAEWLVERGARHLVLTGRRAPSAA---------------ARQAIAALEEAGaEVVVLAADVSDRDALAAALAQIRASL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2557 gVPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDD 2636
Cdd:cd08955    228 -PPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQANYAAANAFLDA 306

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2637 LALRRRREGLPGQSLAWSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFD 2689
Cdd:cd08955    307 LAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALG 359
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 452-969 1.66e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 126.33  E-value: 1.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  452 PRVTRTLPQLFEARVAEspGRTAVSYAGETLSYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTG 530
Cdd:PRK07867     1 TSSAPTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  531 AAYLPLDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDARVVVVD-DARTVADLAGRAPHDLTDADRAGATgpyDTA 609
Cdd:PRK07867    79 IVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINvDSPAWADELAAHRDAEPPFRVADPD---DLF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  610 YVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV----WTLFHSYAfdfsVWELWGPLLHGGRLVVVPYEVSRS 685
Cdd:PRK07867   156 MLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVcyvsMPLFHSNA----VMAGWAVALAAGASIALRRKFSAS 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  686 prEFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRyVVLGGEAlVAERLRPWADRHGLdapELVNMYGITETTV 765
Cdd:PRK07867   232 --GFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLR-IVYGNEG-APGDIARFARRFGC---VVVDGFGSTEGGV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  766 HVTfhrlvRADLEDPrrrGVIGRPLADLRVY-----------VLDAAGRPVPPGATGEMY-VSGPGVAPGYLNRPELTEE 833
Cdd:PRK07867   305 AIT-----RTPDTPP---GALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAE 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  834 RFlpdpfgAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVA 913
Cdd:PRK07867   377 RM------RGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  914 YAVPAEEGGADPAGLRAHLAAR--LPAYMVPAACVLLDALPLTANGKLDTAALPAPDF 969
Cdd:PRK07867   449 ALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
prpE PRK10524
propionyl-CoA synthetase; Provisional
 481-959 1.70e-29

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 127.37  E-value: 1.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:PRK10524    84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSA 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 TAGS--GRL----PATD----------ARVVVVDdaRTVADLAGRAPHDLTDAD-RA---GATGPY------DTAYVIHT 614
Cdd:PRK10524   164 DAGSrgGKVvpykPLLDeaialaqhkpRHVLLVD--RGLAPMARVAGRDVDYATlRAqhlGARVPVewlesnEPSYILYT 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  615 SGSTGRPKGV-------PVPHAHVVR-LFEA-SGEHFrFGADDV-WTLFHSYAfdfsvweLWGPLLHGgrLVVVPYE--- 681
Cdd:PRK10524   242 SGTTGKPKGVqrdtggyAVALATSMDtIFGGkAGETF-FCASDIgWVVGHSYI-------VYAPLLAG--MATIMYEglp 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  682 VSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAA--TDRATGSLRYVVLGGEALVAERLRpWADRhGLDAPeLVNMYG 759
Cdd:PRK10524   312 TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEPLDEPTAS-WISE-ALGVP-VIDNYW 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHV-TFHRlvraDLED-PRRRGVIGRPLADLRVYVLD-AAGRPVPPGATGEMYVSGPgVAPGYLNRPELTEERFL 836
Cdd:PRK10524   389 QTETGWPIlAIAR----GVEDrPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGP-LPPGCMQTVWGDDDRFV 463

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  837 PDPFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLT-QL-VAY 914
Cdd:PRK10524   464 KTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVV--GVKDALKgQVaVAF 541

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  915 AVPAEEGGADPAGLRAHLAA--------RLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK10524   542 VVPKDSDSLADREARLALEKeimalvdsQLGAVARPARVWFVSALPKTRSGKL 594
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 607-959 2.16e-29

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: 121.98  E-value: 2.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHahvvRLFEASGEHF-----RFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVvpYE 681
Cdd:cd17635      2 DPLAVIFTSGTTGEPKAVLLAN----KTFFAVPDILqkeglNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  682 VSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAerlrpwADRHGLDAPELVNM---Y 758
Cdd:cd17635     76 ENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIA------ADVRFIEATGLTNTaqvY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  759 GITETT--VHVTFHRlvradleDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFL 836
Cdd:cd17635    150 GLSETGtaLCLPTDD-------DSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  837 PDPFgapgtrmyRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAV 916
Cdd:cd17635    223 DGWV--------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV 294

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1573930569  917 PAEEGGADPA-GLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:cd17635    295 ASAELDENAIrALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
PRK08315 PRK08315
AMP-binding domain protein; Validated
 445-958 2.40e-29

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 126.08  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  445 VRRDEPAPRVTRTLPQLFEARVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPA 522
Cdd:PRK08315     5 VRGPTDVPLLEQTIGQLLDRTAARYPDREALVYRdqGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  523 LLAVLKTGAAYLPLDPGHPAERL----------ALVMADA----EPVAVVTDTAG-----------SGRLPATdARVVVV 577
Cdd:PRK08315    85 QFATAKIGAILVTINPAYRLSELeyalnqsgckALIAADGfkdsDYVAMLYELAPelatcepgqlqSARLPEL-RRVIFL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  578 DDART-----VADLA--GRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVR--LFeaSGEHFRFGADD 648
Cdd:PRK08315   164 GDEKHpgmlnFDELLalGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngYF--IGEAMKLTEED 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  649 -----VwTLFHSYAfdfSVWELWGPLLHGGRLVVvPYEvSRSPREFLRLLDEEKVTVLNQTPSAF-EQLVLADAAT-Dra 721
Cdd:PRK08315   242 rlcipV-PLYHCFG---MVLGNLACVTHGATMVY-PGE-GFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARfD-- 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  722 TGSLRYVVLGGEALVAERLRPWADRHGLdaPELVNMYGITETTvHVTFHRLVRADLEdpRRRGVIGRPLADLRVYVLDAA 801
Cdd:PRK08315   314 LSSLRTGIMAGSPCPIEVMKRVIDKMHM--SEVTIAYGMTETS-PVSTQTRTDDPLE--KRVTTVGRALPHLEVKIVDPE 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  802 -GRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrMyRSGDLARWRPDGTLVHAGRADQQVkIRGFR-I 879
Cdd:PRK08315   389 tGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW------M-HTGDLAVMDEEGYVNIVGRIKDMI-IRGGEnI 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  880 EPGEIEAVLTAHPAVAGGAVV----PRAAEdgltQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTA 955
Cdd:PRK08315   461 YPREIEEFLYTHPKIQDVQVVgvpdEKYGE----EVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTV 536


                   ...
gi 1573930569  956 NGK 958
Cdd:PRK08315   537 TGK 539
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1838-2205 2.70e-29

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: 121.28  E-value: 2.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGvVMFHLRDVYLGcRQIHAPTswile 1917
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAG-AELVLLE----- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1918 dpVRWPELADRHRVSVTWApnfafGLLAEQAHRFQDRDWDLSP---VRLVMNAGEVVVASAARRFlhvlAPFGLPqdvMH 1994
Cdd:cd17630     74 --RNQALAEDLAPPGVTHV-----SLVPTQLQRLLDSGQGPAAlksLRAVLLGGAPIPPELLERA----ADRGIP---LY 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1995 PGWGMSETCSVVTdsvlASEAPDHDEAfvSCGLPYPGFAMRVVDDqdallpegdvGRLQVRGTSVTHGYHDNARANAesF 2074
Cdd:cd17630    140 TTYGMTETASQVA----TKRPDGFGRG--GVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE--F 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2075 TEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATDELALFLRLA 2153
Cdd:cd17630    202 NEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAV----RDAFVVGVPDEELGQRPVAVIVGR 277

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2154 PGQDPAGALREIAGKVtreigvsPAFLIPVE---AEAIPKTEIGKIQRTKLRKSF 2205
Cdd:cd17630    278 GPADPAELRAWLKDKL-------ARFKLPKRiypVPELPRTGGGKVDRRALRAWL 325
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 1711-2125 3.05e-29

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 123.71  E-value: 3.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyatTSAAVSKLEGIWEMLDRP 1790
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLN-------TRLTENERTNQLEDLDVQ 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTSAA-GEPGLRELAARRewsglrlTTADALREEPEDRDWyeaRPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT 1869
Cdd:TIGR01923   74 LLLTDSLlEEKDFQADSLDR-------IEAAGRYETSLSASF---NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGS 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1870 EAMNGLGSGDVSLNWIPLDHVTGVVMFhLRDVYLGCR-QIHAPTSWILEDpvrwpelADRHRVSVTwapnfafGLLAEQA 1948
Cdd:TIGR01923  144 KENLGFTEDDNWLLSLPLYHISGLSIL-FRWLIEGATlRIVDKFNQLLEM-------IANERVTHI-------SLVPTQL 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1949 HRFQDRDWDLSPVRLVMNAGEVVVASAARRflhvLAPFGLPqdvMHPGWGMSETCSVVTDSvlaseAPDHDEAFVSCGLP 2028
Cdd:TIGR01923  209 NRLLDEGGHNENLRKILLGGSAIPAPLIEE----AQQYGLP---IYLSYGMTETCSQVTTA-----TPEMLHARPDVGRP 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2029 YPGFAMRV-VDDQDallpegDVGRLQVRGTSVTHGYHDNARANaESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVN 2106
Cdd:TIGR01923  277 LAGREIKIkVDNKE------GHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELdGEGFLYVLGRRDDLIISG 349

                          410
                   ....*....|....*....
gi 1573930569 2107 GVNHYSHEIEACVEELPSV 2125
Cdd:TIGR01923  350 GENIYPEEIETVLYQHPGI 368
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1686-2201 3.34e-29

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: 124.70  E-value: 3.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1686 ALLRAAGRPDGEVVHVRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLT 1765
Cdd:cd17646      2 ALVAEQAARTPDAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1766 vpvsyatTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARRewsglrLTTADALREEPEDRDWYEARPDDLVLMLMT 1845
Cdd:cd17646     80 -------PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVA------LLGDEALAAPPATPPLVPPRPDNLAYVIYT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1846 SGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSwiLEDPVRWPEL 1925
Cdd:cd17646    147 SGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGG--HRDPAYLAAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1926 ADRHRVSVTWAPNFAFGLLAEQAhrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHvlapfgLPQDVMHPGWGMSETcsv 2005
Cdd:cd17646    225 IREHGVTTCHFVPSMLRVFLAEP-----AAGSCASLRRVFCSGEALPPELAARFLA------LPGAELHNLYGPTEA--- 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2006 VTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDgWFD---- 2081
Cdd:cd17646    291 AIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD-PFGpgsr 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2082 ---TGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAPGQD 2157
Cdd:cd17646    370 myrTGDLArWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV----THAVVVARAAPAGAARLVGYVVPAAGAA 445

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 2158 P--AGALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd17646    446 GpdTAALRAHLAERL------PEYMVPaafVVLDALPLTANGKLDRAAL 488
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1685-2229 3.36e-29

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 126.61  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGR-PDGEVVHVRADGSETRR----SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGF 1759
Cdd:PRK07529    29 ELLSRAAARhPDAPALSFLLDADPLDRpetwTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1760 VAvpltvPVSYATTSAAVSKL-----------------EGIW----EMLD-----RPWIVTSAAG-EPGLRELAAR--RE 1810
Cdd:PRK07529   109 AN-----PINPLLEPEQIAELlraagakvlvtlgpfpgTDIWqkvaEVLAalpelRTVVEVDLARyLPGPKRLAVPliRR 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1811 WSGLRLTTADA-LREEPEDR--DWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPL 1887
Cdd:PRK07529   184 KAHARILDFDAeLARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1888 DHVTGVVMFHLRDVYLGCRQIHA-PTSWILEDPVR--WpELADRHRVSVTWAPNFAFGLLAEQ---AHrfqdrdwDLSPV 1961
Cdd:PRK07529   264 FHVNALLVTGLAPLARGAHVVLAtPQGYRGPGVIAnfW-KIVERYRINFLSGVPTVYAALLQVpvdGH-------DISSL 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1962 RLVMNAGEVVVASAARRFLHVLapfGLPqdvMHPGWGMSETCSVVTDSvlaseAPDHDEAFVSCGLPYPGFAMRVV--DD 2039
Cdd:PRK07529   336 RYALCGAAPLPVEVFRRFEAAT---GVR---IVEGYGLTEATCVSSVN-----PPDGERRIGSVGLRLPYQRVRVVilDD 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2040 QDALL---PEGDVGRLQVRGTSVTHGYHdNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEI 2115
Cdd:PRK07529   405 AGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAI 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2116 EACVEELPSVvrSFTAAVAvRSDASAAtdELAL-FLRLAPGQD-PAGALREIAGKVTREIGVSPAFLIPVeaEAIPKTEI 2193
Cdd:PRK07529   484 EEALLRHPAV--ALAAAVG-RPDAHAG--ELPVaYVQLKPGASaTEAELLAFARDHIAERAAVPKHVRIL--DALPKTAV 556

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1573930569 2194 GKIQRTKLRKSFEAGEFDGAVRETQLLLGTAATVPD 2229
Cdd:PRK07529   557 GKIFKPALRRDAIRRVLRAALRDAGVEAEVVDVVED 592
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1708-2145 3.67e-29

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 125.46  E-value: 3.67e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1708 TRRSYASLVPEASRVLAGLRRR-GLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvPVS-------YATTSAAVSK 1779
Cdd:PRK08314    34 RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN-PMNreeelahYVTDSGARVA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1780 LEGIwEMLDRpwiVTSAAGEPGLRELAARRewsglrltTADALREEPEDR--DW-------------------------- 1831
Cdd:PRK08314   113 IVGS-ELAPK---VAPAVGNLRLRHVIVAQ--------YSDYLPAEPEIAvpAWlraepplqalapggvvawkealaagl 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 ----YEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQ 1907
Cdd:PRK08314   181 apppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATV 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 IHAPtswiledpvRW-----PELADRHRVSVTWA-PNFAFGLLAEQahRFQDRdwDLSPVRLVMNAGEVVVASAARRfLH 1981
Cdd:PRK08314   261 VLMP---------RWdreaaARLIERYRVTHWTNiPTMVVDFLASP--GLAER--DLSSLRYIGGGGAAMPEAVAER-LK 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1982 VLapFGLPqdvMHPGWGMSETCSvvtdsvlASEAPDHDEAFVSC-GLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSV 2059
Cdd:PRK08314   327 EL--TGLD---YVEGYGLTETMA-------QTHSNPPDRPKLQClGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQV 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2060 THGYHDNARANAESFTE-DG--WFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIE-----------ACVEELPS 2124
Cdd:PRK08314   395 FKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVEnllykhpaiqeACVIATPD 474

                          490       500
                   ....*....|....*....|...
gi 1573930569 2125 VVRSFT--AAVAVRSDASAATDE 2145
Cdd:PRK08314   475 PRRGETvkAVVVLRPEARGKTTE 497
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 459-958 6.47e-29

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: 123.56  E-value: 6.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAES-PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:cd12118      6 PLSFLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 pghpaERLalvmaDAEPVAVVtdtagsgrLPATDARVVVVDDARTVADL-AGRAPhdltDADRAGATGPYDTAYVIHTSG 616
Cdd:cd12118     86 -----TRL-----DAEEIAFI--------LRHSEAKVLFVDREFEYEDLlAEGDP----DFEWIPPADEWDPIALNYTSG 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPH--AHVVRLfeASGEHFRFGADDV--WTL--FHSYAFDFSvwelWGPLLHGGRLVVVPyEVsrSPREFL 690
Cdd:cd12118    144 TTGRPKGVVYHHrgAYLNAL--ANILEWEMKQHPVylWTLpmFHCNGWCFP----WTVAAVGGTNVCLR-KV--DAKAIY 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  691 RLLDEEKVTVLNQTPSAFEQLVlADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETTVHVTF- 769
Cdd:cd12118    215 DLIEKHKVTHFCGAPTVLNMLA-NAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFD---VTHVYGLTETYGPATVc 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  770 ---------HRLVRADLEdpRRRGVigRPLADLRVYVLDAAG-RPVP-PGAT-GEMYVSGPGVAPGYLNRPELTEERFlp 837
Cdd:cd12118    291 awkpewdelPTEERARLK--ARQGV--RYVGLEEVDVLDPETmKPVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-- 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  838 dpfgAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVP 917
Cdd:cd12118    365 ----RGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL 438

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1573930569  918 AEEGGADPAGLRAHLAARLPAYMVPAACVLLDaLPLTANGK 958
Cdd:cd12118    439 KEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 463-964 7.83e-29

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: 124.14  E-value: 7.83e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  463 EARVAESPGRTAVSY---AGET--LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP-- 535
Cdd:cd05970     24 DAMAKEYPDKLALVWcddAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPat 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 --LDPGHPAER-----LALVMADAEPVAVVTDTAGSGRLPATDARVVVVDDAR----TVADLAGRAPHDLTDADRAGATG 604
Cdd:cd05970    104 hqLTAKDIVYRiesadIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPegwiDFRKLIKNASPDFERPTANSYPC 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  605 PYDTAYVIHTSGSTGRPKGVP----VPHAHVV-----RLFEASGEHFRFgADDVWTLfhsyafdfSVW-ELWGPLLHGGR 674
Cdd:cd05970    184 GEDILLVYFSSGTTGMPKMVEhdftYPLGHIVtakywQNVREGGLHLTV-ADTGWGK--------AVWgKIYGQWIAGAA 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVVPYEvSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAaTDRATGSLRYVVLGGEALVAERLRPWADRHGLdapEL 754
Cdd:cd05970    255 VFVYDYD-KFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGI---KL 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  755 VNMYGITETTVHV-TFHRLvradleDPRRrGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGP-----GVAPGYLNRP 828
Cdd:cd05970    330 MEGFGQTETTLTIaTFPWM------EPKP-GSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDA 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  829 ELTEERFLPDpfgapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAV--VPraaeD 906
Cdd:cd05970    403 EKTAEVWHDG--------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVtgVP----D 470

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  907 GLTQLVAYAVPAEEGGADPAG-----LRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05970    471 PIRGQVVKATIVLAKGYEPSEelkkeLQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 466-958 9.12e-29

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: 124.98  E-value: 9.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  466 VAESPGRTAVSYAGE------TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG 539
Cdd:cd05966     63 LKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAGS--GRL----PATDA---------RVVVVDDA-RTVADLAGRaphDLTDADRAGAT 603
Cdd:cd05966    143 FSAESLADRINDAQCKLVITADGGYrgGKViplkEIVDEalekcpsveKVLVVKRTgGEVPMTEGR---DLWWHDLMAKQ 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 GPY---------DTAYVIHTSGSTGRPKGVPvpHAHVVRLFEASGEH---FRFGADDV--------WTLFHSYAfdfsvw 663
Cdd:cd05966    220 SPEcepewmdseDPLFILYTSGSTGKPKGVV--HTTGGYLLYAATTFkyvFDYHPDDIywctadigWITGHSYI------ 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  664 eLWGPLLHGGRLVVvpYE-------VSRspreFLRLLDEEKVTVLNQTPSAFEQLVLAD----AATDRAtgSLRyvVLG- 731
Cdd:cd05966    292 -VYGPLANGATTVM--FEgtptypdPGR----YWDIVEKHKVTIFYTAPTAIRALMKFGdewvKKHDLS--SLR--VLGs 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  732 -GEALVAERLRpWADRH-GLDAPELVNMYGITETTVHVTFHRLVRADLedprRRGVIGRPLADLRVYVLDAAGRPVPPGA 809
Cdd:cd05966    361 vGEPINPEAWM-WYYEViGKERCPIVDTWWQTETGGIMITPLPGATPL----KPGSATRPFFGIEPAILDEEGNEVEGEV 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  810 TGEMYVSG--PGVAPGYLNRPELTEERFLPdPFgaPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAV 887
Cdd:cd05966    436 EGYLVIKRpwPGMARTIYGDHERYEDTYFS-KF--PG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  888 LTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPA---GLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:cd05966    511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1711-2203 9.91e-29

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: 121.68  E-value: 9.91e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVpvsyattsaavsklegiwemldrp 1790
Cdd:cd05912      3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNT------------------------ 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 wivtsaagepglrelaarrewsglRLTTADaLREEPEDRDwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05912     59 ------------------------RLTPNE-LAFQLKDSD---VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSA 110

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGV-VMfhLRDVYLGCrqihapTSWILE--DPVRWPELADRHRVS-VTWAPNFAFGLLAE 1946
Cdd:cd05912    111 LNLGLTEDDNWLCALPLFHISGLsIL--MRSVIYGM------TVYLVDkfDAEQVLHLINSGKVTiISVVPTMLQRLLEI 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1947 QAHRFQdrdwdlSPVRLVMNAGevvvASAARRFLHVLAPFGLPqdvMHPGWGMSETCS-VVTdsvLASEapDHDEAFVSC 2025
Cdd:cd05912    183 LGEGYP------NNLRCILLGG----GPAPKPLLEQCKEKGIP---VYQSYGMTETCSqIVT---LSPE--DALNKIGSA 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2026 GLPYPGFAMRVVDDqdaLLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVII 2104
Cdd:cd05912    245 GKPLFPVELKIEDD---GQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLdEEGFLYVLDRRSDLII 320

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2105 VNGVNHYSHEIEACVEELPSVVRsftAAVA--------------VRSDASAATDELALFLRlapgqdpagalREIAG-KV 2169
Cdd:cd05912    321 SGGENIYPAEIEEVLLSHPAIKE---AGVVgipddkwgqvpvafVVSERPISEEELIAYCS-----------EKLAKyKV 386

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569 2170 TREIgvspaflipVEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05912    387 PKKI---------YFVDELPRTASGKLLRHELKQ 411
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 1709-2203 1.01e-28

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 123.41  E-value: 1.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1709 RRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVS-----YATTSAAVSKLEGI 1783
Cdd:TIGR02262   30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTaddyaYMLEDSRARVVFVS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1784 WEMLdrPWIVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNvL 1863
Cdd:TIGR02262  110 GALL--PVIKAALGKSPHLEHRVVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSN-P 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1864 TRAAATEAMNGLG--SGDVSLNWIPLDHVTGvvmfhLRDVYLGCRQIHAPTSWILEDPV--RWPELADRHRVSVTWA-PN 1938
Cdd:TIGR02262  187 YWTAELYARNTLGirEDDVCFSAAKLFFAYG-----LGNALTFPMSVGATTVLMGERPTpdAVFDRLRRHQPTIFYGvPT 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1939 FAFGLLAEQAHRFQDRDwdlsPVRLVMNAGEVVVASAARRFLhvlAPFGLpqDVMHpGWGMSETCSVvtdsvLASEAPdH 2018
Cdd:TIGR02262  262 LYAAMLADPNLPSEDQV----RLRLCTSAGEALPAEVGQRWQ---ARFGV--DIVD-GIGSTEMLHI-----FLSNLP-G 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2019 DEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDlAFLRDGELYIT-- 2096
Cdd:TIGR02262  326 DVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGD-KYVRNDDGSYTya 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2097 GRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELAlFLRLAPGQdpaGALR-EIAGKVTREIG- 2174
Cdd:TIGR02262  404 GRTDDMLKVSGIYVSPFEIESALIQHPAVLE---AAVVGVADEDGLIKPKA-FVVLRPGQ---TALEtELKEHVKDRLAp 476

                          490       500       510
                   ....*....|....*....|....*....|
gi 1573930569 2175 -VSPAFLIPVEAeaIPKTEIGKIQRTKLRK 2203
Cdd:TIGR02262  477 yKYPRWIVFVDD--LPKTATGKIQRFKLRE 504
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 478-963 1.11e-28

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 123.95  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  478 AGETLSYAELNAEANRLARLLVEQGAGPGRFVALaLPRGPRLV-PALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVa 556
Cdd:PRK07768    26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVEIaPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRV- 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  557 vvtdtagsgrLPATDARVVVVDD---------------ARTVADLAGRAPHDLTDadragaTGPYDTAYVIHTSGSTGRP 621
Cdd:PRK07768   104 ----------IGMIGAKAVVVGEpflaaapvleekgirVLTVADLLAADPIDPVE------TGEDDLALMQLTSGSTGSP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGAD-DV---W-TLFHSYAFdfsVWELWGPLLHGGRLVVV-PYEVSRSPREFLRLLDE 695
Cdd:PRK07768   168 KAVQITHGNLYANAEAMFVAAEFDVEtDVmvsWlPLFHDMGM---VGFLTVPMYFGAELVKVtPMDFLRDPLLWAELISK 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  696 EKVTVLNQTPSAFEQL--VLADAATDRA--TGSLRYVVLGGEAL---VAERLRPWADRHGLDAPELVNMYGITETTVHVT 768
Cdd:PRK07768   245 YRGTMTAAPNFAYALLarRLRRQAKPGAfdLSSLRFALNGAEPIdpaDVEDLLDAGARFGLRPEAILPAYGMAEATLAVS 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  769 FHRL--------VRADLEDPRRRGV------------IGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYlnrp 828
Cdd:PRK07768   325 FSPCgaglvvdeVDADLLAALRRAVpatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY---- 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  829 eLTEERFLP--DPFGapgtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIE-AVLTAHPAVAGGAVVPRAAE 905
Cdd:PRK07768   401 -LTMDGFIPaqDADG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIErAAARVEGVRPGNAVAVRLDA 474

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  906 DGLTQlvAYAVPAEEGGADPAG----LRAHLAARLPAY--MVPAACVLLDA--LPLTANGKLDTAA 963
Cdd:PRK07768   475 GHSRE--GFAVAVESNAFEDPAevrrIRHQVAHEVVAEvgVRPRNVVVLGPgsIPKTPSGKLRRAN 538
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 1709-2208 3.30e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 121.45  E-value: 3.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1709 RRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWEMLD 1788
Cdd:PRK09088    22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1789 rpwiVTSAAGEPGLRELAArrewsglrlTTADALREEPEDRDwyEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA 1868
Cdd:PRK09088   102 ----DAVAAGRTDVEDLAA---------FIASADALEPADTP--SIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHN 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 TEAMNGLGSGDVSLNWIPLDHVTGVVMfHLRDVYLGCRQIHAPTSWILEDPVRW---PELADRHRVSVtwaPNFAfglla 1945
Cdd:PRK09088   167 FGVLGRVDAHSSFLCDAPMFHIIGLIT-SVRPVLAVGGSILVSNGFEPKRTLGRlgdPALGITHYFCV---PQMA----- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1946 eQAHRFQDrDWDLSPVR---LVMNAGEVVVASAARRFLHVlapfGLPqdvMHPGWGMSETCSVVTDSVlasEAPDHDEAF 2022
Cdd:PRK09088   238 -QAFRAQP-GFDAAALRhltALFTGGAPHAAEDILGWLDD----GIP---MVDGFGMSEAGTVFGMSV---DCDVIRAKA 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2023 VSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAfLRDGELYIT--GRAK 2100
Cdd:PRK09088   306 GAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIA-RRDADGFFWvvDRKK 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2101 DVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRSDASAATDELALFLRLAPGQDPAGALREIAGKVTReigvspaFL 2180
Cdd:PRK09088   385 DMFISGGENVYPAEIEAVLADHPGIRE--CAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAK-------YK 455

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569 2181 IPVE---AEAIPKTEIGKIQRTKLRKSFEAG 2208
Cdd:PRK09088   456 VPKHlrlVDALPRTASGKLQKARLRDALAAG 486
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1686-2208 4.28e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 122.02  E-value: 4.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1686 ALLRAAGRPdgevvhVRADGsETRRSYASLVPEASRVLAGLRRRGLRPGDRV-ILQCDDTEDFVATLWGCVLGgFVAVPL 1764
Cdd:PRK06188    21 ALKRYPDRP------ALVLG-DTRLTYGQLADRISRYIQAFEALGLGTGDAVaLLSLNRPEVLMAIGAAQLAG-LRRTAL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 TVPVS-----YATTSAAVSKLegiwemldrpwIVTSAAGEPGLRELAARRewSGLR--LTTADAlreePEDRDWYE---- 1833
Cdd:PRK06188    93 HPLGSlddhaYVLEDAGISTL-----------IVDPAPFVERALALLARV--PSLKhvLTLGPV----PDGVDLLAaaak 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1834 ---------ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVvMFhlrdvylg 1904
Cdd:PRK06188   156 fgpaplvaaALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA-FF-------- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1905 crqihAPTSW------ILE--DPVRWPELADRHRVSVTW-APNFAFGLLaeQAHRFQDRDWD-----------LSPVRLv 1964
Cdd:PRK06188   227 -----LPTLLrggtviVLAkfDPAEVLRAIEEQRITATFlVPTMIYALL--DHPDLRTRDLSsletvyygaspMSPVRL- 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1965 mnagevvvASAARRFLHVLAPFglpqdvmhpgWGMSETCSVVTdsVLASE--APDHDEAFVSCGLPYPGFAMRVVDDQDA 2042
Cdd:PRK06188   299 --------AEAIERFGPIFAQY----------YGQTEAPMVIT--YLRKRdhDPDDPKRLTSCGRPTPGLRVALLDEDGR 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2043 LLPEGDVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEE 2121
Cdd:PRK06188   359 EVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREdEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE 437

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2122 LPSVV-------------RSFTAAVAVRSDASAATDELALFLRLAPGqdPAGALREIagkvtreigvspaflipVEAEAI 2188
Cdd:PRK06188   438 HPAVAqvavigvpdekwgEAVTAVVVLRPGAAVDAAELQAHVKERKG--SVHAPKQV-----------------DFVDSL 498

                          570       580
                   ....*....|....*....|
gi 1573930569 2189 PKTEIGKIQRTKLRKSFEAG 2208
Cdd:PRK06188   499 PLTALGKPDKKALRARYWEG 518
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1073-1492 6.13e-28

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: 118.83  E-value: 6.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELHV 1152
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRVDT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1153 VDcpdeeraahVAAAMRRSFDLTRDSALwaGVFGTGDTrtLLLVLHHSAADGWSLRPLADDLGTAYAARRAgaapdwAPP 1232
Cdd:cd19537     83 LD---------VWKEINRPFDLEREDPI--RVFISPDT--LLVVMSHIICDLTTLQLLLREVSAAYNGKLL------PPV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1233 ALQYADFALWQRRVLapapegpgrlERLTSFWRQALDGLPeesaPPPDRPRPAAPSGRGGGVTVPLDAGTHRELLRLAdh 1312
Cdd:cd19537    144 RREYLDSTAWSRPAS----------PEDLDFWSEYLSGLP----LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFS-- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1313 enASLFMVLH----GALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLR--ADASGDPTFRELLARVRAFD 1386
Cdd:cd19537    208 --TSSGITLHqlalAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVRRSS 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1387 VQALDHQdLPFDRLVEEVNPRRHPARHPLFQVMLALQNNERAVLTLGEDRV-PLRPAATGtAKFDLFVDVLERhgadgTA 1465
Cdd:cd19537    286 QAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSLALPIPGVePLYTWAEG-AKFPLMFEFTAL-----SD 358

                          410       420
                   ....*....|....*....|....*..
gi 1573930569 1466 DGLDLHVEYAADLYDPATAERFAGALR 1492
Cdd:cd19537    359 DSLLLRLEYDTDCFSEEEIDRIESLIL 385
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 1684-2203 6.87e-28

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 121.83  E-value: 6.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1684 AEALLRAAGRPDGEVVHVRADgseTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP 1763
Cdd:PLN02860    10 CQCLTRLATLRGNAVVTISGN---RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 LTVPVSYATTSAAVSKLEGIWEMLD---RPWIVTSAAGE-PGLR------ELAARREWSGLRLTTADALREE---PEDRD 1830
Cdd:PLN02860    87 LNYRWSFEEAKSAMLLVRPVMLVTDetcSSWYEELQNDRlPSLMwqvfleSPSSSVFIFLNSFLTTEMLKQRalgTTELD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1831 wYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGV------VM--------- 1895
Cdd:PLN02860   167 -YAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLssalamLMvgachvllp 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1896 -FHLRDVYLGCRQiHAPTSWILEdPVRWPELADRHRVSVTWAPNfafgllaeqahrfqdrdwdlSPVRLVMNAGEVVVA- 1973
Cdd:PLN02860   246 kFDAKAALQAIKQ-HNVTSMITV-PAMMADLISLTRKSMTWKVF--------------------PSVRKILNGGGSLSSr 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1974 --SAARRFLhvlapfglPQDVMHPGWGMSETCSVVT-----DSVLASEAPDHDEAF------------VSCGLPYPGFAM 2034
Cdd:PLN02860   304 llPDAKKLF--------PNAKLFSAYGMTEACSSLTfmtlhDPTLESPKQTLQTVNqtksssvhqpqgVCVGKPAPHVEL 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2035 RVVDDQDAllpegDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLRD-GELYITGRAKDVIIVNGVNHYSH 2113
Cdd:PLN02860   376 KIGLDESS-----RVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPE 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2114 EIEACVEELPSVVrsftAAVAVRSDASAATDELALFLRLAPG--------QDPAGAL---REIAGKVTREIGVSpAFLIP 2182
Cdd:PLN02860   451 EVEAVLSQHPGVA----SVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekENAKKNLtlsSETLRHHCREKNLS-RFKIP 525

                          570       580
                   ....*....|....*....|....*
gi 1573930569 2183 ----VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PLN02860   526 klfvQWRKPFPLTTTGKIRRDEVRR 550
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 607-960 1.41e-27

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: 117.10  E-value: 1.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHahvVRLFEASGEHFRFG----ADDVWTLFHSYAFDFSVWELWGPLLHG---------- 672
Cdd:cd05924      4 DDLYILYTGGTTGMPKGVMWRQ---EDIFRMLMGGADFGtgefTPSEDAHKAAAAAAGTVMFPAPPLMHGtgswtafggl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  673 --GRLVVVPyEVSRSPREFLRLLDEEKVTVLNQTPSAFEQ-LVLA-DAATDRATGSLRYVVLGGeALVAERLRPWADRHG 748
Cdd:cd05924     81 lgGQTVVLP-DDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDAlRDAGPYDLSSLFAISSGG-ALLSPEVKQGLLELV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  749 LDApELVNMYGITETTVHVTFHRLVRADLEDPRRRgvigrplADLRVYVLDAAGRPVPPGATGEMYVSGPGVAP-GYLNR 827
Cdd:cd05924    159 PNI-TLVDAFGSSETGFTGSGHSAGSGPETGPFTR-------ANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPlGYYGD 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  828 PELTEERFlpdpFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDG 907
Cdd:cd05924    231 EAKTAETF----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  908 LTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd05924    307 GQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1719-2202 1.69e-27

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: 119.08  E-value: 1.69e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1719 ASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWE---------MLDR 1789
Cdd:cd05922      3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGgrivladagAADR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1790 PWIVTSAAGEPGLrelaarrewsglrLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT 1869
Cdd:cd05922     83 LRDALPASPDPGT-------------VLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1870 EAMNGLGSGDVSLNWIPL--DHVTGVVMFHLRdvyLGCRQIHAPTSwILEDPVrWPELADRHRVSVTWAPNfafglLAEQ 1947
Cdd:cd05922    150 AEYLGITADDRALTVLPLsyDYGLSVLNTHLL---RGATLVLTNDG-VLDDAF-WEDLREHGATGLAGVPS-----TYAM 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1948 AHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLapfglPQDVMHPGWGMSETCSVVT--DSVLASEAPDhdeafvSC 2025
Cdd:cd05922    220 LTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELL-----PGAQVYVMYGQTEATRRMTylPPERILEKPG------SI 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2026 GLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYITGRAKDVII 2104
Cdd:cd05922    289 GLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDeDGFLFIVGRRDRMIK 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2105 VNGVNHYSHEIEACVEELPSVVrsftaAVAVRSDASAATDELALFLRLAPGQDPAGALREIAGKVtrEIGVSPAFLIPVe 2184
Cdd:cd05922    369 LFGNRISPTEIEAAARSIGLII-----EAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERL--PPYKVPATVRVV- 440

                          490
                   ....*....|....*...
gi 1573930569 2185 aEAIPKTEIGKIQRTKLR 2202
Cdd:cd05922    441 -DELPLTASGKVDYAALR 457
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 465-959 2.04e-27

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 120.25  E-value: 2.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVsyaGETLSYAELNAEANRLARLLV-EQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAE 543
Cdd:PRK05677    36 RFADKPAFSNL---GKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  544 RLALVMADAEPVAVV-----TDTAgSGRLPATDARVVVVDDartVADL---------------------AGRAP--HDLT 595
Cdd:PRK05677   113 EMEHQFNDSGAKALVclanmAHLA-EKVLPKTGVKHVIVTE---VADMlpplkrllinavvkhvkkmvpAYHLPqaVKFN 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRAGATGPY--------DTAYVIHTSGSTGRPKGVPVPH----AHVVRLFEASGEHFRFGADDVWT---LFHSYAFDF 660
Cdd:PRK05677   189 DALAKGAGQPVteanpqadDVAVLQYTGGTTGVAKGAMLTHrnlvANMLQCRALMGSNLNEGCEILIAplpLYHIYAFTF 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  661 SVWELwgpLLHGGRLVVVPyevsrSPRE---FLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAL-- 735
Cdd:PRK05677   269 HCMAM---MLIGNHNILIS-----NPRDlpaMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALql 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  736 -VAERlrpWADRHGLDAPElvnMYGITETTVHVTFhrlvradleDPR---RRGVIGRPLADLRVYVLDAAGRPVPPGATG 811
Cdd:PRK05677   341 aTAER---WKEVTGCAICE---GYGMTETSPVVSV---------NPSqaiQVGTIGIPVPSTLCKVIDDDGNELPLGEVG 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  812 EMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAH 891
Cdd:PRK05677   406 ELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  892 PAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK05677   479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI 546
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1073-1502 2.66e-27

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: 117.55  E-value: 2.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1073 PASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEED-GAIHQRVLPPGTLrpELH 1151
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQV--PVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVDC-PDEERA----AHVAAAMRRSFDLTRDSALWAGVFGTGDTRTLLLVL--HHSAADGWSLRPLADDLgTAYAARRAG 1224
Cdd:cd19536     81 ELDLtPLEEQLdplrAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVIsdHHSILDGWSLYLLVKEI-LAVYNQLLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1225 AAPDWAPPALQYADFALWQRRVLAPAPegpgrlerLTSFWRQALDGLpEESAPPPDRPRPAAPSGRGGGVTVPLDAGTHR 1304
Cdd:cd19536    160 YKPLSLPPAQPYRDFVAHERASIQQAA--------SERYWREYLAGA-TLATLPALSEAVGGGPEQDSELLVSVPLPVRS 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1305 ELLRLADHENASlfMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALD--EVVGLLTNTLVLRADASgDPTFRELLARV 1382
Cdd:cd19536    231 RSLAKRSGIPLS--TLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGaeRLLGLFLNTLPLRVTLS-EETVEDLLKRA 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1383 RAFDVQALDHQDLPFdrlveeVNPRRHPARHPLFQVMLALQN------NERAVLTLGEDRVPLRPAATGTAKFDLFVDVL 1456
Cdd:cd19536    308 QEQELESLSHEQVPL------ADIQRCSEGEPLFDSIVNFRHfdldfgLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPK 381

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569 1457 ErhgadgtaDGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19536    382 Q--------DRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 1711-2208 2.89e-27

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 119.76  E-value: 2.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRR-GLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVSYA-------TTSAAVSK-LE 1781
Cdd:cd05905     16 TWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQqlgfllgTCKVRVALtVE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1782 GIWEMLDRPWIVTSAAGepglrELAARREWSGLRLTTADALREEPEDRDW---YEARPDDLVLMLMTSGSTGLPKAVRLT 1858
Cdd:cd05905     96 ACLKGLPKKLLKSKTAA-----EIAKKKGWPKILDFVKIPKSKRSKLKKWgphPPTRDGDTAYIEYSFSSDGSLSGVAVS 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1859 HRNVLTRAAA-TEAMNGLGSGDVSLNwipLDHVTGVVMFH--LRDVYLGCRQIHAPTSWILEDPVRWPELADRHRVSVTW 1935
Cdd:cd05905    171 HSSLLAHCRAlKEACELYESRPLVTV---LDFKSGLGLWHgcLLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAY 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1936 AP----NFAF-GLLAEQAHRFQdRDWDLSPVRLVM-NAGEVVVASAARRFLHVLAPFGLPQDV-----MH-----PGW-G 1998
Cdd:cd05905    248 VKlrtlHWCLkDLSSTLASLKN-RDVNLSSLRMCMvPCENRPRISSCDSFLKLFQTLGLSPRAvstefGTrvnpfICWqG 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1999 MSETCSvvTDSVLASEAPDHDEAFVS------------CGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGY-- 2063
Cdd:cd05905    327 TSGPEP--SRVYLDMRALRHGVVRLDerdkpnslplqdSGKVLPGAQVAIVNpETKGLCKDGEIGEIWVNSPANASGYfl 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2064 ----------HDNARANAESFTEDGWFDTGDLAFLRDGE-----------LYITGRAKDVIIVNGVNHYSHEIEACVEEl 2122
Cdd:cd05905    405 ldgetndtfkVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdlLFVVGSIDETLEVRGLRHHPSDIEATVMR- 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2123 psvVRSFTAAVAVRSdasaATDELALFLRLAPG-QDPAGAL--REIAgKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRT 2199
Cdd:cd05905    484 ---VHPYRGRCAVFS----ITGLVVVVAEQPPGsEEEALDLvpLVLN-AILEEHQVIVDCVALVPPGSLPKNPLGEKQRM 555


                   ....*....
gi 1573930569 2200 KLRKSFEAG 2208
Cdd:cd05905    556 EIRQAFLAG 564
PRK13382 PRK13382
bile acid CoA ligase;
461-967 2.99e-27

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 119.48  E-value: 2.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  461 LFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALaLPRGPR-LVPALLAVLKTGAAYLPLDPG 539
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGI-MCRNHRgFVEALLAANRIGADILLLNTS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  540 HPAERLALVMADAEPVAVVTDTAGSGRLP-ATDARVvvvDDARTVA--DLAGRAPHDLTDADRAGAT---GPYDTAYVIH 613
Cdd:PRK13382   127 FAGPALAEVVTREGVDTVIYDEEFSATVDrALADCP---QATRIVAwtDEDHDLTVEVLIAAHAGQRpepTGRKGRVILL 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  614 TSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHSYAFdfsvwelwGPLLHGGRLVVVPYEVSR-SPRE 688
Cdd:PRK13382   204 TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEptviVAPMFHAWGF--------SQLVLAASLACTIVTRRRfDPEA 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  689 FLRLLDEEKVTVLNQTPSAFEQLV-LADAATDRATG-SLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVH 766
Cdd:PRK13382   276 TLDLIDRHRATGLAVVPVMFDRIMdLPAEVRNRYSGrSLRFAAASGSRMRPDVVIAFMDQFG---DVIYNNYNATEAGMI 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  767 VTfhrlvrADLEDPRRR-GVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYlnrpelteerflpdpfgAPGT 845
Cdd:PRK13382   353 AT------ATPADLRAApDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY-----------------TSGS 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  846 R------MYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAE 919
Cdd:PRK13382   410 TkdfhdgFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1573930569  920 EGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAALPAP 967
Cdd:PRK13382   490 GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
470-964 3.18e-27

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 119.32  E-value: 3.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAylPLDPGHPAERL---- 545
Cdd:PRK10946    37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSelna 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  546 -------ALVMADAEPvAVVTDTAGSGRLPA--TDARVVVVDDARTVADLAGRAPHDLTDADrAGATGPYDTAYVIHTSG 616
Cdd:PRK10946   115 yasqiepALLIADRQH-ALFSDDDFLNTLVAehSSLRVVLLLNDDGEHSLDDAINHPAEDFT-ATPSPADEVAFFQLSGG 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPHA---HVVRlfeASGEHFRFGADdvwTLF-------HSYAFDfSVWELwGPLLHGGRLVVVPyevSRSP 686
Cdd:PRK10946   193 STGTPKLIPRTHNdyyYSVR---RSVEICGFTPQ---TRYlcalpaaHNYPMS-SPGAL-GVFLAGGTVVLAP---DPSA 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  687 REFLRLLDEEKVTVLNQTPSAFEQLVLADAATDR--ATGSLRYVVLGGeALVAERLrpwADRhgldAPELVN-----MYG 759
Cdd:PRK10946   262 TLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSraQLASLKLLQVGG-ARLSETL---ARR----IPAELGcqlqqVFG 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  760 ITETTVHVTfhrlvRADLEDPRRRGVIGRPLA-DLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPD 838
Cdd:PRK10946   334 MAEGLVNYT-----RLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDAN 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  839 PFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGL--TQLVAYAV 916
Cdd:PRK10946   409 GF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALV--SMEDELmgEKSCAFLV 479

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569  917 PAEEggADPAGLRAHLAARLPA-YMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK10946   480 VKEP--LKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 482-939 1.30e-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: 1.30e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAaylpldpghpaerlalvmadaepvaVVtdt 561
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA-------------------------VV--- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 agsgrLPATDarVVVVDDARTVADLAGRAPHDLTDADRAGatgpyDTAYVIHTSGSTGRPKgvPVPHAHVVRLFEASGEH 641
Cdd:cd05974     53 -----IPATT--LLTPDDLRDRVDRGGAVYAAVDENTHAD-----DPMLLYFTSGTTSKPK--LVEHTHRSYPVGHLSTM 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGAD--DVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAAtd 719
Cdd:cd05974    119 YWIGLKpgDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-- 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  720 RATGSLRYVVLGGEAL---VAERLRPWADRHGLDApelvnmYGITETTVhvtfhrLVRADLEDPRRRGVIGRPLADLRVY 796
Cdd:cd05974    197 SFDVKLREVVGAGEPLnpeVIEQVRRAWGLTIRDG------YGQTETTA------LVGNSPGQPVKAGSMGRPLPGYRVA 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  797 VLDAAGRPVPPG-ATGEMYVSGP-GVAPGYLNRPELTEerflpdpfGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKI 874
Cdd:cd05974    265 LLDPDGAPATEGeVALDLGDTRPvGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  875 RGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAV---PAEEGGADPAGLRAHLAARLPAY 939
Cdd:cd05974    337 SDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlraGYEPSPETALEIFRFSRERLAPY 404
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 1836-2203 1.34e-26

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: 116.66  E-value: 1.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHV---TGVVMFHLrdvYLGCRQIHAPT 1912
Cdd:cd05909    146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSfglTGCLWLPL---LSGIKVVFHPN 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 SWileDPVRWPELADRHRVSVTWA-PNFaFGLLAEQAHRFqdrdwDLSPVRLVMNAGEVVVASAARRFLHvlaPFGLPqd 1991
Cdd:cd05909    223 PL---DYKKIPELIYDKKATILLGtPTF-LRGYARAAHPE-----DFSSLRLVVAGAEKLKDTLRQEFQE---KFGIR-- 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1992 vMHPGWGMSETCSVVtdSVLASEAPDHDEafvSCGLPYPGFAMRVVDDQDAL-LPEGDVGRLQVRGTSVTHGYHDNARAN 2070
Cdd:cd05909    289 -ILEGYGTTECSPVI--SVNTPQSPNKEG---TVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELT 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2071 AESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGvNHYSHEIeacVEELPSVV--RSFTAAVAVRSDASAATDELA 2147
Cdd:cd05909    363 SFAF-GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAG-EMVSLEA---IEDILSEIlpEDNEVAVVSVPDGRKGEKIVL 437

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2148 LFLRLAPGQDPagaLREIAgkvtREIGVS----PAFLIPVeaEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05909    438 LTTTTDTDPSS---LNDIL----KNAGISnlakPSYIHQV--EEIPLLGTGKPDYVTLKA 488
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 467-966 2.12e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 116.63  E-value: 2.12e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  467 AESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLA 546
Cdd:PRK13383    46 ARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALA 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  547 LVMADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPhdltdadRAGATGpydtAYVIHTSGSTGRPKGVP- 625
Cdd:PRK13383   126 AALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRP-------AVAAPG----RIVLLTSGTTGKPKGVPr 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  626 ---VPHAHVVRLFEASGEHFRFGA--DDVWTLFHSYAFDFSVWELwgpLLHGGRLVVVPYEVSRSprefLRLLDEEKVTV 700
Cdd:PRK13383   195 apqLRSAVGVWVTILDRTRLRTGSriSVAMPMFHGLGLGMLMLTI---ALGGTVLTHRHFDAEAA----LAQASLHRADA 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  701 LNQTPSAFEQLV-LADAATDR-ATGSLRYVVLGGEALVAERLRPWADRHGldaPELVNMYGITETTVHVTfhrLVRADLE 778
Cdd:PRK13383   268 FTAVPVVLARILeLPPRVRARnPLPQLRVVMSSGDRLDPTLGQRFMDTYG---DILYNGYGSTEVGIGAL---ATPADLR 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 DPRRrgVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGpgvapgylnrpELTEERFLPDPFGAPGTRMYRSGDLARWRP 858
Cdd:PRK13383   342 DAPE--TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRYTDGGGKAVVDGMTSTGDMGYLDN 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPA 938
Cdd:PRK13383   409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSR 488

                          490       500
                   ....*....|....*....|....*...
gi 1573930569  939 YMVPAACVLLDALPLTANGKLDTAALPA 966
Cdd:PRK13383   489 FEQPRDINIVSSIPRNPTGKVLRKELPG 516
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 480-892 3.31e-26

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: 115.15  E-value: 3.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVT 559
Cdd:cd17640      4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  560 DTAGSgrlpatdarvvvvddartvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASG 639
Cdd:cd17640     84 ENDSD------------------------------------------DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLS 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  640 EHFRFGADDVWTLF----HSY--AFDFSVWeLWGpllhggrlVVVPYEvsrSPREFLRLLDEEKVTVLNQTPSAFEQL-- 711
Cdd:cd17640    122 DIVPPQPGDRFLSIlpiwHSYerSAEYFIF-ACG--------CSQAYT---SIRTLKDDLKRVKPHYIVSVPRLWESLys 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  712 -----VLADAATDRAT-------GSLRYVVLGGEALVaerlrPWADRH----GLdapELVNMYGITETTVHVTFHRLVRA 775
Cdd:cd17640    190 giqkqVSKSSPIKQFLflfflsgGIFKFGISGGGALP-----PHVDTFfeaiGI---EVLNGYGLTETSPVVSARRLKCN 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  776 dledprRRGVIGRPLADLRVYVLDAAGR-PVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLA 854
Cdd:cd17640    262 ------VRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLG 328

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1573930569  855 RWRPDGTLVHAGRA-DQQVKIRGFRIEPGEIEAVLTAHP 892
Cdd:cd17640    329 WLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSP 367
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 10-326 3.60e-26

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: 114.44  E-value: 3.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALR---------RTVreadtfalrFLDTPDGPRAV---R 77
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALAdvvarheslRTV---------FPEDDGGPYQVvlpA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   78 DGDPDEMPVHRVDVSGEADPaaaaeewIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLA 157
Cdd:cd19540     74 AEARPDLTVVDVTEDELAAR-------LAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLA 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  158 DTYTALAAGEEP--PPAGFESADrLAAEEAAYLGSDRH-----RRDRAYWTERLAGLPEPVRL-TDRTAPPRAPFL-RRT 228
Cdd:cd19540    147 TAYAARRAGRAPdwAPLPVQYAD-YALWQRELLGDEDDpdslaARQLAYWRETLAGLPEELELpTDRPRPAVASYRgGTV 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  229 AVLSPAET-RALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRlGSAAL-RTPGTASDILPLRVAASADT 306
Cdd:cd19540    226 EFTIDAELhARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR-GDEALdDLVGMFVNTLVLRTDVSGDP 304

                          330       340
                   ....*....|....*....|
gi 1573930569  307 PVGGFVRAVADDLRGLRAHQ 326
Cdd:cd19540    305 TFAELLARVRETDLAAFAHQ 324
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1072-2201 4.46e-26

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 118.22  E-value: 4.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1072 VPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLrPELH 1151
Cdd:PRK10252     8 LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTF-PLPE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1152 VVDCPDEERAAHVAAA-----MRRSFDLTRDSALWAGV-FGTGDTRTLL-LVLHHSAADGWSLRPLADDLGTAYAARRAG 1224
Cdd:PRK10252    87 IIDLRTQPDPHAAAQAlmqadLQQDLRVDSGKPLVFHQlIQLGDNRWYWyQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1225 AAPD---WAPPALQYADFALWQrrvlapapEGPGRlERLTSFWRQALDGLPEESAPPPDRPRPAAPSGRGGGVTVPLDAG 1301
Cdd:PRK10252   167 EPTPaspFTPFADVVEEYQRYR--------ASEAW-QRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1302 THRELLRLADheNASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPALDEVVGLLTNTLVLRADASGDPTFRELLAR 1381
Cdd:PRK10252   238 AFRQLAAQAS--GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1382 VRAFDVQALDHQDLPFDRLVEEVNprRHPARHPLFQVMLALQNNERAvLTLGEDRVPLRPAATGTAK---FDLFVDVler 1458
Cdd:PRK10252   316 LAAQLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQ-LDFPGVQAQTHTLATGPVNdleLALFPDE--- 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1459 hgadgtADGLDLHVEYAADLYDPATAERFAGALRDLLTVVCADPEVRTGALPRAdrpSPATADTTARAGaltravlevpg 1538
Cdd:PRK10252   390 ------HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDIL---LPGEYAQLAQVN----------- 449

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1539 vgdavvlpgpdgepATVYVVPnragaadrtEQVVSSLapgtrvvaisglprtaeggLDEGALKDlpvidqvaagawrerl 1618
Cdd:PRK10252   450 --------------ATAVEIP---------ETTLSAL-------------------VAQQAAKT---------------- 471

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1619 arlpgvreaevvleevpeelerrhvgrpraaggaaePDAPSverpasvpalsegpalpepsvsgwaealLRAAGRpdgev 1698
Cdd:PRK10252   472 ------------------------------------PDAPA----------------------------LADARY----- 482

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1699 vhvradgsetRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpVSYATTSAAVs 1778
Cdd:PRK10252   483 ----------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD--TGYPDDRLKM- 549

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1779 klegiweMLD--RPWIVTSAAgepglrELAAR-REWSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAV 1855
Cdd:PRK10252   550 -------MLEdaRPSLLITTA------DQLPRfADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGV 616

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1856 RLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLrDVYLGCRQIHAPTSwILEDPVRWPELADRHRVSVT- 1934
Cdd:PRK10252   617 MVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFW-PFIAGAKLVMAEPE-AHRDPLAMQQFFAEYGVTTTh 694

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1935 WAPNFAFGLLAEQAHrfQDRDWDLSPVRLVMNAGEVVVASAARRF-------LHVL-APFGLPQDVM-HPGWGmSETCSV 2005
Cdd:PRK10252   695 FVPSMLAAFVASLTP--EGARQSCASLRQVFCSGEALPADLCREWqqltgapLHNLyGPTEAAVDVSwYPAFG-EELAAV 771

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2006 VTDSvlaseapdhdeafVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW------ 2079
Cdd:PRK10252   772 RGSS-------------VPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgerm 838

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2080 FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAVRSDASAATDELALFLRLAPGQD- 2157
Cdd:PRK10252   839 YRTGDVArWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARQLVGYLVSQSGl 918

                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2158 --PAGALRE-IAGKVtreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:PRK10252   919 plDTSALQAqLRERL-------PPHMVPvvlLQLDQLPLSANGKLDRKAL 961
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 2284-2700 5.29e-26

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 114.29  E-value: 5.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2284 VTEGPAPERNGAAAYRVRPGEAGDLAAVLERLEADGRTPDTVVHLAATEDAEDGAAPGSDVSLLVLAQA---LA-GRTGG 2359
Cdd:cd08956     15 AAAPPDWALLGLAAAGAAGAAHADLDALAAALAAGAAVPDVVVVPCPAAAGGDLAAAAHAAAARALALLqawLAdPRLAD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2360 ERpvdLLFVTAGAQAVTPEERPTA-SHAAAGALLKSLREELPwLRGVHLDLSGGSAGDRAAAVLAEAagfpADTEVARRE 2438
Cdd:cd08956     95 SR---LVVVTRGAVAAGPDEDVPDlAAAAVWGLVRSAQAEHP-GRFVLVDLDDDAASAAALPAALAS----GEPQLALRD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2439 GLRYVRRLAPL-PDSAPRTAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTR-LLLIGRTGlppedtwerhladagPA 2516
Cdd:cd08956    167 GRLLVPRLARVaPAATLPPVPRPLDPDGTVLITGGTGTLGALLARHLVTEHGVRhLLLVSRRG---------------PD 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2517 SSRIEAFRR-LRGLG-EVRYETADVTDAAQVRAAVRRAADAWgvPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGA 2594
Cdd:cd08956    232 APGAAELVAeLAALGaEVTVAACDVADRAALAALLAAVPADH--PLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAA 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2595 WALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLAWSMWRERGMsLGYQLTSLTEAR 2674
Cdd:cd08956    310 WHLHELTRDLDLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLPATSLAWGLWAQASG-MTAHLSDADLAR 388

                          410       420       430
                   ....*....|....*....|....*....|
gi 1573930569 2675 ----GYRVLDAQAALRSFDLARTLDLPHLL 2700
Cdd:cd08956    389 largGLRPLSAEEGLALFDAALAADEPVLV 418
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1716-2202 5.50e-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: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 114.07  E-value: 5.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1716 VPEASRVLAG-LRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvPVSYATTSaavsklegiwemldrpwivt 1794
Cdd:cd05971     12 LKTASNRFANvLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL--FALFGPEA-------------------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1795 saagepglreLAARREWSGLRLTTADAlreepedrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNG 1874
Cdd:cd05971     70 ----------LEYRLSNSGASALVTDG--------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFN 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1875 LGSGDVSLNWIPLDH--VTGVVMFHLRDVYLGCRQI-HAPTSWileDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHrf 1951
Cdd:cd05971    126 LFPRDGDLYWTPADWawIGGLLDVLLPSLYFGVPVLaHRMTKF---DPKAALDLMSRYGVTTAFLPPTALKMMRQQGE-- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1952 QDRDWDLSpVRLVMNAGEvvvaSAARRFLH-VLAPFGLPqdvMHPGWGMSETCSVVTD-SVLASEAPDhdeafvSCGLPY 2029
Cdd:cd05971    201 QLKHAQVK-LRAIATGGE----SLGEELLGwAREQFGVE---VNEFYGQTECNLVIGNcSALFPIKPG------SMGKPI 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2030 PGFAMRVVDDQDALLPEGDVGRLQVR-GTSVTH-GYHDNARANAESFTEDgWFDTGDLAFL-RDGELYITGRAKDVIIVN 2106
Cdd:cd05971    267 PGHRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDDDVITSS 345

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2107 GVNHYSHEIEACVEELPSVVrsfTAAVAVRSDAsAATDELALFLRLAPGQDPAGAL-REIAGKVTREIGvspAFLIPVEA 2185
Cdd:cd05971    346 GYRIGPAEIEECLLKHPAVL---MAAVVGIPDP-IRGEIVKAFVVLNPGETPSDALaREIQELVKTRLA---AHEYPREI 418

                          490       500
                   ....*....|....*....|
gi 1573930569 2186 EAI---PKTEIGKIQRTKLR 2202
Cdd:cd05971    419 EFVnelPRTATGKIRRRELR 438
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1836-2202 6.15e-26

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 115.54  E-value: 6.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLT-----RAAATEAMNGlgSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIha 1910
Cdd:PRK08974   205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqaKAAYGPLLHP--GKELVVTALPLYHIFALTVNCLLFIELGGQNL-- 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 ptswILEDPVRWP----ELAdRHRVSVTWAPNFAFGLLA--EQAHRFqdrdwDLSPVRLVMNAGEVVVASAARRF----- 1979
Cdd:PRK08974   281 ----LITNPRDIPgfvkELK-KYPFTAITGVNTLFNALLnnEEFQEL-----DFSSLKLSVGGGMAVQQAVAERWvkltg 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1980 LHVLApfglpqdvmhpGWGMSEtCSvvtdSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSV 2059
Cdd:PRK08974   351 QYLLE-----------GYGLTE-CS----PLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2060 THGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSD 2138
Cdd:PRK08974   415 MLGYWQRPEATDEVI-KDGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV--AAVGVPSE 491

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2139 ASAAT--------------DELALFLRlapgqdpagalREIAG-KVTREIgvspAFlipveAEAIPKTEIGKIQRTKLR 2202
Cdd:PRK08974   492 VSGEAvkifvvkkdpslteEELITHCR-----------RHLTGyKVPKLV----EF-----RDELPKSNVGKILRRELR 550
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 2223-2701 6.26e-26

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 114.58  E-value: 6.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2223 TAATVPDWFLHPLWRPAENLHAATLpAGHRVLVLagPAPHAHAVAEEVAGAVRDAGGLCTVVTEGPAPERNGAAAYRVRP 2302
Cdd:cd08952      7 ERAAVDSWRYRVTWRPLPDPPAARL-TGTWLVVV--PAGADDALAAAVARALAAAGAEVVVLEVDAADADAAAAAALAAA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2303 GEAGDLAAVLERLEADGRTpdtvvhlaateDAEDGAAPGSDVSLLVLAQALaGRTGGERPvdLLFVTAGAQAVTPEERPT 2382
Cdd:cd08952     84 AAGGPVAGVLSLLALDERP-----------HPDHPAVPAGLAATLALVQAL-GDAGVDAP--LWCVTRGAVAVGPDDPLP 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2383 A-SHAAAGALLKSLREELPWLRGVHLDLSGGSAGDRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDSAPRTAPAPA 2461
Cdd:cd08952    150 DpAQAAVWGLGRVAALEHPDRWGGLVDLPADLDARALRRLAAVLAGAGGEDQVAVRASGVFARRLVRAPAPAPAARPWRP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2462 P-------ADGfhlvsgglgGVGSEVAAHLLKEPGTRLLLIGRTGlpPEDTWERHLADAgpassrieafrrLRGLG-EVR 2533
Cdd:cd08952    230 RgtvlvtgGTG---------ALGAHVARWLARRGAEHLVLTSRRG--PDAPGAAELVAE------------LTALGaRVT 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2534 YETADVTDAAQVRAAVRRAADawGVPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFS 2613
Cdd:cd08952    287 VAACDVADRDALAALLAALPA--GHPLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFS 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2614 SVNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLAWSMWRERGMSLGYQLTSLtEARGYRVLDAQAALRSFDLART 2693
Cdd:cd08952    365 SIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAWGPWAGGGMAAGAAAERL-RRRGLRPMDPELALAALRRALD 443


                   ....*...
gi 1573930569 2694 LDLPHLLI 2701
Cdd:cd08952    444 HDETAVVV 451
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1837-2202 6.90e-26

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 115.69  E-value: 6.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEA-MNGLGSG---------DVSLNWIPLDHV---TGVVMfhlrdvyl 1903
Cdd:PRK12492   207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRAcLSQLGPDgqplmkegqEVMIAPLPLYHIyafTANCM-------- 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1904 gCRQIHAPTSWILEDPVRWP----ELAdRHRVSVTWAPNFAFGLLAEQAhrfQDRDWDLSPVRLVMNAGEVVVASAARRF 1979
Cdd:PRK12492   279 -CMMVSGNHNVLITNPRDIPgfikELG-KWRFSALLGLNTLFVALMDHP---GFKDLDFSALKLTNSGGTALVKATAERW 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1980 LHVLAPfglpqdVMHPGWGMSETcsvvtdSVLASEAPDHDEAFV-SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTS 2058
Cdd:PRK12492   354 EQLTGC------TIVEGYGLTET------SPVASTNPYGELARLgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQ 421

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2059 VTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRS 2137
Cdd:PRK12492   422 VMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVAN--CAAIGVPD 499

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2138 DASAATDELALFLRlapgqDPAGALREI---------AGKVTREIgvspaflipVEAEAIPKTEIGKIQRTKLR 2202
Cdd:PRK12492   500 ERSGEAVKLFVVAR-----DPGLSVEELkayckenftGYKVPKHI---------VLRDSLPMTPVGKILRRELR 559
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1707-2203 7.43e-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: 114.32  E-value: 7.43e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIWEM 1786
Cdd:cd12118     27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1787 LDRPWIVTS--AAGEPGLRELAARREWsglrlttadalreepedrdwyearpdDLVLMLMTSGSTGLPKAVRLTHRNVLT 1864
Cdd:cd12118    107 VDREFEYEDllAEGDPDFEWIPPADEW--------------------------DPIALNYTSGTTGRPKGVVYHHRGAYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1865 RAAATEAMNGLGSGDVSLNWIPLDHVTG----VVMFHLRDVYLGCRQIHAPTSWiledpvrwpELADRHRVSVTWAPNFA 1940
Cdd:cd12118    161 NALANILEWEMKQHPVYLWTLPMFHCNGwcfpWTVAAVGGTNVCLRKVDAKAIY---------DLIEKHKVTHFCGAPTV 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1941 FGLLAEQAHRFQDR-DWdlsPVRlVMNAGevvvASAARRFLHVLAPFGLpqDVMHpGWGMSETCSVVTDSVLASE---AP 2016
Cdd:cd12118    232 LNMLANAPPSDARPlPH---RVH-VMTAG----APPPAAVLAKMEELGF--DVTH-VYGLTETYGPATVCAWKPEwdeLP 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2017 DHDEAFVSC--GLPYPGF-AMRVVDDQDALLPEGD---VGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFLR- 2089
Cdd:cd12118    301 TEERARLKArqGVRYVGLeEVDVLDPETMKPVPRDgktIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHp 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2090 DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELAlFLRLAPGQDPAGAlrEIAgKV 2169
Cdd:cd12118    380 DGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLE---AAVVARPDEKWGEVPCA-FVELKEGAKVTEE--EII-AF 452

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1573930569 2170 TREigVSPAFLIP--VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd12118    453 CRE--HLAGFMVPktVVFGELPKTSTGKIQKFVLRD 486
PRK09274 PRK09274
peptide synthase; Provisional
 456-900 8.02e-26

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 115.00  E-value: 8.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLfeARvaESPGRTAV----------SYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLA 525
Cdd:PRK09274    10 RHLPRA--AQ--ERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  526 VLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTAGS------GRLPATDARVVVVDD-----ARTVADL-AGRAPHD 593
Cdd:PRK09274    86 LFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHlarrlfGWGKPSVRRLVTVGGrllwgGTTLATLlRDGAAAP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  594 LTDADragaTGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVwtlfhsyafD---FSVWELWGPLL 670
Cdd:PRK09274   166 FPMAD----LAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI---------DlptFPLFALFGPAL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  671 hGGRLVVVPYEVSR----SPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGG---EALVAERLRPW 743
Cdd:PRK09274   233 -GMTSVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGapvPIAVIERFRAM 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  744 ADrhglDAPELVNMYGITE----TTVHvtfhrlVRADLEDPRRR-----GV-IGRPLADLRVYVLD---------AAGRP 804
Cdd:PRK09274   312 LP----PDAEILTPYGATEalpiSSIE------SREILFATRAAtdngaGIcVGRPVDGVEVRIIAisdapipewDDALR 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  805 VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMyrsGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEI 884
Cdd:PRK09274   382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRM---GDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPC 458

                          490
                   ....*....|....*.
gi 1573930569  885 EAVLTAHPAVAGGAVV 900
Cdd:PRK09274   459 ERIFNTHPGVKRSALV 474
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 1705-2120 8.46e-26

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: 113.99  E-value: 8.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1705 GSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPltvpvsyATTSAAVSKLEgiw 1784
Cdd:cd17640      1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV-------RGSDSSVEELL--- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1785 emldrpWIVTSAagepglrelaarrEWSGLRLttadalreepedrdwyEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLT 1864
Cdd:cd17640     71 ------YILNHS-------------ESVALVV----------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLH 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1865 RAAATEAMNGLGSGDVSLNWIPLDHvtgvvMFHLRDVYL----GCRQIHAPTSWILEDPVRW-PELAdrhrVSVtwaPNF 1939
Cdd:cd17640    116 QIRSLSDIVPPQPGDRFLSILPIWH-----SYERSAEYFifacGCSQAYTSIRTLKDDLKRVkPHYI----VSV---PRL 183

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1940 AFGLLAeqahRFQDRDWDLSPVR-------LVMNAGEVVVASAARRFLHVLAPF---GLPQDVmhpGWGMSETCSVVTds 2009
Cdd:cd17640    184 WESLYS----GIQKQVSKSSPIKqflflffLSGGIFKFGISGGGALPPHVDTFFeaiGIEVLN---GYGLTETSPVVS-- 254

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2010 vlaseAPDHDEAFV-SCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAF 2087
Cdd:cd17640    255 -----ARRLKCNVRgSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGW 329

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1573930569 2088 L-RDGELYITGRAKDVIIV-NGVNHYSHEIE-ACVE 2120
Cdd:cd17640    330 LtCGGELVLTGRAKDTIVLsNGENVEPQPIEeALMR 365
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 10-423 9.01e-26

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: 112.94  E-value: 9.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDgpravrDGDP-----DEM 84
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPE------DGEPmqgvlASS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   85 PVH--RVDVSGEADPAAAAeewirRDLATPV-DVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYt 161
Cdd:cd19532     77 PLRleHVQISDEAEVEEEF-----ERLKNHVyDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  162 alaAGEEPPPAGFESADrLAAEEAAYLGSDRHRRDRAYWTERLAGLPEPV------RLTDRTAPPRAPFLRRTAVLSPAE 235
Cdd:cd19532    151 ---NGQPLLPPPLQYLD-FAARQRQDYESGALDEDLAYWKSEFSTLPEPLpllpfaKVKSRPPLTRYDTHTAERRLDAAL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  236 TRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRVAASADTPVGGFVRAV 315
Cdd:cd19532    227 AARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKET 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  316 ADDLRGLRAHQRHRGESIRRDLGVlgrgRR--VHGP----VVN-IVPFSEDLTFGGHPSTSHHLSGGAVD-DLQISVRPG 387
Cdd:cd19532    307 RDKAYAALAHSRVPFDVLLDELGV----PRsaTHSPlfqvFINyRQGVAESRPFGDCELEGEEFEDARTPyDLSLDIIDN 382

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1573930569  388 AEADTLwLAFDAHPDLYEEDGLALFLERFLKVLREL 423
Cdd:cd19532    383 PDGDCL-LTLKVQSSLYSEEDAELLLDSYVNLLEAF 417
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 607-959 1.66e-25

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: 110.28  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHSYAFDFSVwelWGPLLHGGrlVVVPYEV 682
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDryliINPFFHTFGYKAGI---VACLLTGA--TVVPVAV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  683 SrSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDApeLVNMYGITE 762
Cdd:cd17638     76 F-DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFET--VLTAYGLTE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  763 TTVhVTfhrLVRADLEDPRRRGVIGRPLADLRVYVLDAagrpvppgatGEMYVSGPGVAPGYLNRPELTEERFLPDPFga 842
Cdd:cd17638    153 AGV-AT---MCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW-- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  843 pgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGltqlVAYAVPA 918
Cdd:cd17638    217 -----LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgvpdERMGEVG----KAFVVAR 287

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1573930569  919 EEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:cd17638    288 PGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1711-2201 2.69e-25

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: 112.75  E-value: 2.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVpvsyaTTSAAvsKLEGIWEMLDRP 1790
Cdd:cd12114     14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI-----DQPAA--RREAILADAGAR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTsaagepgLRELAARREWSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd12114     87 LVLT-------DGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGVVmfhlrDVYLGCR---QIHAPTSWILEDPVRWPELADRHRVSVtWapNFA---FGLL 1944
Cdd:cd12114    160 RRFAVGPDDRVLALSSLSFDLSVY-----DIFGALSagaTLVLPDEARRRDPAHWAELIERHGVTL-W--NSVpalLEML 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1945 AEQAHRFQDRdwdLSPVRLVMNAGEVVVASAARRfLHVLAPFGlpqDVMHPGwGMSETCsvVTDSVLASEAPDHDEAFVS 2024
Cdd:cd12114    232 LDVLEAAQAL---LPSLRLVLLSGDWIPLDLPAR-LRALAPDA---RLISLG-GATEAS--IWSIYHPIDEVPPDWRSIP 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2025 CGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG----WFDTGDLAFLR-DGELYITGRA 2099
Cdd:cd12114    302 YGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRpDGTLEFLGRR 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2100 KDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATdeLALFLRLAPGQDPAG--ALREIAGKVTREIGVSP 2177
Cdd:cd12114    382 DGQVKVRGYRIELGEIEAALQAHPGVAR---AVVVVLGDPGGKR--LAAFVVPDNDGTPIApdALRAFLAQTLPAYMIPS 456

                          490       500
                   ....*....|....*....|....
gi 1573930569 2178 AFLIpveAEAIPKTEIGKIQRTKL 2201
Cdd:cd12114    457 RVIA---LEALPLTANGKVDRAAL 477
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 2479-2658 5.10e-25

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 104.49  E-value: 5.10e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  2479 EVAAHLLKEPGTRLLLIGRTGLPPEDTWErhladagpassrieAFRRLRGLG-EVRYETADVTDAAQVRAAVRRAADAWG 2557
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAA--------------LLAELEAAGaRVTVVACDVADRDALAAVLAAIPAVEG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  2558 vPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDL 2637
Cdd:smart00822   81 -PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDAL 159

                           170       180
                    ....*....|....*....|.
gi 1573930569  2638 ALRRRREGLPGQSLAWSMWRE 2658
Cdd:smart00822  160 AEYRRARGLPALSIAWGAWAE 180
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1707-2202 6.61e-25

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: 110.65  E-value: 6.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRR-GLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV---PLTVPVSYAttsaavskleg 1782
Cdd:cd05958      8 EREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVatmPLLRPKELA----------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1783 iwEMLDRPWIVTSAAGEpglrelaarrewsglRLTTADalreepedrdwyearpdDLVLMLMTSGSTGLPKAVRLTHRNV 1862
Cdd:cd05958     77 --YILDKARITVALCAH---------------ALTASD-----------------DICILAFTSGTTGAPKATMHFHRDP 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1863 LTrAAATEAMNGLG--SGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSwileDPVRWPELADRHRVSVTW-APNF 1939
Cdd:cd05958    123 LA-SADRYAVNVLRlrEDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIARYKPTVLFtAPTA 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1940 ---AFGLLAEQAHrfqdrdwDLSPVRLVMNAGEVVVASAARRFLHVlapFGLPqdvMHPGWGMSETCSVvtdsvLASEAP 2016
Cdd:cd05958    198 yraMLAHPDAAGP-------DLSSLRKCVSAGEALPAALHRAWKEA---TGIP---IIDGIGSTEMFHI-----FISARP 259

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2017 DHDEAFVScGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSvthGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYI 2095
Cdd:cd05958    260 GDARPGAT-GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDpDGYFRH 335

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2096 TGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRSDASAATdeLALFLRLAPGQDPAGAL-REIAGKVTREIG 2174
Cdd:cd05958    336 QGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE--CAVVGHPDESRGVV--VKAFVVLRPGVIPGPVLaRELQDHAKAHIA 411

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569 2175 vspAFLIPVEAE---AIPKTEIGKIQRTKLR 2202
Cdd:cd05958    412 ---PYKYPRAIEfvtELPRTATGKLQRFALR 439
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1685-2202 6.74e-25

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 112.21  E-value: 6.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGR-PDGEVVHVRADGseTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGfvAVP 1763
Cdd:PRK08315    20 QLLDRTAARyPDREALVYRDQG--LRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIG--AIL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 LTV-P------VSYATTSAAVSKL---EGIW-----EMLD--RPWIVTSAAGE------PGLRE---LAARR-----EWS 1812
Cdd:PRK08315    96 VTInPayrlseLEYALNQSGCKALiaaDGFKdsdyvAMLYelAPELATCEPGQlqsarlPELRRvifLGDEKhpgmlNFD 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1813 GLRLTTADAlreepeDRDWYEAR-----PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAA-ATEAMNgLGSGD-----Vs 1881
Cdd:PRK08315   176 ELLALGRAV------DDAELAARqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYfIGEAMK-LTEEDrlcipV- 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1882 lnwiPLDHVTGVVMFHLRDVYLGCRQIhaptsWILE--DPVRWPELADRHRVSvtwapnfafGL-------LAEQAH-RF 1951
Cdd:PRK08315   248 ----PLYHCFGMVLGNLACVTHGATMV-----YPGEgfDPLATLAAVEEERCT---------ALygvptmfIAELDHpDF 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1952 QDrdWDLSPVRL-VMnAGEVVVASAARRFlhvlapfglpQDVMHP-----GWGMSETCSVVTdsvlASEAPDHDEAFVS- 2024
Cdd:PRK08315   310 AR--FDLSSLRTgIM-AGSPCPIEVMKRV----------IDKMHMsevtiAYGMTETSPVST----QTRTDDPLEKRVTt 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2025 CGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYITGRAKDV 2102
Cdd:PRK08315   373 VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDeEGYVNIVGRIKDM 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2103 IIVNGVNHYSHEIE-----------ACV---------EELpsvvrsfTAAVAVRSDASAATDELALFLRlapGQdpagal 2162
Cdd:PRK08315   453 IIRGGENIYPREIEeflythpkiqdVQVvgvpdekygEEV-------CAWIILRPGATLTEEDVRDFCR---GK------ 516

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1573930569 2163 reIAG-KVTREIGVSPAFlipveaeaiPKTEIGKIQRTKLR 2202
Cdd:PRK08315   517 --IAHyKIPRYIRFVDEF---------PMTVTGKIQKFKMR 546
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 1694-2213 7.54e-25

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 112.15  E-value: 7.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1694 PDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVlgGFVAVPLTV-P----- 1767
Cdd:PRK06018    24 GNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIM--GIGAICHTVnPrlfpe 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1768 -----VSYATTSAA------VSKLEGIWEML---DRPWIVTSAAGEPG--LRELAARREWsglrlttadaLREEPEDRDW 1831
Cdd:PRK06018   102 qiawiINHAEDRVVitdltfVPILEKIADKLpsvERYVVLTDAAHMPQttLKNAVAYEEW----------IAEADGDFAW 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHR-NVLTRAAAT--EAMnGLGSGDVSLNWIPLDHVT--GVVM----FHLRDVY 1902
Cdd:PRK06018   172 KTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLHALMANngDAL-GTSAADTMLPVVPLFHANswGIAFsapsMGTKLVM 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1903 LGCRQihaptswileDPVRWPELADRHRVSVTWA-PNFAFGLLaeqaHRFQDRDWDLSPVRLVMNAGevvvASAARRFLH 1981
Cdd:PRK06018   251 PGAKL----------DGASVYELLDTEKVTFTAGvPTVWLMLL----QYMEKEGLKLPHLKMVVCGG----SAMPRSMIK 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1982 VLAPFGLpqDVMHpGWGMSETCSVVTDSVLA---SEAPDHDEAFVSCGLPYPGFA--MRVVDDQDALLP-EGDV-GRLQV 2054
Cdd:PRK06018   313 AFEDMGV--EVRH-AWGMTEMSPLGTLAALKppfSKLPGDARLDVLQKQGYPPFGveMKITDDAGKELPwDGKTfGRLKV 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2055 RGTSVTHGYHdnaRANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAV 2133
Cdd:PRK06018   390 RGPAVAAAYY---RVDGEILDDDGFFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKV-----AEA 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2134 AVRSDASAATDELALFL-RLAPGQDPAGA--LREIAGKVTReigvspaFLIP---VEAEAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:PRK06018   462 AVIGVYHPKWDERPLLIvQLKPGETATREeiLKYMDGKIAK-------WWMPddvAFVDAIPHTATGKILKTALREQFKD 534


                   ....*.
gi 1573930569 2208 GEFDGA 2213
Cdd:PRK06018   535 YKLPTA 540
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1689-2203 1.05e-24

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 110.82  E-value: 1.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDgEVVHVRADGSETrrsYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVpv 1768
Cdd:PRK03640    11 RAFLTPD-RTAIEFEEKKVT---FMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 syattsaAVSKLEGIWEMLDRPwiVTSAAGEPGLrelaARREWSGLRLTTADALREEPEDRDWYEARPDDLVLMLM-TSG 1847
Cdd:PRK03640    85 -------RLSREELLWQLDDAE--VKCLITDDDF----EAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMyTSG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1848 STGLPKAVRLTHRNVLTRAAATeAMN-GLGSGDVSLNWIPLDHVTGV-VMFhlRDVYLGCR-------QIHAPTSWILED 1918
Cdd:PRK03640   152 TTGKPKGVIQTYGNHWWSAVGS-ALNlGLTEDDCWLAAVPIFHISGLsILM--RSVIYGMRvvlvekfDAEKINKLLQTG 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1919 PVRwpeladrhRVSVTwaPNFAFGLLAE-QAHRFQDRdwdlspVRLVMNAGevvvASAARRFLHVLAPFGLPqdvMHPGW 1997
Cdd:PRK03640   229 GVT--------IISVV--STMLQRLLERlGEGTYPSS------FRCMLLGG----GPAPKPLLEQCKEKGIP---VYQSY 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1998 GMSETCS-VVTdsvLASEapDHDEAFVSCGLPYPGFAMRVVDDQDALlPEGDVGRLQVRGTSVTHGYHDNARANAESFtE 2076
Cdd:PRK03640   286 GMTETASqIVT---LSPE--DALTKLGSAGKPLFPCELKIEKDGVVV-PPFEEGEIVVKGPNVTKGYLNREDATRETF-Q 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2077 DGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVA--------------VRSDASA 2141
Cdd:PRK03640   359 DGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAE---AGVVgvpddkwgqvpvafVVKSGEV 435

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2142 ATDELALFLRlapgqdpagalREIAG-KVTREIgvspaflipVEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK03640   436 TEEELRHFCE-----------EKLAKyKVPKRF---------YFVEELPRNASGKLLRHELKQ 478
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1836-2204 1.10e-24

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 111.89  E-value: 1.10e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRN-VLTRAAATEAMNGLGS----GDVSLNWIPLDHVTGVVMFHLrdVYL---GCRQ 1907
Cdd:PRK08751   207 PDDIAFLQYTGGTTGVAKGAMLTHRNlVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANGL--VFMkigGCNH 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 IhaptswiLEDPVRWP----ELaDRHRVSVTWAPNFAF-GLLAEQAHRfqdrDWDLSPVRLVMNAGEVVVASAARRFLHV 1982
Cdd:PRK08751   285 L-------ISNPRDMPgfvkEL-KKTRFTAFTGVNTLFnGLLNTPGFD----QIDFSSLKMTLGGGMAVQRSVAERWKQV 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1983 LapfGLPqdvMHPGWGMSETcsvvtdSVLASEAP-DHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTH 2061
Cdd:PRK08751   353 T---GLT---LVEAYGLTET------SPAACINPlTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMK 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2062 GYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRSDAS 2140
Cdd:PRK08751   421 GYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE--VAAVGVPDEKS 498

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2141 AATDELALFlrlapGQDPAGALREI-AGKVTREIGVSPAFLIPVEAEaIPKTEIGKIQRTKLRKS 2204
Cdd:PRK08751   499 GEIVKVVIV-----KKDPALTAEDVkAHARANLTGYKQPRIIEFRKE-LPKTNVGKILRRELRDA 557
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 445-939 2.81e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 110.91  E-value: 2.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  445 VRRDEPAPRVTRTLPQLFEARVAESPG------RTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPR 518
Cdd:PRK12582    38 IKSRHPLGPYPRSIPHLLAKWAAEAPDrpwlaqREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIE 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  519 LVPALLAVLKTGAAYLPLDPG-----HPAERLALVMADAEPVAVVTD-----TAGSGRLPATDARVVVVD------DART 582
Cdd:PRK12582   118 HALMTLAAMQAGVPAAPVSPAyslmsHDHAKLKHLFDLVKPRVVFAQsgapfARALAALDLLDVTVVHVTgpgegiASIA 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  583 VADLAGRAPHDLTDADRAgATGPYDTAYVIHTSGSTGRPKGVPVPHAHV---------VRLFEASGEHfrfgADDV-WTL 652
Cdd:PRK12582   198 FADLAATPPTAAVAAAIA-AITPDTVAKYLFTSGSTGMPKAVINTQRMMcaniamqeqLRPREPDPPP----PVSLdWMP 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  653 FH-----SYAFDFSVWElwGPLLH--GGRLVvvpyevsrsPREF---LRLLDEEKVTVLNQTPSAFEQLVLA---DAATD 719
Cdd:PRK12582   273 WNhtmggNANFNGLLWG--GGTLYidDGKPL---------PGMFeetIRNLREISPTVYGNVPAGYAMLAEAmekDDALR 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  720 RATGS-LRYVVLGGEAL---VAERLRPWADRHGLDAPELVNMYGITETT-VHVTFHRlvradleDPRRRGVIGRPLADLR 794
Cdd:PRK12582   342 RSFFKnLRLMAYGGATLsddLYERMQALAVRTTGHRIPFYTGYGATETApTTTGTHW-------DTERVGLIGLPLPGVE 414

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  795 VYVldaagrpVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARW----RPDGTLVHAGRADQ 870
Cdd:PRK12582   415 LKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARFvdpdDPEKGLIFDGRVAE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  871 QVKI-RGFRIEPGEIEA-VLTAHPAVAGGAVVprAAED-------------GLTQLVAYAVPAEEGGADPAGLRAHLAAR 935
Cdd:PRK12582   481 DFKLsTGTWVSVGTLRPdAVAACSPVIHDAVV--AGQDrafigllawpnpaACRQLAGDPDAAPEDVVKHPAVLAILREG 558


                   ....
gi 1573930569  936 LPAY 939
Cdd:PRK12582   559 LSAH 562
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 456-959 3.45e-24

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 110.11  E-value: 3.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:PRK07059    23 PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLA--LVMADAEPVAVVTDTAGSGR--LPATDARVVVVddaRTVADLAG--------------------RAP 591
Cdd:PRK07059   103 VNPLYTPRELEhqLKDSGAEAIVVLENFATTVQqvLAKTAVKHVVV---ASMGDLLGfkghivnfvvrrvkkmvpawSLP 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  592 HDLT--DADRAGA--------TGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASG-----EHFRFGADDVWT----- 651
Cdd:PRK07059   180 GHVRfnDALAEGArqtfkpvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpAFEKKPRPDQLNfvcal 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  652 -LFHSYAFdfSVWELWGpLLHGGRLVVVPyevsrSPRE---FLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRY 727
Cdd:PRK07059   260 pLYHIFAL--TVCGLLG-MRTGGRNILIP-----NPRDipgFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIV 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  728 VVLGGEAL---VAERlrpWADRHGldAPeLVNMYGITETTVHVTFHRLVRADLEdprrrGVIGRPLADLRVYVLDAAGRP 804
Cdd:PRK07059   332 ANGGGMAVqrpVAER---WLEMTG--CP-ITEGYGLSETSPVATCNPVDATEFS-----GTIGLPLPSTEVSIRDDDGND 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  805 VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEI 884
Cdd:PRK07059   401 LPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEI 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  885 EAVLTAHPAVAGGAVVpraaedgltqlvayAVPAEEGG---------ADP----AGLRAHLAARLPAYMVPAACVLLDAL 951
Cdd:PRK07059   474 EEVVASHPGVLEVAAV--------------GVPDEHSGeavklfvvkKDPalteEDVKAFCKERLTNYKRPKFVEFRTEL 539


                   ....*...
gi 1573930569  952 PLTANGKL 959
Cdd:PRK07059   540 PKTNVGKI 547
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 1711-2203 3.94e-24

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: 109.54  E-value: 3.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVS--YATTSAAVSKLEGIW---E 1785
Cdd:cd17642     46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNerELDHSLNISKPTIVFcskK 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1786 MLDRpwIVTSAAGEP---GLRELAARREWSGLRLTTADALREEPEDRDWYEARP------DDLVLMLMTSGSTGLPKAVR 1856
Cdd:cd17642    126 GLQK--VLNVQKKLKiikTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPpsfdrdEQVALIMNSSGSTGLPKGVQ 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1857 LTHRNVLTR---AAATEAMNGLGSGDVSLNWIPLDHVTGvvMFHLRDvYLGC--RQIHAPTswiLEDPVRWPELADRHRV 1931
Cdd:cd17642    204 LTHKNIVARfshARDPIFGNQIIPDTAILTVIPFHHGFG--MFTTLG-YLICgfRVVLMYK---FEEELFLRSLQDYKVQ 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1932 SVTWAPNFaFGLLAEqaHRFQDRdWDLSPVRLVMNAG-----EVVVASAARrflhvlapFGLPqdVMHPGWGMSETcsvv 2006
Cdd:cd17642    278 SALLVPTL-FAFFAK--STLVDK-YDLSNLHEIASGGaplskEVGEAVAKR--------FKLP--GIRQGYGLTET---- 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2007 TDSVLASeaPDHDEAFVSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDL 2085
Cdd:cd17642    340 TSAILIT--PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDI 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2086 AFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsFTAAVAVRSDASAatdelalflrlapGQDPAGALRE 2164
Cdd:cd17642    418 AYYdEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKI---FDAGVAGIPDEDA-------------GELPAAVVVL 481

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2165 IAGKVTRE--------IGVSPA--------FLipveaEAIPKTEIGKIQRTKLRK 2203
Cdd:cd17642    482 EAGKTMTEkevmdyvaSQVSTAkrlrggvkFV-----DEVPKGLTGKIDRRKIRE 531
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 456-959 4.25e-24

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 109.91  E-value: 4.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYL 534
Cdd:PRK12492    24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PLDPGHPAERLALVMADAEPVAVV-------------TDTA--------GSGRLPATDARVV--VVDDARTVADlAGRAP 591
Cdd:PRK12492   104 NTNPLYTAREMRHQFKDSGARALVylnmfgklvqevlPDTGieylieakMGDLLPAAKGWLVntVVDKVKKMVP-AYHLP 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  592 HDLT--DADRAGA--------TGPYDTAYVIHTSGSTGRPKGVPVPHAHVV-----------RLFEASGEHFRFGADDVW 650
Cdd:PRK12492   183 QAVPfkQALRQGRglslkpvpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlqvraclsQLGPDGQPLMKEGQEVMI 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  651 T---LFHSYAFDFSVWELwgpLLHGGRLVVVPyevsrSPRE---FLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGS 724
Cdd:PRK12492   263 AplpLYHIYAFTANCMCM---MVSGNHNVLIT-----NPRDipgFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSA 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  725 LRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETT-VHVTFHRLVRAdledprRRGVIGRPLADLRVYVLDAAGR 803
Cdd:PRK12492   335 LKLTNSGGTALVKATAERWEQLTGC---TIVEGYGLTETSpVASTNPYGELA------RLGTVGIPVPGTALKVIDDDGN 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  804 PVPPGATGEMYVSGPGVAPGYLNRPELTEErflpdPFGAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGE 883
Cdd:PRK12492   406 ELPLGERGELCIKGPQVMKGYWQQPEATAE-----ALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  884 IEAVLTAHPAVAGGAVVPRAAEDGlTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK12492   479 IEDVVMAHPKVANCAAIGVPDERS-GEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 460-926 5.39e-24

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: 109.15  E-value: 5.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  460 QLFEA--RVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP 535
Cdd:cd17642     19 QLHKAmkRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  536 LDPGHPAERLALVMADAEPVAVVTDTAGSGRLPATDARV-----VVVDDARTvaDLAG-------RAPHDLTDADRAGAT 603
Cdd:cd17642     99 TNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiiktIIILDSKE--DYKGyqclytfITQNLPPGFNEYDFK 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 GPY-----DTAYVIHTSGSTGRPKGVPVPHAHVVRLFEasgeHFR---FGAD--------DVWTLFHSyafdFSVWELWG 667
Cdd:cd17642    177 PPSfdrdeQVALIMNSSGSTGLPKGVQLTHKNIVARFS----HARdpiFGNQiipdtailTVIPFHHG----FGMFTTLG 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  668 PLLHGGRLVVVP-YEvsrsPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADR 746
Cdd:cd17642    249 YLICGFRVVLMYkFE----EELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKR 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  747 HGLdaPELVNMYGITETTVHVtfhrLVRADLEDprRRGVIGR--PLADLRVYVLDAaGRPVPPGATGEMYVSGPGVAPGY 824
Cdd:cd17642    325 FKL--PGIRQGYGLTETTSAI----LITPEGDD--KPGAVGKvvPFFYAKVVDLDT-GKTLGPNERGELCVKGPMIMKGY 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  825 LNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVpraa 904
Cdd:cd17642    396 VNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA---- 464

                          490       500
                   ....*....|....*....|..
gi 1573930569  905 edgltqlvayAVPAEEGGADPA 926
Cdd:cd17642    465 ----------GIPDEDAGELPA 476
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 1711-2103 1.00e-23

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: 108.07  E-value: 1.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVplTVpvsYATTsaavsklegiwemldrp 1790
Cdd:cd17639      7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIV--TV---YATL----------------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 wivtsaaGEPGLRElaarrewsGLRLTTADALREEPEdrdwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVltrAAATE 1870
Cdd:cd17639     65 -------GEDALIH--------SLNETECSAIFTDGK--------PDDLACIMYTSGSTGNPKGVMLTHGNL---VAGIA 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNG-----LGSGDVSLNWIPLDHV-----TGVVMFH------------LRDVYLGCR-QIHA--PTswILedpVRWPEL 1925
Cdd:cd17639    119 GLGDrvpelLGPDDRYLAYLPLAHIfelaaENVCLYRggtigygsprtlTDKSKRGCKgDLTEfkPT--LM---VGVPAI 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1926 ADRHR----VSVTWAPNFAFGL--LAEQAHRFQDRDWDLSP-----------------VRLVMNAGEVVVASAaRRFLHV 1982
Cdd:cd17639    194 WDTIRkgvlAKLNPMGGLKRTLfwTAYQSKLKALKEGPGTPlldelvfkkvraalggrLRYMLSGGAPLSADT-QEFLNI 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1983 lapFGLPqdvMHPGWGMSETCSVVTDSVLASEAPDhdeafvSCGLPYPGFAMRVVD------DQDALLPEGDVgrlQVRG 2056
Cdd:cd17639    273 ---VLCP---VIQGYGLTETCAGGTVQDPGDLETG------RVGPPLPCCEIKLVDweeggySTDKPPPRGEI---LIRG 337

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1573930569 2057 TSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYITGRAKDVI 2103
Cdd:cd17639    338 PNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKIIDRKKDLV 385
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1838-2135 1.61e-23

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: 104.51  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHV----TGVVMFHLRDVYLGCRQIHapts 1913
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTfgykAGIVACLLTGATVVPVAVF---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1914 wileDPVRWPELADRHRVSVT-WAPNFAFGLLAEQAHRfqdrDWDLSPVRLVMNAGEVVVASAARRFLHvlapfGLPQDV 1992
Cdd:cd17638     77 ----DVDAILEAIERERITVLpGPPTLFQSLLDHPGRK----KFDLSSLRAAVTGAATVPVELVRRMRS-----ELGFET 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 MHPGWGMSEtCSVVTDSvlaseAPDHDEAFVS--CGLPYPGFAMRVVDDqdallpegdvGRLQVRGTSVTHGYHDNARAN 2070
Cdd:cd17638    144 VLTAYGLTE-AGVATMC-----RPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEAT 207

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 2071 AESFTEDGWFDTGDLAFLRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAV 2135
Cdd:cd17638    208 AEAIDADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV-----AQVAV 268
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 483-964 1.98e-23

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: 107.55  E-value: 1.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLP----LDPGHPAERLALVMADA----E 553
Cdd:cd05928     43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPgtiqLTAKDILYRLQASKAKCivtsD 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  554 PVAVVTDTAGSgRLPATDARVVVVDDAR----TVADLAGRAPHDLTDADragaTGPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:cd05928    123 ELAPEVDSVAS-ECPSLKTKLLVSEKSRdgwlNFKELLNEASTEHHCVE----TGSQEPMAIYFTSGTTGSPKMAEHSHS 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFR--FGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVvpYEVSR-SPREFLRLLDEEKVTVLNQTPS 706
Cdd:cd05928    198 SLGLGLKVNGRYWLdlTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFV--HHLPRfDPLVILKTLSSYPITTFCGAPT 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  707 AFEQLVLADAATDRATgSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITETTvhvtfhrLVRADLEDPR-RRGV 785
Cdd:cd05928    276 VYRMLVQQDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG-------LICANFKGMKiKPGS 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  786 IGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAP-----GYLNRPELTEERFLPDpfgapgtrMYRSGDLARWRPDG 860
Cdd:cd05928    345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPfglfsGYVDNPEKTAATIRGD--------FYLTGDRGIMDEDG 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  861 TLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVprAAEDGLTQLV--AYAVPAEE-GGADP----AGLRAHLA 933
Cdd:cd05928    417 YFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV--SSPDPIRGEVvkAFVVLAPQfLSHDPeqltKELQQHVK 494

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:cd05928    495 SVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 475-920 2.07e-23

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: 106.76  E-value: 2.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  475 VSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEP 554
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  555 VAVVTdtagsgrlpatdarvvvvddartvadlagraphdlTDADragatgpyDTAYVIHTSGSTGRPKGVPVPHAHVVRL 634
Cdd:cd05914     81 KAIFV-----------------------------------SDED--------DVALINYTSGTTGNSKGVMLTYRNIVSN 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  635 FEASGEHFRFGADDV----WTLFHSY--AFDFSVwelwgPLLHGGRLVVvpyeVSRSPREFLRLLDEEKVTV-------- 700
Cdd:cd05914    118 VDGVKEVVLLGKGDKilsiLPLHHIYplTFTLLL-----PLLNGAHVVF----LDKIPSAKIIALAFAQVTPtlgvpvpl 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  701 ----------LNQTPSAFEQLVLA-------------DAATDRATGSLRYVVLGGEALVAERLRpwaDRHGLDAPELVNm 757
Cdd:cd05914    189 viekifkmdiIPKLTLKKFKFKLAkkinnrkirklafKKVHEAFGGNIKEFVIGGAKINPDVEE---FLRTIGFPYTIG- 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  758 YGITETTVHVTFHRLVRADLedprrrGVIGRPLADLRVYVLDaagrPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLP 837
Cdd:cd05914    265 YGMTETAPIISYSPPNRIRL------GSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  838 DPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQ-VKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRaaeDGLTQLVAYAV 916
Cdd:cd05914    335 DGW-------FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQ---EKKLVALAYID 404


                   ....
gi 1573930569  917 PAEE 920
Cdd:cd05914    405 PDFL 408
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1685-2151 2.07e-23

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: 107.21  E-value: 2.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGRPDGEVVHVRADGSeTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGfvAVPl 1764
Cdd:cd05923      5 EMLRRAASRAPDACAIADPARG-LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG--AVP- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 tVPVSYATTSAAVSKLEGIWEMLdRPWIVTSAAGEPGLRELAARRewsgLRLTTADALREEPEDRDWYEA---RPDDLVL 1841
Cdd:cd05923     81 -ALINPRLKAAELAELIERGEMT-AAVIAVDAQVMDAIFQSGVRV----LALSDLVGLGEPESAGPLIEDpprEPEQPAF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1842 MLMTSGSTGLPKAVRLTHRNVLTRAA--ATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGcrqihapTSWIL--- 1916
Cdd:cd05923    155 VFYTSGTTGLPKGAVIPQRAAESRVLfmSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALD-------GTYVVvee 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1917 EDPVRWPELADRHRVSVTWA-PNFAFGLLA--EQAHRfqdrdwDLSPVRLVMNAGEVVVASAARRfLHVLAPfGLPQDVm 1993
Cdd:cd05923    228 FDPADALKLIEQERVTSLFAtPTHLDALAAaaEFAGL------KLSSLRHVTFAGATMPDAVLER-VNQHLP-GEKVNI- 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1994 hpgWGMSETCSVVTDSVLASEAPDHdeafvscglpyPGF-----AMRVVDDQDALLPEGDVGRLQVR--GTSVTHGYHDN 2066
Cdd:cd05923    299 ---YGTTEAMNSLYMRDARTGTEMR-----------PGFfsevrIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2067 ARANAESFtEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVR------------SFTAAV 2133
Cdd:cd05923    365 PEATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEvvvigvaderwgQSVTAC 443

                          490
                   ....*....|....*...
gi 1573930569 2134 AVRSDASAATDELALFLR 2151
Cdd:cd05923    444 VVPREGTLSADELDQFCR 461
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 455-964 2.33e-23

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 107.81  E-value: 2.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  455 TRTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYL 534
Cdd:PRK06710    23 IQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PLDPGHPAERLALVMADAEPVAV---------VTDTAGSGRL--------------------PATDAR----VVVVDDAR 581
Cdd:PRK06710   103 QTNPLYTERELEYQLHDSGAKVIlcldlvfprVTNVQSATKIehvivtriadflpfpknllyPFVQKKqsnlVVKVSESE 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  582 TVaDLAGRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVR--------LFEA-SGEHFRFGaddVWTL 652
Cdd:PRK06710   183 TI-HLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqwLYNCkEGEEVVLG---VLPF 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  653 FHSYAFDfSVWELwgPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGG 732
Cdd:PRK06710   259 FHVYGMT-AVMNL--SIMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGS 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  733 EALVAERLRPWADRHGldaPELVNMYGITETT--VHVTFhrlvradLEDPRRRGVIGRPLADLRVYVLD-AAGRPVPPGA 809
Cdd:PRK06710   333 APLPVEVQEKFETVTG---GKLVEGYGLTESSpvTHSNF-------LWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGE 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  810 TGEMYVSGPGVAPGYLNRPELTEErFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLT 889
Cdd:PRK06710   403 IGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569  890 AHPAVAGGAVV----PRAAEdgltQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK06710   475 EHEKVQEVVTIgvpdPYRGE----TVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1690-2202 2.63e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 107.14  E-value: 2.63e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDgevvHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL----- 1764
Cdd:PRK06164    20 ARARPD----AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVntryr 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 TVPVSYATTS--AAVSKLEGIWEMLDRPWIVTSAAGE--PGLRELAARRE--------WSGLRLTTAD-ALREEPEDRDW 1831
Cdd:PRK06164    96 SHEVAHILGRgrARWLVVWPGFKGIDFAAILAAVPPDalPPLRAIAVVDDaadatpapAPGARVQLFAlPDPAPPAAAGE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFhlrdvyLGCrqIHAP 1911
Cdd:PRK06164   176 RAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL------LGA--LAGG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1912 TSWILE---DPVRWPELADRHRVSVTWAPNFAFGLLAEQAhrfqDRDWDLSPVRLVMnagevvVASAARRFlHVLAPFGL 1988
Cdd:PRK06164   248 APLVCEpvfDAARTARALRRHRVTHTFGNDEMLRRILDTA----GERADFPSARLFG------FASFAPAL-GELAALAR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1989 PQDVMHPG-WGMSETCSVVTdsvLASEAPDHDEAFVSCGLP-YPGFAMRVVDDQD-ALLPEGDVGRLQVRGTSVTHGYHD 2065
Cdd:PRK06164   317 ARGVPLTGlYGSSEVQALVA---LQPATDPVSVRIEGGGRPaSPEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLD 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2066 NARANAESFTEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrSFTAAVAVRSDASAatd 2144
Cdd:PRK06164   394 NPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV--AAAQVVGATRDGKT--- 468

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2145 ELALFLRLAPGQDPA-----GALRE-IAG-KVtreigvsPAFLIPVeaEAIPKTEIG---KIQRTKLR 2202
Cdd:PRK06164   469 VPVAFVIPTDGASPDeaglmAACREaLAGfKV-------PARVQVV--EAFPVTESAngaKIQKHRLR 527
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 468-950 2.64e-23

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 106.11  E-value: 2.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  468 ESPGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLAl 547
Cdd:PRK09029    15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE- 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  548 vmadaepvAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLtDADRAgatgpydtAYVIHTSGSTGRPKGVpvp 627
Cdd:PRK09029    94 --------ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAW-QPQRL--------ATMTLTSGSTGLPKAA--- 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  628 hAHVVR--LFEASG--EHFRFGADDVW----TLFHsyafdFS----VWElWgpLLHGGRLVVVPYE-----------VSR 684
Cdd:PRK09029   154 -VHTAQahLASAEGvlSLMPFTAQDSWllslPLFH-----VSgqgiVWR-W--LYAGATLVVRDKQpleqalagcthASL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  685 SPREFLRLLDEekvtvlnqtpsafeqlvladaatDRATGSLRYVVLGGEALVAErLRPWADRHGLdapELVNMYGITETT 764
Cdd:PRK09029   225 VPTQLWRLLDN-----------------------RSEPLSLKAVLLGGAAIPVE-LTEQAEQQGI---RCWCGYGLTEMA 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  765 VHVTfhrLVRADledpRRRGViGRPLADLRVYVLDaagrpvppgatGEMYVSGPGVAPGYLNRPELTEerfLPDPFGAPG 844
Cdd:PRK09029   278 STVC---AKRAD----GLAGV-GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP---LVNDEGWFA 335

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  845 TRmyrsgDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRA-AEDGLTQLvayAVPAEEGGA 923
Cdd:PRK09029   336 TR-----DRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVAdAEFGQRPV---AVVESDSEA 406

                          490       500
                   ....*....|....*....|....*..
gi 1573930569  924 DPAGLRAHLAARLPAYMVPAACVLLDA 950
Cdd:PRK09029   407 AVVNLAEWLQDKLARFQQPVAYYLLPP 433
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1836-2201 5.09e-23

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: 105.24  E-value: 5.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDV---SLNWIPLDHVTGVVmfhLRDVYLGCRQIHAPT 1912
Cdd:cd17650     92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVrllQMASFSFDVFAGDF---ARSLLNGGTLVICPD 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 SWILeDPVRWPELADRHRVSVTWA-PNFAFGLLAEQAHrfqdRDWDLSPVRLVMNAGEVVvasAARRFLHVLAPFGLPQD 1991
Cdd:cd17650    169 EVKL-DPAALYDLILKSRITLMEStPALIRPVMAYVYR----NGLDLSAMRLLIVGSDGC---KAQDFKTLAARFGQGMR 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1992 VMHpGWGMSETCsvvTDSVLASEAPDH--DEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARA 2069
Cdd:cd17650    241 IIN-SYGVTEAT---IDSTYYEEGRDPlgDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPEL 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2070 NAESFTEDGW------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAA 2142
Cdd:cd17650    317 TAERFVENPFapgermYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE---AVVAVREDKGGE 393

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2143 TdELALFLRLAPGQDPAgALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd17650    394 A-RLCAYVVAAATLNTA-ELRAFLAKEL------PSYMIPsyyVQLDALPLTPNGKVDRRAL 447
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 1711-2102 5.13e-23

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: 106.01  E-value: 5.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtVPVSYATTSAAV-----SKLEGIWE 1785
Cdd:cd05932      8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL-YPTLNPDTIRYVlehseSKALFVGK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1786 MLDRPWIVTSAAGEPGLR------ELAARREWSGLrLTTADALREEPEdRDwyearPDDLVLMLMTSGSTGLPKAVRLTH 1859
Cdd:cd05932     87 LDDWKAMAPGVPEGLISIslpppsAANCQYQWDDL-IAQHPPLEERPT-RF-----PEQLATLIYTSGTTGQPKGVMLTF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1860 RNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAptswilEDPVRWPELADRHRvsvtwaPNF 1939
Cdd:cd05932    160 GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFA------ESLDTFVEDVQRAR------PTL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1940 AFG---LLAEQAHRFQDRdwdLSPVRLVMNAGEVVVASAARRflHVLAPFGL-------------PQDVMH--------- 1994
Cdd:cd05932    228 FFSvprLWTKFQQGVQDK---IPQQKLNLLLKIPVVNSLVKR--KVLKGLGLdqcrlagcgsapvPPALLEwyrslglni 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1995 -PGWGMSETCSVVTDSVlaseaP-DHDEAFVscGLPYPGFAMRVVDDqdallpegdvGRLQVRGTSVTHGYHDNARANAE 2072
Cdd:cd05932    303 lEAYGMTENFAYSHLNY-----PgRDKIGTV--GNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAE 365

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1573930569 2073 SFTEDGWFDTGDLAFL-RDGELYITGRAKDV 2102
Cdd:cd05932    366 AFTADGFLRTGDKGELdADGNLTITGRVKDI 396
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 479-958 5.43e-23

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: 105.13  E-value: 5.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  479 GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAylpldpghpaerLALVMAD--AEPVA 556
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV------------AALINYNlrGESLA 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  557 VVTDTAgsgrlpatDARVVVVDdartvadlagraphdltdadragatgpydTAYVIHTSGSTGRPKGVPVPHAHVVR--- 633
Cdd:cd05940     69 HCLNVS--------SAKHLVVD-----------------------------AALYIYTSGTTGLPKAAIISHRRAWRgga 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  634 LFEASGehFRFGADDVWT---LFHSYAfdfSVWELWGPLLHGGRLVVvpyEVSRSPREFLRLLDEEKVTV---------- 700
Cdd:cd05940    112 FFAGSG--GALPSDVLYTclpLYHSTA---LIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIfqyigelcry 183

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  701 -LNQTPSafeqlvladaATDRATgSLRYVVLGGealvaerLRP--WAD---RHGLdaPELVNMYGITETTV--------- 765
Cdd:cd05940    184 lLNQPPK----------PTERKH-KVRMIFGNG-------LRPdiWEEfkeRFGV--PRIAEFYAATEGNSgfinffgkp 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  766 -----------HVTFHRLVRADLEDprrrgviGRPLADLRVYVldaagRPVPPGATGEMYVSGPGVAP--GYLNrPELTE 832
Cdd:cd05940    244 gaigrnpsllrKVAPLALVKYDLES-------GEPIRDAEGRC-----IKVPRGEPGLLISRINPLEPfdGYTD-PAATE 310

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  833 ERFLPDPFgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHP----AVAGGAVVPRAaeDGL 908
Cdd:cd05940    311 KKILRDVF-KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPgveeANVYGVQVPGT--DGR 387

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569  909 TQLVAYAVPAEEgGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:cd05940    388 AGMAAIVLQPNE-EFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFK 436
PRK12467 PRK12467
peptide synthase; Provisional
 1040-2203 5.52e-23

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 108.71  E-value: 5.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1040 TPTPAALAERLTAGADAgrpLPaLTASERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHpLDLDALRAALGDVA 1119
Cdd:PRK12467  2619 TPSDFPLAGLSQEQLDR---LP-VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVI 2693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1120 DRHESLRTVFGEEDG------AIHQRVLPPGTlrpELHVVDCPDEERA--AHVAAAMRRSFDLTRDSALWAGVFGTG-DT 1190
Cdd:PRK12467  2694 DRHEILRSGFLWDGEleeplqVVYKQARLPFS---RLDWRDRADLEQAldALAAADRQQGFDLLSAPLLRLTLVRTGeDR 2770

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1191 RTLLLVLHHSAADGWSLRPLaddLGTAYAARRAGAAPdwaPPALQYADFALWQRRVLAPAPEgpgrlerltSFWRQALDG 1270
Cdd:PRK12467  2771 HHLIYTNHHILMDGWSGSQL---LGEVLQRYFGQPPP---AREGRYRDYIAWLQAQDAEASE---------AFWKEQLAA 2835

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1271 LPEESAPPPDRPRPAAPSGRG-GGVTVPLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRte 1349
Cdd:PRK12467  2836 LEEPTRLARALYPAPAEAVAGhGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR-- 2913

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1350 PA----LDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPfdrlVEEVNPRRHPARHPLFQVMLALQNn 1425
Cdd:PRK12467  2914 PAqlrgAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTP----LADIQRWAGQGGEALFDSILVFEN- 2988

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1426 eravltlgedrVPLRPAATGTAKFDLFVDVLERHG--------ADGTADGLDLHVEYAADLYDPATAERFAGALRDLLTV 1497
Cdd:PRK12467  2989 -----------YPISEALKQGAPSGLRFGAVSSREqtnypltlAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQA 3057

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1498 VCADPEVRTGALPRADRPspatadttaragaltravlevpgvgdavvlpgpdgEPATVYVVPNRAGAADRTEQVVSSLap 1577
Cdd:PRK12467  3058 MLNNPAARLGELPTLAAH-----------------------------------ERRQVLHAWNATAAAYPSERLVHQL-- 3100

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1578 gtrvvaisglprtaeggldegalkdlpVIDQVaagawrerlarlpgvreaevvleevpeelerrhvgrpraaggAAEPDA 1657
Cdd:PRK12467  3101 ---------------------------IEAQV------------------------------------------ARTPEA 3111

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1658 PSVerpasvpalsegpalpepsVSGwaeallraagrpdgevvhvradgsETRRSYASLVPEASRVLAGLRRRGLRPGDRV 1737
Cdd:PRK12467  3112 PAL-------------------VFG------------------------DQQLSYAELNRRANRLAHRLIAIGVGPDVLV 3148

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1738 ILQCDDTEDFVATLWGCVLGGFVAVPLTvPVSYATTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRELAARRewsglrlt 1817
Cdd:PRK12467  3149 GVAVERSVEMIVALLAVLKAGGAYVPLD-PEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDR-------- 3219

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1818 taDALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFH 1897
Cdd:PRK12467  3220 --LDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFL 3297

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1898 LRDVYLGCRQIHAPTSWileDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRfqdrdWDLSPVRLVMNAGEVVVASAAR 1977
Cdd:PRK12467  3298 WTLICGGCLVVRDNDLW---DPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-----ADCASLDIYVFGGEAVPPAAFE 3369

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1978 RFLHVLAPFGLpqdvmHPGWGMSETCSVVTDSVLASEAPDhDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGT 2057
Cdd:PRK12467  3370 QVKRKLKPRGL-----TNGYGPTEAVVTVTLWKCGGDAVC-EAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV 3443

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2058 SVTHGYHDNARANAESFTEDGWFD-------TGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsf 2129
Cdd:PRK12467  3444 GLARGYHQRPSLTAERFVADPFSGsggrlyrTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV---- 3519

                         1130      1140      1150      1160      1170      1180      1190
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2130 TAAVAVRSDaSAATDELALFLRLapgQDPAGALREiagKVTREIGVS-PAFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK12467  3520 REAVVLARD-GAGGKQLVAYVVP---ADPQGDWRE---TLRDHLAASlPDYMVPaqlLVLAAMPLGPNGKVDRKALPD 3590
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1836-2203 6.83e-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: 103.33  E-value: 6.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHA-PTSW 1914
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgPAGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1915 ILEDPVR--WpELADRHRVSVTWAPNFAFGLLAEQAhrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVLapfGLPqdv 1992
Cdd:cd05944     81 RNPGLFDnfW-KLVERYRITSLSTVPTVYAALLQVP-----VNADISSLRFAMSGAAPLPVELRARFEDAT---GLP--- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 MHPGWGMSETCSVVTDSvlaseAPDHDEAFVSCGL--PYPGFAMRVVDDQDALLPE---GDVGRLQVRGTSVTHGYHDNA 2067
Cdd:cd05944    149 VVEGYGLTEATCLVAVN-----PPDGPKRPGSVGLrlPYARVRIKVLDGVGRLLRDcapDEVGEICVAGPGVFGGYLYTE 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2068 RaNAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrSFTAAVAvRSDASAATDEL 2146
Cdd:cd05944    224 G-NKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV--AFAGAVG-QPDAHAGELPV 299

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2147 AlFLRLAPGQD-PAGALREIAGKVTREIGVSPAFLIPVeaEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05944    300 A-YVQLKPGAVvEEEELLAWARDHVPERAAVPKHIEVL--EELPVTAVGKVFKPALRA 354
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 459-959 1.23e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 105.03  E-value: 1.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAES-PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:PRK08162    20 PLSFLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTDTAGSG-------RLPATDARVVVVDDArtvADLAGRAPHDLT--------DADRAgA 602
Cdd:PRK08162   100 TRLDAASIAFMLRHGEAKVLIVDTEFAEvarealaLLPGPKPLVIDVDDP---EYPGGRFIGALDyeaflasgDPDFA-W 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  603 TGPYDTAYVI---HTSGSTGRPKGVpVPHAHVVRLFEASGE-HFRFGADDV--WTL--FHSYAFDFSvwelWGPLLHGGR 674
Cdd:PRK08162   176 TLPADEWDAIalnYTSGTTGNPKGV-VYHHRGAYLNALSNIlAWGMPKHPVylWTLpmFHCNGWCFP----WTVAARAGT 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 LVVVpyevsR--SPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRAtgsLRYVVlggEALVAERLRPWADRHGLDAP 752
Cdd:PRK08162   251 NVCL-----RkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG---IDHPV---HAMVAGAAPPAAVIAKMEEI 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  753 --ELVNMYGITETTVHVT-------FHRL---VRADLEdpRRRGVIGRPLADLRVyvLDAA-GRPVP-PGAT-GEMYVSG 817
Cdd:PRK08162   320 gfDLTHVYGLTETYGPATvcawqpeWDALpldERAQLK--ARQGVRYPLQEGVTV--LDPDtMQPVPaDGETiGEIMFRG 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  818 PGVAPGYLNRPELTEERFlpdpfgAPGtrMYRSGDLARWRPDGtlvhagradqQVKIR----------GFRIEPGEIEAV 887
Cdd:PRK08162   396 NIVMKGYLKNPKATEEAF------AGG--WFHTGDLAVLHPDG----------YIKIKdrskdiiisgGENISSIEVEDV 457

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  888 LTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAAcVLLDALPLTANGKL 959
Cdd:PRK08162   458 LYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKI 528
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1836-2202 1.23e-22

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 105.10  E-value: 1.23e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE-----AMNGLGSGDVsLNWI---PLDHVTGVVMFHLRDVYLGCRQ 1907
Cdd:PRK07059   203 PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpAFEKKPRPDQ-LNFVcalPLYHIFALTVCGLLGMRTGGRN 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 IHAPtswileDPVRWP----ELAdRHRVSVTWAPNFAF-GLLaeQAHRFqdRDWDLSPVRLVMNAGEVVVASAARRFLHV 1982
Cdd:PRK07059   282 ILIP------NPRDIPgfikELK-KYQVHIFPAVNTLYnALL--NNPDF--DKLDFSKLIVANGGGMAVQRPVAERWLEM 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1983 LapfGLPqdvMHPGWGMSETCSVVTdsvlaSEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHG 2062
Cdd:PRK07059   351 T---GCP---ITEGYGLSETSPVAT-----CNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAG 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2063 YHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsfTAAVAVRSDASA 2141
Cdd:PRK07059   420 YWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE--VAAVGVPDEHSG 497

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2142 ATDELALFLRlapgqDPAGALREIAG---------KVTREIgvspAFLipveaEAIPKTEIGKIQRTKLR 2202
Cdd:PRK07059   498 EAVKLFVVKK-----DPALTEEDVKAfckerltnyKRPKFV----EFR-----TELPKTNVGKILRRELR 553
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 481-900 1.53e-22

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: 103.69  E-value: 1.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVtd 560
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 tagsgrlpatdarvvvvddartvadlagraphdltdadraGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGE 640
Cdd:cd05910     80 ----------------------------------------GIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  641 HF--RFGADDVWTlfhsyafdFSVWELWGPLLhGGRLVVVPYEVSR----SPREFLRLLDEEKVTVLNQTPSAFEQLVLA 714
Cdd:cd05910    120 LYgiRPGEVDLAT--------FPLFALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARY 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  715 DAATDRATGSLRYVVLGGEAL---VAERLRPWADrhglDAPELVNMYGITET-TVHVTFHRLVRADLEDPRRRG---VIG 787
Cdd:cd05910    191 CAQHGITLPSLRRVLSAGAPVpiaLAARLRKMLS----DEAEILTPYGATEAlPVSSIGSRELLATTTAATSGGagtCVG 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  788 RPLADLRVYVLDAAGRP---------VPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPfgaPGTRMYRSGDLARWRP 858
Cdd:cd05910    267 RPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDD 343

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV 900
Cdd:cd05910    344 EGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 1838-2198 1.59e-22

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: 101.57  E-value: 1.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTraaATEAMNGLG----SGDVSLNWIPLDHVTG-----VVMFHLRDVYLGCRQI 1908
Cdd:cd17635      2 DPLAVIFTSGTTGEPKAVLLANKTFFA---VPDILQKEGlnwvVGDVTYLPLPATHIGGlwwilTCLIHGGLCVTGGENT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 HAPTSWiledpvrwpELADRHRVSVT-WAPNfafgLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHvlapFG 1987
Cdd:cd17635     79 TYKSLF---------KILTTNAVTTTcLVPT----LLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEA----TG 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1988 LPQDVMHpgWGMSETCSVVTdsvlaseAPDHDEAFV--SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHD 2065
Cdd:cd17635    142 LTNTAQV--YGLSETGTALC-------LPTDDDSIEinAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWN 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2066 NARANAESFTeDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAAtd 2144
Cdd:cd17635    213 NPERTAEVLI-DGWVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE---CACYEISDEEFG-- 286

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2145 ELALFLRLAPGQDPAGALREIAGKVTREigvSPAFLIP---VEAEAIPKTEIGKIQR 2198
Cdd:cd17635    287 ELVGLAVVASAELDENAIRALKHTIRRE---LEPYARPstiVIVTDIPRTQSGKVKR 340
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1711-2206 1.70e-22

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 104.20  E-value: 1.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTV-----PVSYATTSAAVSKLEGIWE 1785
Cdd:PRK06145    29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYrlaadEVAYILGDAGAKLLLVDEE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1786 M-----LDRPWIVTSAAGEPGLRELAArrewSGLRLTTAdalreepedrdwYEARPDDLVLMLMTSGSTGLPKAVRLTHR 1860
Cdd:PRK06145   109 FdaivaLETPKIVIDAAAQADSRRLAQ----GGLEIPPQ------------AAVAPTDLVRLMYTSGTTDRPKGVMHSYG 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1861 NVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLG-CRQIHAPTswileDPVRWPELADRHRVSVTW-APN 1938
Cdd:PRK06145   173 NLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGgTLRIHREF-----DPEAVLAAIERHRLTCAWmAPV 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1939 FAFGLLAeqahrFQDRD-WDLSPVRLVMNAGEVVVASAARRFLHVLApfglpQDVMHPGWGMSETCSvvTDSVLasEAPD 2017
Cdd:PRK06145   248 MLSRVLT-----VPDRDrFDLDSLAWCIGGGEKTPESRIRDFTRVFT-----RARYIDAYGLTETCS--GDTLM--EAGR 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2018 HDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTeDGWFDTGDLAFLRD-GELYIT 2096
Cdd:PRK06145   314 EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEeGFLYLT 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2097 GRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELALFLrLAPGQD-PAGALRE-----IAG-KV 2169
Cdd:PRK06145   393 DRKKDMIISGGENIASSEVERVIYELPEVAE---AAVIGVHDDRWGERITAVVV-LNPGATlTLEALDRhcrqrLASfKV 468

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1573930569 2170 TREIGVspaflipveAEAIPKTEIGKIQRTKLRKSFE 2206
Cdd:PRK06145   469 PRQLKV---------RDELPRNPSGKVLKRVLRDELN 496
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 610-960 2.03e-22

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: 100.94  E-value: 2.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  610 YVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVW----TLFHSYAFDFSVWELWGpllhgGRLVVVpyEVSRS 685
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAIlapgPLSHSLFLYGAISALYL-----GGTFIG--QRKFN 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  686 PREFLRLLDEEKVTVLNQTPSAFEQLVLadaaTDRATGSLRYVVLGGEALVAERLRPWadRHGLDAPELVNMYGITETTv 765
Cdd:cd17633     77 PKSWIRKINQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKL--KNIFPKANLIEFYGTSELS- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  766 HVTFhrlvRADlEDPRRRGVIGRPLADLRVYVLDAAGrpvppGATGEMYVSGPGVAPGYLNRPELTEerflpdpfgapgT 845
Cdd:cd17633    150 FITY----NFN-QESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP------------D 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  846 RMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEdGLTQLVAYAVPAEegGADP 925
Cdd:cd17633    208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA-RFGEIAVALYSGD--KLTY 284

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1573930569  926 AGLRAHLAARLPAYMVPAACVLLDALPLTANGKLD 960
Cdd:cd17633    285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 457-959 2.44e-22

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 104.29  E-value: 2.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  457 TLPQLFEARVAESPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYL 534
Cdd:PLN02330    29 TLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PLDP-GHPAERLALVMAdAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRaphDLTDA-DRAGATGPY------ 606
Cdd:PLN02330   109 GANPtALESEIKKQAEA-AGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNWK---ELLEAaDRAGDTSDNeeilqt 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVV-----RLFEASGEHFrfgaDDVWTL-----FHSYAFdfsVWELWGPLLHGGRLV 676
Cdd:PLN02330   185 DLCALPFSSGTTGISKGVMLTHRNLVanlcsSLFSVGPEMI----GQVVTLglipfFHIYGI---TGICCATLRNKGKVV 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  677 VVP-YEVsrspREFLRLLDEEKVTVLNQTPSAFEQLVLADAAT--DRATGSLRYVVLGGEALVAERLRPWADRH-GLDAP 752
Cdd:PLN02330   258 VMSrFEL----RTFLNALITQEVSFAPIVPPIILNLVKNPIVEefDLSKLKLQAIMTAAAPLAPELLTAFEAKFpGVQVQ 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  753 ElvnMYGITEttvhvtfHRLVRADLEDPRR------RGVIGRPLADLRVYVLDA-AGRPVPPGATGEMYVSGPGVAPGYL 825
Cdd:PLN02330   334 E---AYGLTE-------HSCITLTHGDPEKghgiakKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELCVRSQCVMQGYY 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  826 NRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAE 905
Cdd:PLN02330   404 NNKEETDRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1573930569  906 DGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PLN02330   477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKI 530
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1711-2201 4.05e-22

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: 102.75  E-value: 4.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyatTSAAVSKLEGIWEMLDRP 1790
Cdd:cd12116     14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLD-------PDYPADRLRYILEDAEPA 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTSAAgepglreLAARREWSGLRLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd12116     87 LVLTDDA-------LPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGD--VSLNWIPLDhVTGVVMfhLRDVYLGCRQIHAPTSwILEDPVRWPELADRHRVSVTWA-PNFAFGLLaeq 1947
Cdd:cd12116    160 ERLGLGPGDrlLAVTTYAFD-ISLLEL--LLPLLAGARVVIAPRE-TQRDPEALARLIEAHSITVMQAtPATWRMLL--- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1948 ahrfqDRDW-DLSPVRLVMnAGEVVVASAARRFLhvlapfgLPQDVMHPGWGMSETC--SVVTDsVLASEAPdhdeafVS 2024
Cdd:cd12116    233 -----DAGWqGRAGLTALC-GGEALPPDLAARLL-------SRVGSLWNLYGPTETTiwSTAAR-VTAAAGP------IP 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2025 CGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG-------WFDTGDLAFLR-DGELYIT 2096
Cdd:cd12116    293 IGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYL 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2097 GRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATdeLALFLRLAPGQDP-AGALREIAGKVTreigv 2175
Cdd:cd12116    373 GRADGQVKIRGHRIELGEIEAALAAHPGVAQ---AAVVVREDGGDRR--LVAYVVLKAGAAPdAAALRAHLRATL----- 442

                          490       500
                   ....*....|....*....|....*....
gi 1573930569 2176 sPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd12116    443 -PAYMVPsafVRLDALPLTANGKLDRKAL 470
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 1838-2198 4.52e-22

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: 100.04  E-value: 4.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVM----FHlrdvyLGCRQIhapts 1913
Cdd:cd17637      1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLalatFH-----AGGANV----- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1914 wILE--DPVRWPELADRHRVSV--TWAPnfAFGLLAEQAhrfQDRDWDLSPVRLV--MNAGEVVvasaaRRFL-HVLAPF 1986
Cdd:cd17637     71 -VMEkfDPAEALELIEEEKVTLmgSFPP--ILSNLLDAA---EKSGVDLSSLRHVlgLDAPETI-----QRFEeTTGATF 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1987 GLpqdvmhpGWGMSETCSVVTDSvLASEAPDhdeafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDN 2066
Cdd:cd17637    140 WS-------LYGQTETSGLVTLS-PYRERPG------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNL 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2067 ARANAESFtEDGWFDTGDL-AFLRDGELYITGR--AKDVIIVNGVNHYSHEIEACVEELPSVVRS---------FTAAV- 2133
Cdd:cd17637    206 PELTAYTF-RNGWHHTGDLgRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVcvigvpdpkWGEGIk 284

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2134 AV---RSDASAATDELALFlrlapgqdpagalreIAGKVTREigVSPAFLipVEAEAIPKTEIGKIQR 2198
Cdd:cd17637    285 AVcvlKPGATLTADELIEF---------------VGSRIARY--KKPRYV--VFVEALPKTADGSIDR 333
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
456-959 4.76e-22

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 103.42  E-value: 4.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSYAGETLSYAELNAEANRLAR-LLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYL 534
Cdd:PRK08751    25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  535 PLDPGHPAERLALVMADA-EPVAVVTDTAGSG---RLPATDARVVVVDDARTVADLAGRA--------------PHDLTD 596
Cdd:PRK08751   105 NVNPLYTPRELKHQLIDSgASVLVVIDNFGTTvqqVIADTPVKQVITTGLGDMLGFPKAAlvnfvvkyvkklvpEYRING 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  597 ADR---AGATG-----------PYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGE------HFRFGADDVWT---LF 653
Cdd:PRK08751   185 AIRfreALALGrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagtgKLEEGCEVVITalpLY 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  654 HSYAFDFS--VWELWGPLLHggrLVVVPyevsRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLG 731
Cdd:PRK08751   265 HIFALTANglVFMKIGGCNH---LISNP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGG 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  732 GEAL---VAERlrpWADRHGLdapELVNMYGITETTVHVTFHRLvraDLEDprRRGVIGRPLADLRVYVLDAAGRPVPPG 808
Cdd:PRK08751   338 GMAVqrsVAER---WKQVTGL---TLVEAYGLTETSPAACINPL---TLKE--YNGSIGLPIPSTDACIKDDAGTVLAIG 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  809 ATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVL 888
Cdd:PRK08751   407 EIGELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  889 TAHPAVAggavvpraaedgltQLVAYAVPAEEGG---------ADPA----GLRAHLAARLPAYMVPAACVLLDALPLTA 955
Cdd:PRK08751   480 AMMPGVL--------------EVAAVGVPDEKSGeivkvvivkKDPAltaeDVKAHARANLTGYKQPRIIEFRKELPKTN 545


                   ....
gi 1573930569  956 NGKL 959
Cdd:PRK08751   546 VGKI 549
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 1686-2203 6.09e-22

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: 103.55  E-value: 6.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1686 ALLRAAGRPDGEVVHVRAD----GSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGC------- 1754
Cdd:cd05967     55 ALDRHVEAGRGDQIALIYDspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACarigaih 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1755 --VLGGFVAVPLTV------PVSYATTSAAV--SKLEGIWEMLDRpwiVTSAAGEPGLRELAARREWSGLRLTTADAlre 1824
Cdd:cd05967    135 svVFGGFAAKELASriddakPKLIVTASCGIepGKVVPYKPLLDK---ALELSGHKPHHVLVLNRPQVPADLTKPGR--- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1825 epeDRDWYE----ARPDDLVL--------MLMTSGSTGLPKAV-RLTHRNVLTRAAATEAMNGLGSGDVSlnWIPLDhvT 1891
Cdd:cd05967    209 ---DLDWSEllakAEPVDCVPvaatdplyILYTSGTTGKPKGVvRDNGGHAVALNWSMRNIYGIKPGDVW--WAASD--V 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1892 GVVMFHLRDVY--LgcrqIHAPTSWILE-DPVRWPE------LADRHRVSVTW-APNfafgllAEQAHRFQDRDW----- 1956
Cdd:cd05967    282 GWVVGHSYIVYgpL----LHGATTVLYEgKPVGTPDpgafwrVIEKYQVNALFtAPT------AIRAIRKEDPDGkyikk 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1957 -DLSPVRLVMNAGE---VVVASAARRFLHVLapfglpqdvMHPGWGMSETCSVVTDSVLASEapDHDEAFVSCGLPYPGF 2032
Cdd:cd05967    352 yDLSSLRTLFLAGErldPPTLEWAENTLGVP---------VIDHWWQTETGWPITANPVGLE--PLPIKAGSPGKPVPGY 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2033 AMRVVDDQDALLPEGDVGRLQVR-----GTSVTHgYHDNARANAESFTED-GWFDTGDLAFL-RDGELYITGRAKDVIIV 2105
Cdd:cd05967    421 QVQVLDEDGEPVGPNELGNIVIKlplppGCLLTL-WKNDERFKKLYLSKFpGYYDTGDAGYKdEDGYLFIMGRTDDVINV 499

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2106 NGVNHYSHEIEACVEELPSVVRSftAAVAVRsDASAATDELALF-LRLAPGQDPAGALREIAGKVTREIGVSPAFLIPVE 2184
Cdd:cd05967    500 AGHRLSTGEMEESVLSHPAVAEC--AVVGVR-DELKGQVPLGLVvLKEGVKITAEELEKELVALVREQIGPVAAFRLVIF 576

                          570
                   ....*....|....*....
gi 1573930569 2185 AEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05967    577 VKRLPKTRSGKILRRTLRK 595
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1711-2202 7.53e-22

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: 101.68  E-value: 7.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvpvsyattsAAVSKLEGIWEMLdrp 1790
Cdd:cd17649     14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL----------DPEYPAERLRYML--- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 wivtsaagepglrelaarrEWSGLRLTTAdalreepedrdwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd17649     81 -------------------EDSGAGLLLT--------------HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGVvmfhlrdvylgcRQIHAP----TSWILEDPVRWP------ELADRHRVSVTWAPNFA 1940
Cdd:cd17649    128 ERYGLTPGDRELQFASFNFDGAH------------EQLLPPlicgACVVLRPDELWAsadelaEMVRELGVTVLDLPPAY 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1941 FGLLAEQAHRFQDRDWdlSPVRLVMNAGEVVVASAARRFlhvlapfgLPQDV-MHPGWGMSETcsVVTDSVLASEAPDHD 2019
Cdd:cd17649    196 LQQLAEEADRTGDGRP--PSLRLYIFGGEALSPELLRRW--------LKAPVrLFNAYGPTEA--TVTPLVWKCEAGAAR 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2020 E-AFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG-------WFDTGDLAFLR-D 2090
Cdd:cd17649    264 AgASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRdD 343

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2091 GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAVRSDASAATDELALFLRLAPGQDPAGALREIAGKVT 2170
Cdd:cd17649    344 GVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGV-----REAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALR 418

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1573930569 2171 REIgvsPAFLIP---VEAEAIPKTEIGKIQRTKLR 2202
Cdd:cd17649    419 ASL---PDYMVPahlVFLARLPLTPNGKLDRKALP 450
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 1719-2102 8.69e-22

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: 102.89  E-value: 8.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1719 ASRVLA---GLRRRGLRPGDRVILQCDDTEDFV-----ATLWGCVLGGFVAVPLTVPVSYATT-SAAVSKLEGIWEMLDR 1789
Cdd:cd17641     18 ADRVRAfalGLLALGVGRGDVVAILGDNRPEWVwaelaAQAIGALSLGIYQDSMAEEVAYLLNyTGARVVIAEDEEQVDK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1790 pwIVTSAAGEPGLR-----ELAARREWSGLRLTTADAL--------REEPE--DRDWYEARPDDLVLMLMTSGSTGLPKA 1854
Cdd:cd17641     98 --LLEIADRIPSVRyviycDPRGMRKYDDPRLISFEDVvalgraldRRDPGlyEREVAAGKGEDVAVLCTTSGTTGKPKL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1855 VRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPL----DHVTGVVMfhlrdvYLGCRQ-IHAPTS--------------WI 1915
Cdd:cd17641    176 AMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigEQMYSVGQ------ALVCGFiVNFPEEpetmmedlreigptFV 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 LEDPVRWPELADRHRVSV---TWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNA----GEVVVASAAR----------- 1977
Cdd:cd17641    250 LLPPRVWEGIAADVRARMmdaTPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLaswlADALLFRPLRdrlgfsrlrsa 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1978 ------------RFLHVLapfGLPqdvMHPGWGMSETCSVVTdsvlasEAPDHDEAFVSCGLPYPGFAMRVVDdqdallp 2045
Cdd:cd17641    330 atggaalgpdtfRFFHAI---GVP---LKQLYGQTELAGAYT------VHRDGDVDPDTVGVPFPGTEVRIDE------- 390

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2046 egdVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYITGRAKDV 2102
Cdd:cd17641    391 ---VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAKDV 445
PRK05857 PRK05857
fatty acid--CoA ligase;
482-966 9.78e-22

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 102.39  E-value: 9.78e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDT 561
Cdd:PRK05857    42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 A---GSGRLPATDARVVVVDDARTVAdlAGRAPHDLtDADRAGA---TGPYDTAYVIHTSGSTGRPKGVPVPHahvvRLF 635
Cdd:PRK05857   122 GskmASSAVPEALHSIPVIAVDIAAV--TRESEHSL-DAASLAGnadQGSEDPLAMIFTSGTTGEPKAVLLAN----RTF 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  636 EASGEHFRfGADDVWTLFHSYAFDFS---------VWELWGPLLHGGrLVVVPYEVSRSPREflrLLDEEKVTVLNQTPS 706
Cdd:PRK05857   195 FAVPDILQ-KEGLNWVTWVVGETTYSplpathiggLWWILTCLMHGG-LCVTGGENTTSLLE---ILTTNAVATTCLVPT 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  707 AFEQLVLADAATDRATGSLRYVVLGGEALVAERLRpWADRHGLDAPELvnmYGITETTVHVTfhrLVRADLEDPRR--RG 784
Cdd:PRK05857   270 LLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR-FIEATGVRTAQV---YGLSETGCTAL---CLPTDDGSIVKieAG 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  785 VIGRPLADLRVYVLDAAGR-PVPPGAT-----GEMYVSGPGVAPGYLNRPELTEErFLPDPFgapgtrmYRSGDLARWRP 858
Cdd:PRK05857   343 AVGRPYPGVDVYLAATDGIgPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAE-VLIDGW-------VNTGDLLERRE 414

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  859 DGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAV--VPRAAEDGLTQLVAYAVpAEEGGADPAGLRAHLAARL 936
Cdd:PRK05857   415 DGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACyeIPDEEFGALVGLAVVAS-AELDESAARALKHTIAARF 493

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569  937 ----PAYMVPAACVLLDALPLTANGKLDTAALPA 966
Cdd:PRK05857   494 rresEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 1704-2135 1.02e-21

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 101.90  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1704 DGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP----LTVP-VSY--ATTSAA 1776
Cdd:PRK08276     6 APSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPinwhLTAAeIAYivDDSGAK 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1777 VsklegiwemldrpwIVTSAAGEPGLRELAARREwSGLRLTTADALREEPEDR--DWYEARPDDLV-------LMLMTSG 1847
Cdd:PRK08276    86 V--------------LIVSAALADTAAELAAELP-AGVPLLLVVAGPVPGFRSyeEALAAQPDTPIadetagaDMLYSSG 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1848 STGLPKAVR--LTHRNVLTRAAATEAMNGL----GSGDVSLNWIPLDHvTGVVMFhlrdvylgCRQIHA--PTSWILE-- 1917
Cdd:PRK08276   151 TTGRPKGIKrpLPGLDPDEAPGMMLALLGFgmygGPDSVYLSPAPLYH-TAPLRF--------GMSALAlgGTVVVMEkf 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1918 DPVRWPELADRHRVSVT-WAPNFAFGLLA---EQAHRFqdrdwDLSPVRLVMNAGevvvasaarrflhvlAPFglPQDV- 1992
Cdd:PRK08276   222 DAEEALALIERYRVTHSqLVPTMFVRMLKlpeEVRARY-----DVSSLRVAIHAA---------------APC--PVEVk 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 --MHPGWGmsetcSVVTDSVLASEApdHDEAFVSCG--LPYPGFA-------MRVVDDQDALLPEGDVGRLQVRGTSVTH 2061
Cdd:PRK08276   280 raMIDWWG-----PIIHEYYASSEG--GGVTVITSEdwLAHPGSVgkavlgeVRILDEDGNELPPGEIGTVYFEMDGYPF 352

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2062 GYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAV 2135
Cdd:PRK08276   353 EYHNDPEKTAAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKV-----ADVAV 422
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 10-427 1.07e-21

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: 100.60  E-value: 1.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFlDTPDGPRAVRDGDPD-EMPVHR 88
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF-IEDGLGQPVQVVHRQaQVPVTE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   89 VDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPD-RFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG- 166
Cdd:cd19536     82 LDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYk 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 --EEPPPAGFesADRLAAEEAAYLgSDRHRRdraYWTERLAG-----LPEPVRLtdRTAPPRAPFLRRTAVLSPAETRAL 239
Cdd:cd19536    162 plSLPPAQPY--RDFVAHERASIQ-QAASER---YWREYLAGatlatLPALSEA--VGGGPEQDSELLVSVPLPVRSRSL 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  240 deaAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRL--GSAALRTPGTASDILPLRVAASaDTPVGGFVRAVAD 317
Cdd:cd19536    234 ---AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeeTTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQE 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  318 DLRGLRAHQRHRGESIRRDlgvlGRGRRVHGPVVNIVPFSEDLTF---GGHPSTSHHLSGGAVD---DLQISVRPGAEAD 391
Cdd:cd19536    310 QELESLSHEQVPLADIQRC----SEGEPLFDSIVNFRHFDLDFGLpewGSDEGMRRGLLFSEFKsnyDVNLSVLPKQDRL 385

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1573930569  392 TLWLAFDAHPdLYEEDGLALFlERFLKVLRELRTCP 427
Cdd:cd19536    386 ELKLAYNSQV-LDEEQAQRLA-AYYKSAIAELATAP 419
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 1670-2203 1.08e-21

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 102.36  E-value: 1.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1670 SEGPALPEPSVSGWAEALLRAAGRPDGEVVHVRADGSETRrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVA 1749
Cdd:PLN02330    17 SRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAV-TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1750 TLWGCVLGGFVavpltvpVSYATTSAAVSKLEGIWEMLDRPWIVTSAA--------GEP----GLRELAARREWSGLrLT 1817
Cdd:PLN02330    96 VALGIMAAGGV-------FSGANPTALESEIKKQAEAAGAKLIVTNDTnygkvkglGLPvivlGEEKIEGAVNWKEL-LE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1818 TADalrEEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATeaMNGLGS---GDV-SLNWIPLDHV--- 1890
Cdd:PLN02330   168 AAD---RAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS--LFSVGPemiGQVvTLGLIPFFHIygi 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1891 TGVVMFHLRD----VYLGCRQIHAPTSWILEDpvrwpeladrhrvSVTWAPNFAFGLLAEQAHRFQDrDWDLSPVRLvmn 1966
Cdd:PLN02330   243 TGICCATLRNkgkvVVMSRFELRTFLNALITQ-------------EVSFAPIVPPIILNLVKNPIVE-EFDLSKLKL--- 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1967 agEVVVASAARRFLHVLAPF--GLPQDVMHPGWGMSETcSVVTdsvLASEAPDHDEAFV---SCGLPYPGFAMRVVDDQD 2041
Cdd:PLN02330   306 --QAIMTAAAPLAPELLTAFeaKFPGVQVQEAYGLTEH-SCIT---LTHGDPEKGHGIAkknSVGFILPNLEVKFIDPDT 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2042 AL-LPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACV 2119
Cdd:PLN02330   380 GRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAIL 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2120 EELPSVVrsfTAAVAVRSDASAATDELA-LFLRLAPGQDPAGALREIAGKVTREIGVSPAFLIpveaEAIPKTEIGKIQR 2198
Cdd:PLN02330   460 LTHPSVE---DAAVVPLPDEEAGEIPAAcVVINPKAKESEEDILNFVAANVAHYKKVRVVQFV----DSIPKSLSGKIMR 532


                   ....*
gi 1573930569 2199 TKLRK 2203
Cdd:PLN02330   533 RLLKE 537
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 464-959 1.13e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 101.62  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  464 ARVAesPGRTAVSYA--GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHP 541
Cdd:PRK13390     7 AQIA--PDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  542 AERLALVMADAEPVAVVTDTAGSGrlpatdarvvvvddarTVADLAGRAPHDLTDADRAGATGPYDT------------- 608
Cdd:PRK13390    85 APEADYIVGDSGARVLVASAALDG----------------LAAKVGADLPLRLSFGGEIDGFGSFEAalagagprlteqp 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  609 --AYVIHTSGSTGRPKG---------VPVPHAHVVRLfeaSGEHFRFGADDVWtlFHSYAFDFSVWELWGPLLH--GGRL 675
Cdd:PRK13390   149 cgAVMLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVAI---ARAFYDISESDIY--YSSAPIYHAAPLRWCSMVHalGGTV 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  676 VVVPyevSRSPREFLRLLDEEKVTVLNQTPSAFEQLVL--ADAATDRATGSLRYVVLGGEALVAERLRPWADRHGldaPE 753
Cdd:PRK13390   224 VLAK---RFDAQATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG---PI 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  754 LVNMYGITETtvhvtfHRLVRADLED-PRRRGVIGRP-LADLrvYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELT 831
Cdd:PRK13390   298 VYEYYSSTEA------HGMTFIDSPDwLAHPGSVGRSvLGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  832 EERFLP-DPFGAPgtrmyrSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAED 906
Cdd:PRK13390   370 AAAQHPaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgvpdPEMGEQ 443

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  907 --GLTQLVAYAVPAEEGGADpagLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK13390   444 vkAVIQLVEGIRGSDELARE---LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1666-2159 1.33e-21

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 101.89  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1666 VPALSEGPALPEPSVSGWAEALLRAAGR-PDGEVVHVRADgsETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDT 1744
Cdd:PRK05852     1 MRFMGGAAPMASDFGPRIADLVEVAATRlPEAPALVVTAD--RIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1745 EDFVATLWGCVLGGFVAVPL--TVPVSYATTSAAVSKLEgiwemldrpwIVTSAAGEPGLRELAARREWSGLRLTTADAL 1822
Cdd:PRK05852    79 AEFVVALLAASRADLVVVPLdpALPIAEQRVRSQAAGAR----------VVLIDADGPHDRAEPTTRWWPLTVNVGGDSG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1823 REEPE---DRDWYEA-----------RPDDLVLMLmTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLD 1888
Cdd:PRK05852   149 PSGGTlsvHLDAATEptpatstpeglRPDDAMIMF-TGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLY 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1889 HVTGVVMFHLRDVYLGcRQIHAPTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLaeQAHRFQDRDWDLSPVRLVMNAG 1968
Cdd:PRK05852   228 HGHGLIAALLATLASG-GAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILL--ERAATEPSGRKPAALRFIRSCS 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1969 EVVVASAArrfLHVLAPFGLPqdvMHPGWGMSETCSVVTDSVLASEAPDHDEAfVSCGL--PYPGFAMRVVDDQDALLPE 2046
Cdd:PRK05852   305 APLTAETA---QALQTEFAAP---VVCAFGMTEATHQVTTTQIEGIGQTENPV-VSTGLvgRSTGAQIRIVGSDGLPLPA 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2047 GDVGRLQVRGTSVTHGYHDNARANAESFTeDGWFDTGDLAFL-RDGELYITGRAKDVI----------IVNGVNHYSHEI 2115
Cdd:PRK05852   378 GAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLsAAGDLSIRGRIKELInrggekispeRVEGVLASHPNV 456

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 2116 -EACVEELPSVV--RSFTAAVAVRSDASAATDELALFLR--LAPGQDPA 2159
Cdd:PRK05852   457 mEAAVFGVPDQLygEAVAAVIVPRESAPPTAEELVQFCRerLAAFEIPA 505
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 571-936 1.61e-21

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 100.22  E-value: 1.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  571 DARVVVVDDARTVADLAgRAP----HDLTDADRAG-ATGPYDTAYVIH-TSGSTGRPKGVP-------VPHAHVVRLFEA 637
Cdd:COG1541     43 DEAGVDPDDIKSLEDLA-KLPfttkEDLRDNYPFGlFAVPLEEIVRIHaSSGTTGKPTVVGytrkdldRWAELFARSLRA 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  638 SGehfrFGADDVwtLFHSYAFDFSVWelwGPLLHGG--RL--VVVPYEVSRSPREfLRLLDEEKVTVLNQTPSAFeqLVL 713
Cdd:COG1541    122 AG----VRPGDR--VQNAFGYGLFTG---GLGLHYGaeRLgaTVIPAGGGNTERQ-LRLMQDFGPTVLVGTPSYL--LYL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  714 ADAA----TDRATGSLRYVVLGGEALvAERLRPW-ADRHGLDApelVNMYGITETTVHVTFhrlvradlEDPRRRGVIgr 788
Cdd:COG1541    190 AEVAeeegIDPRDLSLKKGIFGGEPW-SEEMRKEiEERWGIKA---YDIYGLTEVGPGVAY--------ECEAQDGLH-- 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  789 pLADLRVYV--LD-AAGRPVPPGATGEMYVSGpgvapgylnrpeLTEErflpdpfGAPGTRmYRSGDLARWRPDG----- 860
Cdd:COG1541    256 -IWEDHFLVeiIDpETGEPVPEGEEGELVVTT------------LTKE-------AMPLIR-YRTGDLTRLLPEPcpcgr 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  861 TLV----HAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGG--AVVPRaaEDGLTQLVayaVPAE-EGGADPAGLRAHLA 933
Cdd:COG1541    315 THPrigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDR--EGGLDELT---VRVElAPGASLEALAEAIA 389


                   ...
gi 1573930569  934 ARL 936
Cdd:COG1541    390 AAL 392
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
594-964 2.40e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 98.58  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  594 LTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVrlfeASGE--HFRFGADDVWTLF---HSYAfDFSVweLWGP 668
Cdd:PRK07824    23 LRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALT----ASADatHDRLGGPGQWLLAlpaHHIA-GLQV--LVRS 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  669 LLHGGRLVVVP----YEVSRSPREFLRLLDEEKVTVLNQTpsafeQLV--LADAATDRATGSLRYVVLGGEALVAerlrP 742
Cdd:PRK07824    96 VIAGSEPVELDvsagFDPTALPRAVAELGGGRRYTSLVPM-----QLAkaLDDPAATAALAELDAVLVGGGPAPA----P 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  743 WADRHGLDAPELVNMYGITETTVHVTFHrlvradledprrrgviGRPLADLRVYVLDaagrpvppgatGEMYVSGPGVAP 822
Cdd:PRK07824   167 VLDAAAAAGINVVRTYGMSETSGGCVYD----------------GVPLDGVRVRVED-----------GRIALGGPTLAK 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  823 GYLNRPElteerflPDPFGAPGtrMYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPr 902
Cdd:PRK07824   220 GYRNPVD-------PDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFG- 288

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  903 AAEDGLTQLVAYAVPAEEGGAD-PAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK07824   289 LPDDRLGQRVVAAVVGDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1836-2201 3.37e-21

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: 99.63  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLD---HVTGVVMFHLRdvylGCRQIHAPT 1912
Cdd:cd17652     92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSfdaSVWELLMALLA----GATLVLAPA 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 swilEDPVRWPELAD---RHRVSVTWAPNFAFGLLAEQahrfqdrdwDLSPVRLVMNAGEVVVASAARRFlhvlapfgLP 1989
Cdd:cd17652    168 ----EELLPGEPLADllrEHRITHVTLPPAALAALPPD---------DLPDLRTLVVAGEACPAELVDRW--------AP 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1990 QDVMHPGWGMSETCSVVTdsvlaSEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARA 2069
Cdd:cd17652    227 GRRMINAYGPTETTVCAT-----MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGL 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2070 NAESFTEDGW-------FDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASA 2141
Cdd:cd17652    302 TAERFVADPFgapgsrmYRTGDLARWRaDGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE---AVVVVRDDRPG 378

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2142 ATDELALFLRLAPGQDPAGALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd17652    379 DKRLVAYVVPAPGAAPTAAELRAHLAERL------PGYMVPaafVVLDALPLTPNGKLDRRAL 435
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1837-2201 7.36e-21

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 99.72  E-value: 7.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVL--TRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTSw 1914
Cdd:PRK06710   206 NDLALLQYTGGTTGFPKGVMLTHKNLVsnTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKF- 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1915 ileDPVRWPELADRHRVSV-TWAPNFAFGLLAEQAHRfqdrDWDLSPVRLVMNAGEVVVASAARRFLHVLApfglpqDVM 1993
Cdd:PRK06710   285 ---DMKMVFEAIKKHKVTLfPGAPTIYIALLNSPLLK----EYDISSIRACISGSAPLPVEVQEKFETVTG------GKL 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1994 HPGWGMSETCSVVTDSVL-ASEAPDhdeafvSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANA 2071
Cdd:PRK06710   352 VEGYGLTESSPVTHSNFLwEKRVPG------SIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2072 eSFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEE-----------LPSVVRSFT--AAVAVRS 2137
Cdd:PRK06710   426 -AVLQDGWLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEhekvqevvtigVPDPYRGETvkAFVVLKE 504

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2138 DASAATDELALFLRlapgqdpagalREIAgkvtreigvspAFLIPVEAE---AIPKTEIGKIQRTKL 2201
Cdd:PRK06710   505 GTECSEEELNQFAR-----------KYLA-----------AYKVPKVYEfrdELPKTTVGKILRRVL 549
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1832-2203 8.12e-21

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: 98.15  E-value: 8.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNW--IPLDHVTGVVMFHLrdvylgCrqiH 1909
Cdd:cd17653    100 TTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVlsIAFDACIGEIFSTL------C---N 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1910 APTSWILEDPVRWPELADRhrVSVTWA-PNFAFGLlaeqahrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVLapfgl 1988
Cdd:cd17653    171 GGTLVLADPSDPFAHVART--VDALMStPSILSTL----------SPQDFPNLKTIFLGGEAVPPSLLDRWSPGR----- 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1989 pqdVMHPGWGMSE-TCSVVTDSVLaseapdhDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNA 2067
Cdd:cd17653    234 ---RLYNAYGPTEcTISSTMTELL-------PGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNP 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2068 RANAESFTEDGW------FDTGDLAFL-RDGELYITGRAKDVIIVNG--VNHYshEIEACVEELPSVVRSftAAVAVRSD 2138
Cdd:cd17653    304 ALTASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQVKVRGfrINLE--EIEEVVLQSQPEVTQ--AAAIVVNG 379

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2139 AsaatdeLALFlrLAPGQDPAGALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd17653    380 R------LVAF--VTPETVDVDGLRSELAKHL------PSYAVPdriIALDSFPLTANGKVDRKALRE 433
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1698-2196 8.19e-21

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: 99.57  E-value: 8.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1698 VVHVRADGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGC---------VLGGFVAVPLTVP 1767
Cdd:cd17634     72 IIYEGDDTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACarigavhsvIFGGFAPEAVAGR 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1768 VSYATTSAAVSKLEGI--WEMLDRPWIVTSAA---GEPGLRELAARRE-----WSGLR------LTTADALREEPEDRDw 1831
Cdd:cd17634    152 IIDSSSRLLITADGGVraGRSVPLKKNVDDALnpnVTSVEHVIVLKRTgsdidWQEGRdlwwrdLIAKASPEHQPEAMN- 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 yearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEA-MNGLGSGDVSlnWIPLDhvTGVVMFHLRDVYLGCrqIHA 1910
Cdd:cd17634    231 ----AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGPGDIY--WCTAD--VGWVTGHSYLLYGPL--ACG 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 PTSWILE------DPVRWPELADRHRVSVTW-APNfafgllAEQAHRFQDRDW----DLSPVRLVMNAGEVVVASAARRF 1979
Cdd:cd17634    301 ATTLLYEgvpnwpTPARMWQVVDKHGVNILYtAPT------AIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWY 374

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1980 LHVLAPFGLPqdvMHPGWGMSETCSVVTDSVLASEAPDHDEAFVscglPYPGFAMRVVDDQDALLPEGDVGRLQVR---- 2055
Cdd:cd17634    375 WKKIGKEKCP---VVDTWWQTETGGFMITPLPGAIELKAGSATR----PVFGVQPAVVDNEGHPQPGGTEGNLVITdpwp 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2056 GTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAV- 2133
Cdd:cd17634    448 GQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIp 527

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2134 -AVRSDASAAtdelalFLRLAPGQDPAGALR-EIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKI 2196
Cdd:cd17634    528 hAIKGQAPYA------YVVLNHGVEPSPELYaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 470-1073 1.21e-20

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: 100.16  E-value: 1.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  470 PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVM 549
Cdd:COG3319      3 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  550 ADAEPVAVVTDTAGSGRLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGVPVPHA 629
Cdd:COG3319     83 ALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVVRLFEASGEHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRLVVVPYEVSRSPREFLRLLDEEKVTVLNQTPSAFE 709
Cdd:COG3319    163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  710 QLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDAPELVNMYGITETTVHVTFHrLVRADLEDPRRRGVIGRP 789
Cdd:COG3319    243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTT-AAAAAPGVAGALGPIGGG 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  790 LADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAGRAD 869
Cdd:COG3319    322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  870 QQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLD 949
Cdd:COG3319    402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  950 ALPLTANGKLDTAALPAPDFGGGTGGAPPATPEERLVCGLFEEVLRLpaDSVGTGGNFFDLGGHSLLATRLLARLRERTG 1029
Cdd:COG3319    482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGL--GLVGDDDDFFGGGGGSLLALLLLLLLLALLL 559

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1573930569 1030 TDVPISALFDTPTPAALAERLTAGADAGRPLPALTASERPSLVP 1073
Cdd:COG3319    560 RLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPP 603
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 1711-2207 1.33e-20

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 98.76  E-value: 1.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRR-GLRPGDRVILQCDDTEDF-VATLWGCVLGGFVAV--PLTVP------VSYATTSAAVSKL 1780
Cdd:PLN02574    68 SYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFpVIFLAVLSLGGIVTTmnPSSSLgeikkrVVDCSVGLAFTSP 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1781 EGIWEM--LDRPWIVTSAAG--EPGLRELAARREwsgLRLTTADALREEPedrdwyeARPDDLVLMLMTSGSTGLPKAVR 1856
Cdd:PLN02574   148 ENVEKLspLGVPVIGVPENYdfDSKRIEFPKFYE---LIKEDFDFVPKPV-------IKQDDVAAIMYSSGTTGASKGVV 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1857 LTHRNVLT------RAAATEAMNGlGSGDVSLNWIPLDHVTGVVMFHLRDVYLGcRQIHAPTSWILEDPVRwpelaDRHR 1930
Cdd:PLN02574   218 LTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSLG-STIVVMRRFDASDMVK-----VIDR 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1931 VSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQdvmhpGWGMSETCSVVTDSV 2010
Cdd:PLN02574   291 FKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ-----GYGMTESTAVGTRGF 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2011 LASEApdhdEAFVSCGLPYPGFAMRVVD-DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FL 2088
Cdd:PLN02574   366 NTEKL----SKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAyFD 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2089 RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAATDELALFLRlapGQDPAGALREIAGK 2168
Cdd:PLN02574   442 EDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEII---DAAVTAVPDKECGEIPVAFVVR---RQGSTLSQEAVINY 515

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1573930569 2169 VTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:PLN02574   516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 1690-2098 1.41e-20

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: 98.66  E-value: 1.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVHVRADGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPltVPV 1768
Cdd:cd05921      5 ARQAPDRTWLAEREGNGGWRRvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAP--VSP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 SYATTSAAVSKLEGIWEMLdRPWIVTSAAGEPGLRELAA-----------RREWSGLRLTTADALREEPEDRDWYEAR-- 1835
Cdd:cd05921     83 AYSLMSQDLAKLKHLFELL-KPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGRGAISFAELAATPPTAAVDAAFaa 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 --PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGD--VSLNWIPLDHVTGV-VMFHLRDVYLGCRQIHA 1910
Cdd:cd05921    162 vgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGnHNFNLVLYNGGTLYIDD 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 --PTSWILEDPVRwpelaDRHRVSVTWAPNF--AFGLLAEQ-------AHRFQDRdwdlspVRLVMNAG----------- 1968
Cdd:cd05921    242 gkPMPGGFEETLR-----NLREISPTVYFNVpaGWEMLVAAlekdealRRRFFKR------LKLMFYAGaglsqdvwdrl 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1969 -EVVVASAARRFlhvlapfglpqdVMHPGWGMSETCSVVTDSVLASEAPDHdeafvsCGLPYPGFAMRVVddqdallPEG 2047
Cdd:cd05921    311 qALAVATVGERI------------PMMAGLGATETAPTATFTHWPTERSGL------IGLPAPGTELKLV-------PSG 365

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 2048 DVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLRDGE-----LYITGR 2098
Cdd:cd05921    366 GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPDdpakgLVFDGR 421
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1838-2198 1.51e-20

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: 95.55  E-value: 1.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHvTGVVMFHLRDVYLGcRQIHAPTSWile 1917
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLG-GTFIGQRKF--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1918 DPVRWPELADRHRVSVTW-APNFAFGLLAEQAHrfqdrdwdLSPVRLVMNAGEVVVASAARRFLHvlapfGLPQDVMHPG 1996
Cdd:cd17633     76 NPKSWIRKINQYNATVIYlVPTMLQALARTLEP--------ESKIKSIFSSGQKLFESTKKKLKN-----IFPKANLIEF 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETcSVVTDSVLASEAPDHdeafvSCGLPYPGFAMRVVDDQDallpeGDVGRLQVRGTSVTHGYHDnaranAESFTE 2076
Cdd:cd17633    143 YGTSEL-SFITYNFNQESRPPN-----SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVR-----GGFSNP 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2077 DGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAAtdELALFLRLAPG 2155
Cdd:cd17633    207 DGWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIE---EAIVVGIPDARFG--EIAVALYSGDK 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1573930569 2156 QDPAGALREIAGKVTR-EIgvsPAFLIPVeaEAIPKTEIGKIQR 2198
Cdd:cd17633    282 LTYKQLKRFLKQKLSRyEI---PKKIIFV--DSLPYTSSGKIAR 320
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 8-280 2.76e-20

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: 96.62  E-value: 2.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    8 RRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALR---------RTVREADTFALRFLDTPDGPRAVRD 78
Cdd:cd20484      1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQfvleqhpilKSVIEEEDGVPFQKIEPSKPLSFQE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   79 GD-----PDEMPVHrvdvsgeadpaaaaeewIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVA 153
Cdd:cd20484     81 EDisslkESEIIAY-----------------LREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLI 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  154 RRLADTYTALAAGEEPPPAGF-ESADRLAAEEAAYLGSDRHRRDRAYWTERLAG-LPEPVRLTDRTAPPRAPFLRRT--A 229
Cdd:cd20484    144 HSLLDAYQALLQGKQPTLASSpASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGtLPILELPADRPRSSAPSFEGQTytR 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  230 VLSPAETRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSR 280
Cdd:cd20484    224 RLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR 274
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 1840-2146 2.78e-20

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: 94.68  E-value: 2.78e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1840 VLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVtGVVMFHLRDVYLGCRQIHAPTSwileDP 1919
Cdd:cd17636      3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRV----DA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1920 VRWPELADRHRVsvTWApnFAFGLLAEQAHRF-QDRDWDLSPVRLVmnagevvvaSAARRFLHVLAPFGLPQDVMHPGWG 1998
Cdd:cd17636     78 EEVLELIEAERC--THA--FLLPPTIDQIVELnADGLYDLSSLRSS---------PAAPEWNDMATVDTSPWGRKPGGYG 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1999 MSETCSVVTDSVLAseapdhDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTeDG 2078
Cdd:cd17636    145 QTEVMGLATFAALG------GGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-GG 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2079 WFDTGDLAfLR--DGELYITGrAKDVIIVNGV-NHYSHEIEACVEELPSV-------------VRSFTAAVAVRSDASAA 2142
Cdd:cd17636    218 WHHTNDLG-RRepDGSLSFVG-PKTRMIKSGAeNIYPAEVERCLRQHPAVadaavigvpdprwAQSVKAIVVLKPGASVT 295


                   ....
gi 1573930569 2143 TDEL 2146
Cdd:cd17636    296 EAEL 299
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1690-2201 3.64e-20

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: 96.62  E-value: 3.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVHVrADGSETrrsYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvs 1769
Cdd:cd12115      9 AARTPDAIALVC-GDESLT---YAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD---- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1770 yatTSAAVSKLEGIwemldrpwivtsaagepgLRELAARrewsgLRLTTadalreepedrdwyearPDDLVLMLMTSGST 1849
Cdd:cd12115     81 ---PAYPPERLRFI------------------LEDAQAR-----LVLTD-----------------PDDLAYVIYTSGST 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1850 GLPKAVRLTHRNVLTRaaateamnglgsgdvsLNW----IPLDHVTGV-----VMFHLRDVYLGCRQIHAPTSWILEDPV 1920
Cdd:cd12115    118 GRPKGVAIEHRNAAAF----------------LQWaaaaFSAEELAGVlastsICFDLSVFELFGPLATGGKVVLADNVL 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1921 RWPELADRHRVS-VTWAPNFAFGLLAEQAhrfqdrdwdLSP-VRLVMNAGEVVVASAARRfLHVLapfgLPQDVMHPGWG 1998
Cdd:cd12115    182 ALPDLPAAAEVTlINTVPSAAAELLRHDA---------LPAsVRVVNLAGEPLPRDLVQR-LYAR----LQVERVVNLYG 247

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1999 MSETCSVVTdsvlASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG 2078
Cdd:cd12115    248 PSEDTTYST----VAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDP 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2079 WFD------TGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATDELALFLR 2151
Cdd:cd12115    324 FGPgarlyrTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV----REAVVVAIGDAAGERRLVAYIV 399

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2152 LAPGQdpAGALREIAGKVTREIgvsPAFLIPVEA---EAIPKTEIGKIQRTKL 2201
Cdd:cd12115    400 AEPGA--AGLVEDLRRHLGTRL---PAYMVPSRFvrlDALPLTPNGKIDRSAL 447
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1082-1495 7.23e-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: 95.40  E-value: 7.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1082 WFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVADRHESLRTVFGEEDGAIHQRVLPPGTLRPELHVVDCPDEERA 1161
Cdd:cd19534     10 WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEVVDLSSLAQA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1162 AHVAAAM---RRSFDLTRDSALWAGVF-GTGDTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWaPPALQYA 1237
Cdd:cd19534     90 AAIEALAaeaQSSLDLEEGPLLAAALFdGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPL-PSKTSFQ 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1238 DFALWQRRvLAPAPEgpgrLERLTSFWRQALDGLPEEsapppDRPRPAAPSGRGGGVTVPLDAGTHRELLRLAdheNASL 1317
Cdd:cd19534    169 TWAELLAE-YAQSPA----LLEELAYWRELPAADYWG-----LPKDPEQTYGDARTVSFTLDEEETEALLQEA---NAAY 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1318 FM----VLHGALALLLNRWGAGDDIVVGTPVAGRtEPALDEV-----VGLLTNTLVLRADASGDPTFRELLARVRAfDVQ 1388
Cdd:cd19534    236 RTeindLLLAALALAFQDWTGRAPPAIFLEGHGR-EEIDPGLdlsrtVGWFTSMYPVVLDLEASEDLGDTLKRVKE-QLR 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1389 ALDHQDLPFDRLvEEVNPRRHP--ARHPLFQVML--------ALQNNERAVLTLGEDRVPLRPAATGTAKFDLFVDVler 1458
Cdd:cd19534    314 RIPNKGIGYGIL-RYLTPEGTKrlAFHPQPEISFnylgqfdqGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVV--- 389

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1573930569 1459 hgADGTadgLDLHVEYAADLYDPATAERFAGALRDLL 1495
Cdd:cd19534    390 --EGGQ---LVITVSYSRNMYHEETIQQLADSYKEAL 421
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 1670-2210 7.56e-20

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 96.38  E-value: 7.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1670 SEGPALPEPSVS---GWAEALLR-AAGRPDGevVHVRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRV-ILQCDDT 1744
Cdd:PRK07786     3 ALTLAQEQPYLArrqNWVNQLARhALMQPDA--PALRFLGNTT--TWRELDDRVAALAGALSRRGVGFGDRVlILMLNRT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1745 EDFVATLWGCVLGGfvavpLTVPVSYATTSAAVSKL---EGIWEMLDRPWIVTSAAG----EPGLRE-LAARREWSGLRL 1816
Cdd:PRK07786    79 EFVESVLAANMLGA-----IAVPVNFRLTPPEIAFLvsdCGAHVVVTEAALAPVATAvrdiVPLLSTvVVAGGSSDDSVL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1817 TTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSG-DVSLNWIPLDHVTGVVM 1895
Cdd:PRK07786   154 GYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1896 FhLRDVYLGCRQIHAPTSWIleDPVRWPELADRHRV-SVTWAPNFAFGLLAEQAHRFQDR-----DWDLSPvrlvmnAGE 1969
Cdd:PRK07786   234 M-LPGLLLGAPTVIYPLGAF--DPGQLLDVLEAEKVtGIFLVPAQWQAVCAEQQARPRDLalrvlSWGAAP------ASD 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1970 VVVASAARRF--LHVLAPFGlpQDVMHPgwgmsETCSVVTDSVLASEApdhdeafvSCGLPYPGFAMRVVDDQDALLPEG 2047
Cdd:PRK07786   305 TLLRQMAATFpeAQILAAFG--QTEMSP-----VTCMLLGEDAIRKLG--------SVGKVIPTVAARVVDENMNDVPVG 369

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2048 DVGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV 2126
Cdd:PRK07786   370 EVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQdEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIV 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 RSFT-------------AAVAVRSDASAAT-DELALFL--RLAPGQdpagalreiagkvtreigvSPAFLIPVeaEAIPK 2190
Cdd:PRK07786   449 EVAVigradekwgevpvAVAAVRNDDAALTlEDLAEFLtdRLARYK-------------------HPKALEIV--DALPR 507

                          570       580
                   ....*....|....*....|
gi 1573930569 2191 TEIGKIQRTKLRKSFEAGEF 2210
Cdd:PRK07786   508 NPAGKVLKTELRERYGACVN 527
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 1685-2208 1.07e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 96.12  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGRPDGEVVHVR--ADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV 1762
Cdd:PRK04319    47 EAIDRHADGGRKDKVALRylDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVG 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 PL-----TVPVSYATTSAAVSKLEGIWEMLDRpwIVtsAAGEPGLREL---AARREWSGLRLTTADALREEPEDRDWYEA 1834
Cdd:PRK04319   127 PLfeafmEEAVRDRLEDSEAKVLITTPALLER--KP--ADDLPSLKHVllvGEDVEEGPGTLDFNALMEQASDEFDIEWT 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSlnWIPLDH--VTGVvmfhlrdVYlgcrQIHAP- 1911
Cdd:PRK04319   203 DREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVY--WCTADPgwVTGT-------SY----GIFAPw 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1912 ----TSWILE---DPVRWPELADRHRVSVtW--APNfAFGLL----AEQAHRFqdrdwDLSPVRLVMNAGEVVVASAARR 1978
Cdd:PRK04319   270 lngaTNVIDGgrfSPERWYRILEDYKVTV-WytAPT-AIRMLmgagDDLVKKY-----DLSSLRHILSVGEPLNPEVVRW 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1979 FLHVlapFGLPqdvMHPGWGMSEtcsvvTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRG-- 2056
Cdd:PRK04319   343 GMKV---FGLP---IHDNWWMTE-----TGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgw 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2057 TSVTHGY-HDNARanAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAV- 2133
Cdd:PRK04319   412 PSMMRGIwNNPEK--YESYFAGDWYVSGDSAYMdEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAE---AGVi 486

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2134 ----AVRSDASAAtdelalFLRLAPGQDPAGALR-EIAGKVTREIGVSPAfliPVE---AEAIPKTEIGKIQRtKLRKSF 2205
Cdd:PRK04319   487 gkpdPVRGEIIKA------FVALRPGYEPSEELKeEIRGFVKKGLGAHAA---PREiefKDKLPKTRSGKIMR-RVLKAW 556


                   ...
gi 1573930569 2206 EAG 2208
Cdd:PRK04319   557 ELG 559
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
607-959 1.11e-19

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 95.89  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  607 DTAYVIHTSGSTGRPKGVPVPHAHVV-RLFEASGEH---FRFGADDVWT---LFHSYAFDFSVwelwgpLLH---GGRLV 676
Cdd:PRK08974   207 DLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYgplLHPGKELVVTalpLYHIFALTVNC------LLFielGGQNL 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  677 VVPyevsrSPRE---FLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEAL---VAERlrpWadrHGLD 750
Cdd:PRK08974   281 LIT-----NPRDipgFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVqqaVAER---W---VKLT 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  751 APELVNMYGITETTVHVTFHRLvraDLEDprRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPEL 830
Cdd:PRK08974   350 GQYLLEGYGLTECSPLVSVNPY---DLDY--YSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEA 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  831 TEErFLPDPFGApgtrmyrSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGlTQ 910
Cdd:PRK08974   425 TDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVS-GE 495

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569  911 LVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK08974   496 AVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 1834-2102 1.50e-19

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: 95.36  E-value: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1834 ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA----TEAMNGLGSGDVSLNWIPLDHVTGVVMFHLrDVYLGCRqI- 1908
Cdd:cd05927    111 PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLEILNKINPTDVYISYLPLAHIFERVVEAL-FLYHGAK-Ig 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 --HAPTSWILED------------PVRWPELADRHRVSVT-------WAPNFAF----GLLAEqAHRFQDRDWDlspvRL 1963
Cdd:cd05927    189 fySGDIRLLLDDikalkptvfpgvPRVLNRIYDKIFNKVQakgplkrKLFNFALnyklAELRS-GVVRASPFWD----KL 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1964 VMN------AGEV---VVASAA-----RRFLHVLapFGLPqdVMHpGWGMSETCSVVTDSVLASEAPDHdeafvsCGLPY 2029
Cdd:cd05927    264 VFNkikqalGGNVrlmLTGSAPlspevLEFLRVA--LGCP--VLE-GYGQTECTAGATLTLPGDTSVGH------VGGPL 332

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2030 PGFAMRVVD------DQDALLPEGDVgrlQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYITGRAKDV 2102
Cdd:cd05927    333 PCAEVKLVDvpemnyDAKDPNPRGEV---CIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGeWLPNGTLKIIDRKKNI 409
PLN02246 PLN02246
4-coumarate--CoA ligase
 461-919 1.64e-19

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 95.43  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  461 LFEaRVAESPGRTAV--SYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDP 538
Cdd:PLN02246    29 CFE-RLSEFSDRPCLidGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  539 GHPAERLALVMADAEPVAVVTDTAGSGRLPA----TDARVVVVDDAR----TVADLAGRAPHDLTDADragaTGPYDTAY 610
Cdd:PLN02246   108 FYTPAEIAKQAKASGAKLIITQSCYVDKLKGlaedDGVTVVTIDDPPegclHFSELTQADENELPEVE----ISPDDVVA 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  611 VIHTSGSTGRPKGVPVPH----AHVVRLFEASGEHFRFGADD----VWTLFHSYAFDfSVweLWGPLLHGGRLVVVP-YE 681
Cdd:PLN02246   184 LPYSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFHSDDvilcVLPMFHIYSLN-SV--LLCGLRVGAAILIMPkFE 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  682 VSRspreFLRLLDEEKVTVLNQTPSafeqLVLADAATDRAT----GSLRyVVLGGEALVAERLRPwADRHGLDAPELVNM 757
Cdd:PLN02246   261 IGA----LLELIQRHKVTIAPFVPP----IVLAIAKSPVVEkydlSSIR-MVLSGAAPLGKELED-AFRAKLPNAVLGQG 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  758 YGITETTvHVTFHRLVRADLEDPRRRGVIGRPLADLRVYVLDA-AGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFL 836
Cdd:PLN02246   331 YGMTEAG-PVLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATANTID 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  837 PDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAV 916
Cdd:PLN02246   410 KDGW-------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482


                   ...
gi 1573930569  917 PAE 919
Cdd:PLN02246   483 RSN 485
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 1835-2098 1.87e-19

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 96.53  E-value: 1.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQI-HA-PT 1912
Cdd:PRK08633   780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVyHPdPT 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 swileDPVRWPELADRHRVSVTWA-PNFaFGLLAeqahrfqdRDWDLSPvrLVMNAGEVVVASAARrflhvlapfgLPQD 1991
Cdd:PRK08633   860 -----DALGIAKLVAKHRATILLGtPTF-LRLYL--------RNKKLHP--LMFASLRLVVAGAEK----------LKPE 913

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1992 V---------MHP--GWGMSETCSVVTDSVlaseaPDHDEAFV---------SCGLPYPGFAMRVVD-DQDALLPEGDVG 2050
Cdd:PRK08633   914 VadafeekfgIRIleGYGATETSPVASVNL-----PDVLAADFkrqtgskegSVGMPLPGVAVRIVDpETFEELPPGEDG 988

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2051 RLQVRGTSVTHGYHDNARANAESFTE---DGWFDTGDLAFL-RDGELYITGR 2098
Cdd:PRK08633   989 LILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLdEDGFLTITDR 1040
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 604-920 2.43e-19

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 94.88  E-value: 2.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 GPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLF----HSYAFDFSVweLWgPLLhGGRLVVVP 679
Cdd:PRK06334   181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFlppfHAYGFNSCT--LF-PLL-SGVPVVFA 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  680 YEvSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALvAERLRPWADRhglDAPELV--NM 757
Cdd:PRK06334   257 YN-PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAF-KDSLYQEALK---TFPHIQlrQG 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  758 YGITETTVHVTFHrlvraDLEDPRRRGVIGRPLADLRVYVLDAAGR-PVPPGATGEMYVSGPGVAPGYLnrpeltEERFL 836
Cdd:PRK06334   332 YGTTECSPVITIN-----TVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYL------GEDFG 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  837 PDPFGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHpavaggavVPRAAEDGLTQLVAYAV 916
Cdd:PRK06334   401 QGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGPLVVCGL 472


                   ....
gi 1573930569  917 PAEE 920
Cdd:PRK06334   473 PGEK 476
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 483-964 3.00e-19

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 94.43  E-value: 3.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDT- 561
Cdd:PRK06018    41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLt 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 ------AGSGRLPATDARVVVVDDARTVAD-----LAGRAPHDLTDADRAGATGPYDTAYVI-HTSGSTGRPKGVPVPHA 629
Cdd:PRK06018   121 fvpileKIADKLPSVERYVVLTDAAHMPQTtlknaVAYEEWIAEADGDFAWKTFDENTAAGMcYTSGTTGDPKGVLYSHR 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  630 HVV--RLFEASGEHFRFGADD----VWTLFHSYAfdfsvwelWGPLLHG---GRLVVVP---------YEvsrspreflr 691
Cdd:PRK06018   201 SNVlhALMANNGDALGTSAADtmlpVVPLFHANS--------WGIAFSApsmGTKLVMPgakldgasvYE---------- 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  692 LLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADrhgLDApELVNMYGITETTVHVTFHR 771
Cdd:PRK06018   263 LLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFED---MGV-EVRHAWGMTEMSPLGTLAA 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  772 LVR--ADLEDPRRRGVI---GRPLADLRVYVLDAAGRPVP--PGATGEMYVSGPGVAPGYLNRPE--LTEERFlpdpfga 842
Cdd:PRK06018   339 LKPpfSKLPGDARLDVLqkqGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF------- 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  843 pgtrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGLtqLVAYAVPA 918
Cdd:PRK06018   412 -----FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgvyhPKWDERPL--LIVQLKPG 484

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569  919 EEggADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK06018   485 ET--ATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1832-2201 4.00e-19

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: 93.69  E-value: 4.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 YEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT-EAMNGLGSGDVslnwipLDHVT---GVVMFHLRDVYLGCRQ 1907
Cdd:cd17656    123 YINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFErEKTNINFSDKV------LQFATcsfDVCYQEIFSTLLSGGT 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 IHAPTSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAEQ---AHRFQDRdwdlspVRLVMNAGE-VVVASAARRFLHVl 1983
Cdd:cd17656    197 LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSErefINRFPTC------VKHIITAGEqLVITNEFKEMLHE- 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1984 apfglPQDVMHPGWGMSETcSVVTDSVLASEapDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGY 2063
Cdd:cd17656    270 -----HNVHLHNHYGPSET-HVVTTYTINPE--AEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGY 341

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2064 HDNARANAESFTEDGW------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVR 2136
Cdd:cd17656    342 LNRQELTAEKFFPDPFdpnermYRTGDLArYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE---AVVLDK 418

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2137 SDASAATDELALFLRLApgQDPAGALREIAGKVTREIGVsPAFLIPVeaEAIPKTEIGKIQRTKL 2201
Cdd:cd17656    419 ADDKGEKYLCAYFVMEQ--ELNISQLREYLAKQLPEYMI-PSFFVPL--DQLPLTPNGKVDRKAL 478
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 499-959 5.03e-19

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 94.04  E-value: 5.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  499 VEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD----PGHpAERLALVMADAEPVAVVTDTAGSG-------RL 567
Cdd:PRK12476    85 LQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGH-AERLDTALRDAEPTVVLTTTAAAEavegflrNL 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  568 PATDA-RVVVVDDA-RTVADLAGRAPHDlTDadragatgpyDTAYVIHTSGSTGRPKGVPVPH----AHVVRLFEASGEH 641
Cdd:PRK12476   164 PRLRRpRVIAIDAIpDSAGESFVPVELD-TD----------DVSHLQYTSGSTRPPVGVEITHravgTNLVQMILSIDLL 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  642 FRFGADDVW-TLFHsyafDFSVWELWGPLLHGGRLVVV-PYEVSRSPREFLRLLDEEKVT--VLNQTPS-AFEQLVLADA 716
Cdd:PRK12476   233 DRNTHGVSWlPLYH----DMGLSMIGFPAVYGGHSTLMsPTAFVRRPQRWIKALSEGSRTgrVVTAAPNfAYEWAAQRGL 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  717 ATDRATGSLRYVVL--GGEALVAERLRPWADR---HGLDAPELVNMYGITETTVHV-------------------TFHRL 772
Cdd:PRK12476   309 PAEGDDIDLSNVVLiiGSEPVSIDAVTTFNKAfapYGLPRTAFKPSYGIAEATLFVatiapdaepsvvyldreqlGAGRA 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  773 VRADLEDPRRR-----GVIGRPLadLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERF-------LPDPF 840
Cdd:PRK12476   389 VRVAADAPNAVahvscGQVARSQ--WAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAEGS 466

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  841 GAPGT----RMYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEA-VLTAHPAVAGGAVvpraaedgltqlVAYA 915
Cdd:PRK12476   467 HADGAaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRGYV------------TAFT 533

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  916 VPAEEGG--------------ADPA----GLRAHLAARlpaYMVPAACVLL---DALPLTANGKL 959
Cdd:PRK12476   534 VPAEDNErlvivaeraagtsrADPApaidAIRAAVSRR---HGLAVADVRLvpaGAIPRTTSGKL 595
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 1690-2202 5.08e-19

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: 93.71  E-value: 5.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGE-VVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFvatlWGCVLG----GFVAVPL 1764
Cdd:cd05970     27 AKEYPDKLaLVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEF----WYSLLAlhklGAIAIPA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 TV-----PVSYATTSAAVSKLEGIWEMlDRPWIVTSAAGEPGLRELAA------RREWSGLRLTTADA--LREEPEDRDw 1831
Cdd:cd05970    103 THqltakDIVYRIESADIKMIVAIAED-NIPEEIEKAAPECPSKPKLVwvgdpvPEGWIDFRKLIKNAspDFERPTANS- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1832 yEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLN-----------------WIpldhvTGVV 1894
Cdd:cd05970    181 -YPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTvadtgwgkavwgkiygqWI-----AGAA 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1895 MFhlrdVYlgcrqihaptSWILEDPVRWPELADRHRVSVTWAPNFAFGLLAeqahRFQDRDWDLSPVRLVMNAGEVVVAS 1974
Cdd:cd05970    255 VF----VY----------DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI----REDLSRYDLSSLRYCTTAGEALNPE 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1975 AARRFLhvlAPFGLPqdvMHPGWGMSETcsVVTDSVLASEAPDHDeafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQV 2054
Cdd:cd05970    317 VFNTFK---EKTGIK---LMEGFGQTET--TLTIATFPWMEPKPG----SMGKPAPGYEIDLIDREGRSCEAGEEGEIVI 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2055 R---GTSVT--HGYHDNARANAESFtEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS 2128
Cdd:cd05970    385 RtskGKPVGlfGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2129 FTAAV--AVRSDASAATdelalfLRLAPGQDPAGAL-REIAGKVTReigVSPAFLIP--VE-AEAIPKTEIGKIQRTKLR 2202
Cdd:cd05970    464 AVTGVpdPIRGQVVKAT------IVLAKGYEPSEELkKELQDHVKK---VTAPYKYPriVEfVDELPKTISGKIRRVEIR 534
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1676-2090 8.95e-19

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 93.40  E-value: 8.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1676 PEPSVSGWAEALLR-AAGRPDGEVVHVRADGSETRR-SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFvATLwg 1753
Cdd:PRK08180    34 LGDYPRRLTDRLVHwAQEAPDRVFLAERGADGGWRRlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEH-ALL-- 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1754 cVLGG-FVAVPlTVPVS--YATTSAAVSKLEGIWEMLdRPWIV-----------TSAAGEPGLRELAARREWSGLRLTTA 1819
Cdd:PRK08180   111 -ALAAmYAGVP-YAPVSpaYSLVSQDFGKLRHVLELL-TPGLVfaddgaafaraLAAVVPADVEVVAVRGAVPGRAATPF 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1820 DALREEPEDRDWYEA----RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA-TEAMNGLGSGD-VSLNWIPLDHVTG- 1892
Cdd:PRK08180   188 AALLATPPTAAVDAAhaavGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMlAQTFPFLAEEPpVLVDWLPWNHTFGg 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1893 VVMFHLRDVYLGCRQIHA--PTswiledPVRWPE-LADRHRVSVTWAPNF--AFGLL-------AEQAHRFqdrdwdLSP 1960
Cdd:PRK08180   268 NHNLGIVLYNGGTLYIDDgkPT------PGGFDEtLRNLREISPTVYFNVpkGWEMLvpalerdAALRRRF------FSR 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1961 VRLVMNAGEVVVASAARRfLHVLAPFGLPQDV-MHPGWGMSETCSVVTDSVLASEAPDHdeafvsCGLPYPGFAMRvvdd 2039
Cdd:PRK08180   336 LKLLFYAGAALSQDVWDR-LDRVAEATCGERIrMMTGLGMTETAPSATFTTGPLSRAGN------IGLPAPGCEVK---- 404

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 2040 qdaLLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLRD 2090
Cdd:PRK08180   405 ---LVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 2479-2658 1.39e-18

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 85.69  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2479 EVAAHLLKEPGTRLLLIGRTGLPPEDtwerhladagpASSRIeafRRLRGLG-EVRYETADVTDAAQVRAAVRRAADAwG 2557
Cdd:pfam08659   15 ELARWLAERGARHLVLLSRSAAPRPD-----------AQALI---AELEARGvEVVVVACDVSDPDAVAALLAEIKAE-G 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2558 VPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDDL 2637
Cdd:pfam08659   80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159

                          170       180
                   ....*....|....*....|.
gi 1573930569 2638 ALRRRREGLPGQSLAWSMWRE 2658
Cdd:pfam08659  160 AEYRRSQGLPATSINWGPWAE 180
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 481-958 1.81e-18

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 92.51  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:PRK00174    98 KITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITA 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 TAG--SGRL----PATDA---------RVVVVDdaRTVADLA---GR--APHDLTDAdrAGATGP------YDTAYVIHT 614
Cdd:PRK00174   178 DEGvrGGKPiplkANVDEalancpsveKVIVVR--RTGGDVDwveGRdlWWHELVAG--ASDECEpepmdaEDPLFILYT 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  615 SGSTGRPKGVPvpHAHVVRLFEASGEH---FRFGADDV--------WTLFHSYAfdfsvweLWGPLLHGGRLVVvpYE-V 682
Cdd:PRK00174   254 SGSTGKPKGVL--HTTGGYLVYAAMTMkyvFDYKDGDVywctadvgWVTGHSYI-------VYGPLANGATTLM--FEgV 322

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  683 SRSPRE--FLRLLDEEKVTVLNQTPSAF-------EQLVladAATDRAtgSLRyvVLGGealVAERLRP----WADRH-G 748
Cdd:PRK00174   323 PNYPDPgrFWEVIDKHKVTIFYTAPTAIralmkegDEHP---KKYDLS--SLR--LLGS---VGEPINPeaweWYYKVvG 392

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  749 LDAPELVNMYGITETTVHVTFHrLVRADledPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEMYV--SGPGVAPGYLN 826
Cdd:PRK00174   393 GERCPIVDTWWQTETGGIMITP-LPGAT---PLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYG 468

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  827 RPElteeRFLPDPFGA-PGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAae 905
Cdd:PRK00174   469 DHE----RFVKTYFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRP-- 540

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  906 DGLT--QLVAYAVPaeEGGADP-----AGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:PRK00174   541 DDIKgqGIYAFVTL--KGGEEPsdelrKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 459-959 2.13e-18

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 92.00  E-value: 2.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAES-PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:PLN03102    16 PITFLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPIN 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLALVMADAEPVAVVTDTAGSGR-------LPATDA----RVVVVDDArtvaDLAGRAPHDLTDAD---RAGAT 603
Cdd:PLN03102    96 TRLDATSIAAILRHAKPKILFVDRSFEPLarevlhlLSSEDSnlnlPVIFIHEI----DFPKRPSSEELDYEcliQRGEP 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 GP--YDTAYVIH----------TSGSTGRPKGVPVPH--AHVVRLFEASGEHFRFGADDVWTL--FHSYAFDFSvwelWG 667
Cdd:PLN03102   172 TPslVARMFRIQdehdpislnyTSGTTADPKGVVISHrgAYLSTLSAIIGWEMGTCPVYLWTLpmFHCNGWTFT----WG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  668 PLLHGG-----RLVVVPyevsrsprEFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRP 742
Cdd:PLN03102   248 TAARGGtsvcmRHVTAP--------EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  743 wADRHGLdapELVNMYGITETTVHVTF-------HRLVR-ADLEDPRRRGVIGRPLADLRVY---VLDAAGRPvppGAT- 810
Cdd:PLN03102   320 -VQRLGF---QVMHAYGLTEATGPVLFcewqdewNRLPEnQQMELKARQGVSILGLADVDVKnkeTQESVPRD---GKTm 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  811 GEMYVSGPGVAPGYLNRPELTEERFlpdpfgapGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTA 890
Cdd:PLN03102   393 GEIVIKGSSIMKGYLKNPKATSEAF--------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569  891 HPAVAGGAVVPRAAEDGLTQLVAYAV--PAEEGGADPAG--------LRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PLN03102   465 YPKVLETAVVAMPHPTWGETPCAFVVleKGETTKEDRVDklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1718-2204 5.08e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 90.76  E-value: 5.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1718 EASRVLA-GLRRRGLRPGDRVILQCDDTEDFVATLWGCvlgGFVAVPLTV--PVSYATTSAAVSKLEGI----------- 1783
Cdd:PRK07788    82 EQSNALArGLLALGVRAGDGVAVLARNHRGFVLALYAA---GKVGARIILlnTGFSGPQLAEVAAREGVkalvyddeftd 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1784 ------WEMLD-RPWIV------TSAAGEPGLRELAARREWSGLRLTTadalreepedrdwyeaRPDDLVLMlmTSGSTG 1850
Cdd:PRK07788   159 llsalpPDLGRlRAWGGnpdddePSGSTDETLDDLIAGSSTAPLPKPP----------------KPGGIVIL--TSGTTG 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1851 LPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLrDVYLGC----RQIHaptswileDPVRWPELA 1926
Cdd:PRK07788   221 TPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTL-AMALGStvvlRRRF--------DPEATLEDI 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1927 DRHRVSVTWA-PNFAFGLLAEQAHRFQDRDwdLSPVRLVMNAGEVVVASAARRflhVLAPFGlpqDVMHPGWGMSEtCSV 2005
Cdd:PRK07788   292 AKHKATALVVvPVMLSRILDLGPEVLAKYD--TSSLKIIFVSGSALSPELATR---ALEAFG---PVLYNLYGSTE-VAF 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2006 VTdsvLASEApDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANaesfTEDGWFDTGDL 2085
Cdd:PRK07788   363 AT---IATPE-DLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQ----IIDGLLSSGDV 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2086 AFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAAtdELALFLRLAPGQDP-AGALR 2163
Cdd:PRK07788   435 GYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA--AVIGVDDEEFGQ--RLRAFVVKAPGAALdEDAIK 510

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1573930569 2164 EIAG------KVTREIgvspAFLipveaEAIPKTEIGKIQRTKLRKS 2204
Cdd:PRK07788   511 DYVRdnlaryKVPRDV----VFL-----DELPRNPTGKVLKRELREM 548
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1711-2203 6.62e-18

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: 89.50  E-value: 6.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyattsaavsklegiwemldrp 1790
Cdd:cd05973      2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLF------------------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 wivtSAAGEPGLrelAARREWSGLRLTTADALREEPEDrdwyearpDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05973     57 ----TAFGPKAI---EHRLRTSGARLVVTDAANRHKLD--------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLR 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQI--HAPTSwileDPVRWPELADRHRVSVTWAPNFAFGLLA--- 1945
Cdd:cd05973    122 DAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTIllEGGFS----VESTWRVIERLGVTNLAGSPTAYRLLMAaga 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1946 EQAHRFQDRdwdlspVRLVMNAGEVVVASAARRFLhvlAPFGLPqdvMHPGWGMSETCSVVTDSvlasEAPDHDEAFVSC 2025
Cdd:cd05973    198 EVPARPKGR------LRRVSSAGEPLTPEVIRWFD---AALGVP---IHDHYGQTELGMVLANH----HALEHPVHAGSA 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2026 GLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVT----HGYHdnaraNAESFTEDG-WFDTGDLA-FLRDGELYITGRA 2099
Cdd:cd05973    262 GRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQ-----LPDTPAIDGgYYLTGDTVeFDPDGSFSFIGRA 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2100 KDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDaSAATDELALFLRLAPGQDPAGALREIAGKVTREIGVSPAF 2179
Cdd:cd05973    337 DDVITMSGYRIGPFDVESALIEHPAVAE---AAVIGVPD-PERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAY 412

                          490       500
                   ....*....|....*....|....*
gi 1573930569 2180 LIPVE-AEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05973    413 PRTIHfVDELPKTPSGKIQRFLLRR 437
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 1693-2102 1.04e-17

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 90.16  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1693 RPDGEVvhvradGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL-------- 1764
Cdd:PLN02736    68 RVDGTV------GEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLydtlgpda 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 -TVPVSYATTSAAV-------SKLEGIWEMLDRPWIVTSAAGEPGLRELAARrewSGLRLTTADAL----REEPedRDWY 1832
Cdd:PLN02736   142 vKFIVNHAEVAAIFcvpqtlnTLLSCLSEIPSVRLIVVVGGADEPLPSLPSG---TGVEIVTYSKLlaqgRSSP--QPFR 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1833 EARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDH----VTGVVMFHLrDVYLGCRQ- 1907
Cdd:PLN02736   217 PPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVNQIVMLHY-GVAVGFYQg 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 --------IHA--PTSWiledpVRWPELADRHRVSVTWAPNfAFGLLAEQ------AHRFQ--DRDWDLSPV--RLVMNA 1967
Cdd:PLN02736   296 dnlklmddLAAlrPTIF-----CSVPRLYNRIYDGITNAVK-ESGGLKERlfnaayNAKKQalENGKNPSPMwdRLVFNK 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1968 GEVVVASAARRFLHVLAPfgLPQDVMH-----------PGWGMSETCSVVTdsvlASEAPDHDEAFVscGLPYPGFAMRV 2036
Cdd:PLN02736   370 IKAKLGGRVRFMSSGASP--LSPDVMEflricfggrvlEGYGMTETSCVIS----GMDEGDNLSGHV--GSPNPACEVKL 441

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2037 VD-------DQDALLPEGDVGrlqVRGTSVTHGYHDNARANAESFTEDGWFDTGDL-AFLRDGELYITGRAKDV 2102
Cdd:PLN02736   442 VDvpemnytSEDQPYPRGEIC---VRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIgLWLPGGRLKIIDRKKNI 512
PRK09274 PRK09274
peptide synthase; Provisional
 1690-2166 1.12e-17

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 89.57  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVHV--RADGSETRR----SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGcvLGGFVAVP 1763
Cdd:PRK09274    16 AQERPDQLAVAVpgGRGADGKLAydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFA--LFKAGAVP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1764 LTV-P----------VSYATTSAAVSKLEGIWEMLDRPWivtsaaGEPGLRELAA---RREWSGLRLTTADALRE--EPE 1827
Cdd:PRK09274    94 VLVdPgmgiknlkqcLAEAQPDAFIGIPKAHLARRLFGW------GKPSVRRLVTvggRLLWGGTTLATLLRDGAaaPFP 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1828 DRDwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLdhvtgvvmFHLRDVYLGCRQ 1907
Cdd:PRK09274   168 MAD---LAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL--------FALFGPALGMTS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1908 I---HAPTSWILEDPVRWPELADRHRVSvtwapNFaFG---LLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLH 1981
Cdd:PRK09274   237 VipdMDPTRPATVDPAKLFAAIERYGVT-----NL-FGspaLLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRA 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1982 VLapfglPQDV-MHPGWGMSET---CSVVTDSVLASEAPDHDEAFVSC-GLPYPGFAMRVVD---------DQDALLPEG 2047
Cdd:PRK09274   311 ML-----PPDAeILTPYGATEAlpiSSIESREILFATRAATDNGAGICvGRPVDGVEVRIIAisdapipewDDALRLATG 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2048 DVGRLQVRGTSVTHGYHDNARANAESFTEDG----WFDTGDLAFLRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEEL 2122
Cdd:PRK09274   386 EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 2123 PSVVRSftAAVAVRSDASAatdELALFLRLAPGQDPAGA-----LREIA 2166
Cdd:PRK09274   466 PGVKRS--ALVGVGVPGAQ---RPVLCVELEPGVACSKSalyqeLRALA 509
PLN02479 PLN02479
acetate-CoA ligase
 459-966 2.88e-17

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 88.36  E-value: 2.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  459 PQLFEARVAES-PGRTAVSYAGETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLD 537
Cdd:PLN02479    22 PLWFLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVN 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  538 PGHPAERLA---------LVMADAEPVAVVTDT----AGSGRLPATDARVVVVDDARTvadlagrAPHDLTDADRAGA-- 602
Cdd:PLN02479   102 IRLNAPTIAfllehskseVVMVDQEFFTLAEEAlkilAEKKKSSFKPPLLIVIGDPTC-------DPKSLQYALGKGAie 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  603 ------TG--------PYDTAYVI---HTSGSTGRPKGVPVPH--AHVVRLFEASGEHFRFGADDVWTL--FHSYAFDFS 661
Cdd:PLN02479   175 yekfleTGdpefawkpPADEWQSIalgYTSGTTASPKGVVLHHrgAYLMALSNALIWGMNEGAVYLWTLpmFHCNGWCFT 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  662 vwelWGPLLHGGRLVVVPYEVSRSPREFLRlldEEKVTVLNQTPSAFEQLVLADAA-TDRATGSLRYVVLGGEALVAERL 740
Cdd:PLN02479   255 ----WTLAALCGTNICLRQVTAKAIYSAIA---NYGVTHFCAAPVVLNTIVNAPKSeTILPLPRVVHVMTAGAAPPPSVL 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  741 RPWADRhGLdapELVNMYGITET----TVHV------TFHRLVRADLEdpRRRGVIGRPLADLRVyVLDAAGRPVPP-GA 809
Cdd:PLN02479   328 FAMSEK-GF---RVTHTYGLSETygpsTVCAwkpewdSLPPEEQARLN--ARQGVRYIGLEGLDV-VDTKTMKPVPAdGK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  810 T-GEMYVSGPGVAPGYLNRPELTEERFlpdpfgAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVL 888
Cdd:PLN02479   401 TmGEIVMRGNMVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  889 TAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEE-GGADPAGLRAHLAA----RLPAYMVPAAcVLLDALPLTANGKLDTAA 963
Cdd:PLN02479   473 YTHPAVLEASVVARPDERWGESPCAFVTLKPGvDKSDEAALAEDIMKfcreRLPAYWVPKS-VVFGPLPKTATGKIQKHV 551


                   ...
gi 1573930569  964 LPA 966
Cdd:PLN02479   552 LRA 554
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 1709-2209 3.45e-17

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 87.83  E-value: 3.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1709 RRSYASLVPEASRVLAGLRRRGLRPGDRV-ILQCDDTEDFVATLwGCVLGGFVAVPL-----TVPVSY----ATTSAAVS 1778
Cdd:PRK12406    11 RRSFDELAQRAARAAGGLAALGVRPGDCVaLLMRNDFAFFEAAY-AAMRLGAYAVPVnwhfkPEEIAYiledSGARVLIA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1779 K---LEGIWEMLDRPWIVTSAAGEPglrELAARREWSglrlttADALREEPEDRDWYE-----ARPDDLVL-----MLMT 1845
Cdd:PRK12406    90 HadlLHGLASALPAGVTVLSVPTPP---EIAAAYRIS------PALLTPPAGAIDWEGwlaqqEPYDGPPVpqpqsMIYT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1846 SGSTGLPKAVRlthRNVLT--RAAATEAMN----GLGSGDVSLNWIPLDHvTGVVMFHLRDVYLGCRQIHAPTSwileDP 1919
Cdd:PRK12406   161 SGTTGHPKGVR---RAAPTpeQAAAAEQMRaliyGLKPGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVLQPRF----DP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1920 VRWPELADRHRVS-VTWAPNFAFGLLAEQAHRfqDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPfglpqdVMHPGWG 1998
Cdd:PRK12406   233 EELLQLIERHRIThMHMVPTMFIRLLKLPEEV--RAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYEYYG 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1999 MSETCSVVTDSvlASEAPDHDEafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVR---GTSVTHGYHDNARANAEsft 2075
Cdd:PRK12406   305 STESGAVTFAT--SEDALSHPG---TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiagNPDFTYHNKPEKRAEID--- 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2076 EDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV---------RSFTAAVA--VRSDASAAT 2143
Cdd:PRK12406   377 RGGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHdcavfgipdAEFGEALMavVEPQPGATL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2144 DELALFLRLApgqdpagalREIAG-KVTREIGVSPaflipveaeAIPKTEIGKIQRTKLRKSFEAGE 2209
Cdd:PRK12406   457 DEADIRAQLK---------ARLAGyKVPKHIEIMA---------ELPREDSGKIFKRRLRDPYWANA 505
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1806-2211 4.65e-17

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 87.92  E-value: 4.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1806 AARREWSGLRLTTADALREE-PEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLG--SGDVSL 1882
Cdd:PRK05620   149 AAAHMPEGIKVYSYEALLDGrSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAvtHGESFL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1883 NWIPLDHVT--GV----VMFHLRDVYLGcRQIHAPT-SWILEDPVrwPELAdrHRVSVTWapnfaFGLLAeqaHRFQDrd 1955
Cdd:PRK05620   229 CCVPIYHVLswGVplaaFMSGTPLVFPG-PDLSAPTlAKIIATAM--PRVA--HGVPTLW-----IQLMV---HYLKN-- 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1956 wdlSPVRlvMNAGEVVVASAARRFLHVLA---PFGLpqDVMHPgWGMSETCSVVT----DSVLASEApdHDEAFVSCGLP 2028
Cdd:PRK05620   294 ---PPER--MSLQEIYVGGSAVPPILIKAweeRYGV--DVVHV-WGMTETSPVGTvarpPSGVSGEA--RWAYRVSQGRF 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2029 YPGFAMRVVDDQDALLP-EGDVGRLQVRGTSVT-HGYHDNARAN---------------AESFTEDGWFDTGDLAFL-RD 2090
Cdd:PRK05620   364 PASLEYRIVNDGQVMEStDRNEGEIQVRGNWVTaSYYHSPTEEGggaastfrgedvedaNDRFTADGWLRTGDVGSVtRD 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2091 GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELALFLrLAPGQDPAgalREIAGKVT 2170
Cdd:PRK05620   444 GFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE---CAVIGYPDDKWGERPLAVTV-LAPGIEPT---RETAERLR 516

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2171 REI-GVSPAFLIP---VEAEAIPKTEIGKIQRTKLRKSFEAGEFD 2211
Cdd:PRK05620   517 DQLrDRLPNWMLPeywTFVDEIDKTSVGKFDKKDLRQHLADGDFE 561
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 10-423 5.49e-17

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: 86.54  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEglWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPDEM-PVHR 88
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELfRLEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   89 VDVSGEADPAAaaeewIRR---DLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAA 165
Cdd:cd19534     81 VDLSSLAQAAA-----IEAlaaEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  166 GEE---PPPAGFES-ADRLaaeeAAYLGSDRHRRDRAYWTERLAGLPEPVrltdrtaPPRAPFLRRTA-----VLSPAET 236
Cdd:cd19534    156 GEPiplPSKTSFQTwAELL----AEYAQSPALLEELAYWRELPAADYWGL-------PKDPEQTYGDArtvsfTLDEEET 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  237 RAL-DEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSR---LGSAAL-RTPGTASDILPLRVAASADTPVGGF 311
Cdd:cd19534    225 EALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGReeiDPGLDLsRTVGWFTSMYPVVLDLEASEDLGDT 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  312 VRAVADDLRglRAHQRHRGESIRRDLGVLGRGRRVHGPVVNIV---------PFSEDLTFGGHPSTSHHLSGGAVDD--- 379
Cdd:cd19534    305 LKRVKEQLR--RIPNKGIGYGILRYLTPEGTKRLAFHPQPEISfnylgqfdqGERDDALFVSAVGGGGSDIGPDTPRfal 382

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1573930569  380 LQISVRpgAEADTLWLAFDAHPDLYEEDGLALFLERFLKVLREL 423
Cdd:cd19534    383 LDINAV--VEGGQLVITVSYSRNMYHEETIQQLADSYKEALEAL 424
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 445-867 7.19e-17

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 87.24  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  445 VRRDEPAPRVTRTLPQLFEARVAESPGRTAVSYAG-----ETLSYAELNAEANRLARLLVEQGAGPGRfvALALPRGPRL 519
Cdd:PRK08180    28 LRSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAER--PLMILSGNSI 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  520 VPALLAV--LKTGAAYLPLDPG------------HPAERL--ALVMA-DAEPVAVVTDTAGSGRLPATDARVVVVDDART 582
Cdd:PRK08180   106 EHALLALaaMYAGVPYAPVSPAyslvsqdfgklrHVLELLtpGLVFAdDGAAFARALAAVVPADVEVVAVRGAVPGRAAT 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  583 -VADLAGRAPHDLTDAdRAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLFHsyafdfs 661
Cdd:PRK08180   186 pFAALLATPPTAAVDA-AHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVD------- 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  662 vwelWGP--------------LLHGGRLVV-----VPYEVSRSprefLRLLDEEKVTVLNQTPSAFEQLVLA---DAA-T 718
Cdd:PRK08180   258 ----WLPwnhtfggnhnlgivLYNGGTLYIddgkpTPGGFDET----LRNLREISPTVYFNVPKGWEMLVPAlerDAAlR 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  719 DRATGSLRYVVLGGEAL---VAERLRPWADRHGLDAPELVNMYGITETTVHVTF--HRLVRAdledprrrGVIGRPLADL 793
Cdd:PRK08180   330 RRFFSRLKLLFYAGAALsqdVWDRLDRVAEATCGERIRMMTGLGMTETAPSATFttGPLSRA--------GNIGLPAPGC 401

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569  794 RVyvldaagRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARW----RPDGTLVHAGR 867
Cdd:PRK08180   402 EV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRFvdpaDPERGLMFDGR 465
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1709-2128 7.60e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 86.36  E-value: 7.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1709 RRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGfvAVPLTVpvsyattsaavsklegiwemld 1788
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAG--AVPVLI---------------------- 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1789 rpwivtsaagEPGLrelaARREWSG-LRLTTADALREEPedrdwyeaRPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAA 1867
Cdd:cd05910     58 ----------DPGM----GRKNLKQcLQEAEPDAFIGIP--------KADEPAAILFTSGSTGTPKGVVYRHGTFAAQID 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1868 ATEAMNGLGSGDVSLNWIPLdhvtgvvmFHLRDVYLGCRQIHA---PTSWILEDPVRWPELADRHRVSVTWAPNFAFGLL 1944
Cdd:cd05910    116 ALRQLYGIRPGEVDLATFPL--------FALFGPALGLTSVIPdmdPTRPARADPQKLVGAIRQYGVSIVFGSPALLERV 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1945 AEQAHRfqdRDWDLSPVRLVMNAGEVV---VASAARRFLHVLAPFGLPqdvmhpgWGMSET---CSVVTDSVLASEAPDH 2018
Cdd:cd05910    188 ARYCAQ---HGITLPSLRRVLSAGAPVpiaLAARLRKMLSDEAEILTP-------YGATEAlpvSSIGSRELLATTTAAT 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2019 DEAFVSC-GLPYPGFAMRVVD---------DQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDG----WFDTGD 2084
Cdd:cd05910    258 SGGAGTCvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGD 337

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2085 LAFLRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS 2128
Cdd:cd05910    338 LGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 483-959 8.50e-17

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 86.68  E-value: 8.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  483 SYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPG-HPaERLALVMADAEPVAVVTDT 561
Cdd:PRK07008    41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFP-EQIAYIVNHAEDRYVLFDL 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  562 -------AGSGRLPATDARVVVVDDARTVAD-LAGRAPHDLTDADRAGATGP-YD---TAYVIHTSGSTGRPKGV----- 624
Cdd:PRK07008   120 tflplvdALAPQCPNVKGWVAMTDAAHLPAGsTPLLCYETLVGAQDGDYDWPrFDenqASSLCYTSGTTGNPKGAlyshr 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  625 -PVPHAHVVRLFEASGEHFRFGADDVWTLFHSYAfdfsvwelWG-PL---LHGGRLVVV-PYEVSRSPREflrLLDEEKV 698
Cdd:PRK07008   200 sTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNA--------WGlPYsapLTGAKLVLPgPDLDGKSLYE---LIEAERV 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  699 TVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTFHRLVRADLE 778
Cdd:PRK07008   269 TFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGV---EVIHAWGMTEMSPLGTLCKLKWKHSQ 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 DPR--RRGVI---GRPLADLRVYVLDAAGRPVP--PGATGEMYVSGPGVAPGYLNRpeltEERFLPDPFgapgtrmYRSG 851
Cdd:PRK07008   346 LPLdeQRKLLekqGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVRGPWVIDRYFRG----DASPLVDGW-------FPTG 414

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  852 DLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PRAAEDGLtqLVAYAVPAEEGGADPag 927
Cdd:PRK07008   415 DVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIacahPKWDERPL--LVVVKRPGAEVTREE-- 490

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1573930569  928 LRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PRK07008   491 LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 494-959 9.78e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 86.78  E-value: 9.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  494 LARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTA--------GSG 565
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETcsswyeelQND 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  566 RLPATDARVVVVDDARTVADLAGRAPHDLTDADRAGAT-------GPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEAS 638
Cdd:PLN02860   125 RLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTteldyawAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  639 GEHFRFGADDVWtlFHSyafdfsvwelwGPLLH-------------GGRLVVVP-YEVSRSprefLRLLDEEKVTVLNQT 704
Cdd:PLN02860   205 IAIVGYGEDDVY--LHT-----------APLCHigglssalamlmvGACHVLLPkFDAKAA----LQAIKQHNVTSMITV 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  705 PSAFEQLV--LADAATDRATGSLRYVVLGGEALVAERLRpwADRHGLDAPELVNMYGITETTVHVTFHRLVRADLEDPRR 782
Cdd:PLN02860   268 PAMMADLIslTRKSMTWKVFPSVRKILNGGGSLSSRLLP--DAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQ 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  783 RGVIGRPLADLRVYVLDAA--GRPVP----------PGATGEMYVSGPGVAPGYLNRP-----ELTEERFLPdpfgapgt 845
Cdd:PLN02860   346 TLQTVNQTKSSSVHQPQGVcvGKPAPhvelkigldeSSRVGRILTRGPHVMLGYWGQNsetasVLSNDGWLD-------- 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  846 rmyrSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPrAAEDGLTQLVAYAV--------- 916
Cdd:PLN02860   418 ----TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVrlrdgwiws 492

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  917 ----PAEEGG--ADPAGLRAHLAAR-LPAYMVPAACVLL-DALPLTANGKL 959
Cdd:PLN02860   493 dnekENAKKNltLSSETLRHHCREKnLSRFKIPKLFVQWrKPFPLTTTGKI 543
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 480-959 1.18e-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: 86.36  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLL-VEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEP---- 554
Cdd:cd17632     66 ETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPrlla 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  555 ---------VAVVTDTAGSGRL------PATDARVVVVDDARTVADLAGRAPHDLTDADRAGATGPYDT----------- 608
Cdd:cd17632    146 vsaehldlaVEAVLEGGTPPRLvvfdhrPEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPlfrpepdddpl 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  609 AYVIHTSGSTGRPKGVPVPHAHVVRLFEASgehFRFGADDVWT--------LFHSYAfdfSVWeLWGPLLHGGR------ 674
Cdd:cd17632    226 ALLIYTSGSTGTPKGAMYTERLVATFWLKV---SSIQDIRPPAsitlnfmpMSHIAG---RIS-LYGTLARGGTayfaaa 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  675 ----------LVVVPYEVSRSPR-------EFLRLLDEEKVtvlnqtpsafeQLVLADAATDRATGSLRYVVLGGE---- 733
Cdd:cd17632    299 sdmstlfddlALVRPTELFLVPRvcdmlfqRYQAELDRRSV-----------AGADAETLAERVKAELRERVLGGRllaa 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  734 ----ALVAERLRPWADRHgLDAPeLVNMYGITETTVHVTFHRLVRADLEDPRRRGVigrplADLRVYVLDaagRPVPpga 809
Cdd:cd17632    368 vcgsAPLSAEMKAFMESL-LDLD-LHDGYGSTEAGAVILDGVIVRPPVLDYKLVDV-----PELGYFRTD---RPHP--- 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  810 TGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGD-LARWRPDgTLVHAGRADQQVKI-RGFRIEPGEIEAV 887
Cdd:cd17632    435 RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAV 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  888 LTAHPAVAGGAVVPRAAEdglTQLVAYAVPAEEG--GADPAGLRAHL---------AARLPAYMVPAAcVLLDALPLT-A 955
Cdd:cd17632    507 FAASPLVRQIFVYGNSER---AYLLAVVVPTQDAlaGEDTARLRAALaeslqriarEAGLQSYEIPRD-FLIETEPFTiA 582


                   ....
gi 1573930569  956 NGKL 959
Cdd:cd17632    583 NGLL 586
PLN02479 PLN02479
acetate-CoA ligase
 1845-2219 1.22e-16

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 86.44  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1845 TSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVV----MFHLRDVYLGCRQIHAPTSWiledpv 1920
Cdd:PLN02479   203 TSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCftwtLAALCGTNICLRQVTAKAIY------ 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1921 rwpELADRHRVSVTWAPNFAFGLLAEQAHrfQDRDWDLSPVRLVMNAGEV----VVASAARRFLHVLAPFGLPQDvmhpg 1996
Cdd:PLN02479   277 ---SAIANYGVTHFCAAPVVLNTIVNAPK--SETILPLPRVVHVMTAGAApppsVLFAMSEKGFRVTHTYGLSET----- 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETCSVVTDsvlASEAPDHDEAFVSC--GLPYPGF-AMRVVDDQDALLPEGD---VGRLQVRGTSVTHGYHDNARAN 2070
Cdd:PLN02479   347 YGPSTVCAWKPE---WDSLPPEEQARLNArqGVRYIGLeGLDVVDTKTMKPVPADgktMGEIVMRGNMVMKGYLKNPKAN 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2071 AESFtEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsFTAAVAVRSDASAATDELAlF 2149
Cdd:PLN02479   424 EEAF-ANGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV---LEASVVARPDERWGESPCA-F 498

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2150 LRLAPGQDPA--GALREIAGKVTREigVSPAFLIP--VEAEAIPKTEIGKIQRTKLRKsfEAGEFdGAVRETQL 2219
Cdd:PLN02479   499 VTLKPGVDKSdeAALAEDIMKFCRE--RLPAYWVPksVVFGPLPKTATGKIQKHVLRA--KAKEM-GPVKKSRL 567
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1078-1502 1.26e-16

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: 85.04  E-value: 1.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1078 QERMWFLSRMDGAAATYNIPLpvALRHPLDLDALRAALGDVADRHESLRTVFGE-EDGAIHQRVLPPGTLrpELHVVDCP 1156
Cdd:cd19545      8 QEGLMALTARQPGAYVGQRVF--ELPPDIDLARLQAAWEQVVQANPILRTRIVQsDSGGLLQVVVKESPI--SWTESTSL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1157 DEERAAHVAAAMRRSFDLTRdsalWAGVFGTGDTRTLLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAP--PAL 1234
Cdd:cd19545     84 DEYLEEDRAAPMGLGGPLVR----LALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRfvKYL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1235 QYADfalwqrrvlapapegpgrLERLTSFWRQALDGLpeeSAPPPDRPRPAAPSGRGGGVtvpldAGTHRELLRLADHeN 1314
Cdd:cd19545    160 RQLD------------------DEAAAEFWRSYLAGL---DPAVFPPLPSSRYQPRPDAT-----LEHSISLPSSASS-G 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1315 ASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRT--EPALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDH 1392
Cdd:cd19545    213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1393 QDLPFDRlVEEVNPRRHPArhPLFQVMLALQNNE----RAVLTLGEDRVPLRPAATGTAKFDLFVDVlerhgadgTADGL 1468
Cdd:cd19545    293 EHTGLQN-IRRLGPDARAA--CNFQTLLVVQPALpsstSESLELGIEEESEDLEDFSSYGLTLECQL--------SGSGL 361

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1573930569 1469 DLHVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19545    362 RVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK05857 PRK05857
fatty acid--CoA ligase;
1685-2204 1.28e-16

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 86.22  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1685 EALLRAAGRPDGEVVHVRADGSeTRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAV-- 1762
Cdd:PRK05857    18 DRVFEQARQQPEAIALRRCDGT-SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVma 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 -----PLTVP-VSYATTSAAVSKLEGiwemldrpwivtSAAGEPGLRELAARREWSGLRLTTADALREEPEDRDWYEARP 1836
Cdd:PRK05857    97 dgnlpIAAIErFCQITDPAAALVAPG------------SKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 ----DDLVLMLMTSGSTGLPKAVRLTHRnvlTRAAATEAMNGLGsgdvsLNWIplDHVTGVVMFH-LRDVYLGcrqihaP 1911
Cdd:PRK05857   165 dqgsEDPLAMIFTSGTTGEPKAVLLANR---TFFAVPDILQKEG-----LNWV--TWVVGETTYSpLPATHIG------G 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1912 TSWIL-------------EDPVRWPELADRHRVSVT-WAPNfafgLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVAsAAR 1977
Cdd:PRK05857   229 LWWILtclmhgglcvtggENTTSLLEILTTNAVATTcLVPT----LLSKLVSELKSANATVPSLRLVGYGGSRAIA-ADV 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1978 RFLHV----LAPFglpqdvmhpgWGMSET-CSVV---TD--SVLASEAPdhdeafvSCGLPYPGFAMRVVDDQDA----- 2042
Cdd:PRK05857   304 RFIEAtgvrTAQV----------YGLSETgCTALclpTDdgSIVKIEAG-------AVGRPYPGVDVYLAATDGIgptap 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2043 -LLPEGDVGRLQVRGTSVTHGYHDNARANAESFTeDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVE 2120
Cdd:PRK05857   367 gAGPSASFGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSSEMIICGGVNIAPDEVDRIAE 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2121 ELPSVVRS---------FTAAVAVRSDASAATDELAlflrlapgqdpAGAL-REIAGKVTREigvSPAFLIP---VEAEA 2187
Cdd:PRK05857   446 GVSGVREAacyeipdeeFGALVGLAVVASAELDESA-----------ARALkHTIAARFRRE---SEPMARPstiVIVTD 511

                          570
                   ....*....|....*..
gi 1573930569 2188 IPKTEIGKIQRTKLRKS 2204
Cdd:PRK05857   512 IPRTQSGKVMRASLAAA 528
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
565-959 2.77e-16

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 84.82  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  565 GRLPATDARVVVVDDARtvadlAGRAPHDLTDAdragATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRF 644
Cdd:PRK05851   120 ERLRAVDSSVTVHDLAT-----AAHTNRSASLT----PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGL 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  645 GAD-DV---W-TLFHSYAFDFSVWELWGpllhGGRLVVVPYEV-SRSPREFLRLLDEEKVTvLNQTPSAFEQLV--LADA 716
Cdd:PRK05851   191 DAAtDVgcsWlPLYHDMGLAFLLTAALA----GAPLWLAPTTAfSASPFRWLSWLSDSRAT-LTAAPNFAYNLIgkYARR 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  717 ATDRATGSLRYVVLGGEALVAERLRPWAD---RHGLDAPELVNMYGITETTVHVT---------FHRLVRADLEDPRRRG 784
Cdd:PRK05851   266 VSDVDLGALRVALNGGEPVDCDGFERFATamaPFGFDAGAAAPSYGLAESTCAVTvpvpgiglrVDEVTTDDGSGARRHA 345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  785 VIGRPLADLRVYVLDAAG-RPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPdpfgapgtrmyrSGDLArWRPDGTLV 863
Cdd:PRK05851   346 VLGNPIPGMEVRISPGDGaAGVAGREIGEIEIRGASMMSGYLGQAPIDPDDWFP------------TGDLG-YLVDGGLV 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  864 HAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQlVAYAVPAEEGGADPAGLRAHLAARLPAY--MV 941
Cdd:PRK05851   413 VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSAR-PGLVIAAEFRGPDEAGARSEVVQRVASEcgVV 491

                          410       420
                   ....*....|....*....|
gi 1573930569  942 PAACVLLD--ALPLTANGKL 959
Cdd:PRK05851   492 PSDVVFVApgSLPRTSSGKL 511
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 481-874 2.79e-16

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: 85.18  E-value: 2.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRfvALALPRGPRLVPALLAV--LKTGAAYLPLDP-----GHPAERLALVMADAE 553
Cdd:cd05921     25 RVTYAEALRQVRAIAQGLLDLGLSAER--PLLILSGNSIEHALMALaaMYAGVPAAPVSPayslmSQDLAKLKHLFELLK 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  554 PVAV-VTDTAGSGRLPAT----DARVVVV------DDARTVADLAGRAPhdLTDADRA-GATGPYDTAYVIHTSGSTGRP 621
Cdd:cd05921    103 PGLVfAQDAAPFARALAAifplGTPLVVSrnavagRGAISFAELAATPP--TAAVDAAfAAVGPDTVAKFLFTSGSTGLP 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  622 KGVPVPHAHVVRLFEASGEHFRFGADDVWTLF------HSYAFDFSVwelwGPLLHGGRLVVVPyEVSRSPREF---LRL 692
Cdd:cd05921    181 KAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwlpwnHTFGGNHNF----NLVLYNGGTLYID-DGKPMPGGFeetLRN 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  693 LDEEKVTVLNQTPSAFEQLVLA----DAATDRATGSLRYVVLGGEAL---VAERLRPWADRHGLDAPELVNMYGITETTV 765
Cdd:cd05921    256 LREISPTVYFNVPAGWEMLVAAlekdEALRRRFFKRLKLMFYAGAGLsqdVWDRLQALAVATVGERIPMMAGLGATETAP 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  766 HVTFHRLVRAdledprRRGVIGRPLADLRVyvldaagRPVPPGATGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgt 845
Cdd:cd05921    336 TATFTHWPTE------RSGLIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF----- 397

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1573930569  846 rmYRSGDLARW----RPDGTLVHAGRADQQVKI 874
Cdd:cd05921    398 --YCLGDAAKLadpdDPAKGLVFDGRVAEDFKL 428
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
456-964 2.92e-16

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 86.17  E-value: 2.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQ-LFEARVAESPGRTAVS-YAGETLSYAELNAEANRLARLLvEQGAGPGRFVALALPRGPRLVPALLAVLKTG--A 531
Cdd:PRK06814   631 RTLFEaLIEAAKIHGFKKLAVEdPVNGPLTYRKLLTGAFVLGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAGrvP 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  532 AYLPLDPGhPAERLALVMAdAEPVAVVTDTA--GSGRLPA------TDARVVVVDDAR---TVAD-----LAGRAPHDLT 595
Cdd:PRK06814   710 AMINFSAG-IANILSACKA-AQVKTVLTSRAfiEKARLGPliealeFGIRIIYLEDVRaqiGLADkikglLAGRFPLVYF 787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  596 DADRagatgPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADD----VWTLFHSYAfdfsvweLWG---- 667
Cdd:PRK06814   788 CNRD-----PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDkvfnALPVFHSFG-------LTGglvl 855

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  668 PLLHGGRLVVVPyevsrSPREFlRLLDE----EKVTVLNQTpSAFeqlvL---ADAATDRATGSLRYVVLGGEALVAERL 740
Cdd:PRK06814   856 PLLSGVKVFLYP-----SPLHY-RIIPEliydTNATILFGT-DTF----LngyARYAHPYDFRSLRYVFAGAEKVKEETR 924

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  741 RPWADRHGLDAPELvnmYGITETT----VHVTFHrlvradledpRRRGVIGR--PLADLRVyvldaagRPVpPG--ATGE 812
Cdd:PRK06814   925 QTWMEKFGIRILEG---YGVTETApviaLNTPMH----------NKAGTVGRllPGIEYRL-------EPV-PGidEGGR 983

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  813 MYVSGPGVAPGYL--NRPELTEErflpdpfgaPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTA 890
Cdd:PRK06814   984 LFVRGPNVMLGYLraENPGVLEP---------PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569  891 HPAVAGGAVVPRAAEDGLTQLVAYavpAEEGGADPAGLRAHLAAR-LPAYMVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK06814  1055 LWPDALHAAVSIPDARKGERIILL---TTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAV 1126
PRK09192 PRK09192
fatty acyl-AMP ligase;
480-963 3.62e-16

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 85.06  E-value: 3.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTG--AAYLPLdP----GHPA--ERLALVMAD 551
Cdd:PRK09192    48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPL-PmgfgGRESyiAQLRGMLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  552 AEPVAVVtdtAGSGRLPATDArvvVVDDARTVADLAGRAPHDLTDADRAGAT-GPYDTAYVIHTSGSTGRPKGVPVPHAH 630
Cdd:PRK09192   127 AQPAAII---TPDELLPWVNE---ATHGNPLLHVLSHAWFKALPEADVALPRpTPDDIAYLQYSSGSTRFPRGVIITHRA 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  631 VVRLFEAsgeHFRFGaddvwtlFHSYAFDFSVweLWGPLLHGGRLV-----------VVPY----EVSRSPREFLRLLDE 695
Cdd:PRK09192   201 LMANLRA---ISHDG-------LKVRPGDRCV--SWLPFYHDMGLVgflltpvatqlSVDYlptrDFARRPLQWLDLISR 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  696 EKVTVLNQTPSAFEQLVLADAATDRATGSL---RYVVLGGEALVAERLRPWADRH---GLDAPELVNMYGITETTVHVTF 769
Cdd:PRK09192   269 NRGTISYSPPFGYELCARRVNSKDLAELDLscwRVAGIGADMIRPDVLHQFAEAFapaGFDDKAFMPSYGLAEATLAVSF 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  770 --------------------HRLVRADLEDPRRRGVI--GRPLADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGYLNR 827
Cdd:PRK09192   349 splgsgivveevdrdrleyqGKAVAPGAETRRVRTFVncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD 428

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  828 PElTEERFLPDpfGAPGTrmyrsGDLArWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVvpraaedg 907
Cdd:PRK09192   429 EE-SQDVLAAD--GWLDT-----GDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDA-------- 491

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  908 ltqlVAYAVPAEEG----------GADP---AGLRAHLAARLPA-YMVPAACVLL--DALPLTANGKLDTAA 963
Cdd:PRK09192   492 ----AAFSIAQENGekivllvqcrISDEerrGQLIHALAALVRSeFGVEAAVELVppHSLPRTSSGKLSRAK 559
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 482-959 3.78e-16

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 85.17  E-value: 3.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  482 LSYAELNAEaNRL--ARLlvEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPL----DPGHpAERLALVMADAEPV 555
Cdd:PRK07769    56 LTWSQFGAR-NRAvgARL--QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGH-VGRLHAVLDDCTPS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  556 AVVTDTAGSGR-------LPATD-ARVVVVDDA-RTVADLAGRAPHDLTDadragatgpydTAYVIHTSGSTGRPKGVPV 626
Cdd:PRK07769   132 AILTTTDSAEGvrkffraRPAKErPRVIAVDAVpDEVGATWVPPEANEDT-----------IAYLQYTSGSTRIPAGVQI 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  627 PH----AHVVRLFEASGehFRFGADDV-W-TLFHsyafDFSVWELWGPLLHGGRLVVV-PYEVSRSPREFLRLL---DEE 696
Cdd:PRK07769   201 THlnlpTNVLQVIDALE--GQEGDRGVsWlPFFH----DMGLITVLLPALLGHYITFMsPAAFVRRPGRWIRELarkPGG 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  697 KVTVLNQTPS-AFEQL----VLADAATDRATGSLRYVVLGGEALVAERLRPWADR---HGLDAPELVNMYGITETTVHVT 768
Cdd:PRK07769   275 TGGTFSAAPNfAFEHAaargLPKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAfapYGLPPTAIKPSYGMAEATLFVS 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  769 F-------------------HRLVRADLEDPR-----RRGVIGRplADLRVYVLDAAGRPVPPGATGEMYVSGPGVAPGY 824
Cdd:PRK07769   355 TtpmdeeptviyvdrdelnaGRFVEVPADAPNavaqvSAGKVGV--SEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  825 LNRPELTEERF---LPDPF------GAP-GTRMYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEA-VLTAHPA 893
Cdd:PRK07769   433 WGKPEETAATFqniLKSRLseshaeGAPdDALWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEYtAQEATKA 511

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  894 VAGGAV----VP-----------------RAAEDGLTQLVAYAVPAEEGG-ADPA----GLRAHLAARlpaYMVPAACVL 947
Cdd:PRK07769   512 LRTGYVaafsVPanqlpqvvfddshaglkFDPEDTSEQLVIVAERAPGAHkLDPQpiadDIRAAIAVR---HGVTVRDVL 588

                          570
                   ....*....|....*
gi 1573930569  948 L---DALPLTANGKL 959
Cdd:PRK07769   589 LvpaGSIPRTSSGKI 603
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 465-958 5.79e-16

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: 84.24  E-value: 5.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  465 RVAESPGRTAVsYAGET-----LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDP- 538
Cdd:cd05943     78 RHADADDPAAI-YAAEDgerteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPd 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  539 -GHPA--ERLALVmadaEPVAVVTDTAGS--GR--------------LPATDARVVVVDDARTVA-DLAGRAP-HDLTDA 597
Cdd:cd05943    157 fGVPGvlDRFGQI----EPKVLFAVDAYTynGKrhdvrekvaelvkgLPSLLAVVVVPYTVAAGQpDLSKIAKaLTLEDF 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  598 DRAGATGPYDTA--------YVIHTSGSTGRPKgvPVPHAHVVRLFEASGEH-----FRFGadDVWTLFHSYAfdfsvWE 664
Cdd:cd05943    233 LATGAAGELEFEplpfdhplYILYSSGTTGLPK--CIVHGAGGTLLQHLKEHilhcdLRPG--DRLFYYTTCG-----WM 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  665 LW----GPLLHGGRLVVvpYEVS---RSPREFLRLLDEEKVTVLNQTPSAFEQLVLADA--ATDRATGSLRYVVLGGEAL 735
Cdd:cd05943    304 MWnwlvSGLAVGATIVL--YDGSpfyPDTNALWDLADEEGITVFGTSAKYLDALEKAGLkpAETHDLSSLRTILSTGSPL 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  736 VAERLRpWADRHGLDAPELVNMYGITEttVHVTFhrlVRADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPpGATGEMYV 815
Cdd:cd05943    382 KPESFD-YVYDHIKPDVLLASISGGTD--IISCF---VGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVC 454

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  816 SGPgvapgYLNRPElteeRFLPDPFGA----------PGTrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIE 885
Cdd:cd05943    455 TKP-----FPSMPV----GFWNDPDGSryraayfakyPGV--WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIY 523

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569  886 AVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAgLRAHLAARLPAYM----VPAACVLLDALPLTANGK 958
Cdd:cd05943    524 RVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE-LRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1719-2202 7.21e-16

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 84.31  E-value: 7.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1719 ASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGG---FVAVPLTVPVSYA----TTSAAVSKLEGiwEMLDRpw 1791
Cdd:PRK06060    40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvmaFLANPELHRDDHAlaarNTEPALVVTSD--ALRDR-- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1792 IVTSAAGEPGlrELaarrewsglrltTADALREEPEDrdwYE-ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLT--RAAA 1868
Cdd:PRK06060   116 FQPSRVAEAA--EL------------MSEAARVAPGG---YEpMGGDALAYATYTSGTTGPPKAAIHRHADPLTfvDAMC 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 TEAMNgLGSGDVSLNWIPLDHVTGV---VMFHLRDvylGCRQIHAPTSWILEDPVRwpeLADRHRVSVTWA-PNF-AFGL 1943
Cdd:PRK06060   179 RKALR-LTPEDTGLCSARMYFAYGLgnsVWFPLAT---GGSAVINSAPVTPEAAAI---LSARFGPSVLYGvPNFfARVI 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1944 LAEQAHRFQDrdwdlspVRLVMNAGEVVVASAARRFLHVLApfGLPqdvMHPGWGMSETC-SVVTDSVlaseapdhDEAF 2022
Cdd:PRK06060   252 DSCSPDSFRS-------LRCVVSAGEALELGLAERLMEFFG--GIP---ILDGIGSTEVGqTFVSNRV--------DEWR 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2023 V-SCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDnaraNAESFTED-GWFDTGDLAFLrDGELYIT--GR 2098
Cdd:PRK06060   312 LgTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWN----RPDSPVANeGWLDTRDRVCI-DSDGWVTyrCR 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2099 AKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAATdeLALFLRLAPGQDPAGA-LREIAGKVTREIGvsp 2177
Cdd:PRK06060   387 ADDTEVIGGVNVDPREVERLIIEDEAVAEA--AVVAVRESTGAST--LQAFLVATSGATIDGSvMRDLHRGLLNRLS--- 459

                          490       500
                   ....*....|....*....|....*...
gi 1573930569 2178 AFLIP---VEAEAIPKTEIGKIQRTKLR 2202
Cdd:PRK06060   460 AFKVPhrfAVVDRLPRTPNGKLVRGALR 487
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 1689-2202 9.58e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 83.20  E-value: 9.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGEVVhVRAdGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP----L 1764
Cdd:PRK13391     6 HAQTTPDKPAV-IMA-STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCvnshL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1765 TVP-VSYAT---------TSAAvsKLEGIWEMLD-----RPWIVTSAAGE-PGlrelaarreWSGLrlttADALREEPED 1828
Cdd:PRK13391    84 TPAeAAYIVddsgaraliTSAA--KLDVARALLKqcpgvRHRLVLDGDGElEG---------FVGY----AEAVAGLPAT 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1829 RDWYEARPDDlvlMLMTSGSTGLPKAVR--LTHRNV---LTRAAATEAMNGLGSGDVSLNWIPLDHVTGvvmfhLRDVYL 1903
Cdd:PRK13391   149 PIADESLGTD---MLYSSGTTGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAP-----QRAVML 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1904 GCRQihAPTSWILE--DPVRWPELADRHRVSVT-WAPNFAFGLL---AEQAHRFqdrdwDLSPVRLVmnagevvvasaar 1977
Cdd:PRK13391   221 VIRL--GGTVIVMEhfDAEQYLALIEEYGVTHTqLVPTMFSRMLklpEEVRDKY-----DLSSLEVA------------- 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1978 rfLHVLAPfgLPQDV---MHPGWGmsetcSVVTDSVLASEApdhdEAFVSCG----LPYPGFAMRVV-------DDQDAL 2043
Cdd:PRK13391   281 --IHAAAP--CPPQVkeqMIDWWG-----PIIHEYYAATEG----LGFTACDseewLAHPGTVGRAMfgdlhilDDDGAE 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2044 LPEGDVGRLQVRGTSvTHGYHDNARANAESFTEDG-WFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIE----- 2116
Cdd:PRK13391   348 LPPGEPGTIWFEGGR-PFEYLNDPAKTAEARHPDGtWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAEnllit 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2117 ------ACV-----EELPSVVRsftaAVAVRSDASAATDELALFLRLAPGQDPAGAlreiagKVTREIGvspaflipVEA 2185
Cdd:PRK13391   427 hpkvadAAVfgvpnEDLGEEVK----AVVQPVDGVDPGPALAAELIAFCRQRLSRQ------KCPRSID--------FED 488

                          570
                   ....*....|....*..
gi 1573930569 2186 EaIPKTEIGKIQRTKLR 2202
Cdd:PRK13391   489 E-LPRLPTGKLYKRLLR 504
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1835-2207 1.31e-15

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: 82.59  E-value: 1.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSG-----------DVSLnwipLDHVTgVVMFHlrdvyl 1903
Cdd:cd05918    104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSEsrvlqfasytfDVSI----LEIFT-TLAAG------ 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1904 GCrqIHAPTSWIledpvRWPELAD---RHRVsvTWA---PNFAFGLlaeqahrfqdrDWDLSP-VRLVMNAGEVVVASAA 1976
Cdd:cd05918    173 GC--LCIPSEED-----RLNDLAGfinRLRV--TWAfltPSVARLL-----------DPEDVPsLRTLVLGGEALTQSDV 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1977 RRFLHVLapfglpqdVMHPGWGMSETC--SVVTDSVLASEAPDhdeafvsCGLPYPGfAMRVVD--DQDALLPEGDVGRL 2052
Cdd:cd05918    233 DTWADRV--------RLINAYGPAECTiaATVSPVVPSTDPRN-------IGRPLGA-TCWVVDpdNHDRLVPIGAVGEL 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2053 QVRGTSVTHGYHDNARANAESFTED-GW------------FDTGDLA-FLRDGELYITGRAKDVIIVNGvnhysH----- 2113
Cdd:cd05918    297 LIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVrYNPDGSLEYVGRKDTQVKIRG-----Qrvelg 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2114 EIEACVEELPSVVRSFTAAVAVRSDASAAtDELALFLRLAPGQ-----------DPAGALREIAGKVTREIGVS------ 2176
Cdd:cd05918    372 EIEHHLRQSLPGAKEVVVEVVKPKDGSSS-PQLVAFVVLDGSSsgsgdgdslflEPSDEFRALVAELRSKLRQRlpsymv 450

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1573930569 2177 PAFLIPVeaEAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:cd05918    451 PSVFLPL--SHLPLTASGKIDRRALRELAES 479
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1816-2201 1.73e-15

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: 82.38  E-value: 1.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1816 LTTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEamnglgsgdvslNWIPLDHVTGVVM 1895
Cdd:cd17655    116 LLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWAN------------KVIYQGEHLRVAL 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1896 FHLRDVYLGCRQIHAP-----TSWILEDPVRWPELA-----DRHRVSVTWAPNFAFGLLAEQahrfqdRDWDLSPVRLVM 1965
Cdd:cd17655    184 FASISFDASVTEIFASllsgnTLYIVRKETVLDGQAltqyiRQNRITIIDLTPAHLKLLDAA------DDSEGLSLKHLI 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1966 NAGEVVVASAARRFLHVlapFGLPQDVMHpGWGMSETCsvVTDSVLASEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLP 2045
Cdd:cd17655    258 VGGEALSTELAKKIIEL---FGTNPTITN-AYGPTETT--VDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQP 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2046 EGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEAC 2118
Cdd:cd17655    332 VGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2119 VEELPSVVRsftAAVAVRSDASaatDELALFLRLAPGQD-PAGALREiagKVTREIgvsPAFLIP---VEAEAIPKTEIG 2194
Cdd:cd17655    412 LLQHPDIKE---AVVIARKDEQ---GQNYLCAYIVSEKElPVAQLRE---FLAREL---PDYMIPsyfIKLDEIPLTPNG 479


                   ....*..
gi 1573930569 2195 KIQRTKL 2201
Cdd:cd17655    480 KVDRKAL 486
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 883-958 1.91e-15

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: 73.35  E-value: 1.91e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569  883 EIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 1845-2210 4.43e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 81.15  E-value: 4.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1845 TSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTG-----------VVMFHLRDVylgcrqihapts 1913
Cdd:PRK08162   190 TSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGwcfpwtvaaraGTNVCLRKV------------ 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1914 wileDPVRWPELADRHRVSVTWAPNFAFGLLA---EQAHRFQDRdwdlsPVRlVMNAG----EVVVASAARRFLHVLAPF 1986
Cdd:PRK08162   258 ----DPKLIFDLIREHGVTHYCGAPIVLSALInapAEWRAGIDH-----PVH-AMVAGaappAAVIAKMEEIGFDLTHVY 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1987 GL-----PQDVM--HPGWgmsetcsvvtdsvlaSEAPDHDEAFVSC--GLPYPGFAMRVVDDQDALLP---EGD-VGRLQ 2053
Cdd:PRK08162   328 GLtetygPATVCawQPEW---------------DALPLDERAQLKArqGVRYPLQEGVTVLDPDTMQPvpaDGEtIGEIM 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2054 VRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsFTAA 2132
Cdd:PRK08162   393 FRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHpDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL--VAAV 469

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2133 VA---------------VRSDASAATDELALFLRLapgqdpagalrEIAG-KVTREIGVSPaflipveaeaIPKTEIGKI 2196
Cdd:PRK08162   470 VAkpdpkwgevpcafveLKDGASATEEEIIAHCRE-----------HLAGfKVPKAVVFGE----------LPKTSTGKI 528

                          410
                   ....*....|....*..
gi 1573930569 2197 QRTKLR---KSFEAGEF 2210
Cdd:PRK08162   529 QKFVLReqaKSLKAIDL 545
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 1833-2202 4.48e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 80.80  E-value: 4.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1833 EARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIH--- 1909
Cdd:PRK07787   124 EPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHtgr 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1910 -------------------APTSW--ILEDPVRWPELAD-RHRVSvtwapnfafGLLAEQAHRFQdrdwdlspvRLVMNA 1967
Cdd:PRK07787   204 ptpeayaqalseggtlyfgVPTVWsrIAADPEAARALRGaRLLVS---------GSAALPVPVFD---------RLAALT 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1968 GEVVVASaarrflhvlapfglpqdvmhpgWGMSETcsVVTDSVLAseapDHDEAFVSCGLPYPGFAMRVVDDQDALLPEG 2047
Cdd:PRK07787   266 GHRPVER----------------------YGMTET--LITLSTRA----DGERRPGWVGLPLAGVETRLVDEDGGPVPHD 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2048 D--VGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFLR-DGELYITGR-AKDVIIVNGVNHYSHEIEACVEELP 2123
Cdd:PRK07787   318 GetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDpDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHP 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2124 SVVRsftAAVA--------------VRSDASAATDELALFL--RLAPGQDPagalreiagkvtREIGVspaflipveAEA 2187
Cdd:PRK07787   398 GVRE---AAVVgvpdddlgqrivayVVGADDVAADELIDFVaqQLSVHKRP------------REVRF---------VDA 453

                          410
                   ....*....|....*
gi 1573930569 2188 IPKTEIGKIQRTKLR 2202
Cdd:PRK07787   454 LPRNAMGKVLKKQLL 468
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 456-924 5.26e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 81.14  E-value: 5.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  456 RTLPQLFEARVAESPGRTAVSY-------AG--ETLSYAELNAEANRLARLLVEQGAGPGRFVALAlPRGPRLVPALLAV 526
Cdd:PRK05850     1 SSVPSLLRERASLQPDDAAFTFidyeqdpAGvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  527 LKTGAAYLPLD---PGHPAERLALVMADAEPVAVVTDTAgsgrlpatdarvvVVDDARTVADLA--GRAPH----DLTDA 597
Cdd:PRK05850    80 LQAGLIAVPLSvpqGGAHDERVSAVLRDTSPSVVLTTSA-------------VVDDVTEYVAPQpgQSAPPvievDLLDL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  598 D-----RAGATGPYDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDVWTLfhsyafDFSVWElWGPLLH- 671
Cdd:PRK05850   147 DsprgsDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVPPP------DTTVVS-WLPFYHd 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 ------------GGRLVVVPYEVS--RSPREFLRLLDEEKVTVLNQTPSAFEqlvLADAAT---DRA---TGSLRYVVLG 731
Cdd:PRK05850   220 mglvlgvcapilGGCPAVLTSPVAflQRPARWMQLLASNPHAFSAAPNFAFE---LAVRKTsddDMAgldLGGVLGIISG 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  732 GEALVAERLRPWADR---HGLDAPELVNMYGITETTVHV------TFHRLVRADLED------PRRRGVIGRPL------ 790
Cdd:PRK05850   297 SERVHPATLKRFADRfapFNLRETAIRPSYGLAEATVYVatrepgQPPESVRFDYEKlsaghaKRCETGGGTPLvsygsp 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  791 ADLRVYVLDA-AGRPVPPGATGEMYVSGPGVAPGYLNRPELTEERF---LPDPF-GAPGTRMYRSGDLArWRPDGTLVHA 865
Cdd:PRK05850   377 RSPTVRIVDPdTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpGTPEGPWLRTGDLG-FISEGELFIV 455

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  866 GRADQQVKIRGFRIEPGEIEAVLTahpAVAGGAVVPRAAEDGLT-QLVAYAVPAEEGGAD 924
Cdd:PRK05850   456 GRIKDLLIVDGRNHYPDDIEATIQ---EITGGRVAAISVPDDGTeKLVAIIELKKRGDSD 512
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1703-2125 7.21e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 80.50  E-value: 7.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1703 ADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyatTSAAVSKLEG 1782
Cdd:PRK08008    31 SGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN-------ARLLREESAW 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1783 IWEMLDRPWIVTSAAGEPGLRELaaRREWSGL---RLTTADALREEPEDRDWY-----------EARP---DDLVLMLMT 1845
Cdd:PRK08008   104 ILQNSQASLLVTSAQFYPMYRQI--QQEDATPlrhICLTRVALPADDGVSSFTqlkaqqpatlcYAPPlstDDTAEILFT 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1846 SGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHV-----TGVVMFHLRDVYLGCRQIHAPTSWileDPV 1920
Cdd:PRK08008   182 SGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIdcqctAAMAAFSAGATFVLLEKYSARAFW---GQV 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1921 RwpeladRHRVSVTWAPNFAFGLLAEQAHRFQDRDWDLSPVRLVMNAGEVVVASAARRFLHVLAPfglpqdvmhpGWGMS 2000
Cdd:PRK08008   259 C------KYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLT----------SYGMT 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2001 ET-CSVVTDSvlaseaPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGT---SVTHGYHDNARANAESFTE 2076
Cdd:PRK08008   323 ETiVGIIGDR------PGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEA 396

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2077 DGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSV 2125
Cdd:PRK08008   397 DGWLHTGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 477-958 9.92e-15

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: 79.78  E-value: 9.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  477 YAGETLSYAELNAEANRLARLLV-EQGAGPGRFVALALPRGPRLVPALLAVLKTGAAylpldpghpaerlalvmadaePV 555
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------------------PA 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  556 AVVTDTAGSGR---LPATDARVVVVDDArtvadlagraphdltdadragatgpyDTAYVIHTSGSTGRPKGVPVPHAHVV 632
Cdd:cd05937     60 FINYNLSGDPLihcLKLSGSRFVIVDPD--------------------------DPAILIYTSGTTGLPKAAAISWRRTL 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  633 R--LFEASGEHFRFGaDDVWT---LFHSYAFDFSvweLWGPLLHGGRLVVVPyevSRSPREFLRLLDEEKVTVLNQTPSA 707
Cdd:cd05937    114 VtsNLLSHDLNLKNG-DRTYTcmpLYHGTAAFLG---ACNCLMSGGTLALSR---KFSASQFWKDVRDSGATIIQYVGEL 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  708 FEQLVLADAATDRATGSLRYVVLGGealvaerLRP--WAD-RHGLDAPELVNMYGITETTVHVTFHRLVRADLEDPRRRG 784
Cdd:cd05937    187 CRYLLSTPPSPYDRDHKVRVAWGNG-------LRPdiWERfRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHG 259

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  785 VIGRPLADLRVYVL-------DAAGRP-------VPPGATGEMYVSGP----GVAPGYLNRPELTEERFLPDPFgAPGTR 846
Cdd:cd05937    260 LIRRWKFENQVVLVkmdpetdDPIRDPktgfcvrAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRDVF-RKGDI 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  847 MYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAG----GAVVP----RAAEDGLTQLVAYAVPA 918
Cdd:cd05937    339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEanvyGVKVPghdgRAGCAAITLEESSAVPT 418

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1573930569  919 EEggaDPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:cd05937    419 EF---TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHK 455
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 570-895 1.08e-14

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: 79.95  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  570 TDARVVVVDDARTV------ADLAGRAPHDLTDADragatgPYDTAYVIHTSGSTGRPKGVPVPHAHVV----RLFEASG 639
Cdd:cd05927     78 AEISIVFCDAGVKVysleefEKLGKKNKVPPPPPK------PEDLATICYTSGTTGNPKGVMLTHGNIVsnvaGVFKILE 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  640 EHFRFGADDVWTLFHSYAFDFSVWELWGPLLHGGRL---------------VVVPYEVSRSPREFLRLLDEEKVTVLNQT 704
Cdd:cd05927    152 ILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIgfysgdirlllddikALKPTVFPGVPRVLNRIYDKIFNKVQAKG 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  705 PSafeQLVLADAATDRAT---------------------------GSLRYVVLGGEAL---VAERLRPwadrhGLDAPeL 754
Cdd:cd05927    232 PL---KRKLFNFALNYKLaelrsgvvraspfwdklvfnkikqalgGNVRLMLTGSAPLspeVLEFLRV-----ALGCP-V 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  755 VNMYGITETTVHVTFhrlvraDLEDPRRRGVIGRPLADLRVYVLDaagrpVP--------PGATGEMYVSGPGVAPGYLN 826
Cdd:cd05927    303 LEGYGQTECTAGATL------TLPGDTSVGHVGGPLPCAEVKLVD-----VPemnydakdPNPRGEVCIRGPNVFSGYYK 371

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  827 RPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKI-RGFRIEPGEIEAVLTAHPAVA 895
Cdd:cd05927    372 DPEKTAEALDEDGW-------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVA 434
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1825-2203 1.98e-14

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: 79.53  E-value: 1.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1825 EPEDRDwyearPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT-EAMNGLGSGDV-----SLNWIpldhvTGvvmfHL 1898
Cdd:cd05966    224 EPEWMD-----SEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTfKYVFDYHPDDIywctaDIGWI-----TG----HS 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1899 RDVY----LGCrqihapTSWILE------DPVRWPELADRHRVSVTW-APN-----FAFGLLAEQAHrfqdrdwDLSPVR 1962
Cdd:cd05966    290 YIVYgplaNGA------TTVMFEgtptypDPGRYWDIVEKHKVTIFYtAPTairalMKFGDEWVKKH-------DLSSLR 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1963 LVMNAGEVVVASAARRFLHVLapfGLPQDVMHPGWGMSETCSVVTdSVLASEAPDHDEafvSCGLPYPGFAMRVVDDQDA 2042
Cdd:cd05966    357 VLGSVGEPINPEAWMWYYEVI---GKERCPIVDTWWQTETGGIMI-TPLPGATPLKPG---SATRPFFGIEPAILDEEGN 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2043 LLPEGDVGRLQVRGT--SVTHG-YHDNARANAESFTED-GWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEA 2117
Cdd:cd05966    430 EVEGEVEGYLVIKRPwpGMARTiYGDHERYEDTYFSKFpGYYFTGDGARRdEDGYYWITGRVDDVINVSGHRLGTAEVES 509

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2118 CVEELPSVVRsftAAVAVRSDasAATDE-LALFLRLAPGQDPAGALR-EIAGKVTREIGvspAFLIP---VEAEAIPKTE 2192
Cdd:cd05966    510 ALVAHPAVAE---AAVVGRPH--DIKGEaIYAFVTLKDGEEPSDELRkELRKHVRKEIG---PIATPdkiQFVPGLPKTR 581

                          410
                   ....*....|.
gi 1573930569 2193 IGKIQRTKLRK 2203
Cdd:cd05966    582 SGKIMRRILRK 592
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 479-959 2.02e-14

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: 78.62  E-value: 2.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  479 GETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVV 558
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  559 TDTagsgrlpatdarvvvvddartVADLAGRAPHDLTDADRAGATgpyDTAYVIHTSGSTGRPKGVPVPHAHVVRLFEAS 638
Cdd:cd05939     81 FNL---------------------LDPLLTQSSTEPPSQDDVNFR---DKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGA 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  639 GEHFRFGADDVW----TLFHSYAFDFSVwelwGPLLHGGRLVVVPYEVSRSprEFLRLLDEEKVTV-----------LNQ 703
Cdd:cd05939    137 YYAFGMRPEDVVydclPLYHSAGGIMGV----GQALLHGSTVVIRKKFSAS--NFWDDCVKYNCTIvqyigeicrylLAQ 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  704 TPSAFEQlvladaatdraTGSLRYVVlgGEALVAERLRPWADRHGLdaPELVNMYGITETT---VHVTFH---------- 770
Cdd:cd05939    211 PPSEEEQ-----------KHNVRLAV--GNGLRPQIWEQFVRRFGI--PQIGEFYGATEGNsslVNIDNHvgacgfnsri 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  771 -------RLVRADlEDprrrgvIGRPLADLrvyvlDAAGRPVPPGATGEMYVSGPGVAP-----GYLNRPElTEERFLPD 838
Cdd:cd05939    276 lpsvypiRLIKVD-ED------TGELIRDS-----DGLCIPCQPGEPGLLVGKIIQNDPlrrfdGYVNEGA-TNKKIARD 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  839 PFgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLT----AHPAVAGGAVVPRAaeDGLTQLVAY 914
Cdd:cd05939    343 VF-KKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSnvlgLEDVVVYGVEVPGV--EGRAGMAAI 419

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569  915 AVPaeEGGADPAGLRAHLAARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:cd05939    420 VDP--ERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKL 462
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 10-325 3.90e-14

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: 77.35  E-value: 3.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFL--DTPDGPRAVRDGDpdEMPVH 87
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwrDRAEPLQYVRDDL--APPWA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   88 RVDVSGEA--DPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAA 165
Cdd:cd19547     81 LLDWSGEDpdRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  166 GEEP---PPAGFESADRLAAEEAAylgsdRHRRDRAYWTERLAGL-PEPVrltdRTAPPRAPFLRRTAVLSPAE--TRAL 239
Cdd:cd19547    161 GREPqlsPCRPYRDYVRWIRARTA-----QSEESERFWREYLRDLtPSPF----STAPADREGEFDTVVHEFPEqlTRLV 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  240 DEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSR---LGSAALRTpGTASDILPLRVAASADTPVGGFVRAVA 316
Cdd:cd19547    232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppeLEGSEHMV-GIFINTIPLRIRLDPDQTVTGLLETIH 310


                   ....*....
gi 1573930569  317 DDLRGLRAH 325
Cdd:cd19547    311 RDLATTAAH 319
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1711-2203 4.87e-14

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: 77.22  E-value: 4.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPltvpvsyATTSAAVSKLEgiwEMLDRP 1790
Cdd:cd05974      2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------ATTLLTPDDLR---DRVDRG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1791 WIVTSAAGEpglrelaarrewsglrlttadalreepedrdwyEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:cd05974     72 GAVYAAVDE---------------------------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGDVSLN--------------WIPLDHVTGVVMFHLRDVylgcrqihaptswileDPVRWPELADRHRVSVTWA 1936
Cdd:cd05974    119 YWIGLKPGDVHWNisspgwakhawscfFAPWNAGATVFLFNYARF----------------DAKRVLAALVRYGVTTLCA 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1937 PNFAFGLLAEQahrfqdrdwDLS----PVRLVMNAGEVVVASAARRflhVLAPFGLpqdVMHPGWGMSETcsvvtdSVLA 2012
Cdd:cd05974    183 PPTVWRMLIQQ---------DLAsfdvKLREVVGAGEPLNPEVIEQ---VRRAWGL---TIRDGYGQTET------TALV 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2013 SEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRL--QVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFLR- 2089
Cdd:cd05974    242 GNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDlgDTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDe 320

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2090 DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAATDELAlFLRLAPGQDPAGALREIAGKV 2169
Cdd:cd05974    321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAE---AAVVPSPDPVRLSVPKA-FIVLRAGYEPSPETALEIFRF 396

                          490       500       510
                   ....*....|....*....|....*....|....
gi 1573930569 2170 TREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05974    397 SRERLAPYKRIRRLEFAELPKTISGKIRRVELRR 430
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 605-919 6.77e-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: 77.26  E-value: 6.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  605 PYDTAYVIHTSGSTGRPKGVPVPHAHVV--------RLFEASGEhfrfgaDDVWT----LFHSYAFDF-SVWELWGPLL- 670
Cdd:cd17639     87 PDDLACIMYTSGSTGNPKGVMLTHGNLVagiaglgdRVPELLGP------DDRYLaylpLAHIFELAAeNVCLYRGGTIg 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  671 ---------------HGG-------RLVVVPyevsrspreflRLLDEEKVTVLNQ--TPSAFEQLV-------------- 712
Cdd:cd17639    161 ygsprtltdkskrgcKGDltefkptLMVGVP-----------AIWDTIRKGVLAKlnPMGGLKRTLfwtayqsklkalke 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  713 -----LADAAT----DRATGS-LRYVVLGGEALVAerlrpwadrhglDAPELVNM--------YGITETTVHVTFHRLvr 774
Cdd:cd17639    230 gpgtpLLDELVfkkvRAALGGrLRYMLSGGAPLSA------------DTQEFLNIvlcpviqgYGLTETCAGGTVQDP-- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  775 ADLEDprrrGVIGRPLADLRVYVLD------AAGRPVPpgaTGEMYVSGPGVAPGYLNRPELTEERFLPDpfgapgtRMY 848
Cdd:cd17639    296 GDLET----GRVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAFDGD-------GWF 361

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  849 RSGDLARWRPDGTLVHAGRADQQVKIR-GFRIEPGEIEAVLTAHPAVAGGAVVPRAAEdglTQLVAYAVPAE 919
Cdd:cd17639    362 HTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK---SYPVAIVVPNE 430
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 609-900 8.04e-14

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: 77.14  E-value: 8.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  609 AYVIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGADDV---W-TLFHSY---AFDFSvwelwgPLLHGGRLVVVPYE 681
Cdd:cd05908    109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRilsWmPLTHDMgliAFHLA------PLIAGMNQYLMPTR 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  682 V-SRSPREFLRLLDEEKVTVLNqTPSAFEQLVLADAATDRAT----GSLRYVVLGGEALVAERLRPWADR---HGLDAPE 753
Cdd:cd05908    183 LfIRRPILWLKKASEHKATIVS-SPNFGYKYFLKTLKPEKANdwdlSSIRMILNGAEPIDYELCHEFLDHmskYGLKRNA 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  754 LVNMYGITETTVHVTF--------------------HRLVRADLEDPRRRGVI--GRPLADLRVYVLDAAGRPVPPGATG 811
Cdd:cd05908    262 ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgEPEPEVDKKDSECLTFVevGKPIDETDIRICDEDNKILPDGYIG 341

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  812 EMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRpDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAH 891
Cdd:cd05908    342 HIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413


                   ....*....
gi 1573930569  892 PAVAGGAVV 900
Cdd:cd05908    414 EGVELGRVV 422
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 480-940 8.95e-14

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: 76.74  E-value: 8.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVT 559
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  560 dtagsGRLPATDARVVVV---------------DDARTVADLAGRAPhDLTDADRagaTGPYDTAYVIHTSGSTGRPKGV 624
Cdd:cd05932     85 -----GKLDDWKAMAPGVpeglisislpppsaaNCQYQWDDLIAQHP-PLEERPT---RFPEQLATLIYTSGTTGQPKGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  625 P----------------------------VPHAHVVRLFEASGEHFRFGAddvwTLFHSYAFD--------------FSV 662
Cdd:cd05932    156 MltfgsfawaaqagiehigteendrmlsyLPLAHVTERVFVEGGSLYGGV----LVAFAESLDtfvedvqrarptlfFSV 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  663 WELWGPLLHGgrlvvvpyEVSRSPREFLRLLdeEKVTVLNqtpSAFEQLVLADAATDRATgslryVVLGGEALVAERLRP 742
Cdd:cd05932    232 PRLWTKFQQG--------VQDKIPQQKLNLL--LKIPVVN---SLVKRKVLKGLGLDQCR-----LAGCGSAPVPPALLE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  743 WADRHGLDAPElvnMYGITETTVHVTFHRLVRadledpRRRGVIGRPLADLRVYVLDaagrpvppgaTGEMYVSGPGVAP 822
Cdd:cd05932    294 WYRSLGLNILE---AYGMTENFAYSHLNYPGR------DKIGTVGNAGPGVEVRISE----------DGEILVRSPALMM 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  823 GYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRADQQVKI-RGFRIEPGEIEAVLTAHPAVAGGAVVp 901
Cdd:cd05932    355 GYYKDPEATAEAFTADGF-------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI- 426

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1573930569  902 raaEDGLTQLVAYAVPAEEGGADP-AGLRAHLAARLPAYM 940
Cdd:cd05932    427 ---GSGLPAPLALVVLSEEARLRAdAFARAELEASLRAHL 463
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 10-274 1.14e-13

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: 76.15  E-value: 1.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADtfALR--FLDTPDGPR-AVRDGDPDEMPV 86
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHE--SLRtvFPEEDGVPYqLILEEDEATPKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   87 HRVDVSGEADPAAaaeewIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAG 166
Cdd:cd19538     81 EIKEVDEEELESE-----INEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  167 EEPP--PAGFESADrLAAEEAAYLGSDRHR-----RDRAYWTERLAGLPEPVRL-TDRTAPPRAPF--LRRTAVLSPAET 236
Cdd:cd19538    156 EAPElaPLPVQYAD-YALWQQELLGDESDPdsliaRQLAYWKKQLAGLPDEIELpTDYPRPAESSYegGTLTFEIDSELH 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1573930569  237 RALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLG 274
Cdd:cd19538    235 QQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIG 272
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 10-427 1.42e-13

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: 75.42  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGlwFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVreaDTFA-LR--FLDTPDGPRAV----RDGDPd 82
Cdd:cd19542      3 PCTPMQEG--MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLV---QRHDiLRtvFVESSAEGTFLqvvlKSLDP- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   83 emPVHRVDVSGEADPAaaaeewIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTA 162
Cdd:cd19542     77 --PIEEVETDEDSLDA------LTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  163 LAAGEEPPPAGFesadrlaaeeAAYLGSDRHRRDRAYWTERLAGLPEPvrlTDRTAPPRAPFLRRTAVlSPAETRALDEA 242
Cdd:cd19542    149 QLLPPAPPFSDY----------ISYLQSQSQEESLQYWRKYLQGASPC---AFPSLSPKRPAERSLSS-TRRSLAKLEAF 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  243 AKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGS--AALRTPGTASDILPLRVAASADTPVGGFVRAVADDLR 320
Cdd:cd19542    215 CASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPvpGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYL 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  321 GLRAHQRHRGESIRRDLGVLGRGRR----VHgpVVNIVPFSEDLTFGGHPSTSHHLSGGAVDDLQISVRPGAEADTLWLA 396
Cdd:cd19542    295 RSLPHQHLSLREIQRALGLWPSGTLfntlVS--YQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLA 372

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1573930569  397 FDahPDLYEEDGLALFLERFLKVLRELRTCP 427
Cdd:cd19542    373 YS--TSVLSEEQAEELLEQFDDILEALLANP 401
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 1687-2205 1.73e-13

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 76.28  E-value: 1.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1687 LLRAAGR--PDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVilqcddtedfvATL-----------WG 1753
Cdd:PRK07008    15 LIAHAARhaGDTEIVSRRVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRV-----------GTLawngyrhleayYG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1754 CvlGGFVAVPLTV-PVSYATTSAavsklegiwemldrpWIVTSAAGE---------PGLRELAAR----REWsgLRLTTA 1819
Cdd:PRK07008    84 V--SGSGAVCHTInPRLFPEQIA---------------YIVNHAEDRyvlfdltflPLVDALAPQcpnvKGW--VAMTDA 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1820 DALreePED-------RDWYEARPDDLVL----------MLMTSGSTGLPKAVRLTHRNVLTRAAAT---EAMnGLGSGD 1879
Cdd:PRK07008   145 AHL---PAGstpllcyETLVGAQDGDYDWprfdenqassLCYTSGTTGNPKGALYSHRSTVLHAYGAalpDAM-GLSARD 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1880 VSLNWIPLDHVTG------VVMFHLRDVYLGCRQihaptswileDPVRWPELADRHRVSVTWA-PNFAFGLLaeqaHRFQ 1952
Cdd:PRK07008   221 AVLPVVPMFHVNAwglpysAPLTGAKLVLPGPDL----------DGKSLYELIEAERVTFSAGvPTVWLGLL----NHMR 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1953 DRDWDLSPVRLVMNAGEVVVASAARRFLHVlapFGLpqDVMHpGWGMSETCSVVTDSVLASEAPDHDEA-----FVSCGL 2027
Cdd:PRK07008   287 EAGLRFSTLRRTVIGGSACPPAMIRTFEDE---YGV--EVIH-AWGMTEMSPLGTLCKLKWKHSQLPLDeqrklLEKQGR 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2028 PYPGFAMRVVDDQDALLPEGDV--GRLQVRGTSVTHGYHdnarANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVII 2104
Cdd:PRK07008   361 VIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYF----RGDASPLVDGWFPTGDVATIdADGFMQITDRSKDVIK 436

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2105 VNGVNHYSHEIE------------ACV-------EELPSVVrsftaaVAVRSDASAATDELALFLRlapgqdpagalrei 2165
Cdd:PRK07008   437 SGGEWISSIDIEnvavahpavaeaACIacahpkwDERPLLV------VVKRPGAEVTREELLAFYE-------------- 496

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1573930569 2166 aGKVTReigvspaFLIP---VEAEAIPKTEIGKIQRTKLRKSF 2205
Cdd:PRK07008   497 -GKVAK-------WWIPddvVFVDAIPHTATGKLQKLKLREQF 531
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 1694-2202 1.79e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 75.82  E-value: 1.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1694 PDGEVVHVRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVP----LTVPV- 1768
Cdd:PRK13390    11 PDRPAVIVAETGEQV--SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAinhhLTAPEa 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 ------SYATTSAAVSKLEGIWEMLDRPWIVTSAAGE--PGLRELAARREWSGLRLTtadalrEEPEDrdwyearpddlV 1840
Cdd:PRK13390    89 dyivgdSGARVLVASAALDGLAAKVGADLPLRLSFGGeiDGFGSFEAALAGAGPRLT------EQPCG-----------A 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1841 LMLMTSGSTGLPKAVR--LTHRNVLTRA----AATEAMNGLGSGDVSLNWIPLDHVTGvvmfhLRdvylGCRQIHAPTSW 1914
Cdd:PRK13390   152 VMLYSSGTTGFPKGIQpdLPGRDVDAPGdpivAIARAFYDISESDIYYSSAPIYHAAP-----LR----WCSMVHALGGT 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1915 IL-------EDPVRWPEladRHRVSVTWAPNFAFGLLAEQAHRFQDRdWDLSPVRLVmnagevvvasaarrfLHVLAPfg 1987
Cdd:PRK13390   223 VVlakrfdaQATLGHVE---RYRITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAV---------------IHAAAP-- 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1988 LPQDVMHP--GWgmseTCSVVTDSVLASEApdHDEAFVSCG--LPYPGFAMRVV-------DDQDALLPEGDVGRLQVRG 2056
Cdd:PRK13390   282 CPVDVKHAmiDW----LGPIVYEYYSSTEA--HGMTFIDSPdwLAHPGSVGRSVlgdlhicDDDGNELPAGRIGTVYFER 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2057 TSVTHGYHDNAR--ANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsFTAAV 2133
Cdd:PRK13390   356 DRLPFRYLNDPEktAAAQHPAHPFWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAV---HDVAV 432

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2134 AVRSDASAAtDELALFLRLAPGQDPAGAL-REIAGKVTREIGVSPAFLIPVEAEAIPKTEIGKIQRTKLR 2202
Cdd:PRK13390   433 IGVPDPEMG-EQVKAVIQLVEGIRGSDELaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 1653-2090 1.96e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 76.24  E-value: 1.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1653 AEPDApSVERPAS---VPALSEGPALPEPSVSGWAEAllRAAGRPDGEVVHVRA--DGSETRRSYASLVPEASRVLAGLR 1727
Cdd:PRK12582    22 KPPDI-SVERRADgsiVIKSRHPLGPYPRSIPHLLAK--WAAEAPDRPWLAQREpgHGQWRKVTYGEAKRAVDALAQALL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1728 RRGLRPGDRV-ILQCDDTEDFVATLwGCVLGGFVAVPLTVPvsYATTSAAVSKLEGIWEMLdRPWIVTSAAGEPGLRELA 1806
Cdd:PRK12582    99 DLGLDPGRPVmILSGNSIEHALMTL-AAMQAGVPAAPVSPA--YSLMSHDHAKLKHLFDLV-KPRVVFAQSGAPFARALA 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1807 ARREwSGLRLTTADALRE------------EPEDRDWYEAR----PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE 1870
Cdd:PRK12582   175 ALDL-LDVTVVHVTGPGEgiasiafadlaaTPPTAAVAAAIaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQE 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1871 AMNGLGSGD---VSLNWIPLDHVT-GVVMFHLRDVYLGCRQIHA--PTSWILEDPVRwpelaDRHRVSVTWAPN--FAFG 1942
Cdd:PRK12582   254 QLRPREPDPpppVSLDWMPWNHTMgGNANFNGLLWGGGTLYIDDgkPLPGMFEETIR-----NLREISPTVYGNvpAGYA 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1943 LLAEQahrfQDRDWDL-----SPVRLVMNAG------------EVVVASAARRFlhvlapfglpqdVMHPGWGMSETCSV 2005
Cdd:PRK12582   329 MLAEA----MEKDDALrrsffKNLRLMAYGGatlsddlyermqALAVRTTGHRI------------PFYTGYGATETAPT 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2006 VTDSVLASEAPDhdeafvSCGLPYPGFAMRvvddqdaLLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDL 2085
Cdd:PRK12582   393 TTGTHWDTERVG------LIGLPLPGVELK-------LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDA 459


                   ....*
gi 1573930569 2086 AFLRD 2090
Cdd:PRK12582   460 ARFVD 464
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 1836-2098 2.08e-13

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 76.01  E-value: 2.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGcrqIHAPTSWI 1915
Cdd:PRK06334   182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG---VPVVFAYN 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 LEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRfqdRDWDLSPVRLVMNAGEVVVASaarrfLHVLAPFGLPQDVMHP 1995
Cdd:PRK06334   259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKK---QESCLPSLRFVVIGGDAFKDS-----LYQEALKTFPHIQLRQ 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1996 GWGMSETCSVVTdsVLASEAPDHDeafvSC-GLPYPGFAMRVVDDQDAL-LPEGDVGRLQVRGTSVTHGYHDNARanAES 2073
Cdd:PRK06334   331 GYGTTECSPVIT--INTVNSPKHE----SCvGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDF--GQG 402

                          250       260
                   ....*....|....*....|....*....
gi 1573930569 2074 FTE---DGWFDTGDLAFL-RDGELYITGR 2098
Cdd:PRK06334   403 FVElggETWYVTGDLGYVdRHGELFLKGR 431
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 1701-2203 3.29e-13

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: 75.19  E-value: 3.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1701 VRADGSETRRSYASLvPEASRVLAGLRRR--GLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPVS-----YATT 1773
Cdd:cd05928     33 VNGKGDEVKWSFREL-GSLSRKAANVLSGacGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTakdilYRLQ 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1774 SaavSKLEGIWEMLDRPWIVTSAAGE-PGLRE--LAARREWSGLrLTTADALREEPEDRDWYEARPDDLVLMLMTSGSTG 1850
Cdd:cd05928    112 A---SKAKCIVTSDELAPEVDSVASEcPSLKTklLVSEKSRDGW-LNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1851 LPKAVRLTHRNVLTRAAateaMNG-----LGSGDVSlnWIPLDhvTGVVMFHLRDVY----LG-CRQIHA----PTSWIL 1916
Cdd:cd05928    188 SPKMAEHSHSSLGLGLK----VNGrywldLTASDIM--WNTSD--TGWIKSAWSSLFepwiQGaCVFVHHlprfDPLVIL 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1917 EDPVRWPeladrhrVSVTWAPNFAFGLLAEQ---AHRFQDrdwdlspVRLVMNAGEVVVASAARRFLHVLapfGLPqdvM 1993
Cdd:cd05928    260 KTLSSYP-------ITTFCGAPTVYRMLVQQdlsSYKFPS-------LQHCVTGGEPLNPEVLEKWKAQT---GLD---I 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1994 HPGWGMSETCSVVTDSVLASEAPDhdeafvSCGLPYPGFAMRVVDDQDALLP---EGDVG-RLQ-VRGTSVTHGYHDNAR 2068
Cdd:cd05928    320 YEGYGQTETGLICANFKGMKIKPG------SMGKASPPYDVQIIDDNGNVLPpgtEGDIGiRVKpIRPFGLFSGYVDNPE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2069 ANAESFTEDGWFdTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftaavAVRSDASAATDELA 2147
Cdd:cd05928    394 KTAATIRGDFYL-TGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVES-----AVVSSPDPIRGEVV 467

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2148 -LFLRLAP---GQDPAGALREIAGKVTReigVSPAFLIPVEAEAI---PKTEIGKIQRTKLRK 2203
Cdd:cd05928    468 kAFVVLAPqflSHDPEQLTKELQQHVKS---VTAPYKYPRKVEFVqelPKTVTGKIQRNELRD 527
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1836-2201 3.74e-13

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: 74.51  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1836 PDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNW--IPLDHVTGVVMFHLrdvyLGCRQIHAPTS 1913
Cdd:cd17645    103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYasFSFDASAWEIFPHL----TAGAALHVVPS 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1914 WILEDPVRWPELADRHRVSVTWAPNfafgLLAEQAHRFqdrdwDLSPVRLVMNAGEVVvasaaRRFlhVLAPFGLPQdvm 1993
Cdd:cd17645    179 ERRLDLDALNDYFNQEGITISFLPT----GAAEQFMQL-----DNQSLRVLLTGGDKL-----KKI--ERKGYKLVN--- 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1994 hpGWGMSETCSVVTdsvlaSEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAES 2073
Cdd:cd17645    240 --NYGPTENTVVAT-----SFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2074 FTEDGW------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVrsfTAAVAVRSDASAATDEL 2146
Cdd:cd17645    313 FIVHPFvpgermYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIE---LAAVLAKEDADGRKYLV 389

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2147 ALFlrLAPGQDPAGALREIAGKVTreigvsPAFLIP---VEAEAIPKTEIGKIQRTKL 2201
Cdd:cd17645    390 AYV--TAPEEIPHEELREWLKNDL------PDYMIPtyfVHLKALPLTANGKVDRKAL 439
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 1835-2125 3.78e-13

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: 75.09  E-value: 3.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRN-VLTRAAATEAMnGLGSGDVS----LNWIPLDHVTGVVMfhlrDVYL-----G 1904
Cdd:cd05933    148 KPNQCCTLIYTSGTTGMPKGVMLSHDNiTWTAKAASQHM-DLRPATVGqesvVSYLPLSHIAAQIL----DIWLpikvgG 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1905 CRQIHAPTS--WILEDPVR-------------WPELADR-----------HRVSVTWAPNFAFgllaEQAHRFQDRDwdl 1958
Cdd:cd05933    223 QVYFAQPDAlkGTLVKTLRevrptafmgvprvWEKIQEKmkavgaksgtlKRKIASWAKGVGL----ETNLKLMGGE--- 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1959 SPVRLVMNAGEVVVASAARRFL-----HVLAPFGLP--QDVMH----------PGWGMSETCSVVTDSVLASEApdhdea 2021
Cdd:cd05933    296 SPSPLFYRLAKKLVFKKVRKALgldrcQKFFTGAAPisRETLEfflslnipimELYGMSETSGPHTISNPQAYR------ 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2022 FVSCGLPYPGFAMRVvDDQDAllpEGDvGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAK 2100
Cdd:cd05933    370 LLSCGKALPGCKTKI-HNPDA---DGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLdEDGFLYITGRIK 444

                          330       340
                   ....*....|....*....|....*...
gi 1573930569 2101 DVIIVNG---VNHYSHEiEACVEELPSV 2125
Cdd:cd05933    445 ELIITAGgenVPPVPIE-DAVKKELPII 471
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 1837-2199 4.93e-13

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 74.03  E-value: 4.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATE---AMNGLGSGDVSLNWIPLDHVTGVVMFHLrdvylGCRQIHAPTS 1913
Cdd:COG1541     83 EEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFArslRAAGVRPGDRVQNAFGYGLFTGGLGLHY-----GAERLGATVI 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1914 WI----LEDPVRwpeLADRHRVSVTWA-PNFAFgLLAEQAHRfQDRDWDLSPVRLVMNAGEVVvASAARRFLHvlAPFGL 1988
Cdd:COG1541    158 PAgggnTERQLR---LMQDFGPTVLVGtPSYLL-YLAEVAEE-EGIDPRDLSLKKGIFGGEPW-SEEMRKEIE--ERWGI 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1989 PqdvMHPGWGMSETCSVVtdsvlASEAPDHDeafvscGLPYPG--FAMRVVD-DQDALLPEGDVGRLqVrgtsVThgyhd 2065
Cdd:COG1541    230 K---AYDIYGLTEVGPGV-----AYECEAQD------GLHIWEdhFLVEIIDpETGEPVPEGEEGEL-V----VT----- 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2066 naranaeSFTEDGW----FDTGDLAFLRDGE----------LYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTa 2131
Cdd:COG1541    286 -------TLTKEAMplirYRTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQ- 357

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2132 AVAVRSDasaATDELALFLRLAPGQDPAGALREIAGKVTREIGVSPAFLIpVEAEAIPKTEiGKIQRT 2199
Cdd:COG1541    358 IVVDREG---GLDELTVRVELAPGASLEALAEAIAAALKAVLGLRAEVEL-VEPGSLPRSE-GKAKRV 420
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 1707-2203 7.90e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 73.95  E-value: 7.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGL--RPGDRVILQcDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLEGIW 1784
Cdd:PRK07867    26 DSFTSWREHIRGSAARAAALRARLDptRPPHVGVLL-DNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1785 EMLDRPWIVTSAAGEPGLREL-AARREWSGLRLTTADAlreEPEDRDwyeARPDDLVLMLMTSGSTGLPKAVRLTHRNVL 1863
Cdd:PRK07867   105 VLTESAHAELLDGLDPGVRVInVDSPAWADELAAHRDA---EPPFRV---ADPDDLFMLIFTSGTSGDPKAVRCTHRKVA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1864 TRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGC-----RQIHAPTSwiledpvrwpeLADRHRVSVTWApN 1938
Cdd:PRK07867   179 SAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGAsialrRKFSASGF-----------LPDVRRYGATYA-N 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1939 F-----AFGLLAEQahRFQDRDwdlSPVRLVM--NAGEVVVASAARRF-LHVLapfglpqdvmhPGWGMSETcsvvtdSV 2010
Cdd:PRK07867   247 YvgkplSYVLATPE--RPDDAD---NPLRIVYgnEGAPGDIARFARRFgCVVV-----------DGFGSTEG------GV 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2011 LASEAPDHDEAfvSCGLPYPGFAMR-----------VVDDQDALLPEGDVGRL-QVRGTSVTHGYHDNARANAESFtEDG 2078
Cdd:PRK07867   305 AITRTPDTPPG--ALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELvNTAGPGGFEGYYNDPEADAERM-RGG 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2079 WFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDAsAATDELALFLRLAPGQ- 2156
Cdd:PRK07867   382 VYWSGDLAYRdADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE---VAVYAVPDP-VVGDQVMAALVLAPGAk 457

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1573930569 2157 -DPAGALREIAGKVTREIGVSPAFlIPVEAEaIPKTEIGKIQRTKLRK 2203
Cdd:PRK07867   458 fDPDAFAEFLAAQPDLGPKQWPSY-VRVCAE-LPRTATFKVLKRQLSA 503
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1805-2158 1.58e-12

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 72.60  E-value: 1.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1805 LAARREWSGLRLTTADALREEPEDrDWyeaRPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGD---VS 1881
Cdd:PRK09029   107 LEGENTFSALTSLHLQLVEGAHAV-AW---QPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDswlLS 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1882 LnwiPLDHVTGVVMFHlRDVYLGCRqIHAPTSWILEDPVRwpeladrhrvSVTWApnfafGLLAEQAHRFQDrdWDLSPV 1961
Cdd:PRK09029   183 L---PLFHVSGQGIVW-RWLYAGAT-LVVRDKQPLEQALA----------GCTHA-----SLVPTQLWRLLD--NRSEPL 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1962 RL--VMNAGEVVVAS----AARRFLHVLApfglpqdvmhpGWGMSETCSVVTdsvlASEAPDHDEAfvscGLPYPGFAMR 2035
Cdd:PRK09029   241 SLkaVLLGGAAIPVElteqAEQQGIRCWC-----------GYGLTEMASTVC----AKRADGLAGV----GSPLPGREVK 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2036 VVDDqdallpegdvgRLQVRGTSVTHGYHDNARANaeSFT-EDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHE 2114
Cdd:PRK09029   302 LVDG-----------EIWLRGASLALGYWRQGQLV--PLVnDEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEE 368

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2115 IEACVEELPSVVRSFTAAVA-----------VRSDASAATDELALFL--RLAPGQDP 2158
Cdd:PRK09029   369 IERVINQHPLVQQVFVVPVAdaefgqrpvavVESDSEAAVVNLAEWLqdKLARFQQP 425
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1834-2201 3.33e-12

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: 71.66  E-value: 3.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1834 ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLT-RAAATEAMNGLGSGDVSLnwipLDHVTGVVMFHLR---DVYLGCRQIH 1909
Cdd:cd17648     91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNlRTSLSERYFGRDNGDEAV----LFFSNYVFDFFVEqmtLALLNGQKLV 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1910 APTSWILEDPVRWPELADRHRVSvtwapnfafgLLAEQAHRFQDRDWD-LSPVRLVMNAGEVVVASaarRFLHVLAPFGL 1988
Cdd:cd17648    167 VPPDEMRFDPDRFYAYINREKVT----------YLSGTPSVLQQYDLArLPHLKRVDAAGEEFTAP---VFEKLRSRFAG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1989 PqdvMHPGWGMSETcsVVTDSVlaSEAPDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNAR 2068
Cdd:cd17648    234 L---IINAYGPTET--TVTNHK--RFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPE 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2069 ANAESFTEDGW--------------FDTGDLA-FLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftaAV 2133
Cdd:cd17648    307 LTAERFLPNPFqteqerargrnarlYKTGDLVrWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVREC---AV 383

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2134 AVRSDASAAT----DELALFLRLAPGQDPAGALREIAGKVTREIGVsPAFLIPVeaEAIPKTEIGKIQRTKL 2201
Cdd:cd17648    384 VAKEDASQAQsriqKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMV-PARLVRL--EGIPVTINGKLDVRAL 452
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 36-275 3.70e-12

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: 71.37  E-value: 3.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   36 YVEIHGP-VDTALFETALRRTVREADTFALRFLDtpDGPRAVRDGDPD-EMPVHrvDVSGEADPAAAAEEW-IRRDLATP 112
Cdd:cd19535     29 YLEFDGEdLDPDRLERAWNKLIARHPMLRAVFLD--DGTQQILPEVPWyGITVH--DLRGLSEEEAEAALEeLRERLSHR 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  113 V-DVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTAlaAGEEPPPAGFESADRLAAEEAayLGSD 191
Cdd:cd19535    105 VlDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYED--PGEPLPPLELSFRDYLLAEQA--LRET 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  192 RHRRDRAYWTERLAGLPEPVRLTDRTAP-----PRapFLRRTAVLSPAETRALDEAAKGMGVARTDLLVAAVAAFLHRMT 266
Cdd:cd19535    181 AYERARAYWQERLPTLPPAPQLPLAKDPeeikePR--FTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWS 258


                   ....*....
gi 1573930569  267 GADDLVLGL 275
Cdd:cd19535    259 GQPRFLLNL 267
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 1835-2103 5.22e-12

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 71.69  E-value: 5.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVL-TRAAATEAMNGLGSGDVSLNWIPLDHV----TGVVMFH------------ 1897
Cdd:PLN02387   248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVaTVAGVMTVVPKLGKNDVYLAYLPLAHIlelaAESVMAAvgaaigygsplt 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1898 LRDV-------YLGCRQIHAPT-----SWILE---DPVRWP------------ELADRHRVSVTWAPNF-AFGLlaeqah 1949
Cdd:PLN02387   328 LTDTsnkikkgTKGDASALKPTlmtavPAILDrvrDGVRKKvdakgglakklfDIAYKRRLAAIEGSWFgAWGL------ 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1950 rfQDRDWD---LSPVRLV-------MNAGEVVVASAARRFLHVLapFGLPqdvMHPGWGMSETCSVVTDSvlaseapDHD 2019
Cdd:PLN02387   402 --EKLLWDalvFKKIRAVlggrirfMLSGGAPLSGDTQRFINIC--LGAP---IGQGYGLTETCAGATFS-------EWD 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2020 EAFVS-CGLPYPGFAMRVVD-------DQDALLPEGDVgrlQVRGTSVTHGYHDNARANAESFTEDG----WFDTGDLA- 2086
Cdd:PLN02387   468 DTSVGrVGPPLPCCYVKLVSweeggylISDKPMPRGEI---VIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGq 544

                          330
                   ....*....|....*..
gi 1573930569 2087 FLRDGELYITGRAKDVI 2103
Cdd:PLN02387   545 FHPDGCLEIIDRKKDIV 561
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1698-2205 5.22e-12

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: 71.75  E-value: 5.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1698 VVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLtvpVSYATTSAAV 1777
Cdd:cd05968     80 LRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI---FSGFGKEAAA 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1778 SKLEGIWEML----------DRPWIVTSAAGE-----PGLRELAA-RREWSGLRLTTADAL--REEPEDRDWYEAR--PD 1837
Cdd:cd05968    157 TRLQDAEAKAlitadgftrrGREVNLKEEADKacaqcPTVEKVVVvRHLGNDFTPAKGRDLsyDEEKETAGDGAERteSE 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEA--MNgLGSGD-----VSLNWI--PLDHVTGVVMFHLRDVYLGcrqi 1908
Cdd:cd05968    237 DPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYfqFD-LKPGDlltwfTDLGWMmgPWLIFGGLILGATMVLYDG---- 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 hAPTswiLEDPVRWPELADRHRVSVTwapnfafgllaeqahrfqdrdwDLSP--VRLVMNAGEVVVASAARRFLHVLAPF 1986
Cdd:cd05968    312 -APD---HPKADRLWRMVEDHEITHL----------------------GLSPtlIRALKPRGDAPVNAHDLSSLRVLGST 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1987 GLPQDVMHPGW----------------GMSETCSVVTDSVLASEApdhdeAFVSCGLPYPGFAMRVVDDQDALLPEgDVG 2050
Cdd:cd05968    366 GEPWNPEPWNWlfetvgkgrnpiinysGGTEISGGILGNVLIKPI-----KPSSFNGPVPGMKADVLDESGKPARP-EVG 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2051 RLQVRG--TSVTHGY-HDNARANAESFTE-DGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSV 2125
Cdd:cd05968    440 ELVLLApwPGMTRGFwRDEDRYLETYWSRfDNVWVHGDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAV 519

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2126 VRSftAAVAVRSDASAatDELALFLRLAPGQDPAGALR-EIAGKVTREIGVSpafLIPVE---AEAIPKTEIGKIQRTKL 2201
Cdd:cd05968    520 LES--AAIGVPHPVKG--EAIVCFVVLKPGVTPTEALAeELMERVADELGKP---LSPERilfVKDLPKTRNAKVMRRVI 592


                   ....
gi 1573930569 2202 RKSF 2205
Cdd:cd05968    593 RAAY 596
PLN02654 PLN02654
acetate-CoA ligase
 481-959 8.95e-12

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 71.08  E-value: 8.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  481 TLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTD 560
Cdd:PLN02654   120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  561 TA---GSGRLPATDarvvVVDDARTVADLAGRAPHDLTDADRAGATGPYDTA---------------------------- 609
Cdd:PLN02654   200 NAvkrGPKTINLKD----IVDAALDESAKNGVSVGICLTYENQLAMKREDTKwqegrdvwwqdvvpnyptkcevewvdae 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  610 ---YVIHTSGSTGRPKGVpvphAHVV---RLFEASGEHFRFG----------ADDVWTLFHSYAfdfsvweLWGPLLHGG 673
Cdd:PLN02654   276 dplFLLYTSGSTGKPKGV----LHTTggyMVYTATTFKYAFDykptdvywctADCGWITGHSYV-------TYGPMLNGA 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  674 RLVVvpYEVSRSPREFLR---LLDEEKVTVLNQTPSAFEQLVLADA--ATDRATGSLRyvVLGGealVAERLRPWADRHg 748
Cdd:PLN02654   345 TVLV--FEGAPNYPDSGRcwdIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLR--VLGS---VGEPINPSAWRW- 416

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  749 ldapeLVNMYG-----ITETTVHVTFHRLVRADLED--PRRRGVIGRPLADLRVYVLDAAGRPVPPGATGemYVSGPGVA 821
Cdd:PLN02654   417 -----FFNVVGdsrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGKEIEGECSG--YLCVKKSW 489

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  822 PGYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVP 901
Cdd:PLN02654   490 PGAFRTLYGDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVG 568

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  902 RAAEDGLTQLVAYaVPAEEGGADPAGLRAHLA----ARLPAYMVPAACVLLDALPLTANGKL 959
Cdd:PLN02654   569 IEHEVKGQGIYAF-VTLVEGVPYSEELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKI 629
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1690-2201 1.02e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 70.41  E-value: 1.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1690 AAGRPDGEVVHVRADGSETRRSyaslVPEASRVLAG-LRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTVPV 1768
Cdd:PRK13383    44 TAARWPGRTAIIDDDGALSYRE----LQRATESLARrLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1769 SYATTSAAvsklegiwemLDRPWIVTSAAGEPGLRELAARREwSGLRLTTADALREEPEDRDWYeARPDDLVLMlmTSGS 1848
Cdd:PRK13383   120 RSDALAAA----------LRAHHISTVVADNEFAERIAGADD-AVAVIDPATAGAEESGGRPAV-AAPGRIVLL--TSGT 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1849 TGLPKAV------------------RLTHRNVLTRAAATEAMNGLGSGDVSLNwIPLDhvtGVVMFHlrdvylgcRQIHA 1910
Cdd:PRK13383   186 TGKPKGVprapqlrsavgvwvtildRTRLRTGSRISVAMPMFHGLGLGMLMLT-IALG---GTVLTH--------RHFDA 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1911 PTSWiledpvrwpELADRHRVSVTWAPNFAFGLLAEQAHRFQDRDwDLSPVRLVMNAGEVVVASAARRFLHVLApfglpq 1990
Cdd:PRK13383   254 EAAL---------AQASLHRADAFTAVPVVLARILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYG------ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1991 DVMHPGWGMSEtcsvVTDSVLASEApDHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNAran 2070
Cdd:PRK13383   318 DILYNGYGSTE----VGIGALATPA-DLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGG--- 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2071 aESFTEDGWFDTGDLAFLRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTAAVAvrsdASAATDELALF 2149
Cdd:PRK13383   390 -GKAVVDGMTSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVP----DERFGHRLAAF 464

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2150 LRLAPGQD-PAGALRE-IAGKVTReigvspaFLIPVE---AEAIPKTEIGKIQRTKL 2201
Cdd:PRK13383   465 VVLHPGSGvDAAQLRDyLKDRVSR-------FEQPRDiniVSSIPRNPTGKVLRKEL 514
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 844-958 1.34e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 69.29  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  844 GTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAgGAVVPRAAEDGLTQLVAYAVPAEEgGA 923
Cdd:PRK08308   289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQ-EAVVYRGKDPVAGERVKAKVISHE-EI 366

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1573930569  924 DPAGLRAHLAARLPAYMVPAACVLLDALPLTANGK 958
Cdd:PRK08308   367 DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGK 401
PRK12467 PRK12467
peptide synthase; Provisional
 2776-2839 1.38e-11

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 70.96  E-value: 1.38e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALA 2839
Cdd:PRK12467  3606 VEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 1722-2163 2.35e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 69.29  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1722 VLAGLRRRGLRPGDRVILqcDDTEDFVATLWGCVLGGFVAVPLTVPVSYATTSAAVSKLegiwemlDRPWIVTSAAGEPG 1801
Cdd:PRK13388    42 ALIALADPDRPLHVGVLL--GNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRA-------DCQLLVTDAEHRPL 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1802 LRELaarrEWSGLRL------TTADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGL 1875
Cdd:PRK13388   113 LDGL----DLPGVRVldvdtpAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1876 GSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPT---SWILEDpVRwpeladrhRVSVTWApNF---AFGLLAEQAH 1949
Cdd:PRK13388   189 TRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsaSGFLDD-VR--------RYGATYF-NYvgkPLAYILATPE 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1950 RFQDRDwdlSPVRLVM--NAGEVVVASAARRFLHVLapfglpqdvmHPGWGMSETCSVVTdsvlaseaPDHDEAFVSCGL 2027
Cdd:PRK13388   259 RPDDAD---NPLRVAFgnEASPRDIAEFSRRFGCQV----------EDGYGSSEGAVIVV--------REPGTPPGSIGR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2028 PYPGFAM-----------RVVDDQDALL-PEGDVGRL-QVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFL-RDGEL 2093
Cdd:PRK13388   318 GAPGVAIynpetltecavARFDAHGALLnADEAIGELvNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRdADGWI 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2094 YITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRS-------------FTAAVAVRSDASAATDELALFLRLAPGQDPAG 2160
Cdd:PRK13388   397 YFAGRTADWMRVDGENLSAAPIERILLRHPAINRVavyavpdervgdqVMAALVLRDGATFDPDAFAAFLAAQPDLGTKA 476


                   ...
gi 1573930569 2161 ALR 2163
Cdd:PRK13388   477 WPR 479
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1707-2207 2.41e-11

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 69.25  E-value: 2.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGfvAVPLTVPVSYATT--SAAVSKLEGIW 1784
Cdd:PRK10946    46 ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSelNAYASQIEPAL 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1785 EMLDRP--------WIVTSAAGEPGLRELAARREWSGLRLttADALREEPEDRDWYEARPDDLVLMLMTSGSTGLPKAVR 1856
Cdd:PRK10946   124 LIADRQhalfsdddFLNTLVAEHSSLRVVLLLNDDGEHSL--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIP 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1857 LTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDH--------VTGVVmfhlrdvYLGCRQIHAPTSwileDPVRWPELADR 1928
Cdd:PRK10946   202 RTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmsspgALGVF-------LAGGTVVLAPDP----SATLCFPLIEK 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1929 HRVSVTWAPNFAFGLLAEQAHRFQDRDwDLSPVRLVMNAGEVVVASAARRflhVLAPFGLP-QDVmhpgWGMSEtcSVVT 2007
Cdd:PRK10946   271 HQVNVTALVPPAVSLWLQAIAEGGSRA-QLASLKLLQVGGARLSETLARR---IPAELGCQlQQV----FGMAE--GLVN 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2008 DSVLaseaPDHDE-AFVSCGLPY-PGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGWFDTGDL 2085
Cdd:PRK10946   341 YTRL----DDSDErIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDL 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2086 AFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVrsdasaaTDEL-----ALFLRLapgQDP- 2158
Cdd:PRK10946   417 VSIDpDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHA--ALVSM-------EDELmgeksCAFLVV---KEPl 484

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2159 -AGALReiagKVTREIGVSpAFLIP--VEA-EAIPKTEIGKIQRTKLRKSFEA 2207
Cdd:PRK10946   485 kAVQLR----RFLREQGIA-EFKLPdrVECvDSLPLTAVGKVDKKQLRQWLAS 532
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1835-2100 3.23e-11

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 69.61  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDH------------VTGVVMF------ 1896
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHsfgltgglvlplLSGVKVFlypspl 870

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1897 HLRDVylgcrqihaptswiledpvrwPELADRHRVSVTWAPNFAFGLLAEQAHRFqdrdwDLSPVRLVMnAGEVVVASAA 1976
Cdd:PRK06814   871 HYRII---------------------PELIYDTNATILFGTDTFLNGYARYAHPY-----DFRSLRYVF-AGAEKVKEET 923

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1977 RRFLhvLAPFGLPqdvMHPGWGMSETCsvvtdSVLASEAPDHDEAFvSCGLPYPGFAMRVvdDQDALLPEGdvGRLQVRG 2056
Cdd:PRK06814   924 RQTW--MEKFGIR---ILEGYGVTETA-----PVIALNTPMHNKAG-TVGRLLPGIEYRL--EPVPGIDEG--GRLFVRG 988

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2057 TSVTHGYHDNARANAESFTEDGWFDTGDL-AFLRDGELYITGRAK 2100
Cdd:PRK06814   989 PNVMLGYLRAENPGVLEPPADGWYDTGDIvTIDEEGFITIKGRAK 1033
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2776-2845 3.62e-11

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: 61.41  E-value: 3.62e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569 2776 LESELAAVWCTVLG--RDRVGRDENFF-DLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:COG0236      6 LEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 2049-2202 4.92e-11

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 68.51  E-value: 4.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2049 VGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVR 2127
Cdd:PLN03102   392 MGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2128 sfTAAVAVRSDASAATDelALFLRLAPGQDpaGALREIAGKVTREIGV-------SPAFLIP---VEAEAIPKTEIGKIQ 2197
Cdd:PLN03102   471 --TAVVAMPHPTWGETP--CAFVVLEKGET--TKEDRVDKLVTRERDLieycrenLPHFMCPrkvVFLQELPKNGNGKIL 544


                   ....*
gi 1573930569 2198 RTKLR 2202
Cdd:PLN03102   545 KPKLR 549
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 775-1056 1.32e-10

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 65.16  E-value: 1.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  775 ADLEDPRRRGVIGRPLADLRVYVLDAAGRPVPPGATGEmyvSGPGVAPGYLNRPELTEERFLPDPFGAPGTRMYRSGDLA 854
Cdd:COG3433      9 APPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE---GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  855 RWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQ-LVAYAVPAEEGGADPAGLRAHLA 933
Cdd:COG3433     86 RLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVgLLLIVGAVAALDGLAAAAALAAL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  934 ARLPAYMVPAACVLLDALPLTANGKLDTAALPAPDFGGGTGGAPPATPE------ERLVCGLFEEVLRLPADSVGTGGNF 1007
Cdd:COG3433    166 DKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPAletaltEEELRADVAELLGVDPEEIDPDDNL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1573930569 1008 FDLGGHSlLATRLLARLRERTGTDVPISALFDTPTPAALAERLTAGADA 1056
Cdd:COG3433    246 FDLGLDS-IRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAA 293
PRK05691 PRK05691
peptide synthase; Validated
 1040-1495 1.44e-10

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 67.89  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1040 TPTPAALAERLTAGADAgRPLPAltaSERPSLVPASFAQERMWFLSRMDGAAATYNIPLPVALRHPLDLDALRAALGDVA 1119
Cdd:PRK05691  3230 TPSDFPLAQLTQAQLDA-LPVPA---AEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVV 3305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1120 DRHESLRTVFGEEDG-AIHQRVLPPGTLRPE-LHVVDCPDEERAAHVAAAMRRS----FDLTRDSALWAGVFGTGDTRT- 1192
Cdd:PRK05691  3306 ARHEALRASFSWNAGeTMLQVIHKPGRTPIDyLDWRGLPEDGQEQRLQALHKQEreagFDLLNQPPFHLRLIRVDEARYw 3385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1193 LLLVLHHSAADGWSLRPLADDLGTAYAARRAGAAPDWAPPAlQYADFALW-QRRVLAPAPEgpgrlerltsFWRQALDGL 1271
Cdd:PRK05691  3386 FMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPP-RYRDYIGWlQRQDLAQARQ----------WWQDNLRGF 3454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1272 PEESAPPPDRPRPAAPSGRGGGVTV-----PLDAGTHRELLRLADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAG 1346
Cdd:PRK05691  3455 ERPTPIPSDRPFLREHAGDSGGMVVgdcytRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAG 3534

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1347 R--TEPALDEVVGLLTNTLVLRA---DASGDPTFRELLARVRAFDVQALDHQDLPfdrLVEEVNPRRHPARHPLFQVMLA 1421
Cdd:PRK05691  3535 RpvSMPQMQRTVGLFINSIALRVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFV 3611

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1422 LQNN--ERAVLtlgeDRVPLRPAATGTAK----FDLFVDVLerhgadgTADGLDLHVEYAADLYDPATAERFAGALRDLL 1495
Cdd:PRK05691  3612 FENApvEVSVL----DRAQSLNASSDSGRthtnFPLTAVCY-------PGDDLGLHLSYDQRYFDAPTVERLLGEFKRLL 3680
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 15-423 1.46e-10

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: 66.17  E-value: 1.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   15 QEGLwFAHRLAPGTAayNTGEYV-EIHGPVDTALFETALRRTVREADTFALRFLDTPDGP--RAVRDgdpdEMPVHRVDV 91
Cdd:cd19545      8 QEGL-MALTARQPGA--YVGQRVfELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGllQVVVK----ESPISWTES 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   92 SGEADPaaaaeewIRRDLATPVDvAAGPLFSHALLTLAPDR--FIWflRAHHILLDGYSYKLVARRLADTYTALAAGEEP 169
Cdd:cd19545     81 TSLDEY-------LEEDRAAPMG-LGGPLVRLALVEDPDTEryFVW--TIHHALYDGWSLPLILRQVLAAYQGEPVPQPP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  170 PPAGFesadrlaaeeAAYLGSDRHRRDRAYWTERLAGLPEPV--RLTDRTAPPRAPFLRRTAVLSPAETRaldeaakgMG 247
Cdd:cd19545    151 PFSRF----------VKYLRQLDDEAAAEFWRSYLAGLDPAVfpPLPSSRYQPRPDATLEHSISLPSSAS--------SG 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  248 VARTDLLVAAVAAFLHRMTGADDLVLGLATMSRlgSAALrtPGTASDI------LPLRVAASADTPVGGFVRAVADDLRG 321
Cdd:cd19545    213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGR--NAPV--PGIEQIVgptiatVPLRVRIDPEQSVEDFLQTVQKDLLD 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  322 LRAHQrHRG-ESIRRDLGVLGRGRRVhGPVVNIVPFSEDLTFGGHPSTSHHLSGGAVD----DLQISVRPGAEADTLWLA 396
Cdd:cd19545    289 MIPFE-HTGlQNIRRLGPDARAACNF-QTLLVVQPALPSSTSESLELGIEEESEDLEDfssyGLTLECQLSGSGLRVRAR 366

                          410       420
                   ....*....|....*....|....*..
gi 1573930569  397 FDahPDLYEEDGLALFLERFLKVLREL 423
Cdd:cd19545    367 YD--SSVISEEQVERLLDQFEHVLQQL 391
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 571-898 1.51e-10

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 66.11  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  571 DARVVVVDDARTVADLAgRAP----HDLTDADRAG-ATGPYDTAYVIH-TSGSTGRPkgVPVPHAH---------VVRLF 635
Cdd:cd05913     38 AAAGIDPDDIKSLDDLR-KLPfttkEDLRDNYPFGlFAVPREKVVRIHaSSGTTGKP--TVVGYTKndldvwaelVARCL 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  636 EASGehfrFGADDVWTLFHSYAFDFSvweLWGplLHGG--RL--VVVPYEVSRSPREFLRLLDEeKVTVLNQTPSAfeQL 711
Cdd:cd05913    115 DAAG----VTPGDRVQNAYGYGLFTG---GLG--FHYGaeRLgaLVIPAGGGNTERQLQLIKDF-GPTVLCCTPSY--AL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  712 VLADAAT----DRATGSLRYVVLGGEALVAERLRPWADRHGLDApelVNMYGITETTvhvtfhrLVRADLEDPRRRG-VI 786
Cdd:cd05913    183 YLAEEAEeegiDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKA---YDIYGLTEII-------GPGVAFECEEKDGlHI 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  787 GRPLADLRVyVLDAAGRPVPPGATGEMYVSgpgvapgylnrpELTEErflpdpfGAPGTRmYRSGDLARWRPD----GTl 862
Cdd:cd05913    253 WEDHFIPEI-IDPETGEPVPPGEVGELVFT------------TLTKE-------AMPLIR-YRTRDITRLLPGpcpcGR- 310

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1573930569  863 VHA------GRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGA 898
Cdd:cd05913    311 THRridritGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHY 352
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2778-2837 3.38e-10

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: 57.96  E-value: 3.38e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2778 SELAAVWCTVLGRD--RVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRA 2837
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 1835-2207 3.76e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 65.02  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGlpkAVRLTHRNVLTRAAATEAMNGLGSGDV--SLNWIPLDHVTGVVMFhLRDVYLGcrqihapT 1912
Cdd:PRK07445   118 NLETGWIMIPTGGSSG---QIRFAIHTWETLTASVQGFQRYFQLQQvnSFCVLPLYHVSGLMQF-MRSFLTG-------G 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1913 SWILEDpvrWPELadrhRVSVTWAPN---FAFGLLAEQAHRFQDRD--WdLSPVRLVMNAGevvvASAARRFLHVLAPFG 1987
Cdd:PRK07445   187 KLVILP---YKRL----KSGQELPPNpsdFFLSLVPTQLQRLLQLRpqW-LAQFRTILLGG----APAWPSLLEQARQLQ 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1988 LPqdvMHPGWGMSETCSVVtdsvlASEAPDhdeAFV----SCGLPYPGFAMRvvddqdalLPEGDVGRLQVRGTSVTHGY 2063
Cdd:PRK07445   255 LR---LAPTYGMTETASQI-----ATLKPD---DFLagnnSSGQVLPHAQIT--------IPANQTGNITIQAQSLALGY 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2064 HDNARANAESFTedgwfdTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEA-----------CVEELP-----SVV 2126
Cdd:PRK07445   316 YPQILDSQGIFE------TDDLGYLdAQGYLHILGRNSQKIITGGENVYPAEVEAailatglvqdvCVLGLPdphwgEVV 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 rsftAAVAVrsdasaatdelalflrlapGQDPAGALREIAGKVTREIgvSPaFLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK07445   390 ----TAIYV-------------------PKDPSISLEELKTAIKDQL--SP-FKQPkhwIPVPQLPRNPQGKINRQQLQQ 443


                   ....
gi 1573930569 2204 SFEA 2207
Cdd:PRK07445   444 IAVQ 447
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1997-2209 4.89e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 64.80  E-value: 4.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1997 WGMSETcSVVTDSVLA-SEAPDHdeafvSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARAnAESFT 2075
Cdd:PRK07638   286 YGASEL-SFVTALVDEeSERRPN-----SVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL-ARELN 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2076 EDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSftAAVAVRSDASAATDELALflrlaP 2154
Cdd:PRK07638   359 ADGWMTVRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEI--VVIGVPDSYWGEKPVAII-----K 431

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573930569 2155 GQDPAGALReiagkvTREIGVSPAFLIPVE---AEAIPKTEIGKIQRTKLRKSFEAGE 2209
Cdd:PRK07638   432 GSATKQQLK------SFCLQRLSSFKIPKEwhfVDEIPYTNSGKIARMEAKSWIENQE 483
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
570-964 6.62e-10

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 64.73  E-value: 6.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  570 TDARVVVVDDAR---TVADLAGRAPHDLTDADRAGATGPYDTAYVIHTSGSTGRPKGvpVPHAHVVRLfeASGEHFR--- 643
Cdd:PRK08043   326 TQVRWVYLEDLKddvTTADKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKG--VVHSHKSLL--ANVEQIKtia 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  644 -FGADDVWT----LFHsyAFDFSVwELWGPLLHGGRLVVVPyevsrSP---REFLRLLDEEKVTVLNQTpSAFeqlvLAD 715
Cdd:PRK08043   402 dFTPNDRFMsalpLFH--SFGLTV-GLFTPLLTGAEVFLYP-----SPlhyRIVPELVYDRNCTVLFGT-STF----LGN 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  716 AAT-----DRAtgSLRYVVLGGEALVAERLRPWADRHGLdapELVNMYGITETTVHVTFHRLVRAdledprRRGVIGRPL 790
Cdd:PRK08043   469 YARfanpyDFA--RLRYVVAGAEKLQESTKQLWQDKFGL---RILEGYGVTECAPVVSINVPMAA------KPGTVGRIL 537

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  791 ADlrvyvLDAAGRPVpPGAT--GEMYVSGPGVAPGYL--NRPELTEERFLPDPFGAPGTRMYRSGDLARWRPDGTLVHAG 866
Cdd:PRK08043   538 PG-----MDARLLSV-PGIEqgGRLQLKGPNIMNGYLrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQG 611

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  867 RADQQVKIRG------------FRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLT--QLVAYAvpaeeggadpaglRAHL 932
Cdd:PRK08043   612 RAKRFAKIAGemvslemveqlaLGVSPDKQHATAIKSDASKGEALVLFTTDSELTreKLQQYA-------------REHG 678

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1573930569  933 AARLPaymVPAACVLLDALPLTANGKLDTAAL 964
Cdd:PRK08043   679 VPELA---VPRDIRYLKQLPLLGSGKPDFVTL 707
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 1819-2202 2.96e-09

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: 62.39  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1819 ADALREEPEDRdwyEARPDDlvlMLMTSGSTGLPKAVRLTH----RNVLTRAAATeAMNGLGSGDVSLNWIPLDHVTGVV 1894
Cdd:cd05929    113 EGGSPETPIED---EAAGWK---MLYSGGTTGRPKGIKRGLpggpPDNDTLMAAA-LGFGPGADSVYLSPAPLYHAAPFR 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1895 MFHLRDVYLGcrqihapTSWILE--DPVRWPELADRHRVS-VTWAPNFAFGLLA---EQAHRFqdrdwDLSPVRLVMNAG 1968
Cdd:cd05929    186 WSMTALFMGG-------TLVLMEkfDPEEFLRLIERYRVTfAQFVPTMFVRLLKlpeAVRNAY-----DLSSLKRVIHAA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1969 EVVVASAARRFLHVLAPfglpqdVMHPGWGMSE---TCSVVTDSVLASEApdhdeafvSCGLPYPGfAMRVVDDQDALLP 2045
Cdd:cd05929    254 APCPPWVKEQWIDWGGP------IIWEYYGGTEgqgLTIINGEEWLTHPG--------SVGRAVLG-KVHILDEDGNEVP 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2046 EGDVGRLQVRGTSvTHGYHDNARANAESFTEDGWFDTGDLAFL-RDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPS 2124
Cdd:cd05929    319 PGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPK 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2125 VVrsfTAAVAVRSDASAATDELALF---LRLAPGQDPAGALREIAGKVTREIGVSPAFLIpvEAEaIPKTEIGKIQRTKL 2201
Cdd:cd05929    398 VL---DAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEF--VAE-LPRDDTGKLYRRLL 471


                   .
gi 1573930569 2202 R 2202
Cdd:cd05929    472 R 472
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 723-964 3.06e-09

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 62.83  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  723 GSLRYVVLGGEALVAerlrpwadrhglDAPELVNM---------YGITETTVHVTFhrlvrADLEDPRRrGVIGRPLADL 793
Cdd:PLN02387   420 GRIRFMLSGGAPLSG------------DTQRFINIclgapigqgYGLTETCAGATF-----SEWDDTSV-GRVGPPLPCC 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  794 RVYVLD-------AAGRPVPpgaTGEMYVSGPGVAPGYLNRPELTEERFLPDpfgAPGTRMYRSGDLARWRPDGTLVHAG 866
Cdd:PLN02387   482 YVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIGQFHPDGCLEIID 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  867 RADQQVKIR-GFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAG------------------ 927
Cdd:PLN02387   556 RKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGidysnfaelcekeeavke 635

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1573930569  928 -----LRAHLAARLPAYMVPAACVLLdALPLTANGKLDTAAL 964
Cdd:PLN02387   636 vqqslSKAAKAARLEKFEIPAKIKLL-PEPWTPESGLVTAAL 676
PRK12316 PRK12316
peptide synthase; Provisional
 2776-2846 3.69e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 63.05  E-value: 3.69e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQG 2846
Cdd:PRK12316  5073 LEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAG 5143
PRK12467 PRK12467
peptide synthase; Provisional
 2776-2845 3.69e-09

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 62.87  E-value: 3.69e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:PRK12467  1031 LEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100
PRK05691 PRK05691
peptide synthase; Validated
 1707-2201 4.99e-09

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 62.49  E-value: 4.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1707 ETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDfvatLWGCVLGGFVAVPLTVPVSYATTSAavsKLEGIWEM 1786
Cdd:PRK05691  3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLD----LLGMIVGSFKAGAGYLPLDPGLPAQ---RLQRIIEL 3815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1787 LDRPWIVTSAA-GEPGLRELAARREWSGLRLTtadaLREEPEDRDWYEARP------DDLVLMLMTSGSTGLPKAVRLTH 1859
Cdd:PRK05691  3816 SRTPVLVCSAAcREQARALLDELGCANRPRLL----VWEEVQAGEVASHNPgiysgpDNLAYVIYTSGSTGLPKGVMVEQ 3891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1860 RNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFhLRDVYLGCRQIHAPTSwILEDPVRWPELADRHRVSVTWA-PN 1938
Cdd:PRK05691  3892 RGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQF-LAAPLFGARVEIVPNA-IAHDPQGLLAHVQAQGITVLESvPS 3969

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1939 FAFGLLAEQAHrfqdrdwDLSPVRLVMNAGEVVVASAARRFLHVLAPFGLPQdvmhpGWGMSEtCSvvtDSV------LA 2012
Cdd:PRK05691  3970 LIQGMLAEDRQ-------ALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVN-----AYGPAE-CS---DDVaffrvdLA 4033

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2013 SEApdhdEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANAESFTEDGW-------FDTGDL 2085
Cdd:PRK05691  4034 STR----GSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDL 4109

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2086 AFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRsftAAVAVRSDASAatDELALFLRLAPG-QDPAGALR 2163
Cdd:PRK05691  4110 ARRRsDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE---AAVAVQEGVNG--KHLVGYLVPHQTvLAQGALLE 4184

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1573930569 2164 EIAGKVTREIgvsPAFLIPVE---AEAIPKTEIGKIQRTKL 2201
Cdd:PRK05691  4185 RIKQRLRAEL---PDYMVPLHwlwLDRLPLNANGKLDRKAL 4222
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 10-315 5.13e-09

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: 61.05  E-value: 5.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   10 PLSGAQEGLWFAHRLAPGTAAYNTgEYV-EIHGPVDTALFETALRRTVREADTFALRFLDTPDGP-RAVRDGDPDEMPVH 87
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSSFNV-SFAcRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrRSYSSSPPRVQRVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   88 RVDVSGEadpaaaaeewIRR--DLAT--PVDVaagplfshallTLAPDRFIwfLRAHHILLDGYSYKLVARRLADTYtal 163
Cdd:cd19537     82 TLDVWKE----------INRpfDLERedPIRV-----------FISPDTLL--VVMSHIICDLTTLQLLLREVSAAY--- 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  164 aAGEEPPPAgfesadrlaaeEAAYLGSDRHRR-----DRAYWTERLAGLPEPVRltdrtaPPRAPFLR-----RTAVLSP 233
Cdd:cd19537    136 -NGKLLPPV-----------RREYLDSTAWSRpaspeDLDFWSEYLSGLPLLNL------PRRTSSKSyrgtsRVFQLPG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  234 AETRALDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALRTPGTASDILPLRV--AASADTPVGGF 311
Cdd:cd19537    198 SLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIrfPSSSDASAADF 277


                   ....
gi 1573930569  312 VRAV 315
Cdd:cd19537    278 LRAV 281
PRK13382 PRK13382
bile acid CoA ligase;
1711-2202 5.82e-09

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 61.70  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLwgCVLGGFVAVPLTVPVSYATTS-AAVSKLEGI------ 1783
Cdd:PRK13382    70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEAL--LAANRIGADILLLNTSFAGPAlAEVVTREGVdtviyd 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1784 ---WEMLDRpwivtSAAGEPGLRELAArreW-SGLRLTTADALREEPEDRDwYEARPDDLVLMLMTSGSTGLPKAVRLTh 1859
Cdd:PRK13382   148 eefSATVDR-----ALADCPQATRIVA---WtDEDHDLTVEVLIAAHAGQR-PEPTGRKGRVILLTSGTTGTPKGARRS- 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1860 rnvltraaateAMNGLGSGDVSLNWIPLDHVTGVV----MFHLrdvyLGCRQIHAPTSWILE-------DPVRWPELADR 1928
Cdd:PRK13382   218 -----------GPGGIGTLKAILDRTPWRAEEPTVivapMFHA----WGFSQLVLAASLACTivtrrrfDPEATLDLIDR 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1929 HRVSVTWAPNFAFGLLAEQAHRFQDRdWDLSPVRLVMNAGEVVVASAARRFLHvlaPFGlpqDVMHPGWGMSETcsvvtd 2008
Cdd:PRK13382   283 HRATGLAVVPVMFDRIMDLPAEVRNR-YSGRSLRFAAASGSRMRPDVVIAFMD---QFG---DVIYNNYNATEA------ 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2009 SVLASEAP-DHDEAFVSCGLPYPGFAMRVVDDQDALLPEGDVGRLQVRGTSVTHGYHDNARANaesfTEDGWFDTGDLAF 2087
Cdd:PRK13382   350 GMIATATPaDLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKD----FHDGFMASGDVGY 425

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2088 LRD-GELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAVRS-DASAATDELALFLRLAPGqdpAGALREI 2165
Cdd:PRK13382   426 LDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV-----AEAAVIGvDDEQYGQRLAAFVVLKPG---ASATPET 497

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1573930569 2166 AG----------KVTREIGVspaflipveAEAIPKTEIGKIQRTKLR 2202
Cdd:PRK13382   498 LKqhvrdnlanyKVPRDIVV---------LDELPRGATGKILRRELQ 535
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1104-1394 1.23e-08

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: 60.19  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1104 HPLDLDALRAALGDVADRHESLRTVFgEEDGaiHQRVLPPgTLRPELHVVDCP--DEERAAHVAAAMR-----RSFDLTR 1176
Cdd:cd19535     35 EDLDPDRLERAWNKLIARHPMLRAVF-LDDG--TQQILPE-VPWYGITVHDLRglSEEEAEAALEELRerlshRVLDVER 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1177 dsalW------AGVFGTGDTRtlllvLHHS----AADGWSLRPLADDLgtayaaRRAGAAPDWAPPALQYaDFAlwqRRV 1246
Cdd:cd19535    111 ----GplfdirLSLLPEGRTR-----LHLSidllVADALSLQILLREL------AALYEDPGEPLPPLEL-SFR---DYL 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1247 LAPAPEGPGRLERLTSFWRQALDGLPE----------ESapppdrprpaapsgrgggVTVP--------LDAGTHRELLR 1308
Cdd:cd19535    172 LAEQALRETAYERARAYWQERLPTLPPapqlplakdpEE------------------IKEPrftrrehrLSAEQWQRLKE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1309 LADHENASLFMVLHGALALLLNRWGAGDDIVVGTPVAGRTE--PALDEVVGLLTNTLVLRADASGDPTFRELLARVRAFD 1386
Cdd:cd19535    234 RARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQL 313


                   ....*...
gi 1573930569 1387 VQALDHQD 1394
Cdd:cd19535    314 WEDLDHSS 321
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1689-1894 1.53e-08

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 60.27  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1689 RAAGRPDGevVHVRADGSETrrSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCV-LGGFVAV----- 1762
Cdd:PRK08279    46 AAARHPDR--PALLFEDQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAkLGAVVALlntqq 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1763 ---PLTVPVSYATTSAAV------SKLEGIWEMLDRPWIVTSAAGEpglrELAARREWSGLRLTTADALREEPEDRDwyE 1833
Cdd:PRK08279   122 rgaVLAHSLNLVDAKHLIvgeelvEAFEEARADLARPPRLWVAGGD----TLDDPEGYEDLAAAAAGAPTTNPASRS--G 195

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 1834 ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVV 1894
Cdd:PRK08279   196 VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGT 256
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 477-959 1.85e-08

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: 60.00  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  477 YAGETLSYAELNAEANRLAR-LLVEQGAGPGRFVALALPRGPRLVPALLAVLKTG--AAYL-------PLDPGHPAERLA 546
Cdd:cd05938      1 FEGETYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLntnirskSLLHCFRCCGAK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  547 LVMADAEPVAVVTDTagsgrLPATDARVVVV---------DDARTVADLAGRAPHDLTDAD-RAGATgPYDTAYVIHTSG 616
Cdd:cd05938     81 VLVVAPELQEAVEEV-----LPALRADGVSVwylshtsntEGVISLLDKVDAASDEPVPASlRAHVT-IKSPALYIYTSG 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  617 STGRPKGVPVPHAHVVR---LFEASGEHfrfgADDV----WTLFHSYAFdfsvweLWGplLHG----GRLVVVPYEVSRS 685
Cdd:cd05938    155 TTGLPKAARISHLRVLQcsgFLSLCGVT----ADDViyitLPLYHSSGF------LLG--IGGcielGATCVLKPKFSAS 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  686 prEFLRLLDEEKVTVL-----------NQTPSAFEQlvlaDAATDRATGSlryvvlggeALVAERLRPWADRHGldAPEL 754
Cdd:cd05938    223 --QFWDDCRKHNVTVIqyigellrylcNQPQSPNDR----DHKVRLAIGN---------GLRADVWREFLRRFG--PIRI 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  755 VNMYGITETTVhvtfhrlvrADLEDPRRRGVIGR---------PLADLRvY-------VLDAAGR--PVPPGATGEMyvs 816
Cdd:cd05938    286 REFYGSTEGNI---------GFFNYTGKIGAVGRvsylykllfPFELIK-FdvekeepVRDAQGFciPVAKGEPGLL--- 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  817 gpgVAP--------GYLNRPELTEERFLPDPFgAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVL 888
Cdd:cd05938    353 ---VAKitqqspflGYAGDKEQTEKKLLRDVF-KKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVL 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  889 TAHPAVAGGAVVpraaedGLTqlvayaVPAEEGGADPAGLR-------------AHLAARLPAYMVPAACVLLDALPLTA 955
Cdd:cd05938    429 GLLDFLQEVNVY------GVT------VPGHEGRIGMAAVKlkpghefdgkklyQHVREYLPAYARPRFLRIQDSLEITG 496


                   ....
gi 1573930569  956 NGKL 959
Cdd:cd05938    497 TFKQ 500
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
480-968 2.10e-08

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 59.80  E-value: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQ-GAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVV 558
Cdd:PRK05620    37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  559 TDTAGSGRL-------PATDARVVV----VDDARTV-----------ADLAGRAPH-DLTDADRAGAtgpydtAYVIHTS 615
Cdd:PRK05620   117 ADPRLAEQLgeilkecPCVRAVVFIgpsdADSAAAHmpegikvysyeALLDGRSTVyDWPELDETTA------AAICYST 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  616 GSTGRPKGVPVPHA----HVVRLFEA------SGEHFRFGAddvwTLFH--SYAFDFSVWELWGPLLHGGRlvvvpyevS 683
Cdd:PRK05620   191 GTTGAPKGVVYSHRslylQSLSLRTTdslavtHGESFLCCV----PIYHvlSWGVPLAAFMSGTPLVFPGP--------D 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  684 RSPREFLRLLDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLGGEALVAERLRPWADRHGLDapeLVNMYGITET 763
Cdd:PRK05620   259 LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVD---VVHVWGMTET 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  764 TVHVTFHRLVRADLEDPRR--RGVIGRPLADLRVYVLDAaGRPVppGAT----GEMYVSGPGVAPGYLNRPELTE----E 833
Cdd:PRK05620   336 SPVGTVARPPSGVSGEARWayRVSQGRFPASLEYRIVND-GQVM--ESTdrneGEIQVRGNWVTASYYHSPTEEGggaaS 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  834 RF-------LPDPFGAPGtrMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTAHPAVAGGAVV----PR 902
Cdd:PRK05620   413 TFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIgypdDK 490

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  903 AAEDGLTQLVAYA--VPAEEGGADpagLRAHLAARLPAYMVPAACVLLDALPLT--------------ANGKLDTAALPA 966
Cdd:PRK05620   491 WGERPLAVTVLAPgiEPTRETAER---LRDQLRDRLPNWMLPEYWTFVDEIDKTsvgkfdkkdlrqhlADGDFEIIKLKG 567


                   ..
gi 1573930569  967 PD 968
Cdd:PRK05620   568 PG 569
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2770-2845 2.24e-08

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: 53.41  E-value: 2.24e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569  2770 ADELRRLESELAAVWCTVLGR---DRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:smart00823    7 AERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1835-2182 2.55e-08

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 59.72  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1835 RPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGDVSLNWIPLDHVTGVVMFHLRDVYLGCRQIHAPTsw 1914
Cdd:PRK08043   363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS-- 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1915 iledPVRW---PELADRHRVSVTWAPNFAFGLLAEQAHRFqdrdwDLSPVRLVMNAGEVVVASAARRFLHvlaPFGLPqd 1991
Cdd:PRK08043   441 ----PLHYrivPELVYDRNCTVLFGTSTFLGNYARFANPY-----DFARLRYVVAGAEKLQESTKQLWQD---KFGLR-- 506

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1992 vMHPGWGMSETCSVVTDSVLASEAPDhdeafvSCGLPYPGFAMRVVDDQDalLPEGdvGRLQVRGTSVTHGY-------- 2063
Cdd:PRK08043   507 -ILEGYGVTECAPVVSINVPMAAKPG------TVGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYlrvekpgv 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2064 -HDNARANAESFTEDGWFDTGDLAFLRD-GELYITGRAKDVIIVNGvNHYSHEIeacVEELPSVVRSFTA-AVAVRSDAS 2140
Cdd:PRK08043   576 lEVPTAENARGEMERGWYDTGDIVRFDEqGFVQIQGRAKRFAKIAG-EMVSLEM---VEQLALGVSPDKQhATAIKSDAS 651

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1573930569 2141 AAtDELALFlrlapgQDPAGALREIAGKVTREIGVsPAFLIP 2182
Cdd:PRK08043   652 KG-EALVLF------TTDSELTREKLQQYAREHGV-PELAVP 685
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 480-912 2.98e-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: 59.36  E-value: 2.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  480 ETLSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVT 559
Cdd:cd17641     10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  560 -------------------------DTAGSGRLpaTDARVVVVDDARTVADLAGRAPHDLTDAdRAGATGPYDTAYVIHT 614
Cdd:cd17641     90 edeeqvdklleiadripsvryviycDPRGMRKY--DDPRLISFEDVVALGRALDRRDPGLYER-EVAAGKGEDVAVLCTT 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  615 SGSTGRPKGVPVPHAHVVRLFEASGE-HFRFGADDV-------WTLFHSYAFDFSVWE---------------------- 664
Cdd:cd17641    167 SGTTGKPKLAMLSHGNFLGHCAAYLAaDPLGPGDEYvsvlplpWIGEQMYSVGQALVCgfivnfpeepetmmedlreigp 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  665 ---LWGPLLHGGRLVVVPYEVSRSPR--EFL-------------RLLDEEKVTVLNQTPSAFEQLVLADAATDRATGS-L 725
Cdd:cd17641    247 tfvLLPPRVWEGIAADVRARMMDATPfkRFMfelgmklglraldRGKRGRPVSLWLRLASWLADALLFRPLRDRLGFSrL 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  726 RYVVLGGEALVAERLRPWadrHGLDAPeLVNMYGITETTVHVTFHRLVRADLEdprrrgVIGRPLADLRVYVLDaagrpv 805
Cdd:cd17641    327 RSAATGGAALGPDTFRFF---HAIGVP-LKQLYGQTELAGAYTVHRDGDVDPD------TVGVPFPGTEVRIDE------ 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  806 ppgaTGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDLARWRPDGTLVHAGRA-DQQVKIRGFRIEPGEI 884
Cdd:cd17641    391 ----VGEILVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFI 459

                          490       500
                   ....*....|....*....|....*...
gi 1573930569  885 EAVLTAHPAVAgGAVVPRAAEDGLTQLV 912
Cdd:cd17641    460 ENKLKFSPYIA-EAVVLGAGRPYLTAFI 486
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1838-2203 3.77e-08

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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 58.98  E-value: 3.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1838 DLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAMNGLGSGD--VSLNWIPLDHVTGVVMFHLRDVYLGcrqIHAPTSWI 1915
Cdd:cd05915    154 AACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGA---KQVLPGPR 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 LEDPVRWPELAdRHRVSVTWAPNFAFGLLAEQAHRFQDR-DWDLSpvrlVMNAGevvvaSAARRFLHVLAPFGLPQDVMh 1994
Cdd:cd05915    231 LDPASLVELFD-GEGVTFTAGVPTVWLALADYLESTGHRlKTLRR----LVVGG-----SAAPRSLIARFERMGVEVRQ- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1995 pGWGMSETCSVVTDSVLASE---APDHDEAFVSC--GLPYPGFAMRVVDDQDALLP-EGDVGR-LQVRGTSVTHGYHDNA 2067
Cdd:cd05915    300 -GYGLTETSPVVVQNFVKSHlesLSEEEKLTLKAktGLPIPLVRLRVADEEGRPVPkDGKALGeVQLKGPWITGGYYGNE 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2068 RANAESFTEDGWFDTGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsFTAAVAVRSDASAAtDEL 2146
Cdd:cd05915    379 EATRSALTPDGFFRTGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKV---KEAAVVAIPHPKWQ-ERP 454

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2147 ALFLRLapgQDPAGALREIAGKVTREIGVSPafLIP---VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05915    455 LAVVVP---RGEKPTPEELNEHLLKAGFAKW--QLPdayVFAEEIPRTSAGKFLKRALRE 509
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 1683-2203 5.62e-08

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: 58.44  E-value: 5.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1683 WAEALLRAAGRPDGEVVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRVI-LQCDDTEDFVATL--------W- 1752
Cdd:cd05943     72 YAENLLRHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAgYLPNIPEAVVAMLatasigaiWs 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1753 GC--------VLGGFV----AVPLTVP-VSYA--------TTSAAVSKLEGIWEMLDRPWIVtsAAGEPGLRELAARREW 1811
Cdd:cd05943    152 SCspdfgvpgVLDRFGqiepKVLFAVDaYTYNgkrhdvreKVAELVKGLPSLLAVVVVPYTV--AAGQPDLSKIAKALTL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1812 SGLRLTTADAlreEPEdrdWYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAM-NGLGSGDVsLNWIPldhV 1890
Cdd:cd05943    230 EDFLATGAAG---ELE---FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDR-LFYYT---T 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1891 TGVVMFH--LRDVYLGCRQIHAPTSWILEDPVRWPELADRHRVSV--TWAPNFAFgllAEQAHRFQDRDWDLSPVRLVMN 1966
Cdd:cd05943    300 CGWMMWNwlVSGLAVGATIVLYDGSPFYPDTNALWDLADEEGITVfgTSAKYLDA---LEKAGLKPAETHDLSSLRTILS 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1967 AGEVVvasAARRFLHVlapfglPQDVMHPGW-----GMSETCS-----VVTDSVLASEapdhdeafVSCglPYPGFAMRV 2036
Cdd:cd05943    377 TGSPL---KPESFDYV------YDHIKPDVLlasisGGTDIIScfvggNPLLPVYRGE--------IQC--RGLGMAVEA 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2037 VDDQDALLPeGDVGRLQVRG---TSVTHGYHDnarANAESFtEDGWFDT-------GDLAFL-RDGELYITGRAKDVIIV 2105
Cdd:cd05943    438 FDEEGKPVW-GEKGELVCTKpfpSMPVGFWND---PDGSRY-RAAYFAKypgvwahGDWIEItPRGGVVILGRSDGTLNP 512

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2106 NGVNHYSHEIEACVEELPSVVRSftaaVAVRSDASAATDELALFLRLAPGQDPAGALREiagKVTREI--GVSPAFlIP- 2182
Cdd:cd05943    513 GGVRIGTAEIYRVVEKIPEVEDS----LVVGQEWKDGDERVILFVKLREGVELDDELRK---RIRSTIrsALSPRH-VPa 584

                          570       580
                   ....*....|....*....|...
gi 1573930569 2183 --VEAEAIPKTEIGKIQRTKLRK 2203
Cdd:cd05943    585 kiIAVPDIPRTLSGKKVEVAVKK 607
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2757-2845 6.62e-08

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 58.52  E-value: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2757 SAGSSGRSEDTGgadelrrLESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVR 2836
Cdd:PRK10252   967 KAQVPGRAPKTG-------TETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVA 1039


                   ....*....
gi 1573930569 2837 ALARHLSQQ 2845
Cdd:PRK10252  1040 KLATLLDAE 1048
PRK03584 PRK03584
acetoacetate--CoA ligase;
469-959 7.24e-08

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 58.27  E-value: 7.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  469 SPGRTAVSYAGET-----LSYAELNAEANRLARLLVEQGAGPGRFVALALPRGPRLVPALLAVLKTGAAYL---PlDPGH 540
Cdd:PRK03584    97 RDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSscsP-DFGV 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  541 PA--ERLA------LVMADA--------EPVAVVTDTAGSgrLPaTDARVVVVDDARTVADLAGRAP-HDLTDADRAGAT 603
Cdd:PRK03584   176 QGvlDRFGqiepkvLIAVDGyryggkafDRRAKVAELRAA--LP-SLEHVVVVPYLGPAAAAAALPGaLLWEDFLAPAEA 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  604 GPYDTA--------YVIHTSGSTGRPKgvPVPHAH---VVRLFEASGEHFRFGADDVwtlfhsyAFDFSV--WELW---- 666
Cdd:PRK03584   253 AELEFEpvpfdhplWILYSSGTTGLPK--CIVHGHggiLLEHLKELGLHCDLGPGDR-------FFWYTTcgWMMWnwlv 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  667 GPLLHGGRLVVvpYEVS---RSPREFLRLLDEEKVTVLNQTPSAFEQLVLADA--ATDRATGSLRYVVLGGEALVAERLR 741
Cdd:PRK03584   324 SGLLVGATLVL--YDGSpfyPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLvpGETHDLSALRTIGSTGSPLPPEGFD 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  742 pWADRHGLDAPELVNMYGITE-TTVHVTFHRLVradledPRRRGVIGRPLADLRVYVLDAAGRPVpPGATGEMYVSGPgv 820
Cdd:PRK03584   402 -WVYEHVKADVWLASISGGTDiCSCFVGGNPLL------PVYRGEIQCRGLGMAVEAWDEDGRPV-VGEVGELVCTKP-- 471

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  821 APgylNRPelteERFLPDPFGA----------PGTrmYRSGDLARWRPDGTLVHAGRADQQVKIRGFRIEPGEIEAVLTA 890
Cdd:PRK03584   472 FP---SMP----LGFWNDPDGSryrdayfdtfPGV--WRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEA 542

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1573930569  891 HPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGADPAgLRAHLAARLPAYM----VPAACVLLDALPLTANGKL 959
Cdd:PRK03584   543 LPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA-LRARIRTTIRTNLsprhVPDKIIAVPDIPRTLSGKK 614
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 5-326 1.27e-07

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: 57.10  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569    5 EDDRRPLSGAQEGLWFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFldtPDGPRAVRDG--DPD 82
Cdd:cd19546      1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF---PGDGGDVHQRilDAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   83 empVHRVDVSGEADPAAAAEEWIRRDLATPVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTA 162
Cdd:cd19546     78 ---AARPELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGA 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  163 LAAGEEP--PPAGFESADRLAAEEAAYLGSDRHRR----DRAYWTERLAGLPEPVRL-TDRTAPPRAPflRRT---AVLS 232
Cdd:cd19546    155 RREGRAPerAPLPLQFADYALWERELLAGEDDRDSligdQIAYWRDALAGAPDELELpTDRPRPVLPS--RRAgavPLRL 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  233 PAETRA-LDEAAKGMGVARTDLLVAAVAAFLHRMTGADDLVLGLATMSRLGSAALR-TPGTASDILPLRVAASADTPVGG 310
Cdd:cd19546    233 DAEVHArLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDLEgMVGPFARPLALRTDLSGDPTFRE 312

                          330
                   ....*....|....*.
gi 1573930569  311 FVRAVADDLRGLRAHQ 326
Cdd:cd19546    313 LLGRVREAVREARRHQ 328
PRK05691 PRK05691
peptide synthase; Validated
 2754-2845 1.33e-07

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 57.87  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2754 VLRSAGSSGRSEDTGGADELrrlESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRP 2833
Cdd:PRK05691   568 LFPALQAVEAAQTAASGDEL---QARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAP 644

                           90
                   ....*....|..
gi 1573930569 2834 TVRALARHLSQQ 2845
Cdd:PRK05691   645 TLAAFSAAVARQ 656
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1837-2205 1.34e-07

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 56.59  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT-EAMNGLGSGDVSLnwiPLDHVTGVVMFhLRDVYLGcrqihaptswi 1915
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAALTASADAThDRLGGPGQWLLAL---PAHHIAGLQVL-VRSVIAG----------- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1916 lEDPVrwpELADRHRVSVTWAPNFAFGLLAEQahrfqdRDWDLSPVRLVMNAGEVVVASAARRFLHVL---APfgLPQDV 1992
Cdd:PRK07824   100 -SEPV---ELDVSAGFDPTALPRAVAELGGGR------RYTSLVPMQLAKALDDPAATAALAELDAVLvggGP--APAPV 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1993 MHPG----------WGMSETCS-VVTDsvlaseapdhdeafvscGLPYPGFAMRVVDdqdallpegdvGRLQVRGTSVTH 2061
Cdd:PRK07824   168 LDAAaaaginvvrtYGMSETSGgCVYD-----------------GVPLDGVRVRVED-----------GRIALGGPTLAK 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2062 GYHDNARANAesFTEDGWFDTGDLAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsftAAVAVrsdASA 2141
Cdd:PRK07824   220 GYRNPVDPDP--FAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAV-----ADCAV---FGL 289

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2142 ATDEL--ALFLRLAPGQDPAGALREIAGKVTREIgvsPAFLIPVE---AEAIPKTEIGKIQRTKLRKSF 2205
Cdd:PRK07824   290 PDDRLgqRVVAAVVGDGGPAPTLEALRAHVARTL---DRTAAPRElhvVDELPRRGIGKVDRRALVRRF 355
PRK05691 PRK05691
peptide synthase; Validated
 2776-2840 1.54e-07

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 57.87  E-value: 1.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVaaqTAVNKA--LGCELGVVDLFSRPTVRALAR 2840
Cdd:PRK05691  2710 LEQQLAQIWREVLNVERVGLGDNFFELGGDSILSI---QVVSRArqLGIHFSPRDLFQHQTVQTLAA 2773
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 2024-2203 1.74e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 57.07  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2024 SCGLPYPGFAMRVVDDQDALLPEGDVGRL--------QVRGTsvthgYHDNARanaesF------TEDGWFDTGDLAFL- 2088
Cdd:PRK00174   425 SATRPLPGIQPAVVDEEGNPLEGGEGGNLvikdpwpgMMRTI-----YGDHER-----FvktyfsTFKGMYFTGDGARRd 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2089 RDGELYITGRAKDVIIVNGvnhysH-----EIEACVEELPSVVRsftAAVAVRSDASAATDELAlFLRLAPGQDPAGALR 2163
Cdd:PRK00174   495 EDGYYWITGRVDDVLNVSG-----HrlgtaEIESALVAHPKVAE---AAVVGRPDDIKGQGIYA-FVTLKGGEEPSDELR 565

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1573930569 2164 -EIAGKVTREIG--VSPAFLIPVeaEAIPKTEIGKIQRTKLRK 2203
Cdd:PRK00174   566 kELRNWVRKEIGpiAKPDVIQFA--PGLPKTRSGKIMRRILRK 606
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 1726-2102 1.88e-07

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 56.95  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1726 LRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL---------TVPVSYATTSAAVSKLEGIWEML-----DRPW 1791
Cdd:PLN02614    96 LRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLydtlgagavEFIISHSEVSIVFVEEKKISELFktcpnSTEY 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1792 IVTSAAGEPGLRELAARREWSGLRLTTADALREEPEDRDwYE---ARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA 1868
Cdd:PLN02614   176 MKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQ-YDlpiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAG 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1869 T-----EAMNGLGSGDVSLNWIPLDHV------------TGVVMFHLRDVYLGCRQIHAPTSWILedpVRWPELADR--- 1928
Cdd:PLN02614   255 VirllkSANAALTVKDVYLSYLPLAHIfdrvieecfiqhGAAIGFWRGDVKLLIEDLGELKPTIF---CAVPRVLDRvys 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1929 ------------HRVSVTWAPNFAFGLLAE-QAHRFQDRDWDL-----------SPVRLVMnAGEVVVASAARRFLHVLA 1984
Cdd:PLN02614   332 glqkklsdggflKKFVFDSAFSYKFGNMKKgQSHVEASPLCDKlvfnkvkqglgGNVRIIL-SGAAPLASHVESFLRVVA 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1985 PFGLPQdvmhpGWGMSETCSVVTDSVlaseaPDHDEAFVSCGLPYPGFAMRVVD----DQDAL--LPEGDVGrlqVRGTS 2058
Cdd:PLN02614   411 CCHVLQ-----GYGLTESCAGTFVSL-----PDELDMLGTVGPPVPNVDIRLESvpemEYDALasTPRGEIC---IRGKT 477

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1573930569 2059 VTHGYHDNARANAESFTeDGWFDTGDLA-FLRDGELYITGRAKDV 2102
Cdd:PLN02614   478 LFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPNGSMKIIDRKKNI 521
PRK12316 PRK12316
peptide synthase; Provisional
 19-322 2.90e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 56.89  E-value: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   19 WFAHRLAPGTAAYNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAVRDGDPDEMPVHRVDVSGEADPA 98
Cdd:PRK12316  1109 WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELL 1188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   99 AAAEEWIRRdlatpVDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEEPPPAGFESAD 178
Cdd:PRK12316  1189 ALCEEAQRS-----LDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWA 1263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  179 RLAAEEAAYLGsdrhrRDRAYWTERLAGLPEPVRLTDRTAPPRAPFLRRTAVLSPAET--RALDEAAKGMGVARTDLLVA 256
Cdd:PRK12316  1264 RRLHEHAGARA-----EELDYWQAQLEDAPHELPCENPDGALENRHERKLELRLDAERtrQLLQEAPAAYRTQVNDLLLT 1338

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  257 AVAAFLHRMTGADDLVLGLATMSR--LGSAA--LRTPGTASDILPLRVAASADtpVGGFVRAVADDLRGL 322
Cdd:PRK12316  1339 ALARVTCRWSGQASVLVQLEGHGRedLFEDIdlSRTVGWFTSLFPVRLTPAAD--LGESIKAIKEQLRAV 1406
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 1837-2100 3.53e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 56.14  E-value: 3.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1837 DDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAA-----TEAMNGLGSGDVSLNWIPLDHV---TGVVMFHLRDVYLGcrqi 1908
Cdd:PTZ00216   264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILAledrlNDLIGPPEEDETYCSYLPLAHImefGVTNIFLARGALIG---- 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1909 hAPTSWILEDpvrwpELADRHRVSVTWAPNFAFGL--------------------LAEQA--HRFQDR--------D--- 1955
Cdd:PTZ00216   340 -FGSPRTLTD-----TFARPHGDLTEFRPVFLIGVprifdtikkaveaklppvgsLKRRVfdHAYQSRlralkegkDtpy 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1956 WD---LSPVRLV-------MNAGEVVVASAARRFLHVLapFGLpqdvMHPGWGMSETCSVVTDSVLASEAPdhdeafVSC 2025
Cdd:PTZ00216   414 WNekvFSAPRAVlggrvraMLSGGGPLSAATQEFVNVV--FGM----VIQGWGLTETVCCGGIQRTGDLEP------NAV 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2026 GLPYPGFAMRVVDDQ-----DALLPEGDVgrlQVRGTSVTHGYHDNARANAESFTEDGWFDTGDLA-FLRDGELYITGRA 2099
Cdd:PTZ00216   482 GQLLKGVEMKLLDTEeykhtDTPEPRGEI---LLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGsIAANGTLRIIGRV 558


                   .
gi 1573930569 2100 K 2100
Cdd:PTZ00216   559 K 559
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 799-965 5.36e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 55.00  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  799 DAAGRPVP-------PGATGEMYVSGPGVAPGYLnrPELTEERflpdpfgapgtRMYRSGDLARWRPDGTLVHAGRADQQ 871
Cdd:PRK07445   283 NSSGQVLPhaqitipANQTGNITIQAQSLALGYY--PQILDSQ-----------GIFETDDLGYLDAQGYLHILGRNSQK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  872 VKIRGFRIEPGEIEAVLTAHPAVAGGAVVPRAAEDGLTQLVAYAVPAEEGGaDPAGLRAHLAARLPAYMVPAACVLLDAL 951
Cdd:PRK07445   350 IITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSI-SLEELKTAIKDQLSPFKQPKHWIPVPQL 428

                          170
                   ....*....|....
gi 1573930569  952 PLTANGKLDTAALP 965
Cdd:PRK07445   429 PRNPQGKINRQQLQ 442
PRK12467 PRK12467
peptide synthase; Provisional
 31-344 7.82e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 55.17  E-value: 7.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569   31 YNTGEYVEIHGPVDTALFETALRRTVREADTFALRFLDTPDGPRAV-RDGDPDEMPVHRVDVSGEADPAAAAEEWIRRDL 109
Cdd:PRK12467  2201 WNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMhRAPEQERRPLLWQVVVADKEELEALCEQAQRSL 2280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  110 atpvDVAAGPLFSHALLTLAPDRFIWFLRAHHILLDGYSYKLVARRLADTYTALAAGEEPP-PAGFESADRLAAEEAAYL 188
Cdd:PRK12467  2281 ----DLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKlPAKTSAFKAWAERLQTYA 2356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  189 GSDRHRRDRAYWTERLAGLPEPVRLTDRTAPPRAPFLR--RTAVLSPAETRALDEAAKGMGVARTDLLVAAVAAFLHRMT 266
Cdd:PRK12467  2357 ASAALADELGYWQAQLQGASTELPCDHPQGGLQRRHAAsvTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWT 2436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  267 GADDLVLGLATMSRL----GSAALRTPGTASDILPLRVAASADtpVGGFVRAVADDLRGLRAHQ------RHRG-ESIRR 335
Cdd:PRK12467  2437 GQASTLIQLEGHGREdlfdEIDLTRTVGWFTSLYPVKLSPTAS--LATSIKTIKEQLRAVPNKGlgfgvlRYLGsEAARQ 2514


                   ....*....
gi 1573930569  336 DLGVLGRGR 344
Cdd:PRK12467  2515 TLQALPVPR 2523
PRK12316 PRK12316
peptide synthase; Provisional
 2776-2845 9.61e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 54.96  E-value: 9.61e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHLSQQ 2845
Cdd:PRK12316  2517 LEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESG 2586
PRK12316 PRK12316
peptide synthase; Provisional
 2776-2840 2.09e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 53.81  E-value: 2.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKAlGCELGVVDLFSRPTVRALAR 2840
Cdd:PRK12316  1019 LERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLAL 1082
PRK05691 PRK05691
peptide synthase; Validated
 2776-2842 2.68e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 53.63  E-value: 2.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALARHL 2842
Cdd:PRK05691  4242 LEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
PLN02654 PLN02654
acetate-CoA ligase
 1828-2203 2.78e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 52.98  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1828 DRDWYEArpDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT---------------EAMNGLGSGDVSLNWIPLDHVTG 1892
Cdd:PLN02654   268 EVEWVDA--EDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTfkyafdykptdvywcTADCGWITGHSYVTYGPMLNGAT 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1893 VVMFHlrdvylgcrqiHAPTswiLEDPVRWPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRdWDLSPVRLVMNAGEVVV 1972
Cdd:PLN02654   346 VLVFE-----------GAPN---YPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTR-HSRKSLRVLGSVGEPIN 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1973 ASAARRFLHVLAPFGLPqdvMHPGWGMSETCSVVTdSVLASEAPDHDEafvSCGLPYPGFAMRVVDDQDALLpEGDV-GR 2051
Cdd:PLN02654   411 PSAWRWFFNVVGDSRCP---ISDTWWQTETGGFMI-TPLPGAWPQKPG---SATFPFFGVQPVIVDEKGKEI-EGECsGY 482

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2052 LQVRGT---SVTHGYHDNARANAESFTE-DGWFDTGD-LAFLRDGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVV 2126
Cdd:PLN02654   483 LCVKKSwpgAFRTLYGDHERYETTYFKPfAGYYFSGDgCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCA 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2127 RSftAAVAVRSDASAATdeLALFLRLAPGQDPAGALRE-IAGKVTREIGvspAFLIPVE---AEAIPKTEIGKIQRTKLR 2202
Cdd:PLN02654   563 EA--AVVGIEHEVKGQG--IYAFVTLVEGVPYSEELRKsLILTVRNQIG---AFAAPDKihwAPGLPKTRSGKIMRRILR 635


                   .
gi 1573930569 2203 K 2203
Cdd:PLN02654   636 K 636
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 1711-2102 3.27e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 52.92  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPL---------TVPVSYATTSAAV---S 1778
Cdd:PLN02861    79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLydtlganavEFIINHAEVSIAFvqeS 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1779 KLEGIWEMLDRpwiVTSaagepGLRELAARREWSGLRLTTADALR------EE-----PEDRDWYEARPDDLVLMLMTSG 1847
Cdd:PLN02861   159 KISSILSCLPK---CSS-----NLKTIVSFGDVSSEQKEEAEELGvscfswEEfslmgSLDCELPPKQKTDICTIMYTSG 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1848 STGLPKAVRLTHRNVLTRAAATEAM-----NGLGSGDVSLNWIPLDHVTGVVM---FHLRDVYLGCRQihAPTSWILED- 1918
Cdd:PLN02861   231 TTGEPKGVILTNRAIIAEVLSTDHLlkvtdRVATEEDSYFSYLPLAHVYDQVIetyCISKGASIGFWQ--GDIRYLMEDv 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1919 ----PVRW---PELADR------HRVS---------VTWAPNFAF-----GLLAEQAHRFQDRdwdlspvrLVMNAGEVV 1971
Cdd:PLN02861   309 qalkPTIFcgvPRVYDRiytgimQKISsggmlrkklFDFAYNYKLgnlrkGLKQEEASPRLDR--------LVFDKIKEG 380

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1972 VASAARRFLHVLAPfgLPQDV-----------MHPGWGMSETCSVVTDSvLASEAPdhdeAFVSCGLPYPGFAMRVVD-- 2038
Cdd:PLN02861   381 LGGRVRLLLSGAAP--LPRHVeeflrvtscsvLSQGYGLTESCGGCFTS-IANVFS----MVGTVGVPMTTIEARLESvp 453

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1573930569 2039 --DQDAL--LPEGDVGrlqVRGTSVTHGYHDNARANAESFTeDGWFDTGDLAFLR-DGELYITGRAKDV 2102
Cdd:PLN02861   454 emGYDALsdVPRGEIC---LRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQpNGAMKIIDRKKNI 518
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 1823-2103 3.33e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 52.90  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1823 REEPEDRdwYEARPDDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAATEAM-----NGLGSGDVSLNWIPLDHV------- 1890
Cdd:PLN02430   208 KENPSET--NPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFmeqfeDKMTHDDVYLSFLPLAHIldrmiee 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1891 ------TGVVMFH-----LRD---------------VYlgcRQIHAPTSWILED--PVR-------------WPELADRH 1929
Cdd:PLN02430   286 yffrkgASVGYYHgdlnaLRDdlmelkptllagvprVF---ERIHEGIQKALQElnPRRrlifnalykyklaWMNRGYSH 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1930 RVSVTWAPNFAFGLLAEqahRFQDRdwdlspVRLVMNAGeVVVASAARRFLHVLAPFGLPQdvmhpGWGMSETCSVVTDS 2009
Cdd:PLN02430   363 KKASPMADFLAFRKVKA---KLGGR------LRLLISGG-APLSTEIEEFLRVTSCAFVVQ-----GYGLTETLGPTTLG 427

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2010 VlaseaPDHDEAFVSCGLP--YPGFAMRVVDDQdALLPEGD--VGRLQVRGTSVTHGYHDNARANAESFtEDGWFDTGDL 2085
Cdd:PLN02430   428 F-----PDEMCMLGTVGAPavYNELRLEEVPEM-GYDPLGEppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDI 500

                          330
                   ....*....|....*....
gi 1573930569 2086 A-FLRDGELYITGRAKDVI 2103
Cdd:PLN02430   501 GeILPNGVLKIIDRKKNLI 519
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 1809-2203 4.11e-06

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 52.24  E-value: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1809 REWSGLR---LTTADALREepedrDWYEARP----DDLVLMLMTSGSTGLPKAVRLTHRNV----------LTRAAATEA 1871
Cdd:cd05913     48 KSLDDLRklpFTTKEDLRD-----NYPFGLFavprEKVVRIHASSGTTGKPTVVGYTKNDLdvwaelvarcLDAAGVTPG 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1872 ---MNGLGSGdvsLNwipldhvTGVVMFHLRDVYLGCRQIHAPTSWILEdpvRWPELADRhRVSVTWA-PNFAFgLLAEQ 1947
Cdd:cd05913    123 drvQNAYGYG---LF-------TGGLGFHYGAERLGALVIPAGGGNTER---QLQLIKDF-GPTVLCCtPSYAL-YLAEE 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1948 AhrfQDRDWDL--SPVRLVMNAGEVVvASAARRFLHVLAP------FGLpQDVMHPGWGMseTCSVVTDSVLASeapDHd 2019
Cdd:cd05913    188 A---EEEGIDPreLSLKVGIFGAEPW-TEEMRKRIERRLGikaydiYGL-TEIIGPGVAF--ECEEKDGLHIWE---DH- 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2020 eafvscglpypgFAMRVVDDQD-ALLPEGDVGRLQVrgTSVTHGYHDNARanaesftedgwFDTGDLAFLRDGE------ 2092
Cdd:cd05913    257 ------------FIPEIIDPETgEPVPPGEVGELVF--TTLTKEAMPLIR-----------YRTRDITRLLPGPcpcgrt 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2093 ----LYITGRAKDVIIVNGVNHYSHEIEACVEELPSVVRSFTaAVAVRSDasaATDELALFLRLAPGQD----PAGALRE 2164
Cdd:cd05913    312 hrriDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQ-LILTRQE---HLDELTIKVEVRPEADddekLEALKQR 387

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1573930569 2165 IAGKVTREIGVSPAFLIpVEAEAIPKTEiGKIQR-TKLRK 2203
Cdd:cd05913    388 LERHIKSVLGVTVEVEL-VEPGSLPRSE-GKAKRvIDKRK 425
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 1652-1892 4.13e-06

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: 52.46  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1652 AAEPDAPSVERPASVPALSEgPALPEPSVSGWAE--AL-LRAAGRPDGEVVHVRADGSETRR---SYASLVPEASRVLAG 1725
Cdd:cd17632      5 AAAAPLEAVTEAIRRPGLRL-AQIIATVMTGYADrpALgQRATELVTDPATGRTTLRLLPRFetiTYAELWERVGAVAAA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1726 LR-RRGLRPGDRVILQCDDTEDFVATLWGCVLGGFVAVPLTvpvsyatTSAAVSKLEGIWEMLDRPWIVTSAAGEPGLRE 1804
Cdd:cd17632     84 HDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQ-------AGASAAQLAPILAETEPRLLAVSAEHLDLAVE 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1805 LAA-------------RREW------------------SGLRLTTADALREE---PEDRDWYEARPDDLVLMLMTSGSTG 1850
Cdd:cd17632    157 AVLeggtpprlvvfdhRPEVdahraalesarerlaavgIPVTTLTLIAVRGRdlpPAPLFRPEPDDDPLALLIYTSGSTG 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1573930569 1851 LPKAVRLTHRNVlTRAAATEAMNGLGSGDVS--LNWIPLDHVTG 1892
Cdd:cd17632    237 TPKGAMYTERLV-ATFWLKVSSIQDIRPPASitLNFMPMSHIAG 279
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 513-921 5.74e-06

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 51.74  E-value: 5.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  513 LPRGPRLVPALLAVLKTGAAYLPLDPGHPAERLALVMADAEPVAVVTDTA---GSGRLP-------ATDARVVVVDDART 582
Cdd:PLN03051     1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVvlrGGRALPlyskvveAAPAKAIVLPAAGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  583 VADLAGRaPHDLTDADRAGAT--------GPYDTAY--------VIHTSGSTGRPKGVPVPHAHVVRLFEASGEHFRFGA 646
Cdd:PLN03051    81 PVAVPLR-EQDLSWCDFLGVAaaqgsvggNEYSPVYapvesvtnILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  647 DDVWTLFHSYAFDFSVWELWGPLLHGGRLVVvpYEVSRSPREFLRLLDEEKVTVLNQTPSAFEQLVLADA-ATDRATGS- 724
Cdd:PLN03051   160 GDVVCWPTNLGWMMGPWLLYSAFLNGATLAL--YGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAfAMEGLDWSk 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  725 LRYVVLGGEALVAERLRPWADRHGLDAPeLVNMYGITETTvhvtfHRLVRADLEDPRRRGVIGRPLADLRVYVLDAAGRP 804
Cdd:PLN03051   238 LRVFASTGEASAVDDVLWLSSVRGYYKP-VIEYCGGTELA-----SGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVP 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  805 VPPGAT--GEMYVSGP--GVAPGYLNRpELTEERFLPDP-FGAPGTRMYRSGDLARWRPDGTLVHAGRADQQVKIRGFRI 879
Cdd:PLN03051   312 YPDDQPcvGEVALAPPmlGASDRLLNA-DHDKVYYKGMPmYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKT 390

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569  880 EPGEIE-AVLTAHPAVAGGAVVPRAAEDG---LTQLVAYAVPAEEG 921
Cdd:PLN03051   391 SSVEIErACDRAVAGIAETAAVGVAPPDGgpeLLVIFLVLGEEKKG 436
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1107-1502 6.09e-06

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: 51.54  E-value: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1107 DLDALRAALGDVADRHESLRTVFGEEDGA-----IHQRVLPPGTL------RPELH---VVDCPDEERAAHVAAAMRRSF 1172
Cdd:cd19547     37 DEDVLREAWRRVADRYEILRTGFTWRDRAeplqyVRDDLAPPWALldwsgeDPDRRaelLERLLADDRAAGLSLADCPLY 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1173 DLTrdsalwagVFGTGDTRTLLLVLHHSA-ADGWSLRPLADDLGTAYAARRAGAAPDWApPALQYADFALWQRRVLAPAP 1251
Cdd:cd19547    117 RLT--------LVRLGGGRHYLLWSHHHIlLDGWCLSLIWGDVFRVYEELAHGREPQLS-PCRPYRDYVRWIRARTAQSE 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1252 EGpgrlERltsFWRQALDGLpeesappPDRPRPAAPSGRGGgvtvPLDAGTH---RELLRLADhENASLFMVLHGAL--- 1325
Cdd:cd19547    188 ES----ER---FWREYLRDL-------TPSPFSTAPADREG----EFDTVVHefpEQLTRLVN-EAARGYGVTTNAIsqa 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1326 --ALLLNRWGAGDDIVVGTPVAGRTePAL---DEVVGLLTNTLVLRADASGDPTFRELLARVRAFDVQALDHQDLPFDRL 1400
Cdd:cd19547    249 awSMLLALQTGARDVVHGLTIAGRP-PELegsEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQI 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1401 VEEVNPRRHPARHpLFQVMLALQNneravltLGEDRVPlrpaatgtaKFDLFVDVLERHGADGTA----------DGLDL 1470
Cdd:cd19547    328 KSWASGERLSGGR-VFDNLVAFEN-------YPEDNLP---------GDDLSIQIIDLHAQEKTEypiglivlplQKLAF 390

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1573930569 1471 HVEYAADLYDPATAERFAGALRDLLTVVCADP 1502
Cdd:cd19547    391 HFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PRK12467 PRK12467
peptide synthase; Provisional
 2776-2839 6.91e-06

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 52.09  E-value: 6.91e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKAlGCELGVVDLFSRPTVRALA 2839
Cdd:PRK12467  2098 LEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLA 2160
PRK12316 PRK12316
peptide synthase; Provisional
 2776-2840 7.06e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 52.27  E-value: 7.06e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKAlGCELGVVDLFSRPTVRALAR 2840
Cdd:PRK12316  3557 LERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQA-GIRFTPKDLFQHQTIQGLAR 3620
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 2082-2209 9.24e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 50.81  E-value: 9.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2082 TGDLAFLR-DGELYITGRAKDVIIVNGVNHYSHEIEACVEELPSVvrsfTAAVAVRSDASAATDELALFLRLAPGQDPAg 2160
Cdd:PRK08308   295 TKDLGYKSeRGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGV----QEAVVYRGKDPVAGERVKAKVISHEEIDPV- 369

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1573930569 2161 ALREIAgkvtreIGVSPAFLIPVEAE---AIPKTEIGKIQrtklRKSFEAGE 2209
Cdd:PRK08308   370 QLREWC------IQHLAPYQVPHEIEsvtEIPKNANGKVS----RKLLELGE 411
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 2754-2845 1.44e-05

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 49.75  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2754 VLRSAGSSGRSEDTGGADELRRLESELAAVWCTVLG--RDRVGRDENFFDLGGNSLLLVAAQTAVNKAlGCELGVVDLFS 2831
Cdd:COG3433    198 ALAAAEALLAAASPAPALETALTEEELRADVAELLGvdPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAE 276

                           90
                   ....*....|....
gi 1573930569 2832 RPTVRALARHLSQQ 2845
Cdd:COG3433    277 HPTLAAWWALLAAA 290
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 983-1052 1.57e-05

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: 45.23  E-value: 1.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569  983 ERLVCGLFEEVLRLPADSVGTGGNFF-DLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAERLTA 1052
Cdd:COG0236      7 EERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
prpE PRK10524
propionyl-CoA synthetase; Provisional
 1705-2207 1.70e-05

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 50.33  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1705 GSETRRSYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGC---------VLGGFVAVPLTVPVSYATTSA 1775
Cdd:PRK10524    80 DEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACarigaihsvVFGGFASHSLAARIDDAKPVL 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1776 AVSKLEGIW--------EMLDRPwiVTSAAGEPGL-----RELAARREWSGLRLTTAdALREEPEDRD----WYEArpDD 1838
Cdd:PRK10524   160 IVSADAGSRggkvvpykPLLDEA--IALAQHKPRHvllvdRGLAPMARVAGRDVDYA-TLRAQHLGARvpveWLES--NE 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1839 LVLMLMTSGSTGLPKAVRlthRNVLTRAAATEAmnglgsgdvSLNWIpLDHVTGVVMFHLRDV-------YLgcrqIHAP 1911
Cdd:PRK10524   235 PSYILYTSGTTGKPKGVQ---RDTGGYAVALAT---------SMDTI-FGGKAGETFFCASDIgwvvghsYI----VYAP 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1912 -----TSWILED-PVR-----WPELADRHRVSVTWAPNFAFGLLAEQAHRFQDRdWDLSPVRLVMNAGEVVVASAARRFL 1980
Cdd:PRK10524   298 llagmATIMYEGlPTRpdagiWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRK-HDLSSLRALFLAGEPLDEPTASWIS 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1981 HVLapfGLP------QdvMHPGWGMSETCSVVTDSVlaseapdhdEAFVSCGLPYPGFAMRVVDDQD-ALLPEGDVGRLQ 2053
Cdd:PRK10524   377 EAL---GVPvidnywQ--TETGWPILAIARGVEDRP---------TRLGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVLV 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2054 VRG-------TSVthgYHDNARanaesFTEDGW----------FDTGdlafLRD--GELYITGRAKDVIIVNGVNHYSHE 2114
Cdd:PRK10524   443 IEGplppgcmQTV---WGDDDR-----FVKTYWslfgrqvystFDWG----IRDadGYYFILGRTDDVINVAGHRLGTRE 510

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2115 IEACVEELPSVvrsftAAVAVRSDASAATDELAL-FLRLAPG---QDPAGALR---EIAGKVTREIG--VSPAFLIPVea 2185
Cdd:PRK10524   511 IEESISSHPAV-----AEVAVVGVKDALKGQVAVaFVVPKDSdslADREARLAlekEIMALVDSQLGavARPARVWFV-- 583

                          570       580
                   ....*....|....*....|..
gi 1573930569 2186 EAIPKTEIGKIqrtkLRKSFEA 2207
Cdd:PRK10524   584 SALPKTRSGKL----LRRAIQA 601
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 984-1045 1.73e-05

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: 44.48  E-value: 1.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1573930569  984 RLVCGLFEEVLRLPADSVGTGGNFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAA 1045
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 2249-2810 2.53e-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: 50.26  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2249 AGHRVLVLAGPAPHAHAVAEEVAGAVRDAGGLCTVVTEGPAPER---------------------NGAAAYRV------- 2300
Cdd:COG3321    789 DGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQlltalaqlwvagvpvdwsalyPGRGRRRVplptypf 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2301 -RPGEAGDLAAVLERLEADGRTPDTVVHLAATEDAEDGAAPGSDVSLLVLAQALAGRTGGERPVDLLFVTAGAQAVTPEE 2379
Cdd:COG3321    869 qREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2380 RPTASHAAAGALLKSLREELPWLRGVHLD-------LSGGSAGDRAAAVLAEAAGFPADTEVARREGLRYVRRLAPLPDS 2452
Cdd:COG3321    949 AAAAAAALAAAEAGALLLLAAAAAAAAAAaaaaaaaAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALL 1028

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2453 APRTAPAPAPADGFHLVSGGLGGVGSEVAAHLLKEPGTRLLLIGRTGLPPEDTWERHLADAGPASSRIEAFRRLRGLGEV 2532
Cdd:COG3321   1029 AAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLL 1108

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2533 RYETADVTDAAQVRAAVRRAADAWGVPLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVAAGHPVTSFVTF 2612
Cdd:COG3321   1109 LALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAA 1188

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2613 SSVNGFFGGAMNAAYSAANAALDDLALRRRREGLPGQSLAWSMWRERGMSLGYQLTSLTEARGYRVLDAQAALRSFDLAR 2692
Cdd:COG3321   1189 LAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAA 1268

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2693 TLDLPHLLIGADRTAPWVRSHVLAPVRQVRRTAARVVLDEGTDLGALYGAAARAAGPEGTFVLRSAGSSGRSEDTGGADE 2772
Cdd:COG3321   1269 AGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAA 1348

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1573930569 2773 LRRLESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLV 2810
Cdd:COG3321   1349 AAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PRK03584 PRK03584
acetoacetate--CoA ligase;
1683-1737 6.84e-05

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 48.64  E-value: 6.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1573930569 1683 WAEALLRAAgRPDGE-VVHVRADGSETRRSYASLVPEASRVLAGLRRRGLRPGDRV 1737
Cdd:PRK03584    88 YAENLLRHR-RDDRPaIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRV 142
PRK05691 PRK05691
peptide synthase; Validated
 2776-2839 7.40e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 48.63  E-value: 7.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1573930569 2776 LESELAAVWCTVLGRDRVGRDENFFDLGGNSLLLVAAQTAVNKALGCELGVVDLFSRPTVRALA 2839
Cdd:PRK05691  1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFA 1702
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 2757-2844 9.30e-05

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: 48.52  E-value: 9.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2757 SAGSSGRSEDTGGAdELRRLESELAAVWCTVLGR--DRVGRDENFFDLGGNSLLLVAAQTAVNKALGCE--LGVVdlFSR 2832
Cdd:TIGR03443  831 AAVAKNRSASAADE-EFTETEREIRDLWLELLPNrpATISPDDSFFDLGGHSILATRMIFELRKKLNVElpLGLI--FKS 907

                           90
                   ....*....|..
gi 1573930569 2833 PTVRALARHLSQ 2844
Cdd:TIGR03443  908 PTIKGFAKEVDR 919
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 1711-1894 4.80e-04

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: 45.42  E-value: 4.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRRRGLRPGDRVILQCDDTEDFVATLWGCV-LGGFVAVpltvpvsyattsaavsklegiwemldr 1789
Cdd:cd05940      5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVkIGAVAAL--------------------------- 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1790 pwIVTSAAGEPglreLAarrewSGLRLTTADALREepedrdwyearpdDLVLMLMTSGSTGLPKAVRLTHRNVLTRAAAT 1869
Cdd:cd05940     58 --INYNLRGES----LA-----HCLNVSSAKHLVV-------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF 113

                          170       180
                   ....*....|....*....|....*
gi 1573930569 1870 EAMNGLGSGDVSLNWIPLDHVTGVV 1894
Cdd:cd05940    114 AGSGGALPSDVLYTCLPLYHSTALI 138
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1318-1521 5.40e-04

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: 45.83  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1318 FMVLHGALALLLNRWGAGDDIVVGTPVAGRTEPaldevvglltntLVLRADASGDPTFRELLARVRAFDVQALDHQDLPF 1397
Cdd:TIGR03443   49 FIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPF 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1398 DRLVEEVNPRRHPARHP-LFQvmLALQNNEravltlgedRVPLRPAATGTAKfDLFVDVlerhgaDGTADGLDLHVEYAA 1476
Cdd:TIGR03443  117 DELSEHIQAAKKLERTPpLFR--LAFQDAP---------DNQQTTYSTGSTT-DLTVFL------TPSSPELELSIYYNS 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1573930569 1477 DLYDPATAERFAGALRDLLTVVCADPEVRTGALP------RADRPSPaTAD 1521
Cdd:TIGR03443  179 LLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSlitpsqKSLLPDP-TKD 228
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 1711-1895 8.21e-04

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: 44.97  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1711 SYASLVPEASRVLAGLRR-RGLRPGDRVILQCDDTEDFVATLWG-CVLGGFVAV--------PL---------TVPVSYA 1771
Cdd:cd05938      7 TYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGlAKLGCPVAFlntnirskSLlhcfrccgaKVLVVAP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1772 TTSAAVSK-LEGIWEMLDRPWIVTSAAGEPGLRELAARrewsglrlttADALREEPEDRDW-YEARPDDLVLMLMTSGST 1849
Cdd:cd05938     87 ELQEAVEEvLPALRADGVSVWYLSHTSNTEGVISLLDK----------VDAASDEPVPASLrAHVTIKSPALYIYTSGTT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1573930569 1850 GLPKAVRLTHRNVLtRAAATEAMNGLGSGDVSLNWIPLDHVTGVVM 1895
Cdd:cd05938    157 GLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGFLL 201
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 520-867 9.91e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 44.58  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  520 VPALLAVLKTGAAylpldPGHPaerlaLVMADAEPVAVvtDTAGSGRLPATDarvVVVDDARTVADLAGRAPhdlTDADr 599
Cdd:PTZ00216   204 VPNLLRLMKSGGM-----PNTT-----IIYLDSLPASV--DTEGCRLVAWTD---VVAKGHSAGSHHPLNIP---ENND- 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  600 agatgpyDTAYVIHTSGSTGRPKGVPVPHAHVV--------RLFEASGEHfrfgADDVWTLfhSYAfdfsvwelwgPLLH 671
Cdd:PTZ00216   265 -------DLALIMYTSGTTGDPKGVMHTHGSLTagilaledRLNDLIGPP----EEDETYC--SYL----------PLAH 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  672 GGRLVVVPYEVSR-------SPREFLRL-------LDEEKVTVLNQTPSAFEQLVLADAATDRATGSLRYVVLggEALVA 737
Cdd:PTZ00216   322 IMEFGVTNIFLARgaligfgSPRTLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVF--DHAYQ 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  738 ERLRpwADRHGLDAP---ELV----------NMYGI----------TETTVHVTFHRLVR----------------ADLE 778
Cdd:PTZ00216   400 SRLR--ALKEGKDTPywnEKVfsapravlggRVRAMlsgggplsaaTQEFVNVVFGMVIQgwgltetvccggiqrtGDLE 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569  779 DprrrGVIGRPLADLRVYVLDAAG-----RPVPpgaTGEMYVSGPGVAPGYLNRPELTEERFLPDPFgapgtrmYRSGDL 853
Cdd:PTZ00216   478 P----NAVGQLLKGVEMKLLDTEEykhtdTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW-------FHTGDV 543

                          410
                   ....*....|....
gi 1573930569  854 ARWRPDGTLVHAGR 867
Cdd:PTZ00216   544 GSIAANGTLRIIGR 557
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 2559-2653 1.03e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 44.36  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 2559 PLVSVLHLAGAFDERPVRELTPQEWREALAAKVDGAWALHRVA--AGHPVTSFVTFSSVNGFFGGAMNAAYSAANAALDD 2636
Cdd:cd08954    301 PIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSikRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDS 380

                           90
                   ....*....|....*..
gi 1573930569 2637 LALRRRREGLPGQSLAW 2653
Cdd:cd08954    381 LSRYRKSIGLPSIAINW 397
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 983-1052 1.80e-03

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: 39.54  E-value: 1.80e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1573930569   983 ERLVCGLFEEVLRL-PADSVGTGGNFFDLGGHSLLATRLLARLRERTGTDVPISALFDTPTPAALAERLTA 1052
Cdd:smart00823   14 LDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1481-1710 7.45e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.54  E-value: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1481 PATAERFAGALRDlltvvCADPEVRTGALPRADRPSPATADTTARAGALTRAVLEVPGVGDAVVLPGPDGEPATVYVVPN 1560
Cdd:COG0515    255 YQSAAELAAALRA-----VLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAA 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1561 RAGAADRTEQVVSSLAPGTRVVAISGLPRTAEGGLDEGALKDLPVIDQVAAGAWRERLARLPGVREAEVVLEEVPEELER 1640
Cdd:COG0515    330 AAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAA 409

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1573930569 1641 RHVGRPRAAGGAAEPDAPSVERPASVPALSEGPALPEPSVSGWAEALLRAAGRPDGEVVHVRADGSETRR 1710
Cdd:COG0515    410 AAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAAL 479
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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