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Conserved domains on  [gi|446807313|ref|WP_000884569|]
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MULTISPECIES: non-ribosomal peptide synthetase [Bacillus]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1002729)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products; may contain C-terminal alpha/beta hydrolase domain

EC:  6.2.1.-
Gene Ontology:  GO:0019184|GO:0016874

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
21-1911 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1391.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   21 EYWLDKLSGDVELSRFPCDclslnNIQASKESYYCQ-----FPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKD 95
Cdd:PRK12467  241 AYWQEQLGGEHTVLELPTD-----RPRPAVPSYRGArlrvdLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQS 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   96 DVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLL 171
Cdd:PRK12467  316 DIRIGVPNANRNRVETErligFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLF 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  172 -------NTIVM-------------LDDIHCYESTDKInsDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNIL 231
Cdd:PRK12467  396 qvmfnhqNTATGgrdregaqlpgltVEELSWARHTAQF--DLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLL 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  232 DILMKDPNKSAMDLDVMPKTEKNQILFDFNhttrvhktlLCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLN 307
Cdd:PRK12467  474 EAIVAEPRRRLGELPLLDAEERARELVRWN---------APATEYAPdcvhQLIEAQARQHPERPALVFGEQVLSYAELN 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  308 IKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIKGV 387
Cdd:PRK12467  545 RQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-QSHLLAQL 623
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  388 AFQGSV----INLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVL 463
Cdd:PRK12467  624 PVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL--QLAADDSML 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 FSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYfVRANQKISLNKLFVGV 542
Cdd:PRK12467  702 MVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGG 780
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 EPIKTELLAKYDHLfRGNLQILNLYGPTEATVCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEIC 622
Cdd:PRK12467  781 EALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELY 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  623 ISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK12467  859 IGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  702 KTAVVIQrEDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:PRK12467  939 REAVVLA-QPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA 1017
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  775 N-LKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK12467 1018 SaVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAV 1097
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  854 LEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI 933
Cdd:PRK12467 1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGS-AAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ 1176
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  934 LDGELVQKIEP--NVDFNIEYVHVNEKDAD----YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSM 1007
Cdd:PRK12467 1177 EDGRTRQVIHPvgSLTLEEPLLLAADKDEAqlkvYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSM 1256
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1008 GILIKEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGN 1081
Cdd:PRK12467 1257 QVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGA 1336
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1082 VCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLEND 1161
Cdd:PRK12467 1337 RLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQ 1416
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1162 DEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDL 1240
Cdd:PRK12467 1417 ASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDL 1496
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1241 SLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLV 1320
Cdd:PRK12467 1497 TLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLV 1576
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK12467 1577 HQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQshlqaRLPLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ-GEKFDVTKLVQVILEEQVTL 1554
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTT 1812
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 1813 LHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDS 1891
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIE 1971
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTeKDIPIPE-----------VRAYLAT 1782
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKA 2049
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSL 1861
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
                        1930      1940      1950      1960      1970
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1862 KGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKG---ID------SECLIPIQ 1911
Cdd:PRK12467 2130 ISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGtvsIDqgpvtgDLPLLPIQ 2187
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
1921-2157 3.85e-28

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00975:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 223  Bit Score: 114.41  E-value: 3.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMA 2000
Cdd:pfam00975    4 FCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2001 RKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAfEELEKFNDQLGIEKISFEqmseeqlIESLLKKFtlnenscqqnf 2080
Cdd:pfam00975   84 RRLERQGEAVRSLFLSDASAPHTVRYEASRAPDDD-EVVAEFTDEGGTPEELLE-------DEELLSML----------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2081 edpmmnkLKVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNE-YTSGEVYALQVPGSHLSMLEKP----- 2154
Cdd:pfam00975  145 -------LPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWVRdHTPGEFDVHVFDGDHFYLIEHLeavle 217

                   ...
gi 446807313  2155 HIH 2157
Cdd:pfam00975  218 IIE 220
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
21-1911 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1391.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   21 EYWLDKLSGDVELSRFPCDclslnNIQASKESYYCQ-----FPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKD 95
Cdd:PRK12467  241 AYWQEQLGGEHTVLELPTD-----RPRPAVPSYRGArlrvdLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQS 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   96 DVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLL 171
Cdd:PRK12467  316 DIRIGVPNANRNRVETErligFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLF 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  172 -------NTIVM-------------LDDIHCYESTDKInsDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNIL 231
Cdd:PRK12467  396 qvmfnhqNTATGgrdregaqlpgltVEELSWARHTAQF--DLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLL 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  232 DILMKDPNKSAMDLDVMPKTEKNQILFDFNhttrvhktlLCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLN 307
Cdd:PRK12467  474 EAIVAEPRRRLGELPLLDAEERARELVRWN---------APATEYAPdcvhQLIEAQARQHPERPALVFGEQVLSYAELN 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  308 IKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIKGV 387
Cdd:PRK12467  545 RQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-QSHLLAQL 623
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  388 AFQGSV----INLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVL 463
Cdd:PRK12467  624 PVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL--QLAADDSML 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 FSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYfVRANQKISLNKLFVGV 542
Cdd:PRK12467  702 MVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGG 780
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 EPIKTELLAKYDHLfRGNLQILNLYGPTEATVCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEIC 622
Cdd:PRK12467  781 EALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELY 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  623 ISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK12467  859 IGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  702 KTAVVIQrEDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:PRK12467  939 REAVVLA-QPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA 1017
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  775 N-LKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK12467 1018 SaVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAV 1097
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  854 LEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI 933
Cdd:PRK12467 1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGS-AAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ 1176
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  934 LDGELVQKIEP--NVDFNIEYVHVNEKDAD----YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSM 1007
Cdd:PRK12467 1177 EDGRTRQVIHPvgSLTLEEPLLLAADKDEAqlkvYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSM 1256
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1008 GILIKEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGN 1081
Cdd:PRK12467 1257 QVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGA 1336
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1082 VCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLEND 1161
Cdd:PRK12467 1337 RLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQ 1416
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1162 DEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDL 1240
Cdd:PRK12467 1417 ASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDL 1496
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1241 SLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLV 1320
Cdd:PRK12467 1497 TLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLV 1576
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK12467 1577 HQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQshlqaRLPLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ-GEKFDVTKLVQVILEEQVTL 1554
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTT 1812
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 1813 LHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDS 1891
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIE 1971
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTeKDIPIPE-----------VRAYLAT 1782
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKA 2049
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSL 1861
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
                        1930      1940      1950      1960      1970
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1862 KGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKG---ID------SECLIPIQ 1911
Cdd:PRK12467 2130 ISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGtvsIDqgpvtgDLPLLPIQ 2187
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
917-1892 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: 982.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  917 FQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVNEKD--------ADYLIHEFISPFDLSKPPLLRVLLLRIAE 988
Cdd:COG1020    61 AALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLealaeaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  989 ERHILVVDMHHIISDGLSMGILIKEFVELY------KGNELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELP 1062
Cdd:COG1020   141 LLLLLLLALHHIISDGLSDGLLLAELLRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPP 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1063 VLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTN 1142
Cdd:COG1020   221 LLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELE 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1143 HMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIG 1222
Cdd:COG1020   301 GLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELP 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1223 ELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHC 1302
Cdd:COG1020   381 GLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1303 IMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMV 1382
Cdd:COG1020   461 LLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMV 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1383 IGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLA 1462
Cdd:COG1020   541 VALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVT 1541
Cdd:COG1020   621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLApPEARRDPA 698
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1542 KLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATVCCTS 1621
Cdd:COG1020   699 ALAELLARHRVTVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTY 775
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1622 YRYESNkEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKT 1700
Cdd:COG1020   776 YEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRT 854
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1701 GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRA 1778
Cdd:COG1020   855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRL 934
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGG 1858
Cdd:COG1020   935 ALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
                         970       980       990
                  ....*....|....*....|....*....|....
gi 446807313 1859 HSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQL 1892
Cdd:COG1020  1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAA 1048
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
279-772 0e+00

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: 649.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17655    81 YPEERIQYILEDSGADILLT-QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17655   160 RGVVNLVEWANKVIYQGEH--LRVALFASISFDASVTEIFASLLSGNTLYIVRKEtVLDGQALTQYIRQNRITIIDLTPA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEIYDyfVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTqNVPIGSP 597
Cdd:cd17655   238 HLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-SVPIGKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  598 LLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd17655   315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDH 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17655   395 QVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
                         490
                  ....*....|....*
gi 446807313  758 LTQNGKIDRKKLPQP 772
Cdd:cd17655   475 LTPNGKVDRKALPEP 489
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
302-706 1.76e-148

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: 466.74  E-value: 1.76e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   302 TYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQ 380
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   381 NSIIKGVAFQGSVINLMDIPFEEE-----QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFS 453
Cdd:TIGR01733   80 SALASRLAGLVLPVILLDPLELAAlddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLarRYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   454 QDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIY--QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQ 531
Cdd:TIGR01733  160 PD----DRVLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA--ALPPA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   532 KISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHR 611
Cdd:TIGR01733  234 LASLRLVILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   612 LQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
                          410
                   ....*....|....*..
gi 446807313   690 EIEASLLKYETIKTAVV 706
Cdd:TIGR01733  393 EIEAALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
868-1299 3.46e-124

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: 399.79  E-value: 3.46e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   868 KQQEYYLaSTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI-LDGELVQKIEPNV 946
Cdd:pfam00668    1 VQDEYPL-SPAQKRMWFLEKLEPHS-SAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   947 DFNIEY---VHVNEKDADYLIHEFI-----SPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY 1018
Cdd:pfam00668   79 PFELEIidiSDLSESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1019 ----KGNELPKLRVQ-YKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTF 1093
Cdd:pfam00668  159 qqllKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1094 KVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKL 1173
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1174 NTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMD-----MNPISIGELEFTPYPFKQSVSKFDLSLVATEID 1248
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsqEEEFQLSELDLSVSSVIEEEAKYDLSLTASERG 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446807313  1249 NNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEE 1299
Cdd:pfam00668  399 GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
1921-2157 3.85e-28

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 114.41  E-value: 3.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMA 2000
Cdd:pfam00975    4 FCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2001 RKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAfEELEKFNDQLGIEKISFEqmseeqlIESLLKKFtlnenscqqnf 2080
Cdd:pfam00975   84 RRLERQGEAVRSLFLSDASAPHTVRYEASRAPDDD-EVVAEFTDEGGTPEELLE-------DEELLSML----------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2081 edpmmnkLKVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNE-YTSGEVYALQVPGSHLSMLEKP----- 2154
Cdd:pfam00975  145 -------LPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWVRdHTPGEFDVHVFDGDHFYLIEHLeavle 217

                   ...
gi 446807313  2155 HIH 2157
Cdd:pfam00975  218 IIE 220
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
1921-2007 1.35e-08

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 57.55  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQsigYD--DSRF---PNLSVEEMAVRYIEEIKQvKKEGPYTLLGWSFGGIV 1995
Cdd:COG3208    10 FCFPYAGGSASAYRPWAAALPPDIEVLAVQ---LPgrGDRLgepPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALL 85
                          90
                  ....*....|..
gi 446807313 1996 AFEMARKLEELG 2007
Cdd:COG3208    86 AFELARRLERRG 97
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
1928-2026 6.45e-06

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 49.15  E-value: 6.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   1928 GGILNYYDLARELGEDKTVYGLQSIGYDDS-RFPnlSVEEMAVRYI-EEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEE 2005
Cdd:smart00824   10 SGPHEYARLAAALRGRRDVSALPLPGFGPGePLP--ASADALVEAQaEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEA 87
                            90       100
                    ....*....|....*....|.
gi 446807313   2006 LGDKVSFLGLLDVHPIEQGRE 2026
Cdd:smart00824   88 RGIPPAAVVLLDTYPPGDPAP 108
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1834-1894 3.79e-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: 38.39  E-value: 3.79e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313   1834 LIDIWSSILGVNN---IGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSD 1894
Cdd:smart00823   17 VREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
21-1911 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1391.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   21 EYWLDKLSGDVELSRFPCDclslnNIQASKESYYCQ-----FPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKD 95
Cdd:PRK12467  241 AYWQEQLGGEHTVLELPTD-----RPRPAVPSYRGArlrvdLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQS 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   96 DVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLL 171
Cdd:PRK12467  316 DIRIGVPNANRNRVETErligFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLF 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  172 -------NTIVM-------------LDDIHCYESTDKInsDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNIL 231
Cdd:PRK12467  396 qvmfnhqNTATGgrdregaqlpgltVEELSWARHTAQF--DLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLL 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  232 DILMKDPNKSAMDLDVMPKTEKNQILFDFNhttrvhktlLCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLN 307
Cdd:PRK12467  474 EAIVAEPRRRLGELPLLDAEERARELVRWN---------APATEYAPdcvhQLIEAQARQHPERPALVFGEQVLSYAELN 544
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  308 IKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIKGV 387
Cdd:PRK12467  545 RQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-QSHLLAQL 623
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  388 AFQGSV----INLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVL 463
Cdd:PRK12467  624 PVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL--QLAADDSML 701
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 FSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYfVRANQKISLNKLFVGV 542
Cdd:PRK12467  702 MVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGG 780
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 EPIKTELLAKYDHLfRGNLQILNLYGPTEATVCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEIC 622
Cdd:PRK12467  781 EALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELY 858
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  623 ISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK12467  859 IGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  702 KTAVVIQrEDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:PRK12467  939 REAVVLA-QPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA 1017
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  775 N-LKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK12467 1018 SaVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAV 1097
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  854 LEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI 933
Cdd:PRK12467 1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGS-AAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ 1176
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  934 LDGELVQKIEP--NVDFNIEYVHVNEKDAD----YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSM 1007
Cdd:PRK12467 1177 EDGRTRQVIHPvgSLTLEEPLLLAADKDEAqlkvYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSM 1256
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1008 GILIKEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGN 1081
Cdd:PRK12467 1257 QVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGA 1336
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1082 VCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLEND 1161
Cdd:PRK12467 1337 RLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQ 1416
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1162 DEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDL 1240
Cdd:PRK12467 1417 ASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDL 1496
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1241 SLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLV 1320
Cdd:PRK12467 1497 TLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLV 1576
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK12467 1577 HQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQshlqaRLPLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ-GEKFDVTKLVQVILEEQVTL 1554
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTT 1812
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 1813 LHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDS 1891
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIE 1971
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTeKDIPIPE-----------VRAYLAT 1782
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKA 2049
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSL 1861
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
                        1930      1940      1950      1960      1970
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1862 KGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKG---ID------SECLIPIQ 1911
Cdd:PRK12467 2130 ISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGtvsIDqgpvtgDLPLLPIQ 2187
PRK12316 PRK12316
peptide synthase; Provisional
76-1913 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1208.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   76 LYTILLSGVKYLLSRYTDKDDV-----VIGMPVFKQGQEETV--FQNNFLLLRTQiNQEDNFKEIIYKIKETILESNEHC 148
Cdd:PRK12316 1791 LNTLVQAAWLLLLQRYTGQETVafgatVAGRPAELPGIEQQIglFINTLPVIAAP-RPDQSVADWLQEVQALNLALREHE 1869
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  149 HFPFNKLTQLLSLDGESnnlpLLNTIVMLDDIHCYESTDKiNSDMVIRF--MKNEEQ--------------LKVQVDYNS 212
Cdd:PRK12316 1870 HTPLYDIQRWAGQGGEA----LFDSLLVFENYPVAEALKQ-GAPAGLVFgrVSNHEQtnypltlavtlgetLSLQYSYDR 1944
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  213 TLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHT-------TRVHktllcetvtapQLFEEQV 285
Cdd:PRK12316 1945 GHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTpeayprgPGVH-----------QRIAEQA 2013
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 YMLTDSGCSHVLTyQNSIIKGVAFQGSVINLM---DIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLT 442
Cdd:PRK12316 2094 YMLEDSGAALLLT-QRHLLERLPLPAGVARLPldrDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  443 NFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEI 522
Cdd:PRK12316 2173 AHCQAAGERY--ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQL 2250
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  523 YDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTK 602
Cdd:PRK12316 2251 AEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRR 2329
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  603 IYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 681
Cdd:PRK12316 2330 AYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  682 RGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLT 759
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  760 QNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIK 838
Cdd:PRK12316 2489 PNGKLDRKALPKPdVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLR 2568
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  839 SLFKFPVLVDFSKYILEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQ 918
Cdd:PRK12316 2569 ILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPES-AAYHLPSALHLRGVLDQAALEQAFD 2647
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  919 SLIERHEILRTSFQILDGELVQKIEPNV---DFNIEYVHVNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILV 994
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQTRQVILPNMslrIVLEDCAGVADAAIRQRVAEEIQrPFDLARGPLLRVRLLALDGQEHVLV 2727
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  995 VDMHHIISDGLSMGILIKEFVELYKGNE------LPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPT 1068
Cdd:PRK12316 2728 ITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPL 2807
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1069 DFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMF 1148
Cdd:PRK12316 2808 DRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFF 2887
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1149 INTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTP 1228
Cdd:PRK12316 2888 VNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIES 2967
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1229 YPFKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFN 1308
Cdd:PRK12316 2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1309 KKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGV 1388
Cdd:PRK12316 3048 ATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1389 LKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLvhQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTS 1468
Cdd:PRK12316 3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL--SQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTS 3205
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 GSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVI 1547
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWMQQAY--GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAgPEDWRDPALLVELI 3283
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1548 LEEQVTLSYIPPTLLNEIYDYfVRDNQKIVLNKLLVGVEPIKTELLAKYDhlfrGNLQILNGYGPTEATVCCTSYRYEsn 1627
Cdd:PRK12316 3284 NSEGVDVLHAYPSMLQAFLEE-EDAHRCTSLKRIVCGGEALPADLQQQVF----AGLPLYNLYGPTEATITVTHWQCV-- 3356
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 kEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWL 1707
Cdd:PRK12316 3357 -EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYR 3435
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAgekyLCAYVVTEKDIP-IPEV-RAYLATKLP 1785
Cdd:PRK12316 3436 ADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAYVVPEDEAGdLREAlKAHLKASLP 3511
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGL 1864
Cdd:PRK12316 3512 EYMVPAHLLFLERMPLTPNGKLDRKALPRPDaALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISL 3591
                        1850      1860      1870      1880      1890
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1865 KLFENIkRMFNVQLPLSLLFQKATIEQLSDVISRNKG--IDSE------CLIPIQNR 1913
Cdd:PRK12316 3592 QVVSRA-RQAGIRFTPKDLFQHQTIQGLARVARVGGGvaVDQGpvsgetLLLPIQQQ 3647
PRK05691 PRK05691
peptide synthase; Validated
7-1921 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1122.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:PRK05691  853 QRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQA 932
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:PRK05691  933 LLHRYSGQGDIRIGVPNANRPRLETQglvgFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQA 1012
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  163 GESN-----------NLPLLNTI--VMLDDIHCYESTDKINSDMvirfmKNEE----QLKVQVDYNSTLYSEGLVSRIVN 225
Cdd:PRK05691 1013 REQGlfqvmfnhqqrDLSALRRLpgLLAEELPWHSREAKFDLQL-----HSEEdrngRLTLSFDYAAELFDAATIERLAE 1087
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  226 HLYNILDILMKDPNKSAMDLDVMPKTEKNQILfdfnhtTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQ 305
Cdd:PRK05691 1088 HFLALLEQVCEDPQRALGDVQLLDAAERAQLA------QWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAE 1161
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  306 LNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIK 385
Cdd:PRK05691 1162 LHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT-QSHLLE 1240
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  386 GV--AFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDigiTDNVL 463
Cdd:PRK05691 1241 RLpqAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALD---DSDVL 1317
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 FSSS-ISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVT-LAYIPPTLlneiyDYFV---RANQKISLNK 537
Cdd:PRK05691 1318 MQKApISFDVSVWECFWPLITGCRLVLAgPGEHRDPQRIAELVQQYGVTtLHFVPPLL-----QLFIdepLAAACTSLRR 1392
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  538 LFVGVEPIKTELLAK-YDHLfrGNLQILNLYGPTEATVCCTSYQYERDKeitTQNVPIGSPLLNTKIYILDSFHRLQPIG 616
Cdd:PRK05691 1393 LFSGGEALPAELRNRvLQRL--PQVQLHNRYGPTETAINVTHWQCQAED---GERSPIGRPLGNVLCRVLDAELNLLPPG 1467
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  617 VPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASL 695
Cdd:PRK05691 1468 VAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL 1547
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  696 LKYETIKTAVVIQREDESGEKyLCAYVVTEK--DIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PRK05691 1548 LAQPGVAQAAVLVREGAAGAQ-LVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV 1626
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  774 NNLKSsHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK05691 1627 WQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQV 1705
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  854 LEMEKSNYIS----IEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRT 929
Cdd:PRK05691 1706 ARIQAAGERNsqgaIARVDRSQPVPLSYSQQRMWFLWQMEPDS-PAYNVGGMARLSGVLDVDRFEAALQALILRHETLRT 1784
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  930 SFQILDGELVQKIEPNVDfnieyVHVNEKD----------------ADYLIHEfisPFDLSKPPLLRVLLLRIAEERHIL 993
Cdd:PRK05691 1785 TFPSVDGVPVQQVAEDSG-----LRMDWQDfsalpadarqqrlqqlADSEAHQ---PFDLERGPLLRACLVKAAEREHYF 1856
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  994 VVDMHHIISDGLSMGILIKEFVELYK----GNELP--KLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFP 1067
Cdd:PRK05691 1857 VLTLHHIVTEGWAMDIFARELGALYEafldDRESPlePLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELP 1936
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1068 TDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGM 1147
Cdd:PRK05691 1937 ADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGA 2016
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1148 FINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNmdmnpisigeleft 1227
Cdd:PRK05691 2017 FLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQR-------------- 2082
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1228 pYPFKQS----------------VSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRN 1291
Cdd:PRK05691 2083 -WEFQQSrqlagmtveylvndarATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1292 INMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIV 1371
Cdd:PRK05691 2162 LPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRV 2241
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1372 GVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCShVLVHQNSIIKGI-EFQGNVID--LMD--MSFEE 1446
Cdd:PRK05691 2242 GLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIG-LLLSDRALFEALgELPAGVARwcLEDdaAALAA 2320
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1447 EPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIY 1526
Cdd:PRK05691 2321 YSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF--GMRADDCELHFYSINFDAASERLLVPLLC 2398
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 GARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNlQI 1606
Cdd:PRK05691 2399 GARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ-LF 2477
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 LNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK05691 2478 FNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERF 2557
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYV 1765
Cdd:PRK05691 2558 VADPFAaDGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYL 2636
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1766 VTEKDIPIPE--------VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLID 1836
Cdd:PRK05691 2637 VSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDpELNRQAYQAPRSELEQQLAQ 2716
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1837 IWSSILGVNNIGINDNFFELGGHSLKGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSE--------CLI 1908
Cdd:PRK05691 2717 IWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEqgplqgasGLT 2795
                        2010
                  ....*....|...
gi 446807313 1909 PIQNrtnkdsqWF 1921
Cdd:PRK05691 2796 PIQH-------WF 2801
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
917-1892 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: 982.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  917 FQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVNEKD--------ADYLIHEFISPFDLSKPPLLRVLLLRIAE 988
Cdd:COG1020    61 AALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLealaeaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  989 ERHILVVDMHHIISDGLSMGILIKEFVELY------KGNELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELP 1062
Cdd:COG1020   141 LLLLLLLALHHIISDGLSDGLLLAELLRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPP 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1063 VLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTN 1142
Cdd:COG1020   221 LLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELE 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1143 HMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIG 1222
Cdd:COG1020   301 GLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELP 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1223 ELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHC 1302
Cdd:COG1020   381 GLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1303 IMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMV 1382
Cdd:COG1020   461 LLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMV 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1383 IGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLA 1462
Cdd:COG1020   541 VALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVT 1541
Cdd:COG1020   621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLApPEARRDPA 698
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1542 KLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATVCCTS 1621
Cdd:COG1020   699 ALAELLARHRVTVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTY 775
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1622 YRYESNkEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKT 1700
Cdd:COG1020   776 YEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRT 854
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1701 GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRA 1778
Cdd:COG1020   855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRL 934
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGG 1858
Cdd:COG1020   935 ALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
                         970       980       990
                  ....*....|....*....|....*....|....
gi 446807313 1859 HSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQL 1892
Cdd:COG1020  1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAA 1048
PRK12467 PRK12467
peptide synthase; Provisional
876-1890 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 813.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:PRK12467   53 SYAQERQWFLWQL-DPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  956 NE---KDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGN------ 1021
Cdd:PRK12467  132 ANeqgRARESQIEAYINeevarPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrep 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:PRK12467  212 SLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQR 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:PRK12467  292 EGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAH 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNM-----DMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVE 1256
Cdd:PRK12467  372 QDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTatggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFT 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1257 YSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKEnSNSNYLLVHKMFEEQVKRNPNQIA 1336
Cdd:PRK12467  452 YATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPA-TEYAPDCVHQLIEAQARQHPERPA 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1337 VVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGC 1416
Cdd:PRK12467  531 LVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1417 SHVLvHQNSIIKGIEFQGNV----IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY 1492
Cdd:PRK12467  611 RLLL-TQSHLLAQLPVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1493 EDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfVR 1571
Cdd:PRK12467  690 ERL--QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SR 766
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 DNQKIVLNKLLVGVEPIKTELLAKYDHLfRGNLQILNGYGPTEATVCCTSYRYeSNKEITTQNVPIGSPLLNTKIYILDS 1651
Cdd:PRK12467  767 VALPRPQRALVCGGEALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDH 844
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 FHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIE 1730
Cdd:PRK12467  845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIE 924
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1731 LGEIEASLLKYETIKTAVVIDQEDEAGEKyLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:PRK12467  925 LGEIEARLLAQPGVREAVVLAQPGDAGLQ-LVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1804 NGKIDRSKLPKL--NTLGNSnYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLS 1881
Cdd:PRK12467 1004 NGKLDRKALPKPdaSAVQAT-FVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLR 1082

                  ....*....
gi 446807313 1882 LLFQKATIE 1890
Cdd:PRK12467 1083 TLFEHQTLA 1091
PRK12316 PRK12316
peptide synthase; Provisional
876-1913 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 806.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQFEDGtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:PRK12316   53 SYAQQRMWFLWQLEPQ-SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDC 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  956 NEKD--------ADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGN------ 1021
Cdd:PRK12316  132 SGLPeaeqearlRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaep 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:PRK12316  212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARR 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:PRK12316  292 QGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAH 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNM--DMNPIS-IGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYS 1258
Cdd:PRK12316  372 QDLPFERLVEALKVERSLSHSPLFQVMYNHQPLvaDIEALDtVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYA 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1259 IKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVV 1338
Cdd:PRK12316  452 TDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALA 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1339 CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSh 1418
Cdd:PRK12316  532 FGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ- 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVHQNSIIKGIEFQGNV----IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 1494
Cdd:PRK12316  611 LLLSQSHLGRKLPLAAGVqvldLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQA 690
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTI-YQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYdYFVRDN 1573
Cdd:PRK12316  691 YGLGVG--DTVLQKTPFSFDVSVWEFFWPLMSGARLVVaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVA 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 QKIVLNKLLVGVEPIKTELLAKYDHLfRGNLQILNGYGPTEAT--VCCTSYRYESNKEittqnVPIGSPLLNTKIYILDS 1651
Cdd:PRK12316  768 SCTSLRRIVCSGEALPADAQEQVFAK-LPQAGLYNLYGPTEAAidVTHWTCVEEGGDS-----VPIGRPIANLACYILDA 841
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 FHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:PRK12316  842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 921
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDeageKYLCAYVVTEKDI-PIPEV-RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK12316  922 GEIEARLLEHPWVREAAVLAVDG----KQLVGYVVLESEGgDWREAlKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1810 SKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMfNVQLPLSLLFQKAT 1888
Cdd:PRK12316  998 KALPAPEaSVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQT 1076
                        1050      1060      1070
                  ....*....|....*....|....*....|...
gi 446807313 1889 IEQLSDVISRNKGIDSE--------CLIPIQNR 1913
Cdd:PRK12316 1077 IRSLALVAKAGQATAADqgpasgevALAPVQRW 1109
PRK05691 PRK05691
peptide synthase; Validated
412-1898 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 761.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  412 TMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGiTDNVLFSssisfdvtifeiFVPL------VCGA 485
Cdd:PRK05691  162 ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN-PDDVIVS------------WLPLyhdmglIGGL 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  486 RMTIYQGekfdVPklvQVILEEQVTLAYiPPTLLNEIYDY-----------FVRANQKISLNKL-----------FVGVE 543
Cdd:PRK05691  229 LQPIFSG----VP---CVLMSPAYFLER-PLRWLEAISEYggtisggpdfaYRLCSERVSESALerldlsrwrvaYSGSE 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  544 PIKTELLAKYDHLFRG----NLQILNLYGPTEATVCCTSYQ-------YERDKEITTQNVPI---GSPLLNT-------K 602
Cdd:PRK05691  301 PIRQDSLERFAEKFAAcgfdPDSFFASYGLAEATLFVSGGRrgqgipaLELDAEALARNRAEpgtGSVLMSCgrsqpghA 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  603 IYILDSfHRLQPIG--VPGEICISGIGLARGYINRKELTADKFIDHPferGEKLYKTGDIArWLPDGNIEYLGRVDHQVK 680
Cdd:PRK05691  381 VLIVDP-QSLEVLGdnRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLI 455
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  681 IRGYRIELGEIEasllkyetiKTavvIQREDESGEK-YLCAYVVT---EKDIPIP-EVRAYLATKLP------------- 742
Cdd:PRK05691  456 VRGHNLYPQDIE---------KT---VEREVEVVRKgRVAAFAVNhqgEEGIGIAaEISRSVQKILPpqaliksirqava 523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  743 --YYMIPQQIISIQ--NIPLTQNGKIDRK---------------KLPQPINNLKSSHLEPTNSTERKLVEIWKDVLGIQR 803
Cdd:PRK05691  524 eaCQEAPSVVLLLNpgALPKTSSGKLQRSacrlrladgsldsyaLFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQ 603
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  804 IGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKSNYIS---IEPVKQQEYYLASTSQK 880
Cdd:PRK05691  604 VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIARLPRGQALPQSLAQN 683
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  881 RMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVN---- 956
Cdd:PRK05691  684 RLWLLWQL-DPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSdlpe 762
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  957 -EKDADYLI---HEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KGNELPKL 1026
Cdd:PRK05691  763 aEREARAAQireEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYaaacqgQTAELAPL 842
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1027 RVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTP 1106
Cdd:PRK05691  843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1107 YMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPF 1186
Cdd:PRK05691  923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPF 1002
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1187 EELLEGLDLHRDTSrnpLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDLSLVATEiDNN--IHLKVEYSIKLFK 1263
Cdd:PRK05691 1003 EQLVEALPQAREQG---LFQVMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEE-DRNgrLTLSFDYAAELFD 1078
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1264 AETIERLMVHFTNIVEEVTNNPRVRLRNINMLSiEEEHCIMNEFNKKENSNSNYLLVhKMFEEQVKRNPNQIAVVCNEKG 1343
Cdd:PRK05691 1079 AATIERLAEHFLALLEQVCEDPQRALGDVQLLD-AAERAQLAQWGQAPCAPAQAWLP-ELLNEQARQTPERIALVWDGGS 1156
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQ 1423
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG-VELLLTQ 1235
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNV--IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDigi 1501
Cdd:PRK05691 1236 SHLLERLPQAEGVsaIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALD--- 1312
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 TDNVLFSSS-ISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVT-LSYIPPTLlneiyDYFVRD---NQK 1575
Cdd:PRK05691 1313 DSDVLMQKApISFDVSVWECFWPLITGCRLVLAgPGEHRDPQRIAELVQQYGVTtLHFVPPLL-----QLFIDEplaAAC 1387
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1576 IVLNKLLVGVEPIKTELLAK-YDHLfrGNLQILNGYGPTEATVCCTSYRYESNKeitTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRNRvLQRL--PQVQLHNRYGPTETAINVTHWQCQAED---GERSPIGRPLGNVLCRVLDAELN 1462
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 1733
Cdd:PRK05691 1463 LLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1734 IEASLLKYETIKTAVVIDQEDEAGEKyLCAYVVTEK--DIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVLVREGAAGAQ-LVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRA 1621
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1812 LPkLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQ 1891
Cdd:PRK05691 1622 LP-EPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGA 1700

                  ....*..
gi 446807313 1892 LSDVISR 1898
Cdd:PRK05691 1701 FAEQVAR 1707
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
7-1018 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: 760.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:COG1020   195 QREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFAL 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFKQGQEET-------VfqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLL 159
Cdd:COG1020   275 LLARYSGQDDVVVGTPVAGRPRPELeglvgffV---NTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEEL 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  160 SLDGESNNLPLLNTIVMLD------------DIHCYE-STDKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNH 226
Cdd:COG1020   352 QPERDLSRNPLFQVMFVLQnapadelelpglTLEPLElDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGH 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  227 LYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKtllcETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQL 306
Cdd:COG1020   432 LVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYP----ADATLHELFEAQAARTPDAVAVVFGDQSLTYAEL 507
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  307 NIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKG 386
Cdd:COG1020   508 NARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  387 VAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSS 466
Cdd:COG1020   588 PELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFA 665
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  467 SISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQkiSLNKLFVGVEPI 545
Cdd:COG1020   666 SLSFDASVWEIFGALLSGATLVLApPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALP--SLRLVLVGGEAL 743
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  546 KTELLAKYDHLFRGnLQILNLYGPTEATVCCTSYQYERDkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISG 625
Cdd:COG1020   744 PPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGG 821
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  626 IGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 704
Cdd:COG1020   822 AGLARGYLNRPELTAERFVADPFGFpGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREA 901
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  705 VVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLE 782
Cdd:COG1020   902 VVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAA 981
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  783 PTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKSNYI 862
Cdd:COG1020   982 PPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAA 1061
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  863 SIEPVKQQEyYLASTSQKRMFIVDQFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQ-- 940
Cdd:COG1020  1062 PLAAAAAPL-PLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLrl 1140
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  941 ----KIEPNVDFNIEYVHVNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVE 1016
Cdd:COG1020  1141 lvalAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220

                  ..
gi 446807313 1017 LY 1018
Cdd:COG1020  1221 LL 1222
PRK12467 PRK12467
peptide synthase; Provisional
866-2046 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 706.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  866 PVKQQE----YYLASTSQKRMFivDQFEDGTNTTYNMPTILKVEG-DIckDKFENIFQSLIERHEILRTSFqILDGELVQ 940
Cdd:PRK12467 2637 PVAVGDiediYPLSPMQQGMLF--HTLYEGGAGDYINQMRVDVEGlDV--ERFRTAWQAVIDRHEILRSGF-LWDGELEE 2711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  941 KIE--------PNVDFNIEYVHVNEKDADYL-IHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILI 1011
Cdd:PRK12467 2712 PLQvvykqarlPFSRLDWRDRADLEQALDALaAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLL 2791
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1012 KEFVELYKGNELPKLRVQYKDYVMW---QNGpyyknliSEQKNYWLTTLKG-ELPVLNFPTDFQRPTiQSFKGNVCSF-N 1086
Cdd:PRK12467 2792 GEVLQRYFGQPPPAREGRYRDYIAWlqaQDA-------EASEAFWKEQLAAlEEPTRLARALYPAPA-EAVAGHGAHYlH 2863
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1087 LGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHS--DTNHMIGMFINTLVMRNYLENDDEF 1164
Cdd:PRK12467 2864 LDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlrGAEQQLGLFINTLPVIASPRAEQTV 2943
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1165 IEFLSRLKLNTLEAYENQDYPFeellegLDLHRDTSR--NPLFDTMFVFQNMdmnPISIGELEFTPYPFK------QSVS 1236
Cdd:PRK12467 2944 SDWLQQVQAQNLALREFEHTPL------ADIQRWAGQggEALFDSILVFENY---PISEALKQGAPSGLRfgavssREQT 3014
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1237 KFDLSLvATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSN 1316
Cdd:PRK12467 3015 NYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS 3093
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1317 YLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL 1396
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1397 PIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIK-GIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPK 3253
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLS 1555
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDAN--DRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIA 3331
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPPTLLNEIY-DYFVRDNQKivLNKLLVGVEPIKTELLAKYDHLFRgNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 3332 CFPPAYLQQFAeDAGGADCAS--LDIYVFGGEAVPPAAFEQVKRKLK-PRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPY 3408
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIE 3488
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTE---KDIPIpEVRAYLATKLPHYMIP 1790
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpqGDWRE-TLRDHLAASLPDYMVP 3566
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1791 QQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENI 1870
Cdd:PRK12467 3567 AQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRI 3646
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1871 KRMFNVQLPLSLLFQKATIEQLSDViSRNKGIDSECLIPIQNRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTVYGLQ 1950
Cdd:PRK12467 3647 RQSLGLKLSLRDLMSAPTIAELAGY-SPLGDVPVNLLLDLNRLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLT 3725
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1951 SIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQGREIlsl 2030
Cdd:PRK12467 3726 CRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLPLPDEFV--- 3802
                        1210
                  ....*....|....*.
gi 446807313 2031 nIKNAFEELEKFNDQL 2046
Cdd:PRK12467 3803 -PQAEFLELLRQLGEL 3817
PRK12316 PRK12316
peptide synthase; Provisional
848-1905 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 661.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  848 DFSKYILEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTNTTYNMpTILKVEG-DIckDKFENIFQSLIERHEI 926
Cdd:PRK12316 4078 DFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQ-MRVDVQGlDV--ERFRAAWQAALDRHDV 4154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  927 LRTSF--QILDGELVQKIEPNVD--FNIEYVHVNEKDADYLI----HEFISPFDLSKPPLLRVLLLRIAEERHILVVDMH 998
Cdd:PRK12316 4155 LRSGFvwQGELGRPLQVVHKQVSlpFAELDWRGRADLQAALDalaaAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNH 4234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  999 HIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMW---QNGpyyknliSEQKNYWLTtlkgELPVLNFPTDF----Q 1071
Cdd:PRK12316 4235 HILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAWlqrQDA-------AASEAFWRE----QLAALDEPTRLaqaiA 4303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1072 RPTIQSFKGNV-CSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHS--DTNHMIGMF 1148
Cdd:PRK12316 4304 RADLRSANGYGeHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAElpGIEGQIGLF 4383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1149 INTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEgldlHRDTSRNPLFDTMFVFQNMdmnPIS-------- 1220
Cdd:PRK12316 4384 INTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQR----WAGQGGEALFDSLLVFENY---PVSealqqgap 4456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1221 -------IGELEFTPYPFKQSVSkfdlslvateIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNIN 1293
Cdd:PRK12316 4457 gglrfgeVTNHEQTNYPLTLAVG----------LGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQ 4526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1294 MLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGV 1373
Cdd:PRK12316 4527 LLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGI 4606
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1374 MMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDlMDMSFEEEP 1448
Cdd:PRK12316 4607 AMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQshllqRLPIPDGL--ASLALD-RDEDWEGFP 4683
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1449 GEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGA 1528
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY--ELTPDDRVLQFMSFSFDGSHEGLYHPLINGA 4761
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELlakYDHLFRG--NLQI 1606
Cdd:PRK12316 4762 SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQAS---YDLAWRAlkPVYL 4838
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 LNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK12316 4839 FNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERF 4918
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYV 1765
Cdd:PRK12316 4919 VPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYV 4997
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1766 V--TEKDIPIPEV--------RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSL 1834
Cdd:PRK12316 4998 VpqDPALADADEAqaelrdelKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDaSLLQQAYVAPRSELEQQV 5077
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1835 IDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSE 1905
Cdd:PRK12316 5078 AAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
279-772 0e+00

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: 649.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17655    81 YPEERIQYILEDSGADILLT-QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17655   160 RGVVNLVEWANKVIYQGEH--LRVALFASISFDASVTEIFASLLSGNTLYIVRKEtVLDGQALTQYIRQNRITIIDLTPA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEIYDyfVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTqNVPIGSP 597
Cdd:cd17655   238 HLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-SVPIGKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  598 LLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd17655   315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDH 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17655   395 QVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
                         490
                  ....*....|....*
gi 446807313  758 LTQNGKIDRKKLPQP 772
Cdd:cd17655   475 LTPNGKVDRKALPEP 489
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1323-1814 0e+00

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: 635.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:cd17655    82 PEERIQYILEDSGAD-ILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd17655   161 GVVNLVEWANKVIYQGEH--LRVALFASISFDASVTEIFASLLSGNTLYIVRKEtVLDGQALTQYIRQNRITIIDLTPAH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIYDyfVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTqNVPIGSPL 1641
Cdd:cd17655   239 LKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-SVPIGKPL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1642 LNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd17655   316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPL 1801
Cdd:cd17655   396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPL 475
                         490
                  ....*....|...
gi 446807313 1802 TQNGKIDRSKLPK 1814
Cdd:cd17655   476 TPNGKVDRKALPE 488
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
289-769 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: 608.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd05930    81 EDSGAKLVLT-----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd05930   126 QEAY--PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQKiSLNKLFVGVEPIKTELLAKYDHLFRGnLQILNLYGPTEATVCCTSYQYERDkEITTQNVPIGSPLLNTKIYILD 607
Cdd:cd05930   204 LAALP-SLRLVLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRVYVLD 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  608 SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIE 687
Cdd:cd05930   281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  688 LGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05930   361 LGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440

                  ....
gi 446807313  766 RKKL 769
Cdd:cd05930   441 RKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1332-1812 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: 594.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd05930    81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEiydyFV 1570
Cdd:cd05930   126 QEAY--PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpEEVRKDPEALADLLAEEGITVLHLTPSLLRL----LL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIVLNKL---LVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATVCCTSYRyESNKEITTQNVPIGSPLLNTKIY 1647
Cdd:cd05930   200 QELELAALPSLrlvLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYR-VPPDDEEDGRVPIGRPIPNTRVY 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 1727
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1728 RIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNG 1805
Cdd:cd05930   358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437

                  ....*..
gi 446807313 1806 KIDRSKL 1812
Cdd:cd05930   438 KVDRKAL 444
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
279-769 3.55e-174

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: 541.02  E-value: 3.55e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTYQNSiiKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSL--AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLC-AMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKF-DVPKLVQVILEEQVTLAYIPP 516
Cdd:cd12117   159 RGVVRLVKnTNYVTLGPD----DRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  517 TLLNEIYDYFVRANQkiSLNKLFVGVEPIKTE----LLAKYDHLfrgnlQILNLYGPTEATVCCTSYQYERDKEITTQnV 592
Cdd:cd12117   235 ALFNQLADEDPECFA--GLRELLTGGEVVSPPhvrrVLAACPGL-----RLVNGYGPTENTTFTTSHVVTELDEVAGS-I 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  593 PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd12117   307 PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd12117   387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVV 466
                         490
                  ....*....|....*..
gi 446807313  753 IQNIPLTQNGKIDRKKL 769
Cdd:cd12117   467 LDELPLTANGKVDRRAL 483
PRK12467 PRK12467
peptide synthase; Provisional
22-1062 3.18e-172

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 590.59  E-value: 3.18e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   22 YWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGM 101
Cdd:PRK12467 1307 YWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGV 1386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  102 PVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNtiVML 177
Cdd:PRK12467 1387 PIANRNRAETEgligFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQ--VMF 1464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  178 D-------------------------------DIHCYESTDKINSDMVirfmkneeqlkvqvdYNSTLYSEGLVSRIVNH 226
Cdd:PRK12467 1465 NhqrddhqaqaqlpglsveslswesqtaqfdlTLDTYESSEGLQASLT---------------YATDLFEASTIERLAGH 1529
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  227 LYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQL 306
Cdd:PRK12467 1530 WLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARL----VHQLIEDQAAATPEAVALVFGEQELTYGEL 1605
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  307 NIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTY-----QN 381
Cdd:PRK12467 1606 NRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQshlqaRL 1685
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  382 SIIKGVafQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDN 461
Cdd:PRK12467 1686 PLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY--QLSAADV 1761
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  462 VLFSSSISFDVTIFEIFVPLVCGARMTIYQ-GEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV 540
Cdd:PRK12467 1762 VLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVC 1841
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  541 GVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGE 620
Cdd:PRK12467 1842 GGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGE 1920
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  621 ICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 699
Cdd:PRK12467 1921 LYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQG 2000
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  700 TIKTAVVIQREDESGeKYLCAYVVTeKDIPIPE-----------VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:PRK12467 2001 GVREAVVIAQDGANG-KQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKA 2078
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  769 LPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLV 847
Cdd:PRK12467 2079 LPAPdASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRA-RQAGIRFTPKDLFQHQTVQ 2157
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  848 DFSKYILEMEKSNYISIEPVKQQeyyLASTSQKRMFIVDQFEDGTNttYNMPTILKVEGDICKDKFENIFQSLIERHEIL 927
Cdd:PRK12467 2158 SLAAVAQEGDGTVSIDQGPVTGD---LPLLPIQQMFFADDIPERHH--WNQSVLLEPREALDAELLEAALQALLVHHDAL 2232
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  928 RTSFQILDGELVQKIEPNVDFNIEY---VHVNEKDA-DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISD 1003
Cdd:PRK12467 2233 RLGFVQEDGGWSAMHRAPEQERRPLlwqVVVADKEElEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVD 2312
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1004 GLSMGILIKE----FVELYKGN--ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKG---ELP 1062
Cdd:PRK12467 2313 GVSWRILLEDlqtaYRQLQGGQpvKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGastELP 2380
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1324-1812 2.49e-171

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: 533.32  E-value: 2.49e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd12117     3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCShVLVHQNSIIKGIEFQGnVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:cd12117    83 AERLAFMLADAGAK-VLLTDRSLAGRAGGLE-VAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLC-AMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd12117   161 VVRLVKnTNYVTLGPD----DRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIydyfVRDNQKIV--LNKLLVGVEPIKTE----LLAKYDHLfrgnlQILNGYGPTEATVCCTSYRYESNKEITTQnV 1635
Cdd:cd12117   237 FNQL----ADEDPECFagLRELLTGGEVVSPPhvrrVLAACPGL-----RLVNGYGPTENTTFTTSHVVTELDEVAGS-I 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd12117   307 PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIP 1795
Cdd:cd12117   387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVV 466
                         490
                  ....*....|....*..
gi 446807313 1796 IHNIPLTQNGKIDRSKL 1812
Cdd:cd12117   467 LDELPLTANGKVDRRAL 483
PRK12316 PRK12316
peptide synthase; Provisional
902-1896 9.33e-171

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 586.15  E-value: 9.33e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  902 LKVEGdICKDKFENIFQSLIERHEILRTSFQILDG--ELVQKIEPNVDFNIEYVHVNEKD------ADYLIHEFISPFDL 973
Cdd:PRK12316 1585 VDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELPFAELDWRGREdlgqalDALAQAERQKGFDL 1663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  974 SKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMWQNGPyyKNLISEqkNYW 1053
Cdd:PRK12316 1664 TRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQ--DAAASE--AFW 1739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1054 lttlKGELPVLNFPTDFQRP--TIQSFKGNVCSFN-LGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVG 1130
Cdd:PRK12316 1740 ----KEQLAALEEPTRLAQAarTEDGQVGYGDHQQlLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFG 1815
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1131 SPIAGRSH--SDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELlEGLDLHRDTSrnpLFDTM 1208
Cdd:PRK12316 1816 ATVAGRPAelPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI-QRWAGQGGEA---LFDSL 1891
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1209 FVFQNMdmnPIS-------IGELEFTPyPFKQSVSKFDLSLvATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEV 1281
Cdd:PRK12316 1892 LVFENY---PVAealkqgaPAGLVFGR-VSNHEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQM 1966
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1282 TNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLL 1361
Cdd:PRK12316 1967 AEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR 2046
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1362 DQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQNSIIKGIEFQGNVIDLM- 1440
Cdd:PRK12316 2047 ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG-AALLLTQRHLLERLPLPAGVARLPl 2125
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1441 --DMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIF 1518
Cdd:PRK12316 2126 drDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY--ELSPADCELQFMSFSFDGAHE 2203
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1519 EIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDH 1598
Cdd:PRK12316 2204 QWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWE 2283
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1599 LFRGNlQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINR 1678
Cdd:PRK12316 2284 ALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNR 2362
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1679 KELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAG 1757
Cdd:PRK12316 2363 PGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1758 EKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSL 1834
Cdd:PRK12316 2442 GKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDvSQLRQAYVAPQEGLEQRL 2521
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1835 IDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVI 1896
Cdd:PRK12316 2522 AAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASL 2583
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
890-2023 4.55e-170

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 558.12  E-value: 4.55e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  890 DGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNI-EYVHVNEKD-----ADYL 963
Cdd:PRK10252   24 SPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLpEIIDLRTQPdphaaAQAL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  964 IH-EFISPFDL-SKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG---------NELPKLRVQYKD 1032
Cdd:PRK10252  104 MQaDLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgeptpaSPFTPFADVVEE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1033 YVMWQNGPYYKnlisEQKNYWL---------TTLKGELPVLNFPT-DFQRPTIQSfkgnvcsfnlgTDLTFkVNKLATET 1102
Cdd:PRK10252  184 YQRYRASEAWQ----RDAAFWAeqrrqlpppASLSPAPLPGRSASaDILRLKLEF-----------TDGAF-RQLAAQAS 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1103 GTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQ 1182
Cdd:PRK10252  248 GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQ 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1183 DYPFEELLEglDLHRDTSRNPLFDTMFVFQNMDmNPISIGELEFTPY-----PFKqsvskfDLSL-VATEIDNNIHLKVE 1256
Cdd:PRK10252  328 RYDAEQIVR--DSGRAAGDEPLFGPVLNIKVFD-YQLDFPGVQAQTHtlatgPVN------DLELaLFPDEHGGLSIEIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1257 YSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSiEEEHCIMNEFNKKENSNSNYLLVhKMFEEQVKRNPNQIA 1336
Cdd:PRK10252  399 ANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILL-PGEYAQLAQVNATAVEIPETTLS-ALVAQQAAKTPDAPA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1337 VVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGC 1416
Cdd:PRK10252  477 LADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1417 SHVLVHQnsiikgiEFQGNVIDLMDMSFEE------EPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 1490
Cdd:PRK10252  557 SLLITTA-------DQLPRFADVPDLTSLCynaplaPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTLLneiyDYF 1569
Cdd:PRK10252  630 MQNHYP--LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHrDPLAMQQFFAEYGVTTTHFVPSML----AAF 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VR--DNQKIV-----LNKLLVGVEPIKTELLAKYDHLFRGNLQilNGYGPTEATVCCTSYRY--ESNKEITTQNVPIGSP 1640
Cdd:PRK10252  704 VAslTPEGARqscasLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPAfgEELAAVRGSSVPIGYP 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 1720
Cdd:PRK10252  782 VWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDD 861
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1721 QVKIRGYRIELGEIEASLLKYETIKTAV----VIDQEDEAG--EKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQ 1792
Cdd:PRK10252  862 QLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGgdARQLVGYLVSQSGLPLdtSALQAQLRERLPPHMVPVV 941
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKR 1872
Cdd:PRK10252  942 LLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSR 1021
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1873 MFNVQLPLSLLFQKATIEQLSDVI------SRNKGIDSecLIPIqnRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTV 1946
Cdd:PRK10252 1022 QFARQVTPGQVMVASTVAKLATLLdaeedeSRRLGFGT--ILPL--REGDGPTLFCFHPASGFAWQFSVLSRYLDPQWSI 1097
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1947 YGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQ 2023
Cdd:PRK10252 1098 YGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPET 1174
PRK12316 PRK12316
peptide synthase; Provisional
21-1062 7.07e-170

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 583.46  E-value: 7.07e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   21 EYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIG 100
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  101 MPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNtiVM 176
Cdd:PRK12316  321 VPIANRNRAEVEgligFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQ--VM 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  177 LDDIHCYESTDKINS------------------DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDP 238
Cdd:PRK12316  399 YNHQPLVADIEALDTvaglefgqlewksrttqfDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENP 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  239 NKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLL 318
Cdd:PRK12316  479 QARVDELPMLDAEERGQLVEGWNATAAEYPLQRG----VHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALI 554
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  319 DQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMD 398
Cdd:PRK12316  555 ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD 634
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  399 IP---FEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIF 475
Cdd:PRK12316  635 RPaawLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVSVW 712
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  476 EIFVPLVCGARMTI-YQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYdYFVRANQKISLNKLFVGVEPIKTELLAKYD 554
Cdd:PRK12316  713 EFFWPLMSGARLVVaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVASCTSLRRIVCSGEALPADAQEQVF 791
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  555 HLfRGNLQILNLYGPTEATVCCTsyqYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYIN 634
Cdd:PRK12316  792 AK-LPQAGLYNLYGPTEAAIDVT---HWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHG 867
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  635 RKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDesg 714
Cdd:PRK12316  868 RPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG--- 944
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  715 eKYLCAYVVTEKDI-PIPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKL 791
Cdd:PRK12316  945 -KQLVGYVVLESEGgDWREAlKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPeASVAQQGYVAPRNALERTL 1023
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  792 VEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLVDFSKyILEMEKSNYISIEPVKQQe 871
Cdd:PRK12316 1024 AAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRSLAL-VAKAGQATAADQGPASGE- 1100
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  872 yyLASTSQKRMFivdqFEDG--TNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFN 949
Cdd:PRK12316 1101 --VALAPVQRWF----FEQAipQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGE 1174
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  950 IEYVH--VNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKgNELPKLR 1027
Cdd:PRK12316 1175 VLWQRqaASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYA-DLDADLP 1253
                        1050      1060      1070
                  ....*....|....*....|....*....|....*....
gi 446807313 1028 VQYKDYVMW-QNGPYYKNLISEQKNYWLTTLKG---ELP 1062
Cdd:PRK12316 1254 ARTSSYQAWaRRLHEHAGARAEELDYWQAQLEDaphELP 1292
PRK12316 PRK12316
peptide synthase; Provisional
7-1136 2.98e-169

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 581.53  E-value: 2.98e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:PRK12316 2776 QRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQV 2855
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:PRK12316 2856 LLHRYSGQSDIRVGVPIANRNRAETErligFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPE 2935
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  163 GESNNLPLLNTIVMLDDIHCYEST-------------DKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYN 229
Cdd:PRK12316 2936 RSLSHSPLFQVMYNHQSGERAAAQlpglhiesfawdgAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQN 3015
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  230 ILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIK 309
Cdd:PRK12316 3016 LLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERG----VHRLFEEQVERTPDAVALAFGEQRLSYAELNRR 3091
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyqNSIIKGVAF 389
Cdd:PRK12316 3092 ANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS--QSHLRLPLA 3169
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  390 QGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSIS 469
Cdd:PRK12316 3170 QGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY--GLGVGDRVLQFTTFS 3247
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  470 FDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVtlAYIPPTLLNEIYDYF--VRANQKISLNKLFVGVEPIKT 547
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEG--VDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALPA 3325
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  548 ELLAKYDhlfrGNLQILNLYGPTEATVCCTSYQYErdkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIG 627
Cdd:PRK12316 3326 DLQQQVF----AGLPLYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEG 3398
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  628 LARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:PRK12316 3399 LARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL 3478
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  708 QREDESgekyLCAYVVTEKDIP-IPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKSSHLEPT 784
Cdd:PRK12316 3479 AVDGRQ----LVAYVVPEDEAGdLREAlKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPdAALLQQDYVAPV 3554
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  785 NSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLVDFSKyILEMEKSNYISI 864
Cdd:PRK12316 3555 NELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLAR-VARVGGGVAVDQ 3632
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  865 EPVK--------QQEYYLASTSQKRMfivdqfedgtnttYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDG 936
Cdd:PRK12316 3633 GPVSgetlllpiQQQFFEEPVPERHH-------------WNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAG 3699
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  937 ----ELVQKIEPN-VDFNIEYVHVNEKDAdyLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILI 1011
Cdd:PRK12316 3700 gwtaEHLPVELGGaLLWRAELDDAEELER--LGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILL 3777
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1012 KEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKG---ELPVLNFPTDFQRPTIQSFKGnv 1082
Cdd:PRK12316 3778 EDLQQAYQQLlqgeapRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGvssELPCDHPQGALQNRHAASVQT-- 3855
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1083 csfNLGTDLTFKVNKLATETGTTPYM-ILLAIYNILLSRYTGQEDIIVGSPIAGR 1136
Cdd:PRK12316 3856 ---RLDRELTRRLLQQAPAAYRTQVNdLLLTALARVVCRWTGEASALVQLEGHGR 3907
PRK12467 PRK12467
peptide synthase; Provisional
87-1042 8.57e-165

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 567.48  E-value: 8.57e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDV-----VIGMPVFKQGQEETV--FQNNFLLLRTqINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLL 159
Cdd:PRK12467 2894 LLQRFTGQDTVcfgatVAGRPAQLRGAEQQLglFINTLPVIAS-PRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWA 2972
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  160 SLDGESnnlpLLNTIVMLDDIHCYES-TDKINSDMVIRFMKNEEQ--------------LKVQVDYNSTLYSEGLVSRIV 224
Cdd:PRK12467 2973 GQGGEA----LFDSILVFENYPISEAlKQGAPSGLRFGAVSSREQtnypltlavglgdtLELEFSYDRQHFDAAAIERLA 3048
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  225 NHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYK 304
Cdd:PRK12467 3049 ESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERL----VHQLIEAQVARTPEAPALVFGDQQLSYA 3124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  305 QLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSII 384
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLE 3204
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  385 K-GVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGitDNVL 463
Cdd:PRK12467 3205 QlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN--DRVL 3282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 FSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKiSLNKLFVGVE 543
Cdd:PRK12467 3283 LFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCA-SLDIYVFGGE 3361
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  544 PIKTELLAKYDHLFRgNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICI 623
Cdd:PRK12467 3362 AVPPAAFEQVKRKLK-PRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYI 3440
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  624 SGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIK 702
Cdd:PRK12467 3441 GGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  703 TAVVIQREDESGeKYLCAYVVTE---KDIPIpEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSS 779
Cdd:PRK12467 3521 EAVVLARDGAGG-KQLVAYVVPAdpqGDWRE-TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSRE 3598
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  780 HLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYIlemeks 859
Cdd:PRK12467 3599 YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS------ 3672
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  860 nyisiePVKQQEYYLASTSQKRmfivdqfedgtnttynmptilkvegdickdkfENIFQSLIERHEILRTSFqilDGELV 939
Cdd:PRK12467 3673 ------PLGDVPVNLLLDLNRL--------------------------------ETGFPALFCRHEGLGTVF---DYEPL 3711
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  940 QKIepnvdfnieyvhvnekdadylihefispfdlskppllrvlllrIAEERHILVVDMHHIISDGlsmgilikefvelYK 1019
Cdd:PRK12467 3712 AVI-------------------------------------------LEGDRHVLGLTCRHLLDDG-------------WQ 3735
                         970       980
                  ....*....|....*....|....*
gi 446807313 1020 GNELPKLRVQYKDYVMWQN--GPYY 1042
Cdd:PRK12467 3736 DTSLQAMAVQYADYILWQQakGPYG 3760
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
279-770 1.15e-164

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: 514.29  E-value: 1.15e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17644     4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17644    84 YPQERLTYILEDAQISVLLT-----------------------------------QPENLAYVIYTSGSTGKPKGVMIEH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKF-DVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17644   129 QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEIYDYFVRANQKI--SLNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIG 595
Cdd:cd17644   207 YWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  596 SPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER--GEKLYKTGDIARWLPDGNIEYLG 673
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD--IPIPEVRAYLATKLPYYMIPQQII 751
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEesPSTVELRQFLKAKLPDYMIPSAFV 446
                         490
                  ....*....|....*....
gi 446807313  752 SIQNIPLTQNGKIDRKKLP 770
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1320-1813 1.76e-164

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: 513.52  E-value: 1.76e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCShVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd17644    82 PNYPQERLTYILEDAQIS-VLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIP 1558
Cdd:cd17644   127 EHQSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1559 PTLLNEIYDYFVRDNQKIV--LNKLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVP 1636
Cdd:cd17644   205 PAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVP 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 IGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER--GEKLYKTGDIARWLPDGNIEY 1714
Cdd:cd17644   285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEY 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1715 LGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD--IPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:cd17644   365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEesPSTVELRQFLKAKLPDYMIPSA 444
                         490       500
                  ....*....|....*....|.
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17644   445 FVVLEELPLTPNGKIDRRALP 465
PRK12316 PRK12316
peptide synthase; Provisional
76-851 1.02e-162

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 561.50  E-value: 1.02e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   76 LYTILLSGVKYLLSRYTDKDDVVIGMPVF-----KQGQEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCH 149
Cdd:PRK12316 4339 LNTLVQAAWLLLLQRYTGQDTVAFGATVAgrpaeLPGIEGQIgLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEH 4418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  150 FPFNKLTQLLSLDGES--------NNLPLLNTI-------VMLDDIHCYESTdkiNSDMVIRfMKNEEQLKVQVDYNSTL 214
Cdd:PRK12316 4419 TPLYEIQRWAGQGGEAlfdsllvfENYPVSEALqqgapggLRFGEVTNHEQT---NYPLTLA-VGLGETLSLQFSYDRGH 4494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  215 YSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAI 294
Cdd:PRK12316 4495 FDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRC----VHQLVAERARMTPDAVAV 4570
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  295 VCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCS 374
Cdd:PRK12316 4571 VFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAA 4650
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  375 HVLTyQNSIIKGVAFQGSVINLMDIPFEEEQ---VEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 451
Cdd:PRK12316 4651 LLLT-QSHLLQRLPIPDGLASLALDRDEDWEgfpAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER 4729
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  452 FsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ 531
Cdd:PRK12316 4730 Y--ELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGE 4807
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  532 KISLNKLFVGVEPIKTELlakYDHLFRG--NLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSF 609
Cdd:PRK12316 4808 PPSLRVYCFGGEAVAQAS---YDLAWRAlkPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ 4884
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  610 HRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 688
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  689 GEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV--TEKDIPIPEV--------RAYLATKLPYYMIPQQIISIQNIPL 758
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVpqDPALADADEAqaelrdelKAALRERLPEYMVPAHLVFLARMPL 5043
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  759 TQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSI 837
Cdd:PRK12316 5044 TPNGKLDRKALPQPdASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPL 5123
                         810
                  ....*....|....
gi 446807313  838 KSLFKFPVLVDFSK 851
Cdd:PRK12316 5124 RELFQTPTLAAFVE 5137
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
278-769 4.29e-159

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: 499.88  E-value: 4.29e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  358 ELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAfQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  438 HRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQ--GEKfDVPKLVQVILEEQVTLAYIP 515
Cdd:cd17646   160 HAGIVNRLLWMQDEY--PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARpgGHR-DPAYLAALIREHGVTTCHFV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  516 PTLLneiyDYFV---RANQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQYERDKEITTqnV 592
Cdd:cd17646   237 PSML----RVFLaepAAGSCASLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHWPVRGPAETPS--V 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  593 PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd17646   309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV---TEKDIPIPEVRAYLATKLPYYMIPQQ 749
Cdd:cd17646   389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAA 468
                         490       500
                  ....*....|....*....|
gi 446807313  750 IISIQNIPLTQNGKIDRKKL 769
Cdd:cd17646   469 FVVLDALPLTANGKLDRAAL 488
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
875-1285 2.63e-158

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: 494.95  E-value: 2.63e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  875 ASTSQKRMFIVDQFEDGtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:cd19531     4 LSFAQQRLWFLDQLEPG-SAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  955 V-------NEKDADYLIHEFIS-PFDLS----------KppllrvlllrIAEERHILVVDMHHIISDGLSMGILIKEFVE 1016
Cdd:cd19531    83 LsglpeaeREAEAQRLAREEARrPFDLArgpllratllR----------LGEDEHVLLLTMHHIVSDGWSMGVLLRELAA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1017 LYKG------NELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTD 1090
Cdd:cd19531   153 LYAAflagrpSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1091 LTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSR 1170
Cdd:cd19531   233 LTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLAR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1171 LKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNN 1250
Cdd:cd19531   313 VRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGG 392
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 446807313 1251 IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19531   393 LRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
289-770 2.27e-156

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: 491.99  E-value: 2.27e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17656    82 LDSGVRVVLT-QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEIydyfv 527
Cdd:cd17656   161 REKTNINFS--DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtKRDVEQLFDLVKRHNIEVVFLPVAFLKFI----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 rANQKISLNKLFVGVEPIKT---ELLAK---YDHLFRGNLQILNLYGPTEATVCCTsyqYERDKEITTQNVP-IGSPLLN 600
Cdd:cd17656   234 -FSEREFINRFPTCVKHIITageQLVITnefKEMLHEHNVHLHNHYGPSETHVVTT---YTINPEAEIPELPpIGKPISN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  601 TKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 680
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  681 IRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd17656   390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
                         490
                  ....*....|
gi 446807313  761 NGKIDRKKLP 770
Cdd:cd17656   470 NGKVDRKALP 479
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1332-1813 1.12e-153

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: 484.29  E-value: 1.12e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVhQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17656    82 LDSGVRVVLT-QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY-- 1568
Cdd:cd17656   161 REKTNINFS--DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEre 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 FVRDNQKIVLNKLLVGVEPIKTELLAKYdhLFRGNLQILNGYGPTEATVCcTSYRYESNKEITtQNVPIGSPLLNTKIYI 1648
Cdd:cd17656   239 FINRFPTCVKHIITAGEQLVITNEFKEM--LHEHNVHLHNHYGPSETHVV-TTYTINPEAEIP-ELPPIGKPISNTWIYI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYR 1728
Cdd:cd17656   315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1729 IELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd17656   395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474

                  ....*
gi 446807313 1809 RSKLP 1813
Cdd:cd17656   475 RKALP 479
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1321-1812 1.58e-153

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: 484.09  E-value: 1.58e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEfQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ--GEKfDVTKLVQVILEEQVTLSYIP 1558
Cdd:cd17646   160 HAGIVNRLLWMQDEY--PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARpgGHR-DPAYLAALIREHGVTTCHFV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1559 PTLLneiyDYFV---RDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQilNGYGPTEATVCCTSYRYESNKEITTqnV 1635
Cdd:cd17646   237 PSML----RVFLaepAAGSCASLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHWPVRGPAETPS--V 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd17646   309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV---TEKDIPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:cd17646   389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAA 468
                         490       500
                  ....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd17646   469 FVVLDALPLTANGKLDRAAL 488
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
279-770 1.19e-151

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: 477.05  E-value: 1.19e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17645     2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17645    82 YPGERIAYMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFlCAMYEDFSQdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17645   127 HNLVNL-CEWHRPYFG-VTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPTG 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEiydYFVRANQkiSLNKLFVGVEPIKTELLAKYdhlfrgnlQILNLYGPTEATVCCTSYqyERDKEitTQNVPIGSP 597
Cdd:cd17645   205 AAEQ---FMQLDNQ--SLRVLLTGGDKLKKIERKGY--------KLVNNYGPTENTVVATSF--EIDKP--YANIPIGKP 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  598 LLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd17645   268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17645   348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALP 427
                         490
                  ....*....|...
gi 446807313  758 LTQNGKIDRKKLP 770
Cdd:cd17645   428 LTANGKVDRKALP 440
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1332-1812 1.25e-151

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: 477.34  E-value: 1.25e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLvhqnsiikgiefqgnvidlmdmsfeeepgedmhmmIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17650    81 EDSGAKLLL-----------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSQDiGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd17650   126 RREYELD-SFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVY 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIVLNKLL-VGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYIL 1649
Cdd:cd17650   205 RNGLDLSAMRLLiVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 DSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd17650   285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17650   365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444

                  ...
gi 446807313 1810 SKL 1812
Cdd:cd17650   445 RAL 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1321-1813 1.73e-150

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: 473.97  E-value: 1.73e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIE 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFlCAMYEDFSQdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17645   126 HHNLVNL-CEWHRPYFG-VTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPT 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEiydYFVRDNQKivLNKLLVGVEPIKTELLAKYdhlfrgnlQILNGYGPTEATVCCTSyrYESNKEitTQNVPIGS 1639
Cdd:cd17645   204 GAAEQ---FMQLDNQS--LRVLLTGGDKLKKIERKGY--------KLVNNYGPTENTVVATS--FEIDKP--YANIPIGK 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd17645   267 PIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLD 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:cd17645   347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
                         490
                  ....*....|....
gi 446807313 1800 PLTQNGKIDRSKLP 1813
Cdd:cd17645   427 PLTANGKVDRKALP 440
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
289-769 3.92e-150

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: 473.11  E-value: 3.92e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17650    81 EDSGAKLLLT-----------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFSQDiGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd17650   126 RREYELD-SFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVY 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQKIS-LNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYIL 606
Cdd:cd17650   205 RNGLDLSaMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  607 DSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd17650   285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17650   365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444

                  ...
gi 446807313  767 KKL 769
Cdd:cd17650   445 RAL 447
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
279-769 5.74e-150

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: 472.57  E-value: 5.74e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd12115     3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd12115    83 YPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEH 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLCAMYEDFSQDIgiTDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQgekfDVPKLVQVILEEQVTLAYIPPTL 518
Cdd:cd12115   128 RNAAAFLQWAAAAFSAEE--LAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSA 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  519 LNEI--YDYFVRANQKISLnklfVGvEPIKTELLAKydhlFRGNLQ---ILNLYGPTEATVCCTSYQYERDKEittQNVP 593
Cdd:cd12115   202 AAELlrHDALPASVRVVNL----AG-EPLPRDLVQR----LYARLQverVVNLYGPSEDTTYSTVAPVPPGAS---GEVS 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  594 IGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLG 673
Cdd:cd12115   270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQII 751
Cdd:cd12115   350 RADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLveDLRRHLGTRLPAYMVPSRFV 429
                         490
                  ....*....|....*...
gi 446807313  752 SIQNIPLTQNGKIDRKKL 769
Cdd:cd12115   430 RLDALPLTPNGKIDRSAL 447
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
289-770 1.27e-149

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: 470.97  E-value: 1.27e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17652    81 ADARPALLLT-----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDV-PKLVQVILEEQVTLAYIPPTLLNEiydyfV 527
Cdd:cd17652   126 IAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADLLREHRITHVTLPPAALAA-----L 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQKISLNKLFVGVEPIKTELLAKYDhlfRGNlQILNLYGPTEATVCCTSYQYERDkeitTQNVPIGSPLLNTKIYILD 607
Cdd:cd17652   199 PPDDLPDLRTLVVAGEACPAELVDRWA---PGR-RMINAYGPTETTVCATMAGPLPG----GGVPPIGRPVPGTRVYVLD 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  608 SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd17652   271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTE-KDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17652   351 ELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApGAAPTAaELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430

                  ....*.
gi 446807313  765 DRKKLP 770
Cdd:cd17652   431 DRRALP 436
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
302-706 1.76e-148

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: 466.74  E-value: 1.76e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   302 TYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQ 380
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   381 NSIIKGVAFQGSVINLMDIPFEEE-----QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFS 453
Cdd:TIGR01733   80 SALASRLAGLVLPVILLDPLELAAlddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLarRYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   454 QDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIY--QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQ 531
Cdd:TIGR01733  160 PD----DRVLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA--ALPPA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   532 KISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHR 611
Cdd:TIGR01733  234 LASLRLVILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   612 LQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
                          410
                   ....*....|....*..
gi 446807313   690 EIEASLLKYETIKTAVV 706
Cdd:TIGR01733  393 EIEAALLRHPGVREAVV 409
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1320-1812 1.06e-147

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: 466.41  E-value: 1.06e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAI 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTNFLCAMYEDFSQDIgiTDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQgekfDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd12115   126 EHRNAAAFLQWAAAAFSAEE--LAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEI--YDYFVRDNQkiVLNklLVGvEPIKTELLAKydhlFRGNLQ---ILNGYGPTEATVcctsyrYESNKEITT-- 1632
Cdd:cd12115   200 SAAAELlrHDALPASVR--VVN--LAG-EPLPRDLVQR----LYARLQverVVNLYGPSEDTT------YSTVAPVPPga 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 -QNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGN 1711
Cdd:cd12115   265 sGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGL 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMI 1789
Cdd:cd12115   345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLveDLRRHLGTRLPAYMV 424
                         490       500
                  ....*....|....*....|...
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd12115   425 PSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
281-770 1.12e-147

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: 467.98  E-value: 1.12e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDSGCSHVLTYQnsiikGVAFQGSVINLMDIPFEEEQVE-----DLQITMEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHP-----ALAGELAVELVAVTLLDQPGAAagadaEPDPALDADDLAYVIYTSGSTGRPKGVV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  436 IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYI 514
Cdd:cd17651   156 MPHRSLANLVAWQARASSLGPG--ARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  515 PPTLLNEIYDYFVRAN-QKISLNKLFVGVEP-IKTELLAkydHLFRG--NLQILNLYGPTEATVCcTSYQYERDKEITTQ 590
Cdd:cd17651   234 PTVALRALAEHGRPLGvRLAALRYLLTGGEQlVLTEDLR---EFCAGlpGLRLHNHYGPTETHVV-TALSLPGDPAAWPA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  591 NVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:cd17651   310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQ 748
Cdd:cd17651   390 FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPS 469
                         490       500
                  ....*....|....*....|..
gi 446807313  749 QIISIQNIPLTQNGKIDRKKLP 770
Cdd:cd17651   470 AFVLLDALPLTPNGKLDRRALP 491
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1332-1813 5.56e-145

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: 458.26  E-value: 5.56e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17652    81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARM------TIYQGEKfdvtkLVQVILEEQVTLSYIPPTLLNEI 1565
Cdd:cd17652   126 IAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLvlapaeELLPGEP-----LADLLREHRITHVTLPPAALAAL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1566 YDYFVRDnqkivLNKLLVGVEPIKTELLAKYDhlfRGNlQILNGYGPTEATVCCTSYRYESnkeiTTQNVPIGSPLLNTK 1645
Cdd:cd17652   199 PPDDLPD-----LRTLVVAGEACPAELVDRWA---PGR-RMINAYGPTETTVCATMAGPLP----GGGVPPIGRPVPGTR 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 1724
Cdd:cd17652   266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1725 RGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE-KDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLT 1802
Cdd:cd17652   346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApGAAPTAaELRAHLAERLPGYMVPAAFVVLDALPLT 425
                         490
                  ....*....|.
gi 446807313 1803 QNGKIDRSKLP 1813
Cdd:cd17652   426 PNGKLDRRALP 436
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
56-855 1.91e-142

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 479.93  E-value: 1.91e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   56 QFPSDIAKRAVAisNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGMPVFKQ----GQEETVFQNNFLLLRTQINQEDNFK 131
Cdd:PRK10252  233 EFTDGAFRQLAA--QASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgsaALTATGPVLNVLPLRVHIAAQETLP 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  132 EIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNL--PLLNtIVMLD---DIHCYESTDKINS-----DMVIRFMKNE 201
Cdd:PRK10252  311 ELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLfgPVLN-IKVFDyqlDFPGVQAQTHTLAtgpvnDLELALFPDE 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  202 E-QLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQiLFDFNHTTRVhktlLCETvTAPQL 280
Cdd:PRK10252  390 HgGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVE----IPET-TLSAL 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK10252  464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITmEPQNLAYVIYTSGSTGQPKGVMIEHRS 440
Cdd:PRK10252  544 DDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTA 622
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  441 LTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPTLL 519
Cdd:PRK10252  623 IVNRLLWMQNHYP--LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPlAMQQFFAEYGVTTTHFVPSML 700
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  520 neiyDYFVRA-------NQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQYERD--KEITTQ 590
Cdd:PRK10252  701 ----AAFVASltpegarQSCASLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPAFGEelAAVRGS 774
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  591 NVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:PRK10252  775 SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVE 854
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV-----IQREDESG-EKYLCAYVVTEKDIPI--PEVRAYLATKLP 742
Cdd:PRK10252  855 YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacviNQAAATGGdARQLVGYLVSQSGLPLdtSALQAQLRERLP 934
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  743 YYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAAR 822
Cdd:PRK10252  935 PHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMK 1014
                         810       820       830
                  ....*....|....*....|....*....|...
gi 446807313  823 LISIVNKEFNVQLSIKSLFKFPVLVDFSKYILE 855
Cdd:PRK10252 1015 LAAQLSRQFARQVTPGQVMVASTVAKLATLLDA 1047
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1324-1813 3.51e-142

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: 452.57  E-value: 3.51e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLVHQNSiikGIEFQGNVIDLM--DMSFEEEPGEDMHMM-IEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPAL---AGELAVELVAVTllDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVMP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17651   158 HRSLANLVAWQARASSLGPG--ARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFLPT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDN-QKIVLNKLLVGVEP-IKTELLAkydHLFRG--NLQILNGYGPTEATVCcTSYRYESNKEITTQNV 1635
Cdd:cd17651   236 VALRALAEHGRPLGvRLAALRYLLTGGEQlVLTEDLR---EFCAGlpGLRLHNHYGPTETHVV-TALSLPGDPAAWPAPP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd17651   312 PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQL 1793
Cdd:cd17651   392 GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPSAF 471
                         490       500
                  ....*....|....*....|
gi 446807313 1794 IPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17651   472 VLLDALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1345-1749 1.63e-141

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: 447.10  E-value: 1.63e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1345 TYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1424 nSIIKGIEFQGNVIDLMDMSFEEE-----PGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFS 1496
Cdd:TIGR01733   81 -ALASRLAGLVLPVILLDPLELAAlddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLarRYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1497 QDigitDNVLFSSSISFDVTIFEIFVPLIYGARMTIY--QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQ 1574
Cdd:TIGR01733  160 PD----DRVLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA--ALPPA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1575 KIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:TIGR01733  234 LASLRLVILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
                          410
                   ....*....|....*..
gi 446807313  1733 EIEASLLKYETIKTAVV 1749
Cdd:TIGR01733  393 EIEAALLRHPGVREAVV 409
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
289-770 3.87e-140

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: 445.27  E-value: 3.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTYqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17649    81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd17649   127 AERY--GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADeLAEMVRELGVTVLDLPPAYLQQLAEEAD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQK--ISLNKLFVGVEPIKTELLAKYdhlFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYI 605
Cdd:cd17649   205 RTGDGrpPSLRLYIFGGEALSPELLRRW---LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  606 LDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 684
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  685 RIELGEIEASLLKYETIKTAVVIQReDESGEKYLCAYVVTEKDIPIPEVRAYLAT----KLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRTalraSLPDYMVPAHLVFLARLPLTP 440
                         490
                  ....*....|
gi 446807313  761 NGKIDRKKLP 770
Cdd:cd17649   441 NGKLDRKALP 450
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
289-769 1.90e-139

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: 444.04  E-value: 1.90e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyQNSIIKGVAFQGSVInLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd12116    81 EDAEPALVLT-DDALPDRLPAGLPVL-LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd12116   159 RERLG--LGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMLLDAGW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQKIslnKLFVGVEPIKTELLAkydHLFRGNLQILNLYGPTEATV--CCTSYQYERDKeittqnVPIGSPLLNTKIYI 605
Cdd:cd12116   237 QGRAGL---TALCGGEALPPDLAA---RLLSRVGSLWNLYGPTETTIwsTAARVTAAAGP------IPIGRPLANTQVYV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  606 LDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 684
Cdd:cd12116   305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  685 RIELGEIEASLLKYETIKTAVVIQREDEsGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNG 762
Cdd:cd12116   385 RIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANG 463

                  ....*..
gi 446807313  763 KIDRKKL 769
Cdd:cd12116   464 KLDRKAL 470
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1332-1813 2.47e-137

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: 437.18  E-value: 2.47e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17649    81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd17649   127 AERY--GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEAD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQK--IVLNKLLVGVEPIKTELLAKYdhlFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYI 1648
Cdd:cd17649   205 RTGDGrpPSLRLYIFGGEALSPELLRRW---LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 1727
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1728 RIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTEKDIPIPEVRAYLAT----KLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRTalraSLPDYMVPAHLVFLARLPLTP 440
                         490
                  ....*....|
gi 446807313 1804 NGKIDRSKLP 1813
Cdd:cd17649   441 NGKLDRKALP 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
289-769 3.74e-137

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: 436.74  E-value: 3.74e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA- 447
Cdd:cd17643    81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAt 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  448 --MYEDFSQDIGitdnVLFSSSiSFDVTIFEIFVPLVCGARMTIyqgekfdVPKLV--------QVILEEQVTLAYIPPT 517
Cdd:cd17643   126 qrWFGFNEDDVW----TLFHSY-AFDFSVWEIWGALLHGGRLVV-------VPYEVarspedfaRLLRDEGVTVLNQTPS 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEIYDYFVRAN-QKISLNKLFVGVEPIKTELLAK-YDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIG 595
Cdd:cd17643   194 AFYQLVEAADRDGrDPLALRYVIFGGEALEAAMLRPwAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIG 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  596 SPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGR 674
Cdd:cd17643   274 RPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGR 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  675 VDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd17643   354 ADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVP 433
                         490
                  ....*....|....*..
gi 446807313  753 IQNIPLTQNGKIDRKKL 769
Cdd:cd17643   434 LDALPLTVNGKLDRAAL 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1332-1812 2.42e-136

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: 434.43  E-value: 2.42e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA- 1490
Cdd:cd17643    81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAt 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 --MYEDFSQDIGitdnVLFSSSiSFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVT-LSYIPPTLLNEIY 1566
Cdd:cd17643   126 qrWFGFNEDDVW----TLFHSY-AFDFSVWEIWGALLHGGRLVVVpYEVARSPEDFARLLRDEGVTvLNQTPSAFYQLVE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLNKLLVGVEPIKTELLAK-YDHLFRGNLQILNGYGPTEATVCcTSYRYESNKEITTQNV-PIGSPLLNT 1644
Cdd:cd17643   201 AADRDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLDRPQLVNMYGITETTVH-VTFRPLDAADLPAAAAsPIGRPLPGL 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1645 KIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:cd17643   280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVK 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1724 IRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPL 1801
Cdd:cd17643   360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVPLDALPL 439
                         490
                  ....*....|.
gi 446807313 1802 TQNGKIDRSKL 1812
Cdd:cd17643   440 TVNGKLDRAAL 450
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1332-1812 1.92e-135

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: 432.49  E-value: 1.92e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCShVLVHQNSIIKGIEFQGNVIDLmDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd12116    81 EDAEPA-LVLTDDALPDRLPAGLPVLLL-ALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd12116   159 RERLG--LGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMLLDAGW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIvlnKLLVGVEPIKTELLAkydHLFRGNLQILNGYGPTEATVCCTSYRYESNKEittqNVPIGSPLLNTKIYILD 1650
Cdd:cd12116   237 QGRAGL---TALCGGEALPPDLAA---RLLSRVGSLWNLYGPTETTIWSTAARVTAAAG----PIPIGRPLANTQVYVLD 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1651 SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd12116   307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEaGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd12116   387 ELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465

                  ....*
gi 446807313 1808 DRSKL 1812
Cdd:cd12116   466 DRKAL 470
PRK05691 PRK05691
peptide synthase; Validated
879-1896 8.17e-132

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 464.26  E-value: 8.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  879 QKRMFIVDQFEDGTNTTYnMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGE-LVQKIEPNVDFNIEYVHVNE 957
Cdd:PRK05691 3264 QEGLLLHTLLEPGTGLYY-MQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGEtMLQVIHKPGRTPIDYLDWRG 3342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  958 KDAD--------YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNElPK 1025
Cdd:PRK05691 3343 LPEDgqeqrlqaLHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYtalgEGRE-AQ 3421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1026 LRV--QYKDYVMWQNgpyyKNLISEQKNYWLTTLKG-ELPVLnFPTDfqRPTIQSFKGNVCSFNLGTDLT-------FKV 1095
Cdd:PRK05691 3422 LPVppRYRDYIGWLQ----RQDLAQARQWWQDNLRGfERPTP-IPSD--RPFLREHAGDSGGMVVGDCYTrldaadgARL 3494
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1096 NKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDE---FIEFLSR 1170
Cdd:PRK05691 3495 RELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPAAGQrcsVRQWLQG 3574
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1171 LKLNTLEAYENQDYPFEELLEGLDLHRDtsrNPLFDTMFVFQNMdmnPISIGELEFTPYPFKQSVS-----KFDLSLVAT 1245
Cdd:PRK05691 3575 LLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFENA---PVEVSVLDRAQSLNASSDSgrthtNFPLTAVCY 3648
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1246 EIDNnIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENsnsNYLLVH---K 1322
Cdd:PRK05691 3649 PGDD-LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSER---DYPLEQsyvR 3724
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGL 3804
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSG-----CSHVLVHQNSIIKGiEFQGNVIDLM----DMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQ 1473
Cdd:PRK05691 3805 PAQRLQRIIELSRtpvlvCSAACREQARALLD-ELGCANRPRLlvweEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGL 3883
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRS-LTNFLCAM-YEDFSQdigiTDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEE 1550
Cdd:PRK05691 3884 PKGVMVEQRGmLNNQLSKVpYLALSE----ADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAiAHDPQGLLAHVQAQ 3959
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLlneIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYdhLFR-GNLQILNGYGPTEATVCCTSYRYEsnk 1628
Cdd:PRK05691 3960 GITVLESVPSL---IQGMLAEDRQALdGLRWMLPTGEAMPPELARQW--LQRyPQIGLVNAYGPAECSDDVAFFRVD--- 4031
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1629 EITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIAR 1705
Cdd:PRK05691 4032 LASTRGsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLAR 4111
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYVV-----TEKDIPIPEVRAYL 1780
Cdd:PRK05691 4112 RRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVphqtvLAQGALLERIKQRL 4190
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1781 ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNT--LGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGG 1858
Cdd:PRK05691 4191 RAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgqLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGG 4270
                        1050      1060      1070
                  ....*....|....*....|....*....|....*...
gi 446807313 1859 HSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVI 1896
Cdd:PRK05691 4271 HSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
279-769 5.46e-131

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: 420.41  E-value: 5.46e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd05918     3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd05918    83 HPLQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLtnflCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLVCGA---------RMTiyqgekfdvpKLVQVILEE 507
Cdd:cd05918   129 RAL----STSALAHGRALGLTSEsrVLQFASYTFDVSILEIFTTLAAGGclcipseedRLN----------DLAGFINRL 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  508 QVTLAYIPPTLLNeiydyFVRANQKISLNKLFVGVEPIKTELLAKYDHlfrgNLQILNLYGPTEATVCCTSYQyeRDKEI 587
Cdd:cd05918   195 RVTWAFLTPSVAR-----LLDPEDVPSLRTLVLGGEALTQSDVDTWAD----RVRLINAYGPAECTIAATVSP--VVPST 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  588 TTQNvpIGSPLlNTKIYILD--SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-------FERGEKLYKTG 658
Cdd:cd05918   264 DPRN--IGRPL-GATCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  659 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK-YETIKTAVV--IQREDESGEKYLCAYVVTEKDIP------ 729
Cdd:cd05918   341 DLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSgsgdgd 420
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446807313  730 -------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05918   421 slflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1320-1812 9.07e-130

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: 416.94  E-value: 9.07e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS----------------------------------PSDAAYVIFTSGSTGKPKGVVI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLtnflCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLIYGArmTIYQGEKFD-VTKLVQVILEEQVTLSY 1556
Cdd:cd05918   127 EHRAL----STSALAHGRALGLTSEsrVLQFASYTFDVSILEIFTTLAAGG--CLCIPSEEDrLNDLAGFINRLRVTWAF 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIydyfvrDNQKIV-LNKLLVGVEPIKTELLAKYDHlfrgNLQILNGYGPTEATVCCTSyryesNKEITTQNV 1635
Cdd:cd05918   201 LTPSVARLL------DPEDVPsLRTLVLGGEALTQSDVDTWAD----RVRLINAYGPAECTIAATV-----SPVVPSTDP 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 P-IGSPLlNTKIYILD--SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-------FERGEKLYKTGDIAR 1705
Cdd:cd05918   266 RnIGRPL-GATCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVR 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK-YETIKTAVV--IDQEDEAGEKYLCAYVVTEKDIP---------- 1772
Cdd:cd05918   345 YNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslfl 424
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 446807313 1773 ---------IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05918   425 epsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
PRK05691 PRK05691
peptide synthase; Validated
7-1019 5.44e-127

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 448.85  E-value: 5.44e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDcLSLNNIQASK-ESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVK 85
Cdd:PRK05691 1906 QRQWLESGERQRQLDYWKAQLGNEHPLLELPAD-RPRPPVQSHRgELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLA 1984
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   86 YLLSRYTDKDDVVIGMPVFKQGQEET-----VFQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:PRK05691 1985 ALLYRYSGQRDLRIGAPVANRIRPESegligAFLNT-QVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQ 2063
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  161 LDGESNNLPLLNtiVMlddihC------YESTDKInSDMVIRFMKNEEQ-----LKVQVD-----------YNSTLYSEG 218
Cdd:PRK05691 2064 PPRSAAYNPLFQ--VM-----CnvqrweFQQSRQL-AGMTVEYLVNDARatkfdLNLEVTdldgrlgccltYSRDLFDEP 2135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  219 LVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTT---RVHKTLlcetvtaPQLFEEQVKQNPNQIAIV 295
Cdd:PRK05691 2136 RIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAgeaRLDQTL-------HGLFAAQAARTPQAPALT 2208
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  296 CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSH 375
Cdd:PRK05691 2209 FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  376 VLTYQ------NSIIKGVA---FQGSVINLMDIPFEEeqvedLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLC 446
Cdd:PRK05691 2289 LLSDRalfealGELPAGVArwcLEDDAAALAAYSDAP-----LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQ 2363
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  447 AMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYF 526
Cdd:PRK05691 2364 AVIERF--GMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWL 2441
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  527 VRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATV----CCTSYQYERDkeitTQNVPIGSPLLNTK 602
Cdd:PRK05691 2442 AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ-LFFNAYGPTETVVmplaCLAPEQLEEG----AASVPIGRVVGARV 2516
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  603 IYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 681
Cdd:PRK05691 2517 AYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAaDGGRLYRTGDLVRLRADGLVEYVGRIDHQVKI 2596
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  682 RGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVVTEKDIPIPE--------VRAYLATKLPYYMIPQQIISI 753
Cdd:PRK05691 2597 RGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYLVSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILL 2675
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  754 QNIPLTQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFN 832
Cdd:PRK05691 2676 DSLPLTANGKLDRRALPAPdPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRA-RQLG 2754
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  833 VQLSIKSLFKFPVLVDFSKYILEMEKSNY--------ISIEPVkqQEYYLASTSQKRMFivdqfedgtnttYNMPTILKV 904
Cdd:PRK05691 2755 IHFSPRDLFQHQTVQTLAAVATHSEAAQAeqgplqgaSGLTPI--QHWFFDSPVPQPQH------------WNQALLLEP 2820
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  905 EGDICKDKFENIFQSLIERHEILRTSFQILDGE-LVQKIEPNVDFNIEYVHVNE-KDADYLIHEFISPFDLSKPPLLRVL 982
Cdd:PRK05691 2821 RQALDPALLEQALQALVEHHDALRLRFSQADGRwQAEYRAVTAQELLWQVTVADfAECAALFADAQRSLDLQQGPLLRAL 2900
                        1050      1060      1070
                  ....*....|....*....|....*....|....*..
gi 446807313  983 LLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYK 1019
Cdd:PRK05691 2901 LVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYR 2937
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
289-769 2.15e-126

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: 407.04  E-value: 2.15e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTYqnsiiKGVAFQGSVINLMDIPFEEEQVEDLQ---ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL 445
Cdd:cd12114    81 ADAGARLVLTD-----GPDAQLDVAVFDVLILDLDALAAPAPpppVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  446 CAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTI-YQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYD 524
Cdd:cd12114   156 LDINRRFA--VGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  525 YFVRANQKI-SLNKLFVGVEPIKTELLAKYdHLFRGNLQILNLYGPTEATVCCTSYqyerdkEITTQN-----VPIGSPL 598
Cdd:cd12114   234 VLEAAQALLpSLRLVLLSGDWIPLDLPARL-RALAPDARLISLGGATEASIWSIYH------PIDEVPpdwrsIPYGRPL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  599 LNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd12114   307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  679 VKIRGYRIELGEIEASLLKYETIKTAVVIQReDESGEKYLCAYVVTEKDIPIP---EVRAYLATKLPYYMIPQQIISIQN 755
Cdd:cd12114   385 VKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIapdALRAFLAQTLPAYMIPSRVIALEA 463
                         490
                  ....*....|....
gi 446807313  756 IPLTQNGKIDRKKL 769
Cdd:cd12114   464 LPLTANGKVDRAAL 477
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
279-769 4.55e-126

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: 404.38  E-value: 4.55e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqiTMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17653    81 LPSARIQAILRTSGATLLLT---------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPH 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  439 RSLTNFLcaMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGArmTIYQGEKFDvpKLVQVIleEQVTLAYIPPTL 518
Cdd:cd17653   128 RGVLNYV--SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLADPSD--PFAHVA--RTVDALMSTPSI 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  519 LNEIydyfvRANQKISLNKLFVGVEPIKTELLAKYdhlfRGNLQILNLYGPTEATVCCTSYQYERDkeittQNVPIGSPL 598
Cdd:cd17653   200 LSTL-----SPQDFPNLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPG-----QPVTIGKPI 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  599 LNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd17653   266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  679 VKIRGYRIELGEIEASLLKYE-TIKTAVVIQREDEsgekyLCAYVVTEkDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17653   346 VKVRGFRINLEEIEEVVLQSQpEVTQAAAIVVNGR-----LVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
                         490
                  ....*....|..
gi 446807313  758 LTQNGKIDRKKL 769
Cdd:cd17653   420 LTANGKVDRKAL 431
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
868-1299 3.46e-124

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: 399.79  E-value: 3.46e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   868 KQQEYYLaSTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI-LDGELVQKIEPNV 946
Cdd:pfam00668    1 VQDEYPL-SPAQKRMWFLEKLEPHS-SAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   947 DFNIEY---VHVNEKDADYLIHEFI-----SPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY 1018
Cdd:pfam00668   79 PFELEIidiSDLSESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1019 ----KGNELPKLRVQ-YKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTF 1093
Cdd:pfam00668  159 qqllKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1094 KVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKL 1173
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1174 NTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMD-----MNPISIGELEFTPYPFKQSVSKFDLSLVATEID 1248
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsqEEEFQLSELDLSVSSVIEEEAKYDLSLTASERG 398
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446807313  1249 NNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEE 1299
Cdd:pfam00668  399 GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1332-1812 9.96e-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: 396.64  E-value: 9.96e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQNSIIKGIEFQGNVIDLMDmsFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD--ALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTI-YQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfV 1570
Cdd:cd12114   159 NRRFA--VGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV-L 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIV--LNKLLVGVEPIKTELLAKYdHLFRGNLQILNGYGPTEATVCCTSYryesnkEITTQN-----VPIGSPLLN 1643
Cdd:cd12114   236 EAAQALLpsLRLVLLSGDWIPLDLPARL-RALAPDARLISLGGATEASIWSIYH------PIDEVPpdwrsIPYGRPLAN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1644 TKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:cd12114   309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1724 IRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTEKDIPIP---EVRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:cd12114   387 VRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIapdALRAFLAQTLPAYMIPSRVIALEALP 465
                         490
                  ....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd12114   466 LTANGKVDRAAL 477
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1324-1812 4.47e-121

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


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 390.13  E-value: 4.47e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd17653     3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCShVLVHQNSiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:cd17653    83 SARIQAILRTSGAT-LLLTTDS--------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLcaMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQGEK----FDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17653   130 VLNYV--SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLADPsdpfAHVARTVDALMSTPSILSTLSP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TllneiyDYfvrDNQKIVLnkllVGVEPIKTELLAKYdhlfRGNLQILNGYGPTEATVCCTSYRYESNkeittQNVPIGS 1639
Cdd:cd17653   206 Q------DF---PNLKTIF----LGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPG-----QPVTIGK 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd17653   264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRED 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYE-TIKTAVVIDQEDEagekyLCAYVVTEkDIPIPEVRAYLATKLPHYMIPQQLIPIHN 1798
Cdd:cd17653   344 NQVKVRGFRINLEEIEEVVLQSQpEVTQAAAIVVNGR-----LVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDS 417
                         490
                  ....*....|....
gi 446807313 1799 IPLTQNGKIDRSKL 1812
Cdd:cd17653   418 FPLTANGKVDRKAL 431
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1332-1813 6.70e-115

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: 373.27  E-value: 6.70e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKR-ESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYM 1410
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1411 LTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 1490
Cdd:cd17648    81 LEDTGARVVIT-----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEiYDYF 1569
Cdd:cd17648   126 LSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQQ-YDLA 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VRDNQKIVLnklLVGvEPIKTELLAKYDHLFRGnlQILNGYGPTEATVCCTSYRYESNKEITTQnvpIGSPLLNTKIYIL 1649
Cdd:cd17648   205 RLPHLKRVD---AAG-EEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQRFDKS---LGRPVRNTKCYVL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 DSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE--------RGEKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd17648   276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQ 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGEKYLCAYVVTEKD-IPIPEVRAYLATKLPHYMIPQQLIP 1795
Cdd:cd17648   356 VKIRGQRIEPGEVEAALASYPGVRECAVVakedaSQAQSRIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVR 435
                         490
                  ....*....|....*...
gi 446807313 1796 IHNIPLTQNGKIDRSKLP 1813
Cdd:cd17648   436 LEGIPVTINGKLDVRALP 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
289-770 2.51e-114

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: 371.73  E-value: 2.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKR-EFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  368 LTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 447
Cdd:cd17648    81 LEDTGARVVIT-----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  448 MYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEiYDyF 526
Cdd:cd17648   126 LSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQQ-YD-L 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  527 VRANqkiSLNKLFVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEATVCCTSYQYERDKEITTQnvpIGSPLLNTKIYIL 606
Cdd:cd17648   204 ARLP---HLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQRFDKS---LGRPVRNTKCYVL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  607 DSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE--------RGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd17648   276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQ 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  679 VKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-----GEKYLCAYVVTEKD-IPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd17648   356 VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVR 435
                         490
                  ....*....|....*...
gi 446807313  753 IQNIPLTQNGKIDRKKLP 770
Cdd:cd17648   436 LEGIPVTINGKLDVRALP 453
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
285-769 1.86e-105

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: 345.77  E-value: 1.86e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  285 VKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRV 364
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  365 EYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNF 444
Cdd:cd05945    81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  445 LCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVT----------LAY 513
Cdd:cd05945   126 TNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKqLFRFLAEHGITvwvstpsfaaMCL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  514 IPPTLLNEIY---DYFvranqkislnkLFVGvEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTsyQYERDKEITTQ 590
Cdd:cd05945   204 LSPTFTPESLpslRHF-----------LFCG-EVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVT--YIEVTPEVLDG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  591 N--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGeklYKTGDIARWLPDGN 668
Cdd:cd05945   269 YdrLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGL 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  669 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP---EVRAYLATKLPYYM 745
Cdd:cd05945   346 LFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYM 425
                         490       500
                  ....*....|....*....|....
gi 446807313  746 IPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05945   426 IPRRFVYLDELPLNANGKIDRKAL 449
PRK05691 PRK05691
peptide synthase; Validated
202-859 2.19e-105

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 379.13  E-value: 2.19e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  202 EQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKtLLCETVtapQLF 281
Cdd:PRK05691 3651 DDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP-LEQSYV---RLF 3726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK05691 3727 EAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  362 QRVEYMLTDSG-----CSHVLTYQ-NSIIKGVAFQGSVINLM--DIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKG 433
Cdd:PRK05691 3807 QRLQRIIELSRtpvlvCSAACREQaRALLDELGCANRPRLLVweEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKG 3886
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  434 VMIEHRS-LTNFLCAM-YEDFSQdigiTDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVT 510
Cdd:PRK05691 3887 VMVEQRGmLNNQLSKVpYLALSE----ADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQgLLAHVQAQGIT 3962
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  511 LAYIPPTLLNEIYdyfvrANQKISLNKL---FVGVEPIKTELLAKYdhLFR-GNLQILNLYGPTEatvCCTSYQYERDKE 586
Cdd:PRK05691 3963 VLESVPSLIQGML-----AEDRQALDGLrwmLPTGEAMPPELARQW--LQRyPQIGLVNAYGPAE---CSDDVAFFRVDL 4032
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  587 ITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARW 663
Cdd:PRK05691 4033 ASTRGsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARR 4112
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  664 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV-----TEKDIPIPEVRAYLA 738
Cdd:PRK05691 4113 RSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVphqtvLAQGALLERIKQRLR 4191
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  739 TKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKS-SHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGH 816
Cdd:PRK05691 4192 AELPDYMVPLHWLWLDRLPLNANGKLDRKALPALdIGQLQSqAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGH 4271
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 446807313  817 SLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKS 859
Cdd:PRK05691 4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1328-1812 2.13e-101

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: 334.22  E-value: 2.13e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNF 1487
Cdd:cd05945    81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQ---GEKFDVTKLVQVILEEQVTLSYIPPTLLne 1564
Cdd:cd05945   126 TNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGA--TLVPvprDATADPKQLFRFLAEHGITVWVSTPSFA-- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1565 iydyfvrdnqkivlnKLLVGVEPIKTELLAKYDH-LFRGN---------LQ-------ILNGYGPTEATVCCTSYRYesN 1627
Cdd:cd05945   200 ---------------AMCLLSPTFTPESLPSLRHfLFCGEvlphktaraLQqrfpdarIYNTYGPTEATVAVTYIEV--T 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGeklYKTGDIAR 1705
Cdd:cd05945   263 PEVLDGYdrLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVR 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP---EVRAYLAT 1782
Cdd:cd05945   340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAE 419
                         490       500       510
                  ....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05945   420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
281-682 3.29e-101

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 332.35  E-value: 3.29e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   281 FEEQVKQNPNQIAIVCN-GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:pfam00501    1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   360 PKQRVEYMLTDSGCSHVLTYQNSIIKGVA---------------FQGSVINLMDIPFEEEQVEDLQITME---PQNLAYV 421
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLealgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPppdPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   422 IYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLVCGARMTIYQGE-KFDV 497
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpdDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFpALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   498 PKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEATVCC 576
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   577 TSYQYERDKEITTqnVPIGSPLLNTKIYILDSFH-RLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLY 655
Cdd:pfam00501  319 TTPLPLDEDLRSL--GSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
                          410       420
                   ....*....|....*....|....*..
gi 446807313   656 KTGDIARWLPDGNIEYLGRVDHQVKIR 682
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
1324-1725 3.62e-101

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 332.35  E-value: 3.62e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1324 FEEQVKRNPNQIAVVCNE-KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1403 PKQRVEYMLTDSGCSHVLVHQNSIIKGI-EFQGN--------VIDLMDMSFEEE---------PGEDMHMMIEPHNLAYV 1464
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELlEALGKlevvklvlVLDRDPVLKEEPlpeeakpadVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1465 IYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLIYGARMTIYQGE-KFDV 1540
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpdDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFpALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1541 TKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEATVCC 1619
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1620 TSYRYESNKEITTqnVPIGSPLLNTKIYILDSFH-RIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLY 1698
Cdd:pfam00501  319 TTPLPLDEDLRSL--GSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
                          410       420
                   ....*....|....*....|....*..
gi 446807313  1699 KTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
876-1285 5.69e-99

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: 326.53  E-value: 5.69e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQFEdGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH- 954
Cdd:cd19538     5 SFAQRRLWFLHQLE-GPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  955 -VNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG------NELPKL 1026
Cdd:cd19538    84 eVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArckgeaPELAPL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1027 RVQYKDYVMWQ-----NGPYYKNLISEQKNYWLTTLKGeLPV-LNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLAT 1100
Cdd:cd19538   164 PVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1101 ETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYE 1180
Cdd:cd19538   243 DNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYE 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1181 NQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSL-----VATEIDNNIHLKV 1255
Cdd:cd19538   323 HQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFelreqYNDGTPNGIEGFI 402
                         410       420       430
                  ....*....|....*....|....*....|
gi 446807313 1256 EYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19538   403 EYRTDLFDHETIEALAQRYLLLLESAVENP 432
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
278-771 3.01e-98

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: 325.23  E-value: 3.01e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:COG0318     2 ADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  358 ELPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqnlAYVIYTSGSTGQPKGVMIE 437
Cdd:COG0318    82 RLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  438 HRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLVCGARMTIYqgEKFDVPKLVQVILEEQVTLAYI 514
Cdd:COG0318   122 HRNL----LANAAAIAAALGLTpgDVVLVALPLFHVFgLTVGLLAPLLAGATLVLL--PRFDPERVLELIERERVTVLFG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  515 PPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTsyqYERDKEITTQNVP 593
Cdd:COG0318   196 VPTMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVT---VNPEDPGERRPGS 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  594 IGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfergekLYKTGDIARWLPDGNIEYLG 673
Cdd:COG0318   271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVG 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQI 750
Cdd:COG0318   344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEkWGER-VVAFVVLRPGAELdaEELRAFLRERLARYKVPRRV 422
                         490       500
                  ....*....|....*....|.
gi 446807313  751 ISIQNIPLTQNGKIDRKKLPQ 771
Cdd:COG0318   423 EFVDELPRTASGKIDRRALRE 443
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1320-1815 1.34e-95

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: 317.52  E-value: 1.34e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMI 1479
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLIYGARMTIYqgEKFDVTKLVQVILEEQVTLSY 1556
Cdd:COG0318   121 THRNL----LANAAAIAAALGLTpgDVVLVALPLFHVFgLTVGLLAPLLAGATLVLL--PRFDPERVLELIERERVTVLF 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITtqnV 1635
Cdd:COG0318   195 GVPTMLARLLRHPEFARYDLsSLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVTVNPEDPGERRP---G 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfergekLYKTGDIARWLPDGNIEYL 1715
Cdd:COG0318   270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIV 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQ 1792
Cdd:COG0318   343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwGER-VVAFVVLRPGAELdaEELRAFLRERLARYKVPRR 421
                         490       500
                  ....*....|....*....|...
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:COG0318   422 VEFVDELPRTASGKIDRRALRER 444
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
879-1285 1.50e-90

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: 302.03  E-value: 1.50e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  879 QKRMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEP--NVDFNIEYVHVN 956
Cdd:cd19540     8 QQRLWFLNRL-DGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPaaEARPDLTVVDVT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  957 EKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNE--LPKLRVQ 1029
Cdd:cd19540    87 EDELAARLAEAARrGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRApdWAPLPVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1030 YKDYVMWQ-------NGPyyKNLISEQKNYWLTTLKGeLP-VLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:cd19540   167 YADYALWQrellgdeDDP--DSLAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALARE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:cd19540   244 HGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAH 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSLVATE------IDNNIHLKV 1255
Cdd:cd19540   324 QDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLTGEL 403
                         410       420       430
                  ....*....|....*....|....*....|
gi 446807313 1256 EYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19540   404 EYATDLFDRSTAERLADRFVRVLEAVVADP 433
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
23-859 1.99e-89

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: 322.40  E-value: 1.99e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    23 WLDKLSgDVELSRFPCDCLSLNNIQASKESYYCQFPSdiAKRAVAISNNSdmllYTILLSGVKYLLSRYTDKDDVVIGMP 102
Cdd:TIGR03443    2 WSERLD-NPTLSVLPHDYLRPANNRLVEATYSLQLPS--AEVTAGGGSTP----FIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   103 VFKQGQEetvfqnnfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNTIvmlddiHC 182
Cdd:TIGR03443   75 SNKSGRP--------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRL------AF 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   183 YESTDKINS--------DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKN 254
Cdd:TIGR03443  141 QDAPDNQQTtystgsttDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKS 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   255 qILFDfnHTTRVHktlLCETVTA-PQLFEEQVKQNPNQIAIV------CNG---KEITYKQLNIKANQLARRLLDQGVKR 324
Cdd:TIGR03443  221 -LLPD--PTKDLD---WSGFRGAiHDIFADNAEKHPDRTCVVetpsflDPSsktRSFTYKQINEASNILAHYLLKTGIKR 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   325 EFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQR-VEYM----------LTDSGC--SHVLTYQN------SIIK 385
Cdd:TIGR03443  295 GDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEKAGTldQLVRDYIDkelelrTEIP 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   386 GVAFQ--GSVI------NLMDI--PFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqd 455
Cdd:TIGR03443  375 ALALQddGSLVggslegGETDVlaPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF--- 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   456 iGITDNVLFS--SSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPT---LLNeiydyfVRA 529
Cdd:TIGR03443  452 -GLSENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPgRLAEWMAKYGATVTHLTPAmgqLLS------AQA 524
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   530 NQKI-SL-NKLFVGvepiktELLAKYDHL----FRGNLQILNLYGPTEaTVCCTSYQyerdkEITTQN------------ 591
Cdd:TIGR03443  525 TTPIpSLhHAFFVG------DILTKRDCLrlqtLAENVCIVNMYGTTE-TQRAVSYF-----EIPSRSsdstflknlkdv 592
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   592 VPIGSPLLNTKIYILDSFHRLQPIGVP--GEICISGIGLARGYINRKELTADKFIDHPF-------------ERGEK--- 653
Cdd:TIGR03443  593 MPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkenNKPERefw 672
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   654 ------LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD 727
Cdd:TIGR03443  673 lgprdrLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDK 752
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   728 IP----------------------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP------- 772
Cdd:TIGR03443  753 SDeleefksevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaqlaa 832
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   773 --INNLKSSHLEPTNSTERKLVEIWKDVLGIQ--RIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVD 848
Cdd:TIGR03443  833 vaKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKG 912
                          970
                   ....*....|.
gi 446807313   849 FSKYILEMEKS 859
Cdd:TIGR03443  913 FAKEVDRLKKG 923
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1053-1904 9.47e-89

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: 320.09  E-value: 9.47e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1053 WLTTLKGeLPVLNFPTDFQRPTIQSFKGNVCSFNLGTDltfkvnKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSp 1132
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1133 iagRSHSDTNhmigmfinTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNP-LFDTMFVF 1211
Cdd:TIGR03443   74 ---SSNKSGR--------PFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQD 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1212 QNmdmnpisigeleftpyPFKQS-VSKF---DLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRV 1287
Cdd:TIGR03443  143 AP----------------DNQQTtYSTGsttDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDE 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1288 RLRNINMLSIEEEHCIMNEfnKKENSNSNYL-LVHKMFEEQVKRNPNQIAVV------CNEKG---ITYNELNIKANQLA 1357
Cdd:TIGR03443  207 PIGKVSLITPSQKSLLPDP--TKDLDWSGFRgAIHDIFADNAEKHPDRTCVVetpsflDPSSKtrsFTYKQINEASNILA 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1358 RRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQR--------------------------VEYM- 1410
Cdd:TIGR03443  285 HYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYId 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1411 -------------LTDSGCshvlvhqnsiIKGIEFQGNVIDLMdMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGV 1477
Cdd:TIGR03443  365 kelelrteipalaLQDDGS----------LVGGSLEGGETDVL-APYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGV 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1478 MIEHRSLTNFLCAMYEDFsqdiGITDNVLFS--SSISFDVTIFEIFVPLIYGARMTIYQGEkfDV---TKLVQVILEEQV 1552
Cdd:TIGR03443  434 LGRHFSLAYYFPWMAKRF----GLSENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTAD--DIgtpGRLAEWMAKYGA 507
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1553 TLSYIPPTLlneiydyfvrdnqkivlNKLLVG--VEPIKT--------ELLAKYDHL----FRGNLQILNGYGPTEaTVC 1618
Cdd:TIGR03443  508 TVTHLTPAM-----------------GQLLSAqaTTPIPSlhhaffvgDILTKRDCLrlqtLAENVCIVNMYGTTE-TQR 569
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1619 CTSY-----RYESNKEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVP--GEICISGIGLARGYINRKELTADKFIDH 1689
Cdd:TIGR03443  570 AVSYfeipsRSSDSTFLKNLKdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1690 PF-------------ERGEK---------LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:TIGR03443  650 WFvdpshwidldkenNKPERefwlgprdrLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1748 VVIDQEDEAGEKYLCAYVVTEKDIP----------------------------IPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:TIGR03443  730 VTLVRRDKDEEPTLVSYIVPQDKSDeleefksevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKL 809
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1800 PLTQNGKIDRSKLPKLNT--------LGNSNYVPPR-NEIDSSLIDIWSSIL--GVNNIGINDNFFELGGHSLKGLKLFE 1868
Cdd:TIGR03443  810 PLNPNGKVDKPALPFPDTaqlaavakNRSASAADEEfTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
                          970       980       990
                   ....*....|....*....|....*....|....*.
gi 446807313  1869 NIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDS 1904
Cdd:TIGR03443  890 ELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEE 925
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
281-775 6.90e-79

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 271.00  E-value: 6.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGV--KREFIV-GVMmerSIEMIVGILGILKAGGAYLPIDT 357
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLpdKSPIIVfGHM---SPEMLATFLGAVKAGHAYIPVDV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  358 ELPKQRVEYMLTDSGCSHVLTYQNSIIKGVafQGSVINLMDIPFEEEQVEDLQIT--MEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:PRK04813   85 SSPAERIEMIIEVAKPSLIIATEELPLEIL--GIPVITLDELKDIFATGNPYDFDhaVKGDDNYYIIFTSGTTGKPKGVQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  436 IEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQV------ 509
Cdd:PRK04813  163 ISHDNLVSFTNWMLEDFA--LPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPinvwvs 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  510 TLAYIPPTLLNEIYDyfvrANQKISLNK-LFVGVE-PIKT--ELLAKYDhlfrgNLQILNLYGPTEATVCCTsyQYERDK 585
Cdd:PRK04813  241 TPSFADMCLLDPSFN----EEHLPNLTHfLFCGEElPHKTakKLLERFP-----SATIYNTYGPTEATVAVT--SIEITD 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  586 EITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARw 663
Cdd:PRK04813  310 EMLDQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY- 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  664 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT-----EKDIPI-PEVRAYL 737
Cdd:PRK04813  386 LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeedfEREFELtKAIKKEL 465
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446807313  738 ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:PRK04813  466 KERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEVNK 503
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
876-1285 1.22e-76

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: 261.93  E-value: 1.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILD-GELVQKIEPNVDFNIEyvH 954
Cdd:cd19539     5 SFAQERLWFIDQGEDGGPA-YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLE--V 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  955 VNEKDADY----LIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNE--- 1022
Cdd:cd19539    82 RDLSDPDSdrerRLEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgp 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1023 ---LPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGeLPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLA 1099
Cdd:cd19539   162 aapLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1100 TETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAY 1179
Cdd:cd19539   241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1180 ENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQN-MDMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYS 1258
Cdd:cd19539   321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNaPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYA 400
                         410       420
                  ....*....|....*....|....*..
gi 446807313 1259 IKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19539   401 TSLFDEETIQGFLADYLQVLRQLLANP 427
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
282-774 6.07e-75

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 259.69  E-value: 6.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGV-KREFIVgVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILpKKSPII-VYGHMEPHMLVAFLGSIKSGHAYIPVDTSIP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   361 KQRVEymltdsgcshvltyqnsIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLA-----------------YVIY 423
Cdd:TIGR01734   86 SERIE-----------------MIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETsggpvsfdhavkgddnyYIIY 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   424 TSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITdnVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQV 503
Cdd:TIGR01734  149 TSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQ--FLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFE 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   504 ILEEQV------TLAYIPPTLLNEiydYFvraNQKI--SLNK-LFVGVE-PIKT--ELLAKYDhlfrgNLQILNLYGPTE 571
Cdd:TIGR01734  227 ELPKTGlnvwvsTPSFVDMCLLDP---NF---NQENypHLTHfLFCGEElPVKTakALLERFP-----KATIYNTYGPTE 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   572 ATVCCTSYQYERdkEITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfe 649
Cdd:TIGR01734  296 ATVAVTSVKITQ--EILDQYprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH--- 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   650 RGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGE-KYLCAYVVT---- 724
Cdd:TIGR01734  371 EGQPAYRTGDAGT-ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPeted 449
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 446807313   725 -EKDIPI-PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:TIGR01734  450 fEKEFQLtKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAEEVN 501
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1353-2164 1.52e-74

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: 268.11  E-value: 1.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1353 ANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSII--KGI 1430
Cdd:COG3319    36 AAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALalALL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1431 EFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSS 1510
Cdd:COG3319   116 ALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1511 ISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLnkLLVGVEPIKT 1590
Cdd:COG3319   196 AALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLL--LLGLLALLLA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1591 ELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIG 1670
Cdd:COG3319   274 LLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGG 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKyETIKTAVVI 1750
Cdd:COG3319   354 AGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAE-AAAVAAAVA 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1751 DQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATK--LPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRN 1828
Cdd:COG3319   433 AAAAAAAAAAALAAAVVAAAALAAAALLLLLLLllLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAA 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1829 EIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSECLI 1908
Cdd:COG3319   513 ALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPL 592
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1909 PIQNRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLG 1988
Cdd:COG3319   593 VPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLG 672
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1989 WSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAFEELEKFNDQLGIEKISFEQMSEEQLIESLLKK 2068
Cdd:COG3319   673 WSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLER 752
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 2069 ftLNENSCQQNFEDPMMNKL-KVMIANRYAYLKYnCKQKIKADIFLFNASINDIHPLVD-YNRWNEYTSGEVYALQVPGS 2146
Cdd:COG3319   753 --LREAGLPAGLDAERLRRLlRVFRANLRALRRY-RPRPYDGPVLLFRAEEDPPGRADDpALGWRPLVAGGLEVHDVPGD 829
                         810
                  ....*....|....*...
gi 446807313 2147 HLSMLEKPHIHELVKSIK 2164
Cdd:COG3319   830 HFSMLREPHVAELAAALR 847
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1322-1812 8.57e-74

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 256.36  E-value: 8.57e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK04813    6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVL--VHQNSIIKGIEfqgnVIDLMD--MSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGV 1477
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIIatEELPLEILGIP----VITLDElkDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 MIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQGEKfDVTK----LVQVILEEQV- 1552
Cdd:PRK04813  162 QISHDNLVSFTNWMLEDFA--LPEGPQFLNQAPYSFDLSVMDLYPTLASGG--TLVALPK-DMTAnfkqLFETLPQLPIn 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 ----TLSYIPPTLLNEIYD--------YFvrdnqkivlnkLLVGVE-PIKT--ELLAKYDhlfrgNLQILNGYGPTEATV 1617
Cdd:PRK04813  237 vwvsTPSFADMCLLDPSFNeehlpnltHF-----------LFCGEElPHKTakKLLERFP-----SATIYNTYGPTEATV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 CCTSYryESNKEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGE 1695
Cdd:PRK04813  301 AVTSI--EITDEMLDQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQ 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1696 KLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVT-----EKD 1770
Cdd:PRK04813  376 PAYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeedfERE 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 446807313 1771 IPI-PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK04813  455 FELtKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
1319-1812 1.02e-69

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 244.28  E-value: 1.02e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1319 LVHKMFEeQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:TIGR01734    2 LIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1399 DTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:TIGR01734   81 DTSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1479 IEHRSLTNFLCAMYEDFSQDIGITdnVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQV------ 1552
Cdd:TIGR01734  161 ISHDNLVSFTNWMLADFPLSEGKQ--FLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGlnvwvs 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1553 TLSYIPPTLLNEiydYFVRDNQKIVLNKLLVGVE-PIKT--ELLAKYDhlfrgNLQILNGYGPTEATVCCTSYryESNKE 1629
Cdd:TIGR01734  239 TPSFVDMCLLDP---NFNQENYPHLTHFLFCGEElPVKTakALLERFP-----KATIYNTYGPTEATVAVTSV--KITQE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1630 ITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfeRGEKLYKTGDIARwL 1707
Cdd:TIGR01734  309 ILDQYprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAGT-I 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGE-KYLCAYVVT-----EKDIPI-PEVRAYL 1780
Cdd:TIGR01734  385 TDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPetedfEKEFQLtKAIKKEL 464
                          490       500       510
                   ....*....|....*....|....*....|..
gi 446807313  1781 ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:TIGR01734  465 KKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
871-1285 4.94e-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: 233.84  E-value: 4.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  871 EYYLaSTSQKRMFIVdQFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKI-EPNVDFN 949
Cdd:cd19066     1 KIPL-SPMQRGMWFL-KKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVlDKTVRFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  950 IEYV---HVNEKDA---DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG--- 1020
Cdd:cd19066    79 IEIIdlrNLADPEArllELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1021 --NELPKLRVQYKDYVMWQNgpyyKNLISEQKN----YWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFK 1094
Cdd:cd19066   159 qkPTLPPPVGSYADYAAWLE----KQLESEAAQadlaYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1095 VNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd19066   235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEF-TPYPFKQSVSKFDLSLVATE-IDNNIH 1252
Cdd:cd19066   315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEdPDGDLL 394
                         410       420       430
                  ....*....|....*....|....*....|...
gi 446807313 1253 LKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19066   395 LRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
418-765 1.25e-64

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: 223.70  E-value: 1.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDVTIFEIFVPLVCGARMTIYqgEKF 495
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNL----LAAAAALAASGGLTegDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  496 DVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLAKYdhLFRGNLQILNLYGPTEATV 574
Cdd:cd04433    76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERF--EEAPGIKLVNGYGLTETGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  575 CCTSYqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKL 654
Cdd:cd04433   154 TVATG---PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  655 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--E 732
Cdd:cd04433   224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeE 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 446807313  733 VRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd04433   304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1461-1808 1.84e-64

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: 223.32  E-value: 1.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDVTIFEIFVPLIYGARMTIYqgEKF 1538
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNL----LAAAAALAASGGLTegDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYdhLFRGNLQILNGYGPTEATV 1617
Cdd:cd04433    76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERF--EEAPGIKLVNGYGLTETGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 CCTSYRYESNKEittQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKL 1697
Cdd:cd04433   154 TVATGPPDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--E 1775
Cdd:cd04433   224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeE 303
                         330       340       350
                  ....*....|....*....|....*....|...
gi 446807313 1776 VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd04433   304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
894-1285 4.67e-64

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: 225.27  E-value: 4.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  894 TTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVNEKDADYLIhEFI----- 968
Cdd:cd20484    22 SAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDISSLKESEII-AYLrekak 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  969 SPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG---NELPKLRV---QYKDYVMWQNgpyy 1042
Cdd:cd20484   101 EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAllqGKQPTLASspaSYYDFVAWEQ---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1043 KNLIS----EQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILL 1118
Cdd:cd20484   177 DMLAGaegeEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1119 SRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRD 1198
Cdd:cd20484   257 HRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRS 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1199 TSRNPLFDTMFVFQNMdmnpISIGELEFTPYPFKQSVS-----------KFDLSLVATEIDNNIHLKVEYSIKLFKAETI 1267
Cdd:cd20484   337 QANSPVFQVAFFYQNF----LQSTSLQQFLAEYQDVLSiefvegihqegEYELVLEVYEQEDRFTLNIKYNPDLFDASTI 412
                         410
                  ....*....|....*...
gi 446807313 1268 ERLMVHFTNIVEEVTNNP 1285
Cdd:cd20484   413 ERMMEHYVKLAEELIANP 430
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
299-772 1.29e-60

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: 218.16  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRveymltdsgcshvlt 378
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  379 yQNsIIKGVAFQGSVINLmdipfeeeqvEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiGI 458
Cdd:cd17647    84 -QN-IYLGVAKPRGLIVI----------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF----NL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  459 TDNVLFS--SSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPTLlNEIYDYFVRANQKISL 535
Cdd:cd17647   148 SENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgRLAEWMAKYGATVTHLTPAM-GQLLTAQATTPFPKLH 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  536 NKLFVGvepiktELLAKYDHL----FRGNLQILNLYGPTEaTVCCTSYqYERDKEITTQN--------VPIGSPLLNTKI 603
Cdd:cd17647   227 HAFFVG------DILTKRDCLrlqtLAENVRIVNMYGTTE-TQRAVSY-FEVPSRSSDPTflknlkdvMPAGRGMLNVQL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  604 YILDSFHRLQ--PIGVPGEICISGIGLARGYINRKELTADKFIDHPF-----------ERGE-----------KLYKTGD 659
Cdd:cd17647   299 LVVNRNDRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkDNNEpwrqfwlgprdRLYRTGD 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  660 IARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIP---------- 729
Cdd:cd17647   379 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqedv 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313  730 -------------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:cd17647   459 pkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
875-1107 1.02e-59

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 206.04  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  875 ASTSQKRMFivdqFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:COG4908     1 LSPAQKRFL----FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  955 VNEKDA--------DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KG 1020
Cdd:COG4908    77 LSALPEpereaeleELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYaallegEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1021 NELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLAT 1100
Cdd:COG4908   157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236

                  ....*..
gi 446807313 1101 ETGTTPY 1107
Cdd:COG4908   237 AHGATVN 243
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
301-769 1.41e-59

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: 213.10  E-value: 1.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQ 380
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  381 NSIIKGVAFQGSVINlMDIPFEEeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcamyEDFSQDIGIT- 459
Cdd:cd17654    97 ELDNAPLSFTPEHRH-FNIRTDE-------------CLAYVIHTSGTTGTPKIVAVPHKCILPNI----QHFRSLFNITs 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  460 DNVLFSSSI-SFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEE--QVTLAYIPPTLLN----EIYDYFVRANQK 532
Cdd:cd17654   159 EDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrhRITVLQATPTLFRrfgsQSIKSTVLSATS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  533 iSLNKLFVGVEPIKTELLAK-YDHLFRGnLQILNLYGPTEatVCCTSYQYERDKEITTqnVPIGSPLLNTKIYILDsfhr 611
Cdd:cd17654   239 -SLRVLALGGEPFPSLVILSsWRGKGNR-TRIFNIYGITE--VSCWALAYKVPEEDSP--VQLGSPLLGTVIEVRD---- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  612 LQPIGVPGEicISGIGLARGYINRKELTADKfidhpfergEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEI 691
Cdd:cd17654   309 QNGSEGTGQ--VFLGGLNRVCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLI 376
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  692 EASLLKYETIKTAVVIQREDesgEKYLCAYVVTEKDIPIPEvRAYLaTKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd17654   377 QQVIESCLGVESCAVTLSDQ---QRLIAFIVGESSSSRIHK-ELQL-TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1323-1812 3.09e-59

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: 212.81  E-value: 3.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:cd05936     4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShvlvhqnSIIKGIEFQGNVIDLMDMSFEEEPgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:cd05936    84 TPRELEHILNDSGAK-------ALIVAVSFTDLLAAGAPLGERVAL--------TPEDVAVLQYTSGTTGVPKGAMLTHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFLCAMYEDFSQDIGITDNVLfsssisfdVTI--FEIF-------VPLIYGARMTIYqgEKFDVTKLVQVILEEQVT 1553
Cdd:cd05936   149 NLVANALQIKAWLEDLLEGDDVVL--------AALplFHVFgltvallLPLALGATIVLI--PRFRPIGVLKEIRKHRVT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1554 LsyIP--PTLLNEIYDYFvrDNQKIVLNKLLV---GVEPIKTELLAKYDHLFRGNlqILNGYGPTEA--TVCCTSYRYEs 1626
Cdd:cd05936   219 I--FPgvPTMYIALLNAP--EFKKRDFSSLRLcisGGAPLPVEVAERFEELTGVP--IVEGYGLTETspVVAVNPLDGP- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARW 1706
Cdd:cd05936   292 RKPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYM 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1707 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPI--PEVRAYLATK 1783
Cdd:cd05936   360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPySGEA-VKAFVVLKEGASLteEEIIAFCREQ 438
                         490       500
                  ....*....|....*....|....*....
gi 446807313 1784 LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05936   439 LAGYKVPRQVEFRDELPKSAVGKILRREL 467
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1344-1812 2.41e-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: 2.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHq 1423
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnviDLMDMSFEEEPGEDMHMMIE-PHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcamyEDFSQDIGIT 1502
Cdd:cd17654    96 --------------KELDNAPLSFTPEHRHFNIRtDECLAYVIHTSGTTGTPKIVAVPHKCILPNI----QHFRSLFNIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 -DNVLFSSSI-SFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEE--QVTLSYIPPTLLNEiydYFVRDNQKIVL 1578
Cdd:cd17654   158 sEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrhRITVLQATPTLFRR---FGSQSIKSTVL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NK------LLVGVEPIKTELLAK-YDHLFRGnLQILNGYGPTEatVCCTSYRYESNKEITTqnVPIGSPLLNTKIYILDs 1651
Cdd:cd17654   235 SAtsslrvLALGGEPFPSLVILSsWRGKGNR-TRIFNIYGITE--VSCWALAYKVPEEDSP--VQLGSPLLGTVIEVRD- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 fhrIQPIGVPGEicISGIGLARGYINRKELTADKfidhpfergEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:cd17654   309 ---QNGSEGTGQ--VFLGGLNRVCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINL 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDeagEKYLCAYVVTEKDIPIPEvRAYLaTKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:cd17654   374 DLIQQVIESCLGVESCAVTLSDQ---QRLIAFIVGESSSSRIHK-ELQL-TLLSSHAIPDTFVQIDKLPLTSHGKVDKSE 448

                  .
gi 446807313 1812 L 1812
Cdd:cd17654   449 L 449
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
876-1281 1.84e-57

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: 206.34  E-value: 1.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQF-EDgtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:cd20483     5 STFQRRLWFLHNFlED--KTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  955 VN-EKDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG-------N 1021
Cdd:cd20483    83 LSeAADPEAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdlA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQN----GPYYKNLISeqknYWLTTLKG---ELPVLNFPTDfQRPTIQSFKGNVCSFNLGTDLTFK 1094
Cdd:cd20483   163 TVPPPPVQYIDFTLWHNallqSPLVQPLLD----FWKEKLEGipdASKLLPFAKA-ERPPVKDYERSTVEATLDKELLAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1095 VNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd20483   238 MKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQnMD--MNPISIGELEFTPYPFKQSVSKFDLSLVATEI-DNNI 1251
Cdd:cd20483   318 CLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-VHgkFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDpDGGL 396
                         410       420       430
                  ....*....|....*....|....*....|
gi 446807313 1252 HLKVEYSIKLFKAETIERLMVHFTNIVEEV 1281
Cdd:cd20483   397 DLRLEFSTTLYDSADMERFLDNFVTFLTSV 426
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
278-769 6.73e-56

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: 202.79  E-value: 6.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:cd05936     2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  358 ELPKQRVEYMLTDSGCShvltyqnSIIKGVAFQGSVINLMDIPFEEEqvedlqitMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd05936    82 LYTPRELEHILNDSGAK-------ALIVAVSFTDLLAAGAPLGERVA--------LTPEDVAVLQYTSGTTGVPKGAMLT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  438 HRSLTNFLCAMYEDFSQDIGITDNVLfsssisfdVTI--FEIF-------VPLVCGARMTIYqgEKFDVPKLVQVILEEQ 508
Cdd:cd05936   147 HRNLVANALQIKAWLEDLLEGDDVVL--------AALplFHVFgltvallLPLALGATIVLI--PRFRPIGVLKEIRKHR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  509 VTLayIP--PTLLNEIYDYFvrANQKISLNKL---FVGVEPIKTELLAKYDHLFRGNlqILNLYGPTEA--TVCCTSYQY 581
Cdd:cd05936   217 VTI--FPgvPTMYIALLNAP--EFKKRDFSSLrlcISGGAPLPVEVAERFEELTGVP--IVEGYGLTETspVVAVNPLDG 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  582 ERdKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIA 661
Cdd:cd05936   291 PR-KPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIG 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  662 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIPI--PEVRAYLA 738
Cdd:cd05936   358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPySGEA-VKAFVVLKEGASLteEEIIAFCR 436
                         490       500       510
                  ....*....|....*....|....*....|.
gi 446807313  739 TKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05936   437 EQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1345-1813 8.18e-55

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


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 201.21  E-value: 8.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRveymltdsgcshvlvhQN 1424
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------------QN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 sIIKGIEFQGNVIDLmdmsfeeepgEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiGITDN 1504
Cdd:cd17647    86 -IYLGVAKPRGLIVI----------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF----NLSEN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFS--SSISFDVTIFEIFVPLIYGARMTIYQGEKFDVT-KLVQVILEEQVTLSYIPPT----LLNEIYDYFVRDNQKIV 1577
Cdd:cd17647   151 DKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgRLAEWMAKYGATVTHLTPAmgqlLTAQATTPFPKLHHAFF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKLLVGVEPIKTELLAKydhlfrgNLQILNGYGPTEatvcctSYRYESNKEITTQN------------VPIGSPLLNTK 1645
Cdd:cd17647   231 VGDILTKRDCLRLQTLAE-------NVRIVNMYGTTE------TQRAVSYFEVPSRSsdptflknlkdvMPAGRGMLNVQ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQ--PIGVPGEICISGIGLARGYINRKELTADKFIDHPF-----------ERGE-----------KLYKTG 1701
Cdd:cd17647   298 LLVVNRNDRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkDNNEpwrqfwlgprdRLYRTG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIP--------- 1772
Cdd:cd17647   378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqed 457
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1773 --------------------IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17647   458 vpkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1317-1812 4.11e-54

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 199.26  E-value: 4.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1317 YLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL 1396
Cdd:PRK06187    5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1397 PIDTDLPKQRVEYMLTDSGCSHVLVHQNSI-----IKG-IEFQGNVI-----DLMDM-----SFEE----EPGEDMHMMI 1456
Cdd:PRK06187   85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVpllaaILPqLPTVRTVIvegdgPAAPLapevgEYEEllaaASDTFDFPDI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLT--NFLCAMYEDFSQDigitdnvlfSSSISFdVTIFEIF------VPLIYGA 1528
Cdd:PRK06187  165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRD---------DVYLVI-VPMFHVHawglpyLALMAGA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMtIYQGEkFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFRGnlQIL 1607
Cdd:PRK06187  235 KQ-VIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREFKEKFGI--DLV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTEATVCCTSYRYEsnKEITTQNVPIGS---PLLNTKIYILDSFHRIQP--IGVPGEICISGIGLARGYINRKELT 1682
Cdd:PRK06187  311 QGYGMTETSPVVSVLPPE--DQLPGQWTKRRSagrPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEAT 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1683 ADKFIDhpferGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYL 1761
Cdd:PRK06187  389 AETIDG-----G--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPV 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446807313 1762 cAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06187  462 -AVVVLKPGATLdaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1328-1812 4.88e-54

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 199.95  E-value: 4.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVV-CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:COG0365    19 AEGRGDKVALIwEGEDGeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQG---------------NVI------------------DLMDMSFEEEPG 1449
Cdd:COG0365    99 GAEALADRIEDAEAKVLITADGGLRGGKVIDLkekvdealeelpsleHVIvvgrtgadvpmegdldwdELLAAASAEFEP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1450 EDM---HMMiephnlaYVIYTSGSTGQPKGVMIEHRSLTNFLcAMYEDFSQDIGITDNVLFSSSISFdVT--IFEIFVPL 1524
Cdd:COG0365   179 EPTdadDPL-------FILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKYVLDLKPGDVFWCTADIGW-ATghSYIVYGPL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLlneiYDYFVRDNQKIVLN------KLLVGV-EPIKTELLAK 1595
Cdd:COG0365   250 LNGATVVLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTA----IRALMKAGDEPLKKydlsslRLLGSAgEPLNPEVWEW 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1596 -YDHLfrgNLQILNGYGPTEATVCCTSYRyesnkeITTQNVP--IGSPLLNTKIYILDSFHRIQPIGVPGEICISG--IG 1670
Cdd:COG0365   326 wYEAV---GVPIVDGWGQTETGGIFISNL------PGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYINRKELTADKFidhpFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 1750
Cdd:COG0365   397 MFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1751 DQEDEAGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:COG0365   473 GVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
873-1285 3.67e-53

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: 193.57  E-value: 3.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  873 YLASTSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQIL-DGELVQKIEPNVDFNIE 951
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGA-YVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEgLGEPLQVVLKDRKLPWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  952 YV---HVNEKDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----- 1018
Cdd:cd19543    81 ELdlsHLSEAEQEAELEALAEedrerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalge 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1019 -KGNELPKLRvQYKDYVMW---QNGpyyknliSEQKNYWLTTLKG--ELPVLnfPTDFQRPTIQSFKGNVCSFNLGTDLT 1092
Cdd:cd19543   161 gQPPSLPPVR-PYRDYIAWlqrQDK-------EAAEAYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAELT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1093 FKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRsHSDTN---HMIGMFINTLVMRNYLENDDEFIEFLS 1169
Cdd:cd19543   231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPgieTMVGLFINTLPVRVRLDPDQTVLELLK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1170 RLKLNTLEAYENQDYPFEELLEGLDLHRdtsrnPLFDTMFVFQNMdmnPI--------SIGELEFTP-YPFKQsvSKFDL 1240
Cdd:cd19543   310 DLQAQQLELREHEYVPLYEIQAWSEGKQ-----ALFDHLLVFENY---PVdesleeeqDEDGLRITDvSAEEQ--TNYPL 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 446807313 1241 SLVATEiDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19543   380 TVVAIP-GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
280-769 7.79e-53

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 196.49  E-value: 7.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  280 LFEEQVKQNPNQIAIVCNG-----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLP 354
Cdd:COG0365    14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  355 IDTELPKQRVEYMLTDSGCSHVLTYQnsiikGVAFQGSVINLM------------------------------DIPFEE- 403
Cdd:COG0365    94 VFPGFGAEALADRIEDAEAKVLITAD-----GGLRGGKVIDLKekvdealeelpslehvivvgrtgadvpmegDLDWDEl 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  404 --EQVEDLQIT-MEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcAMYEDFSQDIGITDNVLFSSSISFdVT--IFEIF 478
Cdd:COG0365   169 laAASAEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKYVLDLKPGDVFWCTADIGW-ATghSYIVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  479 VPLVCGARMTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLlneiYDYFVRANQKI-------SLNKLF-VGvEPIKTE 548
Cdd:COG0365   247 GPLLNGATVVLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTA----IRALMKAGDEPlkkydlsSLRLLGsAG-EPLNPE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  549 LLAK-YDHLfrgNLQILNLYGPTEATVCCTSyqyerdkeittqNVP--------IGSPLLNTKIYILDSFHRLQPIGVPG 619
Cdd:COG0365   322 VWEWwYEAV---GVPIVDGWGQTETGGIFIS------------NLPglpvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEG 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  620 EICISG--IGLARGYINRKELTADKFidhpFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK 697
Cdd:COG0365   387 ELVIKGpwPGMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVS 462
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313  698 YETIKTAVVIQREDESGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:COG0365   463 HPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
297-764 1.92e-52

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: 193.20  E-value: 1.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTYQNS---IIKGVAFQGSV--INLMDI-------------PFEEEQVEDLQITME--PQNLAYVIYTSGSTGQPKGVMI 436
Cdd:cd05911    87 FTDPDGlekVKEAAKELGPKdkIIVLDDkpdgvlsiedllsPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  437 EHRSLTnFLCAMYEDFSQDIGITDNVLFSSSISFDVT-IFEIFVPLVCGARMTIYQgeKFDVPKLVQVILEEQVTLAYIP 515
Cdd:cd05911   167 SHRNLI-ANLSQVQTFLYGNDGSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKITFLYLV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  516 PTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpi 594
Cdd:cd05911   244 PPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRF-PNATIKQGYGMTETGGILTVNPDGDDKPGSV----- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  595 GSPLLNTKIYILDSFHR-LQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLG 673
Cdd:cd05911   318 GRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TEKdipipEVRAYLATKLP-YYM 745
Cdd:cd05911   392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkpgeklTEK-----EVKDYVAKKVAsYKQ 466
                         490
                  ....*....|....*....
gi 446807313  746 IPQQIISIQNIPLTQNGKI 764
Cdd:cd05911   467 LRGGVVFVDEIPKSASGKI 485
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
876-1285 2.00e-51

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: 188.43  E-value: 2.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQF-EDgtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF--QILDGELVQKIEPNVDFNIEY 952
Cdd:cd19532     5 SFGQSRFWFLQQYlED--PTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  953 VHV-NEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKLRVQY 1030
Cdd:cd19532    83 VQIsDEAEVEEEFERLKNhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1031 KDYVMWQNGPYYKNLISEQKNYW---LTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPY 1107
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWkseFSTLPEPLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1108 MILLAIYNILLSRYTGQEDIIVGspI--AGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYP 1185
Cdd:cd19532   243 HFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1186 FEELLEGLDLHRDTSRNPLFDTMF-----VFQNMDMNPISIGELEF----TPYpfkqsvskfDLSLvatEIDNN------ 1250
Cdd:cd19532   321 FDVLLDELGVPRSATHSPLFQVFInyrqgVAESRPFGDCELEGEEFedarTPY---------DLSL---DIIDNpdgdcl 388
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 446807313 1251 IHLKV-EYsikLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19532   389 LTLKVqSS---LYSEEDAELLLDSYVNLLEAFARDP 421
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
299-769 9.66e-51

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: 186.87  E-value: 9.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVlt 378
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  379 yqnsiikgvafqgsvinlmdipfeeeqvedlqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY---EDFSQD 455
Cdd:cd05971    83 --------------------------------VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  456 igitDNVLFSSS----ISfdvTIFEIFVP-LVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEI-YDYFVRA 529
Cdd:cd05971   131 ----GDLYWTPAdwawIG---GLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  530 NQKISLNKLFVGVEPIKTELLA-KYDHLfrgNLQILNLYGPTEATVCCTSYQYERDkeitTQNVPIGSPLLNTKIYILDS 608
Cdd:cd05971   204 HAQVKLRAIATGGESLGEELLGwAREQF---GVEVNEFYGQTECNLVIGNCSALFP----IKPGSMGKPIPGHRVAIVDD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  609 FHRLQPIGVPGEICI---SGIGLArGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYR 685
Cdd:cd05971   277 NGTPLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMAG-------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  686 IELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd05971   349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTA 428

                  ....*....
gi 446807313  761 NGKIDRKKL 769
Cdd:cd05971   429 TGKIRRREL 437
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
276-773 1.90e-50

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 188.47  E-value: 1.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK06187    7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTELPKQRVEYMLTDSGCSHVLTYQN--SIIKGVA----FQGSVINLMDIPFEEEQV--------------EDLQITMEP 415
Cdd:PRK06187   87 NIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILpqlpTVRTVIVEGDGPAAPLAPevgeyeellaaasdTFDFPDIDE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  416 QNLAYVIYTSGSTGQPKGVMIEHRSLT--NFLCAMYEDFSQDigitdnvlfSSSISFdVTIFEIF------VPLVCGARM 487
Cdd:PRK06187  167 NDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRD---------DVYLVI-VPMFHVHawglpyLALMAGAKQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  488 tIYQGEkFDVPKLVQVILEEQVTLAYIPPT----LLNEIYDYFVRANqkiSLNKLFVGVEPIKTELLAKYDHLFRGnlQI 563
Cdd:PRK06187  237 -VIPRR-FDPENLLDLIETERVTFFFAVPTiwqmLLKAPRAYFVDFS---SLRLVIYGGAALPPALLREFKEKFGI--DL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  564 LNLYGPTEATVCCTSYQYERDkeiTTQNVPI----GSPLLNTKIYILDSFHRLQP--IGVPGEICISGIGLARGYINRKE 637
Cdd:PRK06187  310 VQGYGMTETSPVVSVLPPEDQ---LPGQWTKrrsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  638 LTADKFIDhpferGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEK 716
Cdd:PRK06187  387 ATAETIDG-----G--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEkWGER 459
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313  717 YLcAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PRK06187  460 PV-AVVVLKPGATLdaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
287-766 3.68e-50

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: 185.12  E-value: 3.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:cd17631     7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  367 MLTDSGcSHVLtyqnsiikgvafqgsvinlmdipfeeeqVEDLQITMepqnlayviYTSGSTGQPKGVMIEHRSLTnflc 446
Cdd:cd17631    87 ILADSG-AKVL----------------------------FDDLALLM---------YTSGTTGRPKGAMLTHRNLL---- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  447 AMYEDFSQDIGIT-DNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY 525
Cdd:cd17631   125 WNAVNALAALDLGpDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQH 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  526 FVRANQKIS-LNKLFVGVEPIKTELLAKYDhlfRGNLQILNLYGPTEAT--VCCTSYQYERDKeittqnvpIGS---PLL 599
Cdd:cd17631   205 PRFATTDLSsLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTETSpgVTFLSPEDHRRK--------LGSagrPVF 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  600 NTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQV 679
Cdd:cd17631   274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMI 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  680 KIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIP--IPEVRAYLATKLPYYMIPQQIISIQNI 756
Cdd:cd17631   347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEA-VVAVVVPRPGAEldEDELIAHCRERLARYKIPKSVEFVDAL 425
                         490
                  ....*....|
gi 446807313  757 PLTQNGKIDR 766
Cdd:cd17631   426 PRNATGKILK 435
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1330-1809 5.80e-49

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: 181.65  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:cd17631     7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGcSHVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLTnflc 1489
Cdd:cd17631    87 ILADSG-AKVLFDD-------------------------------------LALLMYTSGTTGRPKGAMLTHRNLL---- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1490 AMYedfsqdigitdnvlFSSSISFDVTIFEIFV---PLIYGARM------TIYQG------EKFDVTKLVQVILEEQVTL 1554
Cdd:cd17631   125 WNA--------------VNALAALDLGPDDVLLvvaPLFHIGGLgvftlpTLLRGgtvvilRKFDPETVLDLIERHRVTS 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDhlfRGNLQILNGYGPTEATVCCTSYRYEsnkEITTQ 1633
Cdd:cd17631   191 FFLVPTMIQALLQHPRFATTDLSsLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTETSPGVTFLSPE---DHRRK 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIE 1713
Cdd:cd17631   265 LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLY 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIP--IPEVRAYLATKLPHYMIP 1790
Cdd:cd17631   338 IVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEA-VVAVVVPRPGAEldEDELIAHCRERLARYKIP 416
                         490
                  ....*....|....*....
gi 446807313 1791 QQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17631   417 KSVEFVDALPRNATGKILK 435
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1345-1812 7.75e-49

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: 181.48  E-value: 7.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVlvhqn 1424
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiefqgnVIDLMDmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY---EDFSQDigi 1501
Cdd:cd05971    83 -----------VTDGSD------------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRD--- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 tDNVLFSSS----ISfdvTIFEIFVP-LIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEI-YDYFVRDNQK 1575
Cdd:cd05971   131 -GDLYWTPAdwawIG---GLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLKHAQ 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1576 IVLNKLLVGVEPIKTELLA-KYDHLfrgNLQILNGYGPTEATVCCTSyryeSNKEITTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:cd05971   207 VKLRAIATGGESLGEELLGwAREQF---GVEVNEFYGQTECNLVIGN----CSALFPIKPGSMGKPIPGHRVAIVDDNGT 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICI---SGIGLArGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:cd05971   280 PLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMAG-------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:cd05971   352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431

                  ....*.
gi 446807313 1807 IDRSKL 1812
Cdd:cd05971   432 IRRREL 437
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1340-1807 5.05e-47

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


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 177.40  E-value: 5.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHV 1419
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1420 LVHQNSI------IKGIEFQGNVI----------DLMDMSFEEEPGEDMHMMIEPH----NLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd05911    87 FTDPDGLekvkeaAKELGPKDKIIvlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKdgkdDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTnflcamyedfsQDIGITDNVLFSSSISFDVTIfeIFVPL--IYGARMTI---YQGE------KFDVTKLVQVIL 1548
Cdd:cd05911   167 SHRNLI-----------ANLSQVQTFLYGNDGSNDVIL--GFLPLyhIYGLFTTLaslLNGAtviimpKFDSELFLDLIE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESN 1627
Cdd:cd05911   234 KYKITFLYLVPPIAAALAKSPLLDKYDLsSLRVILSGGAPLSKELQELLAKRF-PNATIKQGYGMTETGGILTVNPDGDD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTqnvpiGSPLLNTKIYILDSFHR-IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARW 1706
Cdd:cd05911   313 KPGSV-----GRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYF 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1707 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKYLcAYVV-------TEKdipipEVRA 1778
Cdd:cd05911   382 DEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEvSGELPR-AYVVrkpgeklTEK-----EVKD 455
                         490       500       510
                  ....*....|....*....|....*....|...
gi 446807313 1779 YLATKLPHYmipQQL----IPIHNIPLTQNGKI 1807
Cdd:cd05911   456 YVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1332-1815 9.40e-47

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 176.31  E-value: 9.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQNSIIK-GIEFQGNVIDLMDMSFEE-EPGEDMHMmiepHNLAYVIYTSGSTGQPKGVMiehRSLTN-FL 1488
Cdd:PRK03640   96 DDAEVKCLITDDDFEAKlIPGISVKFAELMNGPKEEaEIQEEFDL----DEVATIMYTSGTTGKPKGVI---QTYGNhWW 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 CAMYEdfSQDIGITDNvlfsssisfD-----VTIFEI------FVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLSYI 1557
Cdd:PRK03640  169 SAVGS--ALNLGLTED---------DcwlaaVPIFHIsglsilMRSVIYG--MRVVLVEKFDAEKINKLLQTGGVTIISV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHlfrGNLQILNGYGPTE--ATVCCTSYRYESNKeittqnv 1635
Cdd:PRK03640  236 VSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE---KGIPVYQSYGMTEtaSQIVTLSPEDALTK------- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 pIGS---PLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNI 1712
Cdd:PRK03640  306 -LGSagkPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:PRK03640  377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKR 456
                         490       500
                  ....*....|....*....|...
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK03640  457 FYFVEELPRNASGKLLRHELKQL 479
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
292-769 3.37e-45

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: 170.93  E-value: 3.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  292 IAIVCNGKEITYKQLNIKANQLARRLLDQG-VKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTD 370
Cdd:cd05941     3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  371 SGCSHVLtyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 450
Cdd:cd05941    83 SEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  451 --DFSQDigitDNVLFSSSIsFDV--TIFEIFVPLVCGARMtIYQGeKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY- 525
Cdd:cd05941   124 awRWTED----DVLLHVLPL-HHVhgLVNALLCPLFAGASV-EFLP-KFDPKEVAISRLMPSITVFMGVPTIYTRLLQYy 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  526 --------FVRANQKISLnKLFV-GVEPIKTELLAKYDHLFrGNlQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGS 596
Cdd:cd05941   197 eahftdpqFARAAAAERL-RLMVsGSAALPVPTLEEWEAIT-GH-TLLERYGMTE-IGMALSNPLDGERRPGT----VGM 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  597 PLLNTKIYILD-SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGR- 674
Cdd:cd05941   269 PLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRs 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  675 -VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIP---IPEVRAYLATKLPYYMIPQQ 749
Cdd:cd05941   343 sVD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGER-VVAVVVLRAGAAalsLEELKEWAKQRLAPYKRPRR 420
                         490       500
                  ....*....|....*....|
gi 446807313  750 IISIQNIPLTQNGKIDRKKL 769
Cdd:cd05941   421 LILVDELPRNAMGKVNKKEL 440
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
289-776 4.46e-45

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 171.68  E-value: 4.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTYQNSIIKgvAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMiehRSLTN-FLCA 447
Cdd:PRK03640   96 DDAEVKCLITDDDFEAK--LIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI---QTYGNhWWSA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  448 MYEdfSQDIGITDNvlfsssisfD-----VTIFEI------FVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLAYIPP 516
Cdd:PRK03640  171 VGS--ALNLGLTED---------DcwlaaVPIFHIsglsilMRSVIYG--MRVVLVEKFDAEKINKLLQTGGVTIISVVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  517 TLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHlfrGNLQILNLYGPTE--ATVCCTSYQYERDKeittqnvpI 594
Cdd:PRK03640  238 TMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE---KGIPVYQSYGMTEtaSQIVTLSPEDALTK--------L 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  595 GS---PLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEY 671
Cdd:PRK03640  307 GSagkPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYV 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  672 LGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQII 751
Cdd:PRK03640  379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFY 458
                         490       500
                  ....*....|....*....|....*
gi 446807313  752 SIQNIPLTQNGKIDRKKLPQPINNL 776
Cdd:PRK03640  459 FVEELPRNASGKLLRHELKQLVEEM 483
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
276-769 1.00e-44

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 171.24  E-value: 1.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTELPKQRVEYMLTDSGCSHVLTYQnsiikgvAFQGSVINLMD--------IPFEEEQVEDLQITM-------------- 413
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLG-------LFLGVDYSATTrlpalehvVICETEEDDPHTEKMktftdflaagdpae 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 -----EPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FsssisfdvtiFEIF---- 478
Cdd:PRK07656  159 rapevDPDDVADILFTSGTTGRPKGAMLTHRQLL----SNAADWAEYLGLTegDRYLaanpF----------FHVFgyka 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  479 ---VPLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLakyd 554
Cdd:PRK07656  225 gvnAPLMRGA--TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtGAASMPVALL---- 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  555 HLFRGNLQ---ILNLYGPTEA--TVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLA 629
Cdd:PRK07656  299 ERFESELGvdiVLTGYGLSEAsgVTTFNRLDDDRKTVAGT----IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVM 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  630 RGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQR 709
Cdd:PRK07656  375 KGYYDDPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313  710 EDES-GEkYLCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07656  449 PDERlGE-VGKAYVVLKPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
1345-1812 5.12e-44

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: 167.24  E-value: 5.12e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1425 SIIKGIEfqgnVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 1504
Cdd:TIGR01923   81 LEEKDFQ----ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1505 VLFSSSIsFDVTIFEI-FVPLIYGarMTIYQGEKFdvTKLVQVILEEQVTLSYIPPTLLNEIYDyfvRDNQKIVLNKLLV 1583
Cdd:TIGR01923  155 WLLSLPL-YHISGLSIlFRWLIEG--ATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRLLD---EGGHNENLRKILL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1584 GVEPIKTELLAKYDHLfrgNLQILNGYGPTE-ATVCCTSyryesNKEITTQNVPIGSPLLNTKIYIldsfhRIQPIGVPG 1662
Cdd:TIGR01923  227 GGSAIPAPLIEEAQQY---GLPIYLSYGMTEtCSQVTTA-----TPEMLHARPDVGRPLAGREIKI-----KVDNKEGHG 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1663 EICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:TIGR01923  294 EIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHP 366
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1743 TIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:TIGR01923  367 GIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1335-1812 2.19e-43

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: 165.54  E-value: 2.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1335 IAVVCNEKGITYNELNIKANQLARRLLDQG-VKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTD 1413
Cdd:cd05941     3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGCSHVLvhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05941    83 SEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 --DFSQDigitDNVLFSSSIsFDV--TIFEIFVPLIYGARMtIYQGeKFDVTKLVQVILEEQVTLSYIPPTL---LNEIY 1566
Cdd:cd05941   124 awRWTED----DVLLHVLPL-HHVhgLVNALLCPLFAGASV-EFLP-KFDPKEVAISRLMPSITVFMGVPTIytrLLQYY 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLN-----KLLV-GVEPIKTELLAKYDHLFrGNlQILNGYGPTEaTVCCTSYRYESNKEITTqnvpIGSP 1640
Cdd:cd05941   197 EAHFTDPQFARAAaaerlRLMVsGSAALPVPTLEEWEAIT-GH-TLLERYGMTE-IGMALSNPLDGERRPGT----VGMP 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGR-- 1717
Cdd:cd05941   270 LPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRss 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1718 VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIP---IPEVRAYLATKLPHYMIPQQL 1793
Cdd:cd05941   344 VD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGER-VVAVVVLRAGAAalsLEELKEWAKQRLAPYKRPRRL 421
                         490
                  ....*....|....*....
gi 446807313 1794 IPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05941   422 ILVDELPRNAMGKVNKKEL 440
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1322-1812 1.44e-42

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 164.69  E-value: 1.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK07656    9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQGNVIDLMDMSfEEEPGEDMHMM---------------IEPHN 1460
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLflgvdySATTRLPALEHVVICETEE-DDPHTEKMKTFtdflaagdpaerapeVDPDD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FsssisfdvtiFEIF-------VPLIYG 1527
Cdd:PRK07656  168 VADILFTSGTTGRPKGAMLTHRQLL----SNAADWAEYLGLTegDRYLaanpF----------FHVFgykagvnAPLMRG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1528 ArmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGVE---PIKTELLakydHLFRGNL 1604
Cdd:PRK07656  234 A--TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAED--LSSLRLAVTgaaSMPVALL----ERFESEL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 Q---ILNGYGPTEAT-VCCTSYRYESNKEITTQnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK07656  306 GvdiVLTGYGLSEASgVTTFNRLDDDRKTVAGT---IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED----EA 1756
Cdd:PRK07656  383 ATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDerlgEV 456
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1757 GekylCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07656  457 G----KAYVVLKPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1345-1812 2.08e-42

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: 162.12  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcshvlvhqn 1424
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAG--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siIKGIefqgnVIDLMDMSFeeepgedmhmmiephnlayVIYTSGSTGQPKGVMIEHRSLTNFLcaMYEDFSQDIGITDN 1504
Cdd:cd05972    73 --AKAI-----VTDAEDPAL-------------------IYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSISFDVTI-FEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPT----LLNEIYDYFVRDNqkivLN 1579
Cdd:cd05972   125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTayrmLIKQDLSSYKFSH----LR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 KLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKeittqnvP--IGSPLLNTKIYILDSFHRIQP 1657
Cdd:cd05972   201 LVVSAGEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTVGNFPDMPVK-------PgsMGRPTPGYDVAIIDDDGRELP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IGVPGEICI--SGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 1735
Cdd:cd05972   272 PGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1736 ASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP-----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRS 1810
Cdd:cd05972   345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424

                  ..
gi 446807313 1811 KL 1812
Cdd:cd05972   425 EL 426
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1344-1812 2.44e-42

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: 161.36  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcshvlvhq 1423
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvIDLMDMsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDfsqdIGITD 1503
Cdd:cd05912    74 -------------VKLDDI-------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN----LGLTE 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSisfdVTIFEI------FVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKiV 1577
Cdd:cd05912   118 DDNWLCA----LPLFHIsglsilMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN-N 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKLLVGVEPIKTELLAKYDHLfrgNLQILNGYGPTEAT--VCCTSYRYESNKeittqnvpIGS---PLLNTKIYILdsf 1652
Cdd:cd05912   191 LRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNK--------IGSagkPLFPVELKIE--- 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1653 HRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:cd05912   257 DDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05912   330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
896-1285 3.07e-42

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: 161.46  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  896 YNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFqILDG--ELVQKIEPNVDFNIEYV---HVNEKDA---DYLIHEF 967
Cdd:cd19536    24 YLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF-IEDGlgQPVQVVHRQAQVPVTELdltPLEEQLDplrAYKEETK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  968 ISPFDLSKPPLLRVLLLRIAEERH-ILVVDMHHIISDGLSMGILIKEFVELYKG------NELPKlRVQYKDYVMWqngp 1040
Cdd:cd19536   103 IRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQlleykpLSLPP-AQPYRDFVAH---- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1041 yykNLISEQK----NYWLTTLKG-ELPVLNFPTDfqrpTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYN 1115
Cdd:cd19536   178 ---ERASIQQaaseRYWREYLAGaTLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1116 ILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMRNYLeNDDEFIEFLSRLKLNTLEAYENQDYPFEellegl 1193
Cdd:cd19536   251 LVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELESLSHEQVPLA------ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1194 DLHRDTSRNPLFDTMFVFQNMDM---NPISIGELEFTPYP-FKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIER 1269
Cdd:cd19536   324 DIQRCSEGEPLFDSIVNFRHFDLdfgLPEWGSDEGMRRGLlFSEFKSNYDVNLSVLPKQDRLELKLAYNSQVLDEEQAQR 403
                         410
                  ....*....|....*.
gi 446807313 1270 LMVHFTNIVEEVTNNP 1285
Cdd:cd19536   404 LAAYYKSAIAELATAP 419
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
302-769 5.86e-42

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: 161.08  E-value: 5.86e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQN 381
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   382 SIIKGVafqgSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 461
Cdd:TIGR01923   81 LEEKDF----QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   462 VLFSSSIsFDVTIFEIFVPLVCGArMTIYQGEKFDvpKLVQVILEEQVTLAYIPPTLLNEIYDyfvRANQKISLNKLFVG 541
Cdd:TIGR01923  155 WLLSLPL-YHISGLSILFRWLIEG-ATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLD---EGGHNENLRKILLG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   542 VEPIKTELLAKYDHLfrgNLQILNLYGPTE-ATVCCTSyqyerDKEITTQNVPIGSPLLNTKIYIldsfhRLQPIGVPGE 620
Cdd:TIGR01923  228 GSAIPAPLIEEAQQY---GLPIYLSYGMTEtCSQVTTA-----TPEMLHARPDVGRPLAGREIKI-----KVDNKEGHGE 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   621 ICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:TIGR01923  295 IMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPG 367
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313   701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:TIGR01923  368 IQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1332-1812 1.74e-41

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: 161.38  E-value: 1.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQ------NSIIKGIEFQGNVIDLMD--------MSFEEEPGEDMHMM----IEPHNLAYVIYTSGSTGQ 1473
Cdd:cd05959    98 EDSRARVVVVSGelapvlAAALTKSEHTLVVLIVSGgagpeagaLLLAELVAAEAEQLkpaaTHADDPAFWLYSSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSLTnflcAMYEDFSQDI-GIT-DNVLFSSSISFdvtiF------EIFVPLIYGArMTIYQGEKFDVTKLVQ 1545
Cdd:cd05959   178 PKGVVHLHADIY----WTAELYARNVlGIReDDVCFSAAKLF----FayglgnSLTFPLSVGA-TTVLMPERPTPAAVFK 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKLLVGV---EPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSY 1622
Cdd:cd05959   249 RIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVsagEALPAEVGERWKARF--GLDILDGIGSTEMLHIFLSN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1623 RYESNKEITTqnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGD 1702
Cdd:cd05959   325 RPGRVRYGTT-----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WTRTGD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1703 IARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVR 1777
Cdd:cd05959   393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELK 472
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 446807313 1778 AYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05959   473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
280-769 7.35e-41

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


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 159.95  E-value: 7.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:TIGR03098    5 LLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   360 PKQRVEYMLTDSGC-------------SHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQV-EDLQITMEPQ--------N 417
Cdd:TIGR03098   85 KAEQVAHILADCNVrllvtsserldllHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwPKLLALGDADpphpvidsD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   418 LAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQgekF 495
Cdd:TIGR03098  165 MAAILYTSGSTGRPKGVVLSHRNLVAgaQSVATYLENRPD----DRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD---Y 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   496 DVPK-LVQVILEEQVT-LAYIPPtLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEAT 573
Cdd:TIGR03098  238 LLPRdVLKALEKHGITgLAAVPP-LWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFL-PNARLFLMYGLTEAF 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   574 VCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-FERGE 652
Cdd:TIGR03098  316 RSTYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPGEL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   653 KLYKT----GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVVTEKD 727
Cdd:TIGR03098  392 HLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTPPGGE 471
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 446807313   728 IPIPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:TIGR03098  472 ELDRAAlLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
298-770 1.16e-40

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: 157.07  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 TyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQ 454
Cdd:cd05934    81 V--------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFglgED 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  455 DIGITDNVLFSSsisfDVTIFEIFVPLVCGARMTIyqGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIs 534
Cdd:cd05934   123 DVYLTVLPLFHI----NAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA- 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  535 lNKL-FVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTsyqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQ 613
Cdd:cd05934   196 -HRLrAAYGAPNPPELHEEFEERF--GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGRPAPGYEVRIVDDDGQEL 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  614 PIGVPGEICI---SGIGLARGYINRKELTADKfidhpFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:cd05934   268 PAGEPGELVIrglRGWGFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  691 IEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05934   341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420

                  ..
gi 446807313  769 LP 770
Cdd:cd05934   421 LR 422
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1345-1812 2.70e-40

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: 156.39  E-value: 2.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQN 1424
Cdd:cd05903     3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK-AKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiEFQGnvidlmdMSFEEEPGEdmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 1504
Cdd:cd05903    82 ------RFRQ-------FDPAAMPDA----------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSIS-FDVTIFEIFVPLIYGARmTIYQgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLL 1582
Cdd:cd05903   137 FLVASPMAhQTGFVYGFTLPLLLGAP-VVLQ-DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrLRTFV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1583 VGVEPIKTELLAKYDHLfrGNLQILNGYGPTE---ATVCCTSyrYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05903   215 CGGATVPRSLARRAAEL--LGAKVCSAYGSTEcpgAVTSITP--APEDRRLYTD----GRPLPGVEIKVVDDTGATLAPG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICISGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDhQVKIR-GYRIELGEIEASL 1738
Cdd:cd05903   287 VEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVEDLL 358
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1739 LKYETIKTAVVIDQEDE-AGEKyLCAYVVTEK--DIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05903   359 LGHPGVIEAAVVALPDErLGER-ACAVVVTKSgaLLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
300-771 4.92e-40

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: 154.81  E-value: 4.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKqrveymltdsgcsHVLTY 379
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTP-------------NELAF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  380 QnsiikgvafqgsvinlmdipfeeeqVEDLQITMEpqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDfsqdIGIT 459
Cdd:cd05912    68 Q-------------------------LKDSDVKLD--DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN----LGLT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  460 DNVLFSSSisfdVTIFEI------FVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKi 533
Cdd:cd05912   117 EDDNWLCA----LPLFHIsglsilMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN- 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  534 SLNKLFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT--VCCTSYQYERDKeittqnvpIGS---PLLNTKIYILds 608
Cdd:cd05912   190 NLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNK--------IGSagkPLFPVELKIE-- 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  609 fHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 688
Cdd:cd05912   257 -DDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  689 GEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05912   329 AEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408

                  ...
gi 446807313  769 LPQ 771
Cdd:cd05912   409 LKQ 411
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
302-769 6.75e-40

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: 154.80  E-value: 6.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyqn 381
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  382 siikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcaMYEDFSQDIGITDN 461
Cdd:cd05972    79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  462 VLFSSSISFDVTI-FEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN---QKISLNK 537
Cdd:cd05972   125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPT----AYRMLIKQDlssYKFSHLR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  538 LFVGV-EPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYqyeRDKEITtqnvP--IGSPLLNTKIYILDSFHRLQP 614
Cdd:cd05972   201 LVVSAgEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTVGNF---PDMPVK----PgsMGRPTPGYDVAIIDDDGRELP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  615 IGVPGEICI--SGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:cd05972   272 PGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  693 ASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP-----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd05972   345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424

                  ..
gi 446807313  768 KL 769
Cdd:cd05972   425 EL 426
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1344-1813 3.68e-39

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: 152.45  E-value: 3.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVhq 1423
Cdd:cd05934     4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQDIG 1500
Cdd:cd05934    82 ------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFglgEDDVY 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNVLFSSsisfDVTIFEIFVPLIYGARMTIyqGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIvlNK 1580
Cdd:cd05934   126 LTVLPLFHI----NAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA--HR 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1581 L-LVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05934   198 LrAAYGAPNPPELHEEFEERF--GVRLLEGYGMTETIVGVIGPRDEPRRPGS-----IGRPAPGYEVRIVDDDGQELPAG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICI---SGIGLARGYINRKELTADKfidhpFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 1736
Cdd:cd05934   271 EPGELVIrglRGWGFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1737 SLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd05934   344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
310-769 1.03e-38

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: 152.21  E-value: 1.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA----YLPIDTELPKQRVEYMLTDSGcSHVLTYQNSIIK 385
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAG-GRIVLADAGAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  386 GVAFQGSVINLMDIPFEEEQVEDLQ-----ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITD 460
Cdd:cd05922    82 RLRDALPASPDPGTVLDADGIRAARasapaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL--GITADD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  461 NVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVpKLVQVILEEQVT-LAYIPPTLlnEIYDYFVRANQKI-SLNKL 538
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD-AFWEDLREHGATgLAGVPSTY--AMLTRLGFDPAKLpSLRYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  539 FVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTSYQYERDKEITTQnvpIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:cd05922   237 TQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGTPTPPGEP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  619 GEICISGIGLARGYINRKELTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:cd05922   313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313  699 ETIKTAVVIQREDESGEKylCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05922   387 GLIIEAAAVGLPDPLGEK--LALFVTAPDKIDPkDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
873-1285 1.23e-38

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: 150.53  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  873 YLASTSQKrMFIVDQFEDGTntTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQ--ILDGELVQKIEPNVDFNI 950
Cdd:cd19542     2 YPCTPMQE-GMLLSQLRSPG--LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  951 EYVHVNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKlRVQY 1030
Cdd:cd19542    79 EEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1031 KDYVmwqngPY-YKNLISEQKNYWLTTLKGELPVLnFPT----DFQRPTIQSFKGNvcsfnlgtdlTFKVNKLATETGTT 1105
Cdd:cd19542   158 SDYI-----SYlQSQSQEESLQYWRKYLQGASPCA-FPSlspkRPAERSLSSTRRS----------LAKLEAFCASLGVT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1106 PYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQD 1183
Cdd:cd19542   222 LASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQH 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1184 YPFEELLEGLdlhRDTSRNPLFDTMFVFQNMDMNPISIGELEFTpypFKQSVSK----FDLSLVATEIDNNIHLKVEYSI 1259
Cdd:cd19542   302 LSLREIQRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSV---FELSAAEdpteYPVAVEVEPSGDSLKVSLAYST 375
                         410       420
                  ....*....|....*....|....*.
gi 446807313 1260 KLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19542   376 SVLSEEQAEELLEQFDDILEALLANP 401
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
289-769 1.48e-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: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGC-------------------SHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITmEPQNLAYVIYTSGSTG 429
Cdd:cd05959    98 EDSRArvvvvsgelapvlaaaltkSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAT-HADDPAFWLYSSGSTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  430 QPKGVMIEHRSLTnflcAMYEDFSQDI-GIT-DNVLFSSSISFdvtiF------EIFVPLVCGARMTIYQGekFDVPKLV 501
Cdd:cd05959   177 RPKGVVHLHADIY----WTAELYARNVlGIReDDVCFSAAKLF----FayglgnSLTFPLSVGATTVLMPE--RPTPAAV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  502 -QVILEEQVTLAYIPPTLlneiYDYFVRAN--QKISLNKLFVGV---EPIKTELLAKYDHLFrgNLQILNLYGPTEATVC 575
Cdd:cd05959   247 fKRIRRYRPTVFFGVPTL----YAAMLAAPnlPSRDLSSLRLCVsagEALPAEVGERWKARF--GLDILDGIGSTEMLHI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  576 CTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLY 655
Cdd:cd05959   321 FLSNRPGRVRYGTT-----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WT 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPI 730
Cdd:cd05959   389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALE 468
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313  731 PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05959   469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
894-1270 2.26e-38

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: 149.26  E-value: 2.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  894 TTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPnvdfniEYVHVNE-KDADylIHEFIS-PF 971
Cdd:cd19537    22 SSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSS------SPPRVQRvDTLD--VWKEINrPF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  972 DLSKppllrvlllriaEE--------RHILVVdMHHIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMWQngpyyK 1043
Cdd:cd19537    94 DLER------------EDpirvfispDTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS-----R 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1044 NLISEQKNYWLTTLKGeLPVLNFPTdfqRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTG 1123
Cdd:cd19537   156 PASPEDLDFWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1124 QEDIIVGSPIAGRSHSDTNHMIGMFINTLVMR-NY-LENDDEFIEFL------SRLKL-NTLeayenqdyPFEELLEGLD 1194
Cdd:cd19537   232 RTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFpSSSDASAADFLravrrsSQAALaHAI--------PWHQLLEHLG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1195 LHRDTSRNPLFDTMFVFQNMDMnpisiGELEFtPYPFKQSV------SKFDLSLVATEIDNN-IHLKVEYSIKLFKAETI 1267
Cdd:cd19537   304 LPPDSPNHPLFDVMVTFHDDRG-----VSLAL-PIPGVEPLytwaegAKFPLMFEFTALSDDsLLLRLEYDTDCFSEEEI 377

                  ...
gi 446807313 1268 ERL 1270
Cdd:cd19537   378 DRI 380
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1319-1814 5.53e-38

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


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 151.09  E-value: 5.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1319 LVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1399 DTDLPKQRVEYMLTDSGC-------------SHVLVHQNSIIKGIEFqgnviDLMDMSFEEEPGEDMHMM---------I 1456
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVrllvtsserldllHPALPGCHDLRTLIIV-----GDPAHASEGHPGEEPASWpkllalgdaD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1457 EPH-----NLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLIYGAR 1529
Cdd:TIGR03098  156 PPHpvidsDMAAILYTSGSTGRPKGVVLSHRNLVAgaQSVATYLENRPD----DRLLAVLPLSFDYGFNQLTTAFYVGAT 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1530 MTIYQgeKFDVTKLVQVILEEQVT-LSYIPP---TLLNEIYDYFVRDNQKIVLNKllVGVEPikTELLAKYDHLFrGNLQ 1605
Cdd:TIGR03098  232 VVLHD--YLLPRDVLKALEKHGITgLAAVPPlwaQLAQLDWPESAAPSLRYLTNS--GGAMP--RATLSRLRSFL-PNAR 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1606 ILNGYGPTEAtvcctsYR--YESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTA 1683
Cdd:TIGR03098  305 LFLMYGLTEA------FRstYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTA 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1684 DKFIDHP-FERGEKLYKT----GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVID-QEDEAG 1757
Cdd:TIGR03098  379 ERFRPLPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGvPDPTLG 458
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  1758 EKYLCAYVVTEKDIPIPEV-RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:TIGR03098  459 QAIVLVVTPPGGEELDRAAlLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
302-769 1.41e-37

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: 148.30  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGcSHVLTyqn 381
Cdd:cd05903     3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK-AKVFV--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  382 siikgvafqgsvinlmdIPFEEEQVEDLQitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 461
Cdd:cd05903    79 -----------------VPERFRQFDPAA---MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  462 VLFSSSIS-FDVTIFEIFVPLVCGARmTIYQgEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV 540
Cdd:cd05903   137 FLVASPMAhQTGFVYGFTLPLLLGAP-VVLQ-DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  541 ----GVEPIKTELLAKydhlfRGNLQILNLYGPTE---ATVCCTSyqYERDKEITTQnvpiGSPLLNTKIYILDSFHRLQ 613
Cdd:cd05903   215 cggaTVPRSLARRAAE-----LLGAKVCSAYGSTEcpgAVTSITP--APEDRRLYTD----GRPLPGVEIKVVDDTGATL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  614 PIGVPGEICISGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDhQVKIR-GYRIELGEIE 692
Cdd:cd05903   284 APGVEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVE 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  693 ASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEK--DIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05903   356 DLLLGHPGVIEAAVVALPDERlGER-ACAVVVTKSgaLLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFR 434

                  .
gi 446807313  769 L 769
Cdd:cd05903   435 L 435
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
875-1285 2.63e-37

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: 147.63  E-value: 2.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  875 ASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKI------EPNvdf 948
Cdd:cd19546     7 ATAGQLRTWLLARLDEET-RGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldadaaRPE--- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  949 nIEYVHVNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KGN 1021
Cdd:cd19546    83 -LPVVPATEEELPALLADRAAhLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarregRAP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQ----NGPYYKN-LISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVN 1096
Cdd:cd19546   162 ERAPLPLQFADYALWErellAGEDDRDsLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1097 KLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRS-HSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNT 1175
Cdd:cd19546   242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1176 LEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGE---LEFTPYPFKQSVSKFDLSLVATEIDNN-- 1250
Cdd:cd19546   322 REARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPElpgLRTSPVPLGTEAMELDLSLALTERRNDdg 401
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 446807313 1251 ----IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19546   402 dpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
876-1285 4.51e-37

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: 146.36  E-value: 4.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  876 STSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:cd19533     5 TSAQRGVWFAEQLDPEGSI-YNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHIDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  956 NEKDA------DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNELP- 1024
Cdd:cd19533    84 SGDPDpegaaqQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPAPp 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1025 ----------KLRVQYKDYVMWQngpyyknlisEQKNYWLTTLKGELPvlnfPTDFQRPTIQSFKGNVC-SFNLGTDLTF 1093
Cdd:cd19533   164 apfgsfldlvEEEQAYRQSERFE----------RDRAFWTEQFEDLPE----PVSLARRAPGRSLAFLRrTAELPPELTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1094 KVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKL 1173
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1174 NTLEAYENQDYPFEELLEglDLHRDTSRNPLFDTMFVFQNMDMnPISIGELEFTPYPFkQSVSKFDLSLVATE-IDNN-I 1251
Cdd:cd19533   310 ELRSLLRHQRYRYEDLRR--DLGLTGELHPLFGPTVNYMPFDY-GLDFGGVVGLTHNL-SSGPTNDLSIFVYDrDDESgL 385
                         410       420       430
                  ....*....|....*....|....*....|....
gi 446807313 1252 HLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19533   386 RIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1353-1812 9.07e-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: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 146.43  E-value: 9.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1353 ANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA----YLPIDTDLPKQRVEYMLTDSGcSHVLVHQNSIIK 1428
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAG-GRIVLADAGAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1429 GIEFQGNVIDLMDMSFEEEPGEDMHMMIEPH-----NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITD 1503
Cdd:cd05922    82 RLRDALPASPDPGTVLDADGIRAARASAPAHevsheDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL--GITADD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTkLVQVILEEQVT-LSYIPPTLlnEIYDYFVRDNQKI-VLNKL 1581
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATgLAGVPSTY--AMLTRLGFDPAKLpSLRYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEATVCCTsyrYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVP 1661
Cdd:cd05922   237 TQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMT---YLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYINRKELTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:cd05922   313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1742 ETIKTAVVIDQEDEAGEKylCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05922   387 GLIIEAAAVGLPDPLGEK--LALFVTAPDKIDPkDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1322-1766 1.28e-36

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 148.71  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:COG1022    15 DLLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLV-------------HQNSIIKGI---EFQGNVIDLMDMSFEE--EPGEDMHMM---- 1455
Cdd:COG1022    95 IYPTSSAEEVAYILNDSGAKVLFVedqeqldkllevrDELPSLRHIvvlDPRGLRDDPRLLSLDEllALGREVADPaele 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1456 -----IEPHNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMyEDFSQDIGITDNvlfSSSISFdv--tIFE--IFVPLIY 1526
Cdd:COG1022   175 arraaVKPDDLATIIYTSGTTGRPKGVMLTHR---NLLSNA-RALLERLPLGPG---DRTLSFlplahVFErtVSYYALA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 gARMTIYQGEkfDVTKLVQVILEEQVTLSYIPPTLLNEIYD--------------------------YFVRDNQ------ 1574
Cdd:COG1022   248 -AGATVAFAE--SPDTLAEDLREVKPTFMLAVPRVWEKVYAgiqakaeeagglkrklfrwalavgrrYARARLAgkspsl 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1575 ----------KIVLNKL-----------LVGVEPIKTELlakyDHLFRG-NLQILNGYGPTEATVCCTSYRYESNKeITT 1632
Cdd:COG1022   325 llrlkhaladKLVFSKLrealggrlrfaVSGGAALGPEL----ARFFRAlGIPVLEGYGLTETSPVITVNRPGDNR-IGT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 qnvpIGSPLLNTKIyildsfhRiqpIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNI 1712
Cdd:COG1022   400 ----VGPPLPGVEV-------K---IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFL 459
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1713 EYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQedeaGEKYLCAYVV 1766
Cdd:COG1022   460 RITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD----GRPFLAALIV 510
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
302-769 6.11e-35

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: 140.33  E-value: 6.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYqn 381
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  382 siikgvafqgsvinlmdipfeeeqvEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDN 461
Cdd:cd05969    80 -------------------------EELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMI----FYYFTGKYVLDLHPD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  462 VLFSSSIS---FDVTIFEIFVPLVCGARMTIYQGeKFDVPKLVQVILEEQVTLAYIPPT---LLNEIYDYFVRANQKISL 535
Cdd:cd05969   131 DIYWCTADpgwVTGTVYGIWAPWLNGVTNVVYEG-RFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  536 NKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTE-ATVCCTSYqyerdkeiTTQNVPIGS---PLLNTKIYILDSFHR 611
Cdd:cd05969   210 RFIHSVGEPLNPEAIRWGMEVF--GVPIHDTWWQTEtGSIMIANY--------PCMPIKPGSmgkPLPGVKAAVVDENGN 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  612 LQPIGVPGEICISG--IGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:cd05969   280 ELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPiP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGK 763
Cdd:cd05969   353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PsdelkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431

                  ....*.
gi 446807313  764 IDRKKL 769
Cdd:cd05969   432 IMRRVL 437
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
276-764 2.11e-34

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: 141.56  E-value: 2.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG 349
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  350 GAYLPIDTELPKQRVEYMLTDSGCSHVLT------------YQNSIIKGVAFQG-SVINLM-------DIPFEE------ 403
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvpLKKNVDDALNPNVtSVEHVIvlkrtgsDIDWQEgrdlww 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  404 -EQVEDLQ-----ITMEPQNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYEDFSQ--DIGITDNVLFSSSISFDVT-I 474
Cdd:cd17634   214 rDLIAKASpehqpEAMNAEDPLFILYTSGTTGKPKGVLHTT---GGYLVYAATTMKYvfDYGPGDIYWCTADVGWVTGhS 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  475 FEIFVPLVCGARMTIYQGeKFDVP---KLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPIKTE 548
Cdd:cd17634   291 YLLYGPLACGATTLLYEG-VPNWPtpaRMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINPE 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  549 LLAKY-DHLFRGNLQILNLYGPTEAT-VCCTSYqyeRDKEITTQNVPIgSPLLNTKIYILDSFHRLQPIGVPGEICISGI 626
Cdd:cd17634   370 AYEWYwKKIGKEKCPVVDTWWQTETGgFMITPL---PGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDP 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  627 --GLARGYINRKeltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 704
Cdd:cd17634   446 wpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  705 VVIQREDE-SGEKYLCAYVVTEKDIPIP----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17634   522 AVVGIPHAiKGQAPYAYVVLNHGVEPSPelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
299-728 3.81e-34

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: 138.50  E-value: 3.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELPKQrVEYMLTDSGCSHVL 377
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEAKALF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 tyqnsiikgvafqgsvinlmdipfeeeqVEDlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIG 457
Cdd:cd05907    83 ----------------------------VED------PDDLATIIYTSGTTGRPKGVMLSHRNI----------LSNALA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 ITDNVLF---SSSISF--DVTIFE----IFVPLVCGARMTIYQGEKFDVPKLVQVileeQVTLAYIPPTLLNEIYDYFVR 528
Cdd:cd05907   119 LAERLPAtegDRHLSFlpLAHVFErragLYVPLLAGARIYFASSAETLLDDLSEV----RPTVFLAVPRVWEKVYAAIKV 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 ANQKISLNKLF------------VGVEPIKTELLakydHLFRG-NLQILNLYGPTE--ATVCCTSyqyERDKEITTqnvp 593
Cdd:cd05907   195 KAVPGLKRKLFdlavggrlrfaaSGGAPLPAELL----HFFRAlGIPVYEGYGLTEtsAVVTLNP---PGDNRIGT---- 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  594 IGSPLLNTKIYILDSfhrlqpigvpGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLG 673
Cdd:cd05907   264 VGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITG 327
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  674 RV-DHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRedesGEKYLCAYVVTEKDI 728
Cdd:cd05907   328 RKkDLIITSGGKNISPEPIENALKASPLISQAVVIGD----GRPFLVALIVPDPEA 379
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1458-1812 4.98e-34

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: 135.48  E-value: 4.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDF-SQDIGITDNVLFSSsisFDVTIfEIFVPLIYGARMtIYQ 1534
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNngYFIGERLGLtEQDRLCIPVPLFHC---FGSVL-GVLACLTHGATM-VFP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1535 GEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPT 1613
Cdd:cd05917    76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSsLRTGIMAGAPCPPELMKRVIEVM-NMKDVTIAYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1614 EATVCCTSYRyeSNKEITTQNVPIGSPLLNTKIYILDSFHRIQP-IGVPGEICISGIGLARGYINRKELTAdKFIDhpfe 1692
Cdd:cd05917   155 ETSPVSTQTR--TDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTA-EAID---- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 rGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVV--TE 1768
Cdd:cd05917   228 -GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERyGEE-VCAWIRlkEG 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446807313 1769 KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05917   305 AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1344-1788 5.08e-34

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: 138.11  E-value: 5.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI-DTDLPKQrVEYMLTDSGCSHVLVh 1422
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEAKALFV- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1423 qnsiikgiefqgnvidlmdmsfeeEPGEDmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGIT 1502
Cdd:cd05907    84 ------------------------EDPDD---------LATIIYTSGTTGRPKGVMLSHRNI----------LSNALALA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 DNVLF---SSSISF--DVTIFE----IFVPLIYGARMTIYQGEKFDVTKLVQVileeQVTLSYIPPTLLNEIYDYFVRDN 1573
Cdd:cd05907   121 ERLPAtegDRHLSFlpLAHVFErragLYVPLLAGARIYFASSAETLLDDLSEV----RPTVFLAVPRVWEKVYAAIKVKA 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 QKIVLNKLL------------VGVEPIKTELLakydHLFRG-NLQILNGYGPTE--ATVCCTsyRYESNKEITtqnvpIG 1638
Cdd:cd05907   197 VPGLKRKLFdlavggrlrfaaSGGAPLPAELL----HFFRAlGIPVYEGYGLTEtsAVVTLN--PPGDNRIGT-----VG 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1639 SPLLNTKIyildsfhRIQPigvPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRV 1718
Cdd:cd05907   266 KPLPGVEV-------RIAD---DGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRK 329
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1719 -DHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQedeaGEKYLCAYVVTEKDIpipeVRAYLATKLPHYM 1788
Cdd:cd05907   330 kDLIITSGGKNISPEPIENALKASPLISQAVVIGD----GRPFLVALIVPDPEA----LEAWAEEHGIAYT 392
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
423-769 6.86e-34

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: 135.10  E-value: 6.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  423 YTSGSTGQPKGVMIEHRSLTN--FLCAMYEDF-SQDIGITDNVLFSSsisFDVTIfEIFVPLVCGARMtIYQGEKFDVPK 499
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNngYFIGERLGLtEQDRLCIPVPLFHC---FGSVL-GVLACLTHGATM-VFPSPSFDPLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  500 LVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLakydhlfRGNLQILNL------YGPTEA 572
Cdd:cd05917    84 VLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSsLRTGIMAGAPCPPELM-------KRVIEVMNMkdvtiaYGMTET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  573 TVCCTsyQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQP-IGVPGEICISGIGLARGYINRKELTAdKFIDhpferG 651
Cdd:cd05917   157 SPVST--QTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTA-EAID-----G 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  652 EKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVV--TEKD 727
Cdd:cd05917   229 DGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERyGEE-VCAWIRlkEGAE 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 446807313  728 IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05917   307 LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
297-769 9.03e-34

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: 138.21  E-value: 9.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05926    11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTYQNSI-------------IKGVAFQGSVINLM----DIPFEEE--QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd05926    91 LTPKGELgpasraasklglaILELALDVGVLIRApsaeSLSNLLAdkKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  438 HR----SLTNfLCAMYEdfsqdigitdnvLFSSSISFDVT-IFEI-------FVPLVCGARMTIyqGEKFD--------- 496
Cdd:cd05926   171 HRnlaaSATN-ITNTYK------------LTPDDRTLVVMpLFHVhglvaslLSTLAAGGSVVL--PPRFSastfwpdvr 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  497 ---------VPKLVQVILEEQVTLAYIPPTLLNeiydyFVRAnqkislnklfvGVEPIKTELLAKYDHLFRgnLQILNLY 567
Cdd:cd05926   236 dynatwytaVPTIHQILLNRPEPNPESPPPKLR-----FIRS-----------CSASLPPAVLEALEATFG--APVLEAY 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  568 GPTEATVCCTSYQYERDKEITTQnVPIGSpllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP 647
Cdd:cd05926   298 GMTEAAHQMTSNPLPPGPRKPGS-VGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  648 FergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEK 726
Cdd:cd05926   374 W------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEE-VAAAVVLRE 446
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 446807313  727 DIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05926   447 GASVteEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1344-1812 1.19e-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: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDFSQDigi 1501
Cdd:cd05935    82 ---------------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAaaNALQSAVWTGLTPS--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 tdNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKL 1581
Cdd:cd05935   126 --DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LV---GVEPIKTELLAKYDHLFrgNLQILNGYGPTEaTVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILD-SFHRIQP 1657
Cdd:cd05935   202 KVltgGGAPMPPAVAEKLLKLT--GLRFVEGYGLTE-TMSQTHTNPPLRPKLQCL----GIP*FGVDARVIDiETGRELP 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEAS 1737
Cdd:cd05935   275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1738 LLKYETIKTAVVIDQEDE-AGEKyLCAYVV---------TEKDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd05935   352 LYKHPAI*EVCVISVPDErVGEE-VKAFIVlrpeyrgkvTEEDI-IEWAREQMAA----YKYPREVEFVDELPRSASGKI 425

                  ....*
gi 446807313 1808 DRSKL 1812
Cdd:cd05935   426 LWRLL 430
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
291-769 2.22e-33

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: 135.67  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  291 QIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTD 370
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  371 SGCSHVLTYQNSIikgvafqgsvinlmdipfeeeqvedlqitmepqnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 450
Cdd:cd05919    81 CEARLVVTSADDI-----------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  451 DFsqdIGITDN-VLFSSSISFdvtiF------EIFVPLVCGARMTIYQGEKfDVPKLVQVILEEQVTLAYIPPTLLNEIY 523
Cdd:cd05919   126 EA---LGLTPGdRVFSSAKMF----FgyglgnSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYANLL 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  524 DYFVRANQKISLNKLFVGV-EPIKTELLAKYDHLFRGnlQILNLYGPTEAT---VCCTSYQYERDkeiTTqnvpiGSPLL 599
Cdd:cd05919   198 DSCAGSPDALRSLRLCVSAgEALPRGLGERWMEHFGG--PILDGIGATEVGhifLSNRPGAWRLG---ST-----GRPVP 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  600 NTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGDIARWLPDGNIEYLGRVDHQV 679
Cdd:cd05919   268 GYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDML 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  680 KIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTE-----KDIPIPEVRAYLATKLPYYMIPQQIISIQ 754
Cdd:cd05919   341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKspaapQESLARDIHRHLLERLSAHKVPRRIAFVD 420
                         490
                  ....*....|....*
gi 446807313  755 NIPLTQNGKIDRKKL 769
Cdd:cd05919   421 ELPRTATGKLQRFKL 435
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
248-773 3.01e-33

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 137.42  E-value: 3.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  248 MPKTEKNQILFdfnhTTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKRE 325
Cdd:PLN02330    5 IQKQEDNEHIF----RSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  326 FIVGVMMERSIEMIVGILGILKAGGAY-----LPIDTELPKQrVEYMLTDSGCSHVLTYQNS-------IIKGVAFQGSV 393
Cdd:PLN02330   81 QVVVVVLPNVAEYGIVALGIMAAGGVFsganpTALESEIKKQ-AEAAGAKLIVTNDTNYGKVkglglpvIVLGEEKIEGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  394 INLMDIPFEEEQVEDLQITME--PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYedFSQDIGITDNVLFSSSISFd 471
Cdd:PLN02330  160 VNWKELLEAADRAGDTSDNEEilQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL--FSVGPEMIGQVVTLGLIPF- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  472 vtiFEIF-VPLVCGARM----TIYQGEKFDVPKLVQVILEEQVTLAYI-PPTLLNEIYDYFVRAN--QKISLNKLFVGVE 543
Cdd:PLN02330  237 ---FHIYgITGICCATLrnkgKVVVMSRFELRTFLNALITQEVSFAPIvPPIILNLVKNPIVEEFdlSKLKLQAIMTAAA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  544 PIKTELLAKYDHLFRGnLQILNLYGPTEATvCCTSYQYERDKE--ITTQNvPIGSPLLNTKIYILDSFHRLQ-PIGVPGE 620
Cdd:PLN02330  314 PLAPELLTAFEAKFPG-VQVQEAYGLTEHS-CITLTHGDPEKGhgIAKKN-SVGFILPNLEVKFIDPDTGRSlPKNTPGE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  621 ICISGIGLARGYINRKELTaDKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:PLN02330  391 LCVRSQCVMQGYYNNKEET-DRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPS 464
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PLN02330  465 VEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1345-1812 4.11e-33

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: 134.94  E-value: 4.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiefqgnVIDLMDMsfeeepgEDMhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDN 1504
Cdd:cd05969    82 -----------LYERTDP-------EDP---------TLLHYTSGTTGTPKGVLHVHDAMI----FYYFTGKYVLDLHPD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSIS---FDVTIFEIFVPLIYGARMTIYQGeKFDVTKLVQVILEEQVTLSYIPPT---LLNEIYDYFVRDNQKIVL 1578
Cdd:cd05969   131 DIYWCTADpgwVTGTVYGIWAPWLNGVTNVVYEG-RFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTE-ATVCCTSYryesnkeiTTQNVPIGS---PLLNTKIYILDSFHR 1654
Cdd:cd05969   210 RFIHSVGEPLNPEAIRWGMEVF--GVPIHDTWWQTEtGSIMIANY--------PCMPIKPGSmgkPLPGVKAAVVDENGN 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISG--IGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:cd05969   280 ELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPiP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:cd05969   353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PsdelkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431

                  ....*.
gi 446807313 1807 IDRSKL 1812
Cdd:cd05969   432 IMRRVL 437
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1334-1812 6.79e-33

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: 134.13  E-value: 6.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1334 QIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTD 1413
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGCSHVLVHQNSIikgiefqgnvidlmdmsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05919    81 CEARLVVTSADDI-----------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 DFsqdIGITDN-VLFSSSISFdvtiF------EIFVPLIYGARMTIYQGEKfDVTKLVQVILEEQVTLSYIPPTLLNEIY 1566
Cdd:cd05919   126 EA---LGLTPGdRVFSSAKMF----FgyglgnSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYANLL 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLNKLLVGV-EPIKTELLAKYDHLFRGnlQILNGYGPTEatvccTSYRYESNKEITTQNVPIGSPLLNTK 1645
Cdd:cd05919   198 DSCAGSPDALRSLRLCVSAgEALPRGLGERWMEHFGG--PILDGIGATE-----VGHIFLSNRPGAWRLGSTGRPVPGYE 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:cd05919   271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVG 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE-----KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:cd05919   344 GQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKspaapQESLARDIHRHLLERLSAHKVPRRIAFVDELP 423
                         490
                  ....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd05919   424 RTATGKLQRFKL 435
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
282-769 1.48e-32

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 134.60  E-value: 1.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDSGCSHVL---TYQNSI--IKGVAFQGSVINLMDiPFEEEQVEDLQITMEPQNLAYVI-YTSGSTGQPKGV 434
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFvekTFQNMAlsMQKVSYVQRVISITS-LKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  435 MIEHRSLtnFLCAMYEDFSQDIGITDnvlfsSSISFdVTIFEI-------FVPLVCGARMTIyqGEKFDVPKLVQVILEE 507
Cdd:PRK06839  168 VLTQENM--FWNALNNTFAIDLTMHD-----RSIVL-LPLFHIggiglfaFPTLFAGGVIIV--PRKFEPTKALSMIEKH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  508 QVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLAKYDHlfRGnLQILNLYGPTEA--TVCCTSYQYERD 584
Cdd:PRK06839  238 KVTVVMGVPTIHQALINCSKFETTNLQSVRWFYnGGAPCPEELMREFID--RG-FLFGQGFGMTETspTVFMLSEEDARR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  585 KEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 664
Cdd:PRK06839  315 KVGS-----IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVD 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLP 742
Cdd:PRK06839  383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFLA 462
                         490       500
                  ....*....|....*....|....*..
gi 446807313  743 YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06839  463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
276-723 1.77e-32

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 136.00  E-value: 1.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVC--NG--KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA 351
Cdd:COG1022    12 TLPDLLRRRAARFPDRVALREkeDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  352 YLPIDTELPKQRVEYMLTDSGCSHV-----------LTYQNS------II----KGVAFQGSVINLMDI------PFEEE 404
Cdd:COG1022    92 TVPIYPTSSAEEVAYILNDSGAKVLfvedqeqldklLEVRDElpslrhIVvldpRGLRDDPRLLSLDELlalgreVADPA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  405 QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMyEDFSQDIGITDNvlfSSSISFdv--tIFE---IFV 479
Cdd:COG1022   172 ELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHR---NLLSNA-RALLERLPLGPG---DRTLSFlplahVFErtvSYY 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  480 PLVCGArmTIYQGEkfDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfvRANQKIS-----LNKLF-----VGVE------ 543
Cdd:COG1022   245 ALAAGA--TVAFAE--SPDTLAEDLREVKPTFMLAVPRVWEKVYA---GIQAKAEeagglKRKLFrwalaVGRRyararl 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  544 ---PIKTELLAKY---------------------------------DHLFRG-NLQILNLYGPTEATVCCTSYQYERDKe 586
Cdd:COG1022   318 agkSPSLLLRLKHaladklvfsklrealggrlrfavsggaalgpelARFFRAlGIPVLEGYGLTETSPVITVNRPGDNR- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  587 ITTqnvpIGSPLLNTKIyildsfhRlqpIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPD 666
Cdd:COG1022   397 IGT----VGPPLPGVEV-------K---IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDED 456
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  667 GNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIqredESGEKYLCAYVV 723
Cdd:COG1022   457 GFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV----GDGRPFLAALIV 510
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1344-1812 4.59e-32

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: 132.82  E-value: 4.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV-- 1421
Cdd:cd05926    15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpk 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 -----------HQNSIIKGIEFQGNVIDLM----DMSFEEEPGEDMHMMIEPHN--LAYVIYTSGSTGQPKGVMIEHR-- 1482
Cdd:cd05926    95 gelgpasraasKLGLAILELALDVGVLIRApsaeSLSNLLADKKNAKSEGVPLPddLALILHTSGTTGRPKGVPLTHRnl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 --SLTNfLCAMYEdfsqdigitdnvLFSSSISFDVT-IFEI-------FVPLIYGARMTIyqGEKFDVTKLVQVILEEQV 1552
Cdd:cd05926   175 aaSATN-ITNTYK------------LTPDDRTLVVMpLFHVhglvaslLSTLAAGGSVVL--PPRFSASTFWPDVRDYNA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNEIYDYFVRDNQKiVLNKLLV---GVEPIKTELLAKYDHLFRgnLQILNGYGPTEATVCCTSyryesNKE 1629
Cdd:cd05926   240 TWYTAVPTIHQILLNRPEPNPES-PPPKLRFirsCSASLPPAVLEALEATFG--APVLEAYGMTEAAHQMTS-----NPL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVP--IGSPLlNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWL 1707
Cdd:cd05926   312 PPGPRKPgsVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPI--PEVRAYLATKL 1784
Cdd:cd05926   385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEE-VAAAVVLREGASVteEELRAFCRKHL 463
                         490       500
                  ....*....|....*....|....*...
gi 446807313 1785 PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05926   464 AAFKVPKKVYFVDELPKTATGKIQRRKV 491
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
297-769 7.74e-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: 132.36  E-value: 7.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYL---PIDT--ELPKQrveymLTDS 371
Cdd:cd05904    29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLSTpaEIAKQ-----VKDS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  372 GCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQN-----------LAYVIYTSGSTGQPKGVMIEHRS 440
Cdd:cd05904   104 GAKLAFT-TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAeppvvvikqddVAALLYSSGTTGRSKGVMLTHRN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  441 LTNfLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV--PLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYI-PPT 517
Cdd:cd05904   183 LIA-MVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFAlgLLRLGA--TVVVMPRFDLEELLAAIERYKVTHLPVvPPI 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  518 LLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATvCCTSYQYERDKEittqNVPIGS- 596
Cdd:cd05904   260 VLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF-PNVDLGQGYGMTEST-GVVAMCFAPEKD----RAKYGSv 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  597 ----PLLNTKIYILDSfHRLQPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd05904   334 grlvPNVEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATA-ATID-----KEGWLHTGDLCYIDEDGYLFIV 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TEKdipipEVRAYLATKLPYYM 745
Cdd:cd05904   407 DRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkpgsslTED-----EIMDFVAKQVAPYK 481
                         490       500
                  ....*....|....*....|....
gi 446807313  746 IPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05904   482 KVRKVAFVDAIPKSPSGKILRKEL 505
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1329-1807 1.53e-31

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 131.55  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK06145   13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCSHVLVHQN-SIIKGIEFQGNVIDLM---DMSFEEEPGEDMHMM--IEPHNLAYVIYTSGSTGQPKGVMIehr 1482
Cdd:PRK06145   93 YILGDAGAKLLLVDEEfDAIVALETPKIVIDAAaqaDSRRLAQGGLEIPPQaaVAPTDLVRLMYTSGTTDRPKGVMH--- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFlcaMYEDFSQDI--GIT-DNVLFSSSISFDVTIFEI--FVPLIYGARMTIYQgeKFDVTKLVQVILEEQVTLSYI 1557
Cdd:PRK06145  170 SYGNL---HWKSIDHVIalGLTaSERLLVVGPLYHVGAFDLpgIAVLWVGGTLRIHR--EFDPEAVLAAIERHRLTCAWM 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEAtvCCTSYRYESNKEITTqnvp 1636
Cdd:PRK06145  245 APVMLSRVLTVPDRDRFDLdSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTET--CSGDTLMEAGREIEK---- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 IGS---PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIE 1713
Cdd:PRK06145  318 IGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLY 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTE-KDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK06145  391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgATLTLEALDRHCRQRLASFKVPR 470
                         490
                  ....*....|....*.
gi 446807313 1792 QLIPIHNIPLTQNGKI 1807
Cdd:PRK06145  471 QLKVRDELPRNPSGKV 486
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
297-769 2.15e-31

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


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 130.91  E-value: 2.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQGVKREFiVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05909     4 LGTSLTYRKLLTGAIALARKLAKMTKEGEN-VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTYQNSIIKG-------VAFQGSVINLMD------------------IPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQP 431
Cdd:cd05909    83 LTSKQFIEKLklhhlfdVEYDARIVYLEDlrakiskadkckaflagkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  432 KGVMIEHRSL-TN-FLCAMYEDFSQDigitDNVL----FSSSISFDVTifeIFVPLVCGARMTIYQgEKFDVPKLVQVIL 505
Cdd:cd05909   163 KGVVLSHKNLlANvEQITAIFDPNPE----DVVFgalpFFHSFGLTGC---LWLPLLSGIKVVFHP-NPLDYKKIPELIY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  506 EEQVTLAYIPPTLLNeiydYFVRANQK---ISLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYE 582
Cdd:cd05909   235 DKKATILLGTPTFLR----GYARAAHPedfSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECSPVISVNTPQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  583 RDKEITTQNVPIgsPLLNTKIYILDSfHRLQPIGVPGEICISGIGLARGYINRKELTAdkfidhpFERGEKLYKTGDIAR 662
Cdd:cd05909   309 SPNKEGTVGRPL--PGMEVKIVSVET-HEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGK 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAV-VIQREDES-GEKYLCayVVTEKDIPIPEVRAYL-AT 739
Cdd:cd05909   379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRkGEKIVL--LTTTTDTDPSSLNDILkNA 456
                         490       500       510
                  ....*....|....*....|....*....|
gi 446807313  740 KLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05909   457 GISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
300-769 2.62e-31

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: 129.52  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLty 379
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  380 qnsiikgvafqgsvinlmdipfeeeqvedlqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDFSQdig 457
Cdd:cd05935    79 -------------------------------VGSELDDLALIPYTSGTTGLPKGCMHTHFSAaaNALQSAVWTGLTP--- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 itDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQKISLNK 537
Cdd:cd05935   125 --SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  538 LFV---GVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILD-SFHRLQ 613
Cdd:cd05935   201 LKVltgGGAPMPPAVAEKLLKLT--GLRFVEGYGLTETMSQTHTNPPLRPKLQC-----LGIP*FGVDARVIDiETGREL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  614 PIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 693
Cdd:cd05935   274 PPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  694 SLLKYETIKTAVVIQREDESGEKYLCAYVV---------TEKDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd05935   351 KLYKHPAI*EVCVISVPDERVGEEVKAFIVlrpeyrgkvTEEDI-IEWAREQMAA----YKYPREVEFVDELPRSASGKI 425

                  ....*
gi 446807313  765 DRKKL 769
Cdd:cd05935   426 LWRLL 430
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1319-1807 6.62e-31

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: 130.77  E-value: 6.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEEQVKRNPNQIAVV------CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG 1392
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1393 GAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKG--IEFQGNVIDLMDMS----------------FEEEPGEDM-- 1452
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGrsVPLKKNVDDALNPNvtsvehvivlkrtgsdIDWQEGRDLww 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMIE------------PHNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYEDFSQ--DIGITDNVLFSSSISFDVT-I 1517
Cdd:cd17634   214 RDLIAkaspehqpeamnAEDPLFILYTSGTTGKPKGVLHTT---GGYLVYAATTMKYvfDYGPGDIYWCTADVGWVTGhS 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKTEL 1592
Cdd:cd17634   291 YLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINPEA 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1593 LAKY-DHLFRGNLQILNGYGPTEAT-VCCTSYRYESNKEITTQNVPIgsplLNTKIYILDSFHRIQPIGVPGEICISGI- 1669
Cdd:cd17634   371 YEWYwKKIGKEKCPVVDTWWQTETGgFMITPLPGAIELKAGSATRPV----FGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1670 -GLARGYINRKeltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAV 1748
Cdd:cd17634   447 pGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1749 VIDQEDE-AGEKYLCAYVVTEKDIPIP----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd17634   523 VVGIPHAiKGQAPYAYVVLNHGVEPSPelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1308-1812 1.14e-30

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: 129.54  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1308 NKKENSNSNYLLVHKMFEEQvkrnPNQIAVV-CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMV 1382
Cdd:cd05970    11 NVPENFNFAYDVVDAMAKEY----PDKLALVwCDDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFW 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1383 IGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSII-----KGIEFQGNVIDLMDMSFEEEPG-EDMHMMI 1456
Cdd:cd05970    87 YSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIpeeieKAAPECPSKPKLVWVGDPVPEGwIDFRKLI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 E--------PHNLAY--------VIYTSGSTGQPKgvMIEHR---SLTNFLCAMYedfSQDIGITDNVLFSSSISFDVTI 1517
Cdd:cd05970   167 KnaspdferPTANSYpcgedillVYFSSGTTGMPK--MVEHDftyPLGHIVTAKY---WQNVREGGLHLTVADTGWGKAV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 F-EIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVR-DNQKIVLNKL---LVGVEPIKTEL 1592
Cdd:cd05970   242 WgKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPT----IYRFLIReDLSRYDLSSLrycTTAGEALNPEV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1593 LAKYDHLfrGNLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICIS----- 1667
Cdd:cd05970   318 FNTFKEK--TGIKLMEGFGQTETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgk 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1668 GIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:cd05970   391 PVGLFGGYYKDAEKTAEVWHD-------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1748 VVIDQEDEAGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05970   464 AVTGVPDPIRGQVVKATIVLAKGYEpseelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
283-783 2.25e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 128.71  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  283 EQVKQNPNQIAIVCN-GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK06087   31 QTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  362 QRVEYMLTDSGcSHVL---TYQNSI---------------IKGVAF------QGSVINLMDIPFEEEQVEDlQITMEPQN 417
Cdd:PRK06087  111 AELVWVLNKCQ-AKMFfapTLFKQTrpvdlilplqnqlpqLQQIVGvdklapATSSLSLSQIIADYEPLTT-AITTHGDE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKGVMIEHrsltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVTIF--EIFVPLVCGARMTIYQgeK 494
Cdd:PRK06087  189 LAAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTwQDVFMMPAPLGHATGFlhGVTAPFLIGARSVLLD--I 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  495 FDVPKLVQVILEEQVT--LAYIPptllnEIYDYFVRANQK---ISLNKLFV-GVEPIKTELLakyDHLFRGNLQILNLYG 568
Cdd:PRK06087  263 FTPDACLALLEQQRCTcmLGATP-----FIYDLLNLLEKQpadLSALRFFLcGGTTIPKKVA---RECQQRGIKLLSVYG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  569 PTEAtvccTSYQYERDKEITTQNVPI-GSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAdKFIDHp 647
Cdd:PRK06087  335 STES----SPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE- 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  648 fergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE 725
Cdd:PRK06087  409 ----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERlGER-SCAYVVLK 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313  726 KDIPIP---EVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI-NNLKSSHLEP 783
Cdd:PRK06087  483 APHHSLtleEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDImRRLTQDVCEE 545
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
288-769 7.71e-30

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: 126.08  E-value: 7.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:cd05923    16 DACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  368 LT-DSGCSHVLTyqnsIIKGVAfQGSVINLMDIPFEEEQVEDLQIT----------MEPQNLAYVIYTSGSTGQPKGVMI 436
Cdd:cd05923    96 IErGEMTAAVIA----VDAQVM-DAIFQSGVRVLALSDLVGLGEPEsagpliedppREPEQPAFVFYTSGTTGLPKGAVI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  437 EHRSLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGARmTIYQGEKFDVPKLVQVILEEQVTLAYIPP 516
Cdd:cd05923   171 PQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDG-TYVVVEEFDPADALKLIEQERVTSLFATP 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  517 TLLNEIYDYFVRANQKI-SLNKL-FVGVEpIKTELLAKYDHLFRGnlQILNLYGPTEATvcctSYQYERDKEITTQnvpi 594
Cdd:cd05923   250 THLDALAAAAEFAGLKLsSLRHVtFAGAT-MPDAVLERVNQHLPG--EKVNIYGTTEAM----NSLYMRDARTGTE---- 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  595 GSPLLNTKIY---ILDSFHRLQPIGVPGEICISGIGLA--RGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNI 669
Cdd:cd05923   319 MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  670 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIPEVRAY-LATKLPYYMIP 747
Cdd:cd05923   392 RILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQFcRASELADFKRP 471
                         490       500
                  ....*....|....*....|..
gi 446807313  748 QQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05923   472 RRYFFLDELPKNAMNKVLRRQL 493
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1326-1814 7.90e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 127.17  E-value: 7.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1326 EQVKRNPNQIAVVCNE-KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PRK06087   31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGCS-----------------HVLVHQNSIIKGIEF------QGNVIDLMDMSFEEEPGEDmHMMIEPHNL 1461
Cdd:PRK06087  111 AELVWVLNKCQAKmffaptlfkqtrpvdliLPLQNQLPQLQQIVGvdklapATSSLSLSQIIADYEPLTT-AITTHGDEL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHrsltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVTIF--EIFVPLIYGARMTIYQgeKF 1538
Cdd:PRK06087  190 AAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTwQDVFMMPAPLGHATGFlhGVTAPFLIGARSVLLD--IF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTKLVQVILEEQVTLSY-IPP---TLLNEIydyfvrDNQKIVLNKL---LVGVEPIKTELLakyDHLFRGNLQILNGYG 1611
Cdd:PRK06087  264 TPDACLALLEQQRCTCMLgATPfiyDLLNLL------EKQPADLSALrffLCGGTTIPKKVA---RECQQRGIKLLSVYG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1612 PTEAtvccTSYRYESNKEITTQNVPI-GSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAdKFIDHp 1690
Cdd:PRK06087  335 STES----SPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE- 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 fergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTE 1768
Cdd:PRK06087  409 ----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDErLGER-SCAYVVLK 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 446807313 1769 KDIPIP---EVRAYLATK-LPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:PRK06087  483 APHHSLtleEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1342-1812 8.97e-30

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 127.02  E-value: 8.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1342 KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAY-----LPIDTDLPKQ----RVEYMLT 1412
Cdd:PLN02330   54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFsganpTALESEIKKQaeaaGAKLIVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1413 DS---------GCSHVLVHQNSIIKGIEFQgNVIDLMDMSFEEEPGEDMHMMiephNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PLN02330  134 NDtnygkvkglGLPVIVLGEEKIEGAVNWK-ELLEAADRAGDTSDNEEILQT----DLCALPFSSGTTGISKGVMLTHRN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLCAMYedFSQDIGITDNVLFSSSISFdvtiFEIF-VPLIYGARM----TIYQGEKFDVTKLVQVILEEQVTLSYI- 1557
Cdd:PLN02330  209 LVANLCSSL--FSVGPEMIGQVVTLGLIPF----FHIYgITGICCATLrnkgKVVVMSRFELRTFLNALITQEVSFAPIv 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVR--DNQKIVLNKLLVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATvCCTSYRYESNKE--ITTQ 1633
Cdd:PLN02330  283 PPIILNLVKNPIVEefDLSKLKLQAIMTAAAPLAPELLTAFEAKFPG-VQVQEAYGLTEHS-CITLTHGDPEKGhgIAKK 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NvPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGYINRKELTaDKFIDHpfergEKLYKTGDIARWLPDGNI 1712
Cdd:PLN02330  361 N-SVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET-DRTIDE-----DGWLHTGDIGYIDDDGDI 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE--VRAYLATKLPHYMIP 1790
Cdd:PLN02330  434 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYKKV 513
                         490       500
                  ....*....|....*....|..
gi 446807313 1791 QQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02330  514 RVVQFVDSIPKSLSGKIMRRLL 535
PRK06178 PRK06178
acyl-CoA synthetase; Validated
286-769 1.16e-29

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 126.69  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK06178   44 RERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 YMLTDSGCSHVLTYQN--SIIKGVAFQGSV----------------------------------INLMDIPfEEEQVEDL 409
Cdd:PRK06178  124 YELNDAGAEVLLALDQlaPVVEQVRAETSLrhvivtsladvlpaeptlplpdslraprlaaagaIDLLPAL-RACTAPVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnFLCAMYEDFSQDIGiTDNVLfsssISFdVTIFEI-------FVPLV 482
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGG-EDSVF----LSF-LPEFWIagenfglLFPLF 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  483 CGARMTIYQgeKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKlfVGVEPIKTELLAKYDHLFR--- 558
Cdd:PRK06178  276 SGATLVLLA--RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHpRFAEYDLSSLRQ--VRVVSFVKKLNPDYRQRWRalt 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  559 GNLQILNLYGPTEATVC--CTSYQYERDKEITTQNVPIGSPLLNTKIYILD-SFHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:PRK06178  352 GSVLAEAAWGMTETHTCdtFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNK 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  636 KELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGE 715
Cdd:PRK06178  432 PEATAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKG 504
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  716 KYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPqQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06178  505 QVPVAFVQlkPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1344-1812 2.62e-29

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: 124.65  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL---PIDT--DLPKQrveymLTDSGCSH 1418
Cdd:cd05904    33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLSTpaEIAKQ-----VKDSGAKL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVhQNSIIKGIEFQGNVIDLMD-----------MSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNf 1487
Cdd:cd05904   108 AFT-TAELAEKLASLALPVVLLDsaefdslsfsdLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIA- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV--PLIYGArmTIYQGEKFDVTKLVQVILEEQVT-LSYIPPTLLNE 1564
Cdd:cd05904   186 MVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFAlgLLRLGA--TVVVMPRFDLEELLAAIERYKVThLPVVPPIVLAL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1565 IYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSyryESNKEitTQNVPIGS----- 1639
Cdd:cd05904   264 VKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF-PNVDLGQGYGMTESTGVVAM---CFAPE--KDRAKYGSvgrlv 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSfHRIQPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd05904   338 PNVEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATA-ATID-----KEGWLHTGDLCYIDEDGYLFIVDRLK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-------TEKdipipEVRAYLATKLPHYMIPQQ 1792
Cdd:cd05904   411 ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkpgsslTED-----EIMDFVAKQVAPYKKVRK 485
                         490       500
                  ....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05904   486 VAFVDAIPKSPSGKILRKEL 505
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1320-1812 3.45e-29

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: 124.16  E-value: 3.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKG--ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:cd05923     3 VFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYmLTDSGCSHVLVHQN------SIIKG---IEFQGNVIDLMDMSFEEEPGEDMHMmiEPHNLAYVIYTS 1468
Cdd:cd05923    83 INPRLKAAELAE-LIERGEMTAAVIAVdaqvmdAIFQSgvrVLALSDLVGLGEPESAGPLIEDPPR--EPEQPAFVFYTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 GSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV-PLIYGArmTIYQGEKFDVTKLVQVI 1547
Cdd:cd05923   160 GTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVaALALDG--TYVVVEEFDPADALKLI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1548 LEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEAtvcctsYRYES 1626
Cdd:cd05923   238 EQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLERVNQHLPG--EKVNIYGTTEA------MNSLY 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITTQNVpiGSPLLNTKIY---ILDSFHRIQPIGVPGEICISGIGLA--RGYINRKELTADKFIDhpfergeKLYKTG 1701
Cdd:cd05923   310 MRDARTGTE--MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTEKDIPIPEVRAY- 1779
Cdd:cd05923   381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQFc 460
                         490       500       510
                  ....*....|....*....|....*....|...
gi 446807313 1780 LATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05923   461 RASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1344-1815 1.30e-28

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: 122.44  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDqGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKG-------IEFQGNVIDLMDM----SFEEEPGEDMHMMI--------------EPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:cd05909    87 QFIEKLklhhlfdVEYDARIVYLEDLrakiSKADKCKAFLAGKFppkwllrifgvapvQPDDPAVILFTSGSEGLPKGVV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1479 IEHRSL-TN-FLCAMYEDFSQDigitDNVL----FSSSISFDVTifeIFVPLIYGARMTIYQgEKFDVTKLVQVILEEQV 1552
Cdd:cd05909   167 LSHKNLlANvEQITAIFDPNPE----DVVFgalpFFHSFGLTGC---LWLPLLSGIKVVFHP-NPLDYKKIPELIYDKKA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNeIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITT 1632
Cdd:cd05909   239 TILLGTPTFLR-GYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECSPVISVNTPQSPNKEGT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 QNVPIgsPLLNTKIYILDSfHRIQPIGVPGEICISGIGLARGYINRKELTAdkfidhpFERGEKLYKTGDIARWLPDGNI 1712
Cdd:cd05909   316 VGRPL--PGMEVKIVSVET-HEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT--AVVIDQEDEAGEKYLCayVVTEKDIPIPEVRAYL-ATKLPHYMI 1789
Cdd:cd05909   386 TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNevAVVSVPDGRKGEKIVL--LTTTTDTDPSSLNDILkNAGISNLAK 463
                         490       500
                  ....*....|....*....|....*.
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05909   464 PSYIHQVEEIPLLGTGKPDYVTLKAL 489
PRK08316 PRK08316
acyl-CoA synthetase; Validated
288-769 1.99e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 122.35  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:PRK08316   24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  368 LTDSGCSHVLT----YQNS----------------IIKGVAFQGSVINLMDIpFEEEQVEDLQITMEPQNLAYVIYTSGS 427
Cdd:PRK08316  104 LDHSGARAFLVdpalAPTAeaalallpvdtlilslVLGGREAPGGWLDFADW-AEAGSVAEPDVELADDDLAQILYTSGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  428 TGQPKGVMIEHRSLtnflcaMYEDFSQ----DIGITDNVLFS----SSISFDVtifeIFVPLV-CGARMTIYQGEkfDVP 498
Cdd:PRK08316  183 ESLPKGAMLTHRAL------IAEYVSCivagDMSADDIPLHAlplyHCAQLDV----FLGPYLyVGATNVILDAP--DPE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  499 KLVQVILEEQVTLAYIPPT----LLNeiYDYFVRANQKiSLNKLFVG-----VEPIKtELLAKYDhlfrgNLQILNLYGP 569
Cdd:PRK08316  251 LILRTIEAERITSFFAPPTvwisLLR--HPDFDTRDLS-SLRKGYYGasimpVEVLK-ELRERLP-----GLRFYNCYGQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  570 TE----ATVCctsyqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFID 645
Cdd:PRK08316  322 TEiaplATVL-------GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  646 HPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT- 724
Cdd:PRK08316  395 GWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPk 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 446807313  725 -EKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08316  468 aGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1325-1817 2.48e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 121.89  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1325 EEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLV---HQNSI--IKGIEFQGNVIDLMDMSFE--------EEPGEDMHMMIephnlayvIYTSGS 1470
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVektFQNMAlsMQKVSYVQRVISITSLKEIedrkidnfVEKNESASFII--------CYTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1471 TGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDnvlfsSSISFdVTIFEI-------FVPLIYGARMTIyqGEKFDVTKL 1543
Cdd:PRK06839  161 TGKPKGAVLTQENM--FWNALNNTFAIDLTMHD-----RSIVL-LPLFHIggiglfaFPTLFAGGVIIV--PRKFEPTKA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1544 VQVILEEQVTLSYIPPTL---LNEIYDYFVRDNQKIVLnkLLVGVEPIKTELLAKYDHlfRGnLQILNGYGPTEA--TVC 1618
Cdd:PRK06839  231 LSMIEKHKVTVVMGVPTIhqaLINCSKFETTNLQSVRW--FYNGGAPCPEELMREFID--RG-FLFGQGFGMTETspTVF 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSyryesnKEITTQNV-PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgekl 1697
Cdd:PRK06839  306 MLS------EEDARRKVgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC----- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 ykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE-- 1775
Cdd:PRK06839  375 --TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkd 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 446807313 1776 VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNT 1817
Cdd:PRK06839  453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
1921-2157 3.85e-28

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 114.41  E-value: 3.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMA 2000
Cdd:pfam00975    4 FCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2001 RKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAfEELEKFNDQLGIEKISFEqmseeqlIESLLKKFtlnenscqqnf 2080
Cdd:pfam00975   84 RRLERQGEAVRSLFLSDASAPHTVRYEASRAPDDD-EVVAEFTDEGGTPEELLE-------DEELLSML----------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2081 edpmmnkLKVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNE-YTSGEVYALQVPGSHLSMLEKP----- 2154
Cdd:pfam00975  145 -------LPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWVRdHTPGEFDVHVFDGDHFYLIEHLeavle 217

                   ...
gi 446807313  2155 HIH 2157
Cdd:pfam00975  218 IIE 220
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1328-1807 7.32e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 120.81  E-value: 7.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLV----------------HQNSI----IKGIEFQGNVIDLMDMSFEEEPGE-DMHMMIEphNLAYVIY 1466
Cdd:PRK08316  101 AYILDHSGARAFLVdpalaptaeaalallpVDTLIlslvLGGREAPGGWLDFADWAEAGSVAEpDVELADD--DLAQILY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1467 TSGSTGQPKGVMIEHRSLtnflcaMYEDFSQ----DIGITDNVLFS----SSISFDVtifeIFVPLIY-GARMTIYQGEk 1537
Cdd:PRK08316  179 TSGTESLPKGAMLTHRAL------IAEYVSCivagDMSADDIPLHAlplyHCAQLDV----FLGPYLYvGATNVILDAP- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1538 fDVTKLVQVILEEQVTLSYIPPT----LLNEIyDYFVRDNQKivLNKLLVG-----VEPIKtELLAKYDhlfrgNLQILN 1608
Cdd:PRK08316  248 -DPELILRTIEAERITSFFAPPTvwisLLRHP-DFDTRDLSS--LRKGYYGasimpVEVLK-ELRERLP-----GLRFYN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1609 GYGPTE----ATVCctsyryeSNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAD 1684
Cdd:PRK08316  318 CYGQTEiaplATVL-------GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1685 KFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAY 1764
Cdd:PRK08316  391 AFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 446807313 1765 VVT--EKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK08316  464 VVPkaGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
286-766 9.96e-28

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


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 120.29  E-value: 9.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIV-CNG----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd05970    28 KEYPDKLALVwCDDageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDSGCSHVLTYQNSII-----KGVAFQGSVINL-------MD--IPFEEEqVEDLQITMEP---------QN 417
Cdd:cd05970   108 AKDIVYRIESADIKMIVAIAEDNIpeeieKAAPECPSKPKLvwvgdpvPEgwIDFRKL-IKNASPDFERptansypcgED 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKgvMIEHR---SLTNFLCAMYedfSQDIGITDNVLFSSSISFDVTIF-EIFVPLVCGARMTIYQGE 493
Cdd:cd05970   187 ILLVYFSSGTTGMPK--MVEHDftyPLGHIVTAKY---WQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYD 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  494 KFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN-QKISLNKL---FVGVEPIKTELLAKYDHLfrGNLQILNLYGP 569
Cdd:cd05970   262 KFDPKALLEKLSKYGVTTFCAPPT----IYRFLIREDlSRYDLSSLrycTTAGEALNPEVFNTFKEK--TGIKLMEGFGQ 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  570 TEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICIS-----GIGLARGYINRKELTADKFI 644
Cdd:cd05970   336 TETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVWH 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  645 DhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT 724
Cdd:cd05970   411 D-------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446807313  725 EKDIP-----IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd05970   484 AKGYEpseelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
PRK06188 PRK06188
acyl-CoA synthetase; Validated
415-769 1.24e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 120.09  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFS--QDIgitdNVLFSSSISFDVTIFeiFVP-LVCGArmTIYQ 491
Cdd:PRK06188  167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEwpADP----RFLMCTPLSHAGGAF--FLPtLLRGG--TVIV 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  492 GEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLqILNLYGPT 570
Cdd:PRK06188  239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHpDLRTRDLSSLETVYYGASPMSPVRLAEAIERF-GPI-FAQYYGQT 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  571 EATVcCTSYQYERDKEITTQNV--PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpf 648
Cdd:PRK06188  317 EAPM-VITYLRKRDHDPDDPKRltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----- 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  649 eRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKD 727
Cdd:PRK06188  391 -RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEA-VTAVVVLRPG 467
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446807313  728 IPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06188  468 AAVdaAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1332-1812 5.85e-27

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


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 117.40  E-value: 5.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQnsiikgiEFQGN-VIDLMDMSFEEEPGEDMHMMIEphnlayVIYTSGSTGQPKGVMIEHRSLtnFLCA 1490
Cdd:cd12118    98 RHSEAKVLFVDR-------EFEYEdLLAEGDPDFEWIPPADEWDPIA------LNYTSGTTGRPKGVVYHHRGA--YLNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MyedfsqdigitDNVLFSSSISFDVTIFEI---------FVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd12118   163 L-----------ANILEWEMKQHPVYLWTLpmfhcngwcFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIYDYFVRDNQKI--VLNKLLVGVEPIKTeLLAKYDHLfrgNLQILNGYGPTE----ATVCctSYRYESNKEITT--- 1632
Cdd:cd12118   232 LNMLANAPPSDARPLphRVHVMTAGAPPPAA-VLAKMEEL---GFDVTHVYGLTEtygpATVC--AWKPEWDELPTEera 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 -----QNVPIgspLLNTKIYILDSfHRIQPigVP------GEICISGIGLARGYINRKELTADKFidhpfeRGeKLYKTG 1701
Cdd:cd12118   306 rlkarQGVRY---VGLEEVDVLDP-ETMKP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF------RG-GWFHSG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYV-------VTEKDIpi 1773
Cdd:cd12118   373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEV-PCAFVelkegakVTEEEI-- 449
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313 1774 pevRAYLATKLPHYMIPQQLIPIHnIPLTQNGKIDRSKL 1812
Cdd:cd12118   450 ---IAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
283-769 8.24e-27

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: 116.66  E-value: 8.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  283 EQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGayLPIdTELPKQ 362
Cdd:cd05920    23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV-LALPSH 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  363 RveymltdsgcSHVLTYQNSIIKGVAFQGS-VINLMDipFEEEQVEDLQITMEPqnlAYVIYTSGSTGQPKGVMIEHRSL 441
Cdd:cd05920   100 R----------RSELSAFCAHAEAVAYIVPdRHAGFD--HRALARELAESIPEV---ALFLLSGGTTGTPKLIPRTHNDY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  442 ----------------TNFLCAMyedfsqdiGITDNVLFSSSISFDVtifeifvpLVCGARMTIYQ----GEKFDVpklv 501
Cdd:cd05920   165 aynvrasaevcgldqdTVYLAVL--------PAAHNFPLACPGVLGT--------LLAGGRVVLAPdpspDAAFPL---- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  502 qvILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQ 580
Cdd:cd05920   225 --IEREGVTVTALVPALVSLWLDAAASRRADLsSLRLLQVGGARLSPALARRVPPVLGCTLQ--QVFGMAEGLLNYTRLD 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  581 YERDKEITTQNVPIgSPllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYI-----NRKELTADKFidhpfergeklY 655
Cdd:cd05920   301 DPDEVIIHTQGRPM-SP--DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYrapehNARAFTPDGF-----------Y 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVV-TEKDIPIPEV 733
Cdd:cd05920   367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGER-SCAFVVlRDPPPSAAQL 445
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446807313  734 RAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05920   446 RRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK06145 PRK06145
acyl-CoA synthetase; Validated
286-769 9.76e-27

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 116.91  E-value: 9.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK06145   13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 YMLTDSGCSHVLTYQN----------SIIKGVAFQGSVINLMDIPFEEEQvedlQITMEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:PRK06145   93 YILGDAGAKLLLVDEEfdaivaletpKIVIDAAAQADSRRLAQGGLEIPP----QAAVAPTDLVRLMYTSGTTDRPKGVM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  436 IehrSLTNFlcaMYEDFSQDI--GIT-DNVLFSSSISFDVTIFEI--FVPLVCGARMTIYQgeKFDVPKLVQVILEEQVT 510
Cdd:PRK06145  169 H---SYGNL---HWKSIDHVIalGLTaSERLLVVGPLYHVGAFDLpgIAVLWVGGTLRIHR--EFDPEAVLAAIERHRLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  511 LAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEAtvCCTSYQYERDKEITT 589
Cdd:PRK06145  241 CAWMAPVMLSRVLTVPDRDRFDLdSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTET--CSGDTLMEAGREIEK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  590 qnvpIGS---PLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPD 666
Cdd:PRK06145  318 ----IGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVVTE-KDIPIPEVRAYLATKLPYY 744
Cdd:PRK06145  387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVVLNPgATLTLEALDRHCRQRLASF 466
                         490       500
                  ....*....|....*....|....*
gi 446807313  745 MIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06145  467 KVPRQLKVRDELPRNPSGKVLKRVL 491
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1320-1812 1.08e-26

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 117.44  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGC----------------------SHVLV--------------------HQNSIIKGIEfQGNVI 1437
Cdd:PRK06710  106 PLYTERELEYQLHDSGAkvilcldlvfprvtnvqsatkiEHVIVtriadflpfpknllypfvqkKQSNLVVKVS-ESETI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 DLMDmSFEEEPGEDMHMMIEPHN-LAYVIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEDFsqdigitdNVLFSSSISFDV 1515
Cdd:PRK06710  185 HLWN-SVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLY--------NCKEGEEVVLGV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TIFEIFVPLIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPI 1588
Cdd:PRK06710  256 LPFFHVYGMTAVMNLSIMQGykmvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpLLKEYDISSIRACISGSAPL 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1589 KTELLAKYDHLFRGNLqiLNGYGPTEAT-VCCTSYRYEsnkeittQNVP--IGSPLLNTKIYI--LDSFHRIQPiGVPGE 1663
Cdd:PRK06710  336 PVEVQEKFETVTGGKL--VEGYGLTESSpVTHSNFLWE-------KRVPgsIGVPWPDTEAMImsLETGEALPP-GEIGE 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 1743
Cdd:PRK06710  406 IVVKGPQIMKGYWNKPEETAAVLQD-------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEK 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1744 IKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE------VRAYLATklphYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06710  479 VQEVVTIGVPDPYRGETVKAFVVLKEGTECSEeelnqfARKYLAA----YKVPKVYEFRDELPKTTVGKILRRVL 549
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
268-766 1.11e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 117.57  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  268 KTLLCETVtaPQLFEEQVKQNPNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGI 345
Cdd:PRK12583   13 KPLLTQTI--GDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  346 LKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLT--------YQN---SIIKGVAFQGS-------------VINL----- 396
Cdd:PRK12583   91 ARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdYHAmlqELLPGLAEGQPgalacerlpelrgVVSLapapp 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  397 ------MDIPFEEEQV--EDL---QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAmyedfsQDIGITDnvl 463
Cdd:PRK12583  171 pgflawHELQARGETVsrEALaerQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNngYFVA------ESLGLTE--- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  464 fSSSISFDVTIFEIF----VPLVC---GARMtIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANqkISLN 536
Cdd:PRK12583  242 -HDRLCVPVPLYHCFgmvlANLGCmtvGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGN--FDLS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  537 KLFVGV---EPIKTELLAK-YDHLFRGNLQILnlYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIyiLDSFHRL 612
Cdd:PRK12583  318 SLRTGImagAPCPIEVMRRvMDEMHMAEVQIA--YGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKV--VDPDGAT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  613 QPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEI 691
Cdd:PRK12583  394 VPRGEIGELCTRGYSVMKGYWNNPEATA-ESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREI 466
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  692 EASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE--KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:PRK12583  467 EEFLFTHPAVADVQVFGVPDEKyGEE-IVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1324-1812 1.17e-26

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 117.08  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKG------ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:PRK13295   30 LDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLVHQnsIIKGIEFQGNVIDLM----------------DMSFEE-------EPGEDMHM 1454
Cdd:PRK13295  110 LMPIFRERELSFMLKHAESKVLVVPK--TFRGFDHAAMARRLRpelpalrhvvvvggdgADSFEAllitpawEQEPDAPA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1455 MIE-----PHNLAYVIYTSGSTGQPKGVMieHRSltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLIY 1526
Cdd:PRK13295  188 ILArlrpgPDDVTQLIYTSGTTGEPKGVM--HTA--NTLMANIVPYAERLGLGaDDVILMASPMAHQTgfMYGLMMPVML 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 GARMtIYQgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfVRDNQKIV--LNKLLVGVEPIKTELLAKYDHLFrgNL 1604
Cdd:PRK13295  264 GATA-VLQ-DIWDPARAAELIRTEGVTFTMASTPFLTDLTRA-VKESGRPVssLRTFLCAGAPIPGALVERARAAL--GA 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPTE-ATVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTA 1683
Cdd:PRK13295  339 KIVSAWGMTEnGAVTLTKLDDPDERASTTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1684 DKFidhpfergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIRG-YRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyL 1761
Cdd:PRK13295  415 TDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERlGER-A 484
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1762 CAYVVTE--KDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK13295  485 CAFVVPRpgQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
301-766 2.01e-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: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 114.92  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyq 380
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  381 nsiikgvafqgsvinlmDIPFEEEQVEDLQITMepqnlayviYTSGSTGQPKGVMIEHRSLTNFlcAMYEDFSQDIGITD 460
Cdd:cd05973    79 -----------------DAANRHKLDSDPFVMM---------FTSGTTGLPKGVPVPLRALAAF--GAYLRDAVDLRPED 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  461 NVLFSSSISFDVTIF-EIFVPLVCGARMTIYQGeKFDVPKLVQVILEEQVTLAYIPPTllneIYDYF------VRANQKI 533
Cdd:cd05973   131 SFWNAADPGWAYGLYyAITGPLALGHPTILLEG-GFSVESTWRVIERLGVTNLAGSPT----AYRLLmaagaeVPARPKG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  534 SLNKLFVGVEPIKTELLakydHLFRGNL--QILNLYGPTE-ATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFH 610
Cdd:cd05973   206 RLRRVSSAGEPLTPEVI----RWFDAALgvPIHDHYGQTElGMVLANHHALEHPVHAGS----AGRAMPGWRVAVLDDDG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  611 RLQPIGVPGEICI----SGIGLARGYINRKELTADKfidhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd05973   278 DELGPGEPGRLAIdianSPLMWFRGYQLPDTPAIDG----------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-TEKDIPIPEVRAYLA----TKLPYYMIPQQIISIQNIPLTQN 761
Cdd:cd05973   348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPS 427

                  ....*
gi 446807313  762 GKIDR 766
Cdd:cd05973   428 GKIQR 432
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
302-769 2.70e-26

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: 115.81  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  302 TYKQLNIKANQLARRLLDQGVKREFIVGVMM---ERSIEMIVGILGIlkagGAYL-PIDTELPKQRVEYMLTDSGcSHVL 377
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM----GAVLhTINPRLFPEQIAYIINHAE-DRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 TYQNSI------IKG--------VAFQGSVINLMDIPFEEEQVEDLQITMEP--------QNLAYVI-YTSGSTGQPKGV 434
Cdd:cd12119   102 FVDRDFlplleaIAPrlptvehvVVMTDDAAMPEPAGVGVLAYEELLAAESPeydwpdfdENTAAAIcYTSGTTGNPKGV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  435 MIEHRSLtnFLCAMyedfsqDIGITDNVLFSSSISF--DVTIFEI------FVPLVCGARMtIYQGEKFDVPKLVQVILE 506
Cdd:cd12119   182 VYSHRSL--VLHAM------AALLTDGLGLSESDVVlpVVPMFHVnawglpYAAAMVGAKL-VLPGPYLDPASLAELIER 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  507 EQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFrgnLQILNLYGPTEATVCCTSYQY---- 581
Cdd:cd12119   253 EGVTFAAGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTETSPLGTVARPpseh 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  582 ------ERDKEITTQNVPIgsPLLNTKIYILDSfhrlqpIGVP------GEICISGIGLARGYINRKELTADKFIDHPFe 649
Cdd:cd12119   330 snlsedEQLALRAKQGRPV--PGVELRIVDDDG------RELPwdgkavGELQVRGPWVTKSYYKNDEESEALTEDGWL- 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  650 rgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLcAYVV----- 723
Cdd:cd12119   401 ------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPL-AVVVlkega 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313  724 --TEKdipipEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd12119   474 tvTAE-----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1323-1812 2.92e-26

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: 116.01  E-value: 2.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPIDTdL 1402
Cdd:COG1021    30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVFA-L 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQR-------------VEYMLTD------------------SGCSHVLVHQNSiikgiefqGNVIDLMDMsfEEEPGED 1451
Cdd:COG1021   107 PAHRraeishfaeqseaVAYIIPDrhrgfdyralarelqaevPSLRHVLVVGDA--------GEFTSLDAL--LAAPADL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR----SL------------TNFLCAMyedfsqdiGITDN----------- 1504
Cdd:COG1021   177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVrasaeicgldadTVYLAAL--------PAAHNfplsspgvlgv 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 ------VLFSSSISFDvTIFeifvPLIygARmtiyqgEKFDVTKLVqvileeqvtlsyiPPTLLN-----EIYDYFVRDn 1573
Cdd:COG1021   249 lyaggtVVLAPDPSPD-TAF----PLI--ER------ERVTVTALV-------------PPLALLwldaaERSRYDLSS- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 qkivLNKLLVG--------VEPIKTELLAKYDHLFrgnlqilngyGPTEATVCCTsyRYESNKEI--TTQNVPIgSPLln 1643
Cdd:COG1021   302 ----LRVLQVGgaklspelARRVRPALGCTLQQVF----------GMAEGLVNYT--RLDDPEEVilTTQGRPI-SPD-- 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1644 TKIYILDSFHRIQPIGVPGEICISGIGLARGY-----INRKELTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRV 1718
Cdd:COG1021   363 DEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYyrapeHNARAFTPDGF-----------YRTGDLVRRTPDGYLVVEGRA 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1719 DHQVkIR-GYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVT-EKDIPIPEVRAYLATK-LPHYMIPQQLI 1794
Cdd:COG1021   432 KDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYlGER-SCAFVVPrGEPLTLAELRRFLRERgLAAFKLPDRLE 509
                         570
                  ....*....|....*...
gi 446807313 1795 PIHNIPLTQNGKIDRSKL 1812
Cdd:COG1021   510 FVDALPLTAVGKIDKKAL 527
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1340-1771 3.61e-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: 114.76  E-value: 3.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCShV 1419
Cdd:cd17640     2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV-A 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1420 LVHQNSiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDI 1499
Cdd:cd17640    81 LVVEND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1500 GitDNVL------FSSSISFDVTIFEIFVPLIYGARMTIyqgeKFDVTKLVQVILeeqVTLSYIPPTLLNEIYDYFVRDN 1573
Cdd:cd17640   129 G--DRFLsilpiwHSYERSAEYFIFACGCSQAYTSIRTL----KDDLKRVKPHYI---VSVPRLWESLYSGIQKQVSKSS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 --QKIVLNKLLVGVEpIKTEL-----LAKY-DHLFRG-NLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNT 1644
Cdd:cd17640   200 piKQFLFLFFLSGGI-FKFGIsgggaLPPHvDTFFEAiGIEVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGT 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1645 KIYILDSFHR-IQPIGVPGEICISGIGLARGYINRKELTAdKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRV-DHQV 1722
Cdd:cd17640   274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATS-KVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIV 347
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 446807313 1723 KIRGYRIELGEIEASLLKYETIKTAVVIDQEdeagEKYLCAYVVTEKDI 1771
Cdd:cd17640   348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNFEE 392
PLN02246 PLN02246
4-coumarate--CoA ligase
297-769 4.70e-26

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 115.08  E-value: 4.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA-------YLPidTELPKQrveymLT 369
Cdd:PLN02246   47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTP--AEIAKQ-----AK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  370 DSGCSHVLTYQNSI--IKGVAFQGSV-INLMDIPFE------------EEQVEDLQItmEPQNLAYVIYTSGSTGQPKGV 434
Cdd:PLN02246  120 ASGAKLIITQSCYVdkLKGLAEDDGVtVVTIDDPPEgclhfseltqadENELPEVEI--SPDDVVALPYSSGTTGLPKGV 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  435 MIEHRSLTNflcamyeDFSQDI-GITDNVLFSSSisfDVTI-----FEIFV---PLVCGARM--TIYQGEKFDVPKLVQV 503
Cdd:PLN02246  198 MLTHKGLVT-------SVAQQVdGENPNLYFHSD---DVILcvlpmFHIYSlnsVLLCGLRVgaAILIMPKFEIGALLEL 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  504 ILEEQVTLA-YIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELlakyDHLFRGNLQILNL---YGPTEA-TVCCTS 578
Cdd:PLN02246  268 IQRHKVTIApFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKEL----EDAFRAKLPNAVLgqgYGMTEAgPVLAMC 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  579 YQYErdKE-ITTQNVPIGSPLLNTKIYILD-----SFHRLQPigvpGEICISGIGLARGYINRKELTAdKFIDHpfergE 652
Cdd:PLN02246  344 LAFA--KEpFPVKSGSCGTVVRNAELKIVDpetgaSLPRNQP----GEICIRGPQIMKGYLNDPEATA-NTIDK-----D 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  653 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE 732
Cdd:PLN02246  412 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE 491
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313  733 --VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PLN02246  492 deIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1326-1812 5.03e-26

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: 114.35  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1326 EQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPIDTdLPKQ 1405
Cdd:cd05920    23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVLA-LPSH 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1406 R---VEYMLTDSGCSHVLVHqnsiikgiefqgnvidlmDMSFEEEPGEDMHMMIEPHN-LAYVIYTSGSTGQPKGVMIEH 1481
Cdd:cd05920   100 RrseLSAFCAHAEAVAYIVP------------------DRHAGFDHRALARELAESIPeVALFLLSGGTTGTPKLIPRTH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1482 RSL----------------TNFLCAMyedfsqdiGITDNVLFSSSISFDVtifeifvpLIYGARMTIYQ-GEKFDVTKLV 1544
Cdd:cd05920   162 NDYaynvrasaevcgldqdTVYLAVL--------PAAHNFPLACPGVLGT--------LLAGGRVVLAPdPSPDAAFPLI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1545 QvilEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLL-VGVEPIKTELLAKYDHLFRGNLQILngYGPTEATVCCTSYR 1623
Cdd:cd05920   226 E---REGVTVTALVPALVSLWLDAAASRRADLSSLRLLqVGGARLSPALARRVPPVLGCTLQQV--FGMAEGLLNYTRLD 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1624 YESNKEITTQNVPIgSPllNTKIYILDSFHRIQPIGVPGEICISGIGLARGYI-----NRKELTADKFidhpfergeklY 1698
Cdd:cd05920   301 DPDEVIIHTQGRPM-SP--DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYrapehNARAFTPDGF-----------Y 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1699 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVV-TEKDIPIPEV 1776
Cdd:cd05920   367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGER-SCAFVVlRDPPPSAAQL 445
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446807313 1777 RAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05920   446 RRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
289-769 5.41e-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: 5.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTYQnsiikgvAFQG-SVINLMDIPFEEEQVEDlqitmEPQNLAyVIYTSGSTGQPKGVMIEHRSLtnFLCA 447
Cdd:cd12118    98 RHSEAKVLFVDR-------EFEYeDLLAEGDPDFEWIPPAD-----EWDPIA-LNYTSGTTGRPKGVVYHHRGA--YLNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  448 MyedfsqdigitDNVLFSSSISFDV--TIFEIF----------VPLVCGarmTIYQGEKFDVPKLVQVILEEQVTLAYIP 515
Cdd:cd12118   163 L-----------ANILEWEMKQHPVylWTLPMFhcngwcfpwtVAAVGG---TNVCLRKVDAKAIYDLIEKHKVTHFCGA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  516 PTLLNEIYDYFVRANQKIS--LNKLFVGVEPIKTeLLAKYDHLfrgNLQILNLYGPTE----ATVCCTSYQY------ER 583
Cdd:cd12118   229 PTVLNMLANAPPSDARPLPhrVHVMTAGAPPPAA-VLAKMEEL---GFDVTHVYGLTEtygpATVCAWKPEWdelpteER 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  584 DKEITTQNVPIgspLLNTKIYILDSfHRLQPigVP------GEICISGIGLARGYINRKELTADKFidhpfeRGeKLYKT 657
Cdd:cd12118   305 ARLKARQGVRY---VGLEEVDVLDP-ETMKP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF------RG-GWFHS 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  658 GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYV-------VTEKDIp 729
Cdd:cd12118   372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEV-PCAFVelkegakVTEEEI- 449
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 446807313  730 ipevRAYLATKLPYYMIPQQIIsIQNIPLTQNGKIDRKKL 769
Cdd:cd12118   450 ----IAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVL 484
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
415-769 6.80e-26

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 117.33  E-value: 6.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRS-LTNFlcamyEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLVCGARM 487
Cdd:PRK08633  781 PDDTATIIFSSGSEGEPKGVMLSHHNiLSNI-----EQISDVFNLRndDVILsslpFFHSFGLTVT---LWLPLLEGIKV 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  488 tIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNeIYDYFVRANQKI--SLNKLFVGVEPIKTELLAKYDHLFrgNLQILN 565
Cdd:PRK08633  853 -VYHPDPTDALGIAKLVAKHRATILLGTPTFLR-LYLRNKKLHPLMfaSLRLVVAGAEKLKPEVADAFEEKF--GIRILE 928
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  566 LYGPTEAT-VCCTSYQYERDKEITTQ----NVPIGSPLLNTKIYILD--SFHRLqPIGVPGEICISGIGLARGYINRKEL 638
Cdd:PRK08633  929 GYGATETSpVASVNLPDVLAADFKRQtgskEGSVGMPLPGVAVRIVDpeTFEEL-PPGEDGLILIGGPQVMKGYLGDPEK 1007
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  639 TAD--KFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY---ETIKTAVVIQREDES 713
Cdd:PRK08633 1008 TAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKK 1082
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313  714 GEKylCAYVVTEKDIPIPEVRAYLA-TKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08633 1083 GEK--LVVLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1332-1808 1.09e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 114.21  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK07798   17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGcSHVLVHQNS-----------------IIK-----GIEFQGNVIDLMDM--------SFEEEPGEDMhmmiephnl 1461
Cdd:PRK07798   97 DDSD-AVALVYEREfaprvaevlprlpklrtLVVvedgsGNDLLPGAVDYEDAlaagsperDFGERSPDDL--------- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 aYVIYTSGSTGQPKGVMIEH----RSLTNFLCAMYEDFSQDI-GITDNVLFSSSisfdvTIFEIFVPLIYGARMT----- 1531
Cdd:PRK07798  167 -YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEeELAKRAAAGPG-----MRRFPAPPLMHGAGQWaafaa 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1532 --------IYQGEKFDVTKLVQVILEEQVTLSYI-------PptLLNEI-----YDyfvrdnqkivLNKLLV----GV-- 1585
Cdd:PRK07798  241 lfsgqtvvLLPDVRFDADEVWRTIEREKVNVITIvgdamarP--LLDALeargpYD----------LSSLFAiasgGAlf 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1586 -EPIKTELLakyDHLfrGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSpllNTKIyILDSFHRIQP-IGVPGE 1663
Cdd:PRK07798  309 sPSVKEALL---ELL--PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV-LDEDGNPVEPgSGEIGW 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISG-IGLarGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:PRK07798  380 IARRGhIPL--GYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHP 454
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1743 TIKTAVVIDQEDEAGEKYLCAyVVTEKDIPIP---EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK07798  455 DVADALVVGVPDERWGQEVVA-VVQLREGARPdlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
276-769 1.43e-25

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: 113.70  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGayLPI 355
Cdd:COG1021    26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTeLPKQR-------------VEYMLTD---------------SGCSHVltyQNSIIKGVAfqGSVINLMDIPfeEEQVE 407
Cdd:COG1021   104 FA-LPAHRraeishfaeqseaVAYIIPDrhrgfdyralarelqAEVPSL---RHVLVVGDA--GEFTSLDALL--AAPAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  408 DLQITMEPQNLAYVIYTSGSTGQPKGVMIEHR----SL------------TNFLCAMyedfsqdiGITDNVLFSSsisfd 471
Cdd:COG1021   176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVrasaeicgldadTVYLAAL--------PAAHNFPLSS----- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  472 vtiFEIFVPLVCGARMTIYQGEKFDVpkLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVG--------V 542
Cdd:COG1021   243 ---PGVLGVLYAGGTVVLAPDPSPDT--AFPLIERERVTVTALVPPLALLWLDAAERSRYDLsSLRVLQVGgaklspelA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 EPIKTELLAKydhlfrgnLQilNLYGPTEATVCCTSYQYERDKEITTQNVPIgSPLlnTKIYILDSFHRLQPIGVPGEIC 622
Cdd:COG1021   318 RRVRPALGCT--------LQ--QVFGMAEGLVNYTRLDDPEEVILTTQGRPI-SPD--DEVRIVDEDGNPVPPGEVGELL 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  623 ISGIGLARGY-----INRKELTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLL 696
Cdd:COG1021   385 TRGPYTIRGYyrapeHNARAFTPDGF-----------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLL 452
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  697 KYETIKTAVVIQREDES-GEKyLCAYVVT-EKDIPIPEVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:COG1021   453 AHPAVHDAAVVAMPDEYlGER-SCAFVVPrGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
870-1285 1.48e-25

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


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 111.62  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  870 QEYYLASTSQkrmfivdqfedgTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF-QILDGELVQKIEPNVDF 948
Cdd:cd19545     8 QEGLMALTAR------------QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  949 NIEYVHVNEkdaDYLIHEFISPFDLSKPPLLRVLLLRIAEERHiLVVDMHHIISDGLSMGILIKEFVELYKGNELPKlRV 1028
Cdd:cd19545    76 SWTESTSLD---EYLEEDRAAPMGLGGPLVRLALVEDPDTERY-FVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1029 QYKDYVmwqngPYYKNLISEQ-KNYWLTTLKGELPVlNFPTdFQRPTIQSFKGNVCSFNLgtdltfkVNKLATETGTTPY 1107
Cdd:cd19545   151 PFSRFV-----KYLRQLDDEAaAEFWRSYLAGLDPA-VFPP-LPSSRYQPRPDATLEHSI-------SLPSSASSGVTLA 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1108 MILLAIYNILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAyenqdYP 1185
Cdd:cd19545   217 TVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM-----IP 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1186 FEELleGL----DLHRDTSRNPLFDTMFVFQ-----------NMDMNPISIGELEFTPYPfkqsvskfdLSLVATEIDNN 1250
Cdd:cd19545   292 FEHT--GLqnirRLGPDARAACNFQTLLVVQpalpsstseslELGIEEESEDLEDFSSYG---------LTLECQLSGSG 360
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 446807313 1251 IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19545   361 LRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1327-1812 1.79e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 112.98  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PRK09088    4 HARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGcSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPgeDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL 1484
Cdd:PRK09088   84 SELDALLQDAE-PRLLLGDDAVAAGRTDVEDLAAFIASADALEP--ADTPSIPPERVSLILFTSGTSGQPKGVMLSERNL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1485 ----TNFlcamyedfsqdiGITDNVLFSSSISFDVTIFEIfVPLIYGARMTIYQGEkfdvTKLVQVILEEQVTLSYIP-P 1559
Cdd:PRK09088  161 qqtaHNF------------GVLGRVDAHSSFLCDAPMFHI-IGLITSVRPVLAVGG----SILVSNGFEPKRTLGRLGdP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLlnEIYDYF--------VRDNQKIV------LNKLLVGVEP-IKTELLAKYDHlfrgNLQILNGYGPTEA------TVC 1618
Cdd:PRK09088  224 AL--GITHYFcvpqmaqaFRAQPGFDaaalrhLTALFTGGAPhAAEDILGWLDD----GIPMVDGFGMSEAgtvfgmSVD 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSYRYESNkeittqNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLY 1698
Cdd:PRK09088  298 CDVIRAKAG------AAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1699 KTGDIARWLPDGnieYLGRVDHQVKI---RGYRIELGEIEASLLKYETIKTAVVIDQED-EAGEKYLCAYVVTEKDIPIP 1774
Cdd:PRK09088  364 RTGDIARRDADG---FFWVVDRKKDMfisGGENVYPAEIEAVLADHPGIRECAVVGMADaQWGEVGYLAIVPADGAPLDL 440
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313 1775 E-VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK09088  441 ErIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
284-769 1.99e-25

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


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 114.27  E-value: 1.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   284 QVKQNPNQIAIVCNG------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILG------------- 344
Cdd:TIGR02188   66 HLEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLAcarigaihsvvfg 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   345 ----------ILKA-------------GGAYLPIdtelpKQRVEYMLTDSGCS--HVLTYQNSIIKGVAFQGSvinlMDI 399
Cdd:TIGR02188  146 gfsaealadrINDAgaklvitadeglrGGKVIPL-----KAIVDEALEKCPVSveHVLVVRRTGNPVVPWVEG----RDV 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   400 PFEEEqVEDLQITMEPQNLA-----YVIYTSGSTGQPKGVMieHRSLTNFLCAMY----------EDF---SQDIG-ITD 460
Cdd:TIGR02188  217 WWHDL-MAKASAYCEPEPMDsedplFILYTSGSTGKPKGVL--HTTGGYLLYAAMtmkyvfdikdGDIfwcTADVGwITG 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   461 NvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPT---LLNEIYDYFVRANQ 531
Cdd:TIGR02188  294 H----SYI--------VYGPLANGATTVMFEG----VPtypdpgRFWEIIEKHKVTIFYTAPTairALMRLGDEWVKKHD 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   532 KISLNKL-FVGvEPIKTELLAKYDHLFrgnlqilnlyGPTEATVCCTSYQYERDKEITTqnvPI--------GS---PLL 599
Cdd:TIGR02188  358 LSSLRLLgSVG-EPINPEAWMWYYKVV----------GKERCPIVDTWWQTETGGIMIT---PLpgatptkpGSatlPFF 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   600 NTKIYILD-SFHRLQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 676
Cdd:TIGR02188  424 GIEPAVVDeEGNPVEGPGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVD 499
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   677 HQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPI-----PEVRAYLATKLPYYMIPQQII 751
Cdd:TIGR02188  500 DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPddelrKELRKHVRKEIGPIAKPDKIR 579
                          570
                   ....*....|....*...
gi 446807313   752 SIQNIPLTQNGKIDRKKL 769
Cdd:TIGR02188  580 FVPGLPKTRSGKIMRRLL 597
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
277-767 2.20e-25

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: 113.74  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  277 APQLFEEQVKQNPNQIAIVCNG-----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA 351
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  352 YLPIDTELPKQRVEYMLTDSG--------------------------CSHVLTYQNSIIK---GVAFQGSVINLMDIPFE 402
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEakalitadgftrrgrevnlkeeadkaCAQCPTVEKVVVVrhlGNDFTPAKGRDLSYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  403 EEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYED--FSQDIGITDNVLFSSSISFDVTIFEIFVP 480
Cdd:cd05968   223 KETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVH---AGFPLKAAQDmyFQFDLKPGDLLTWFTDLGWMMGPWLIFGG 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  481 LVCGARMTIYQG-EKFDVP-KLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPIKTE-LLAKYD 554
Cdd:cd05968   300 LILGATMVLYDGaPDHPKAdRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEpWNWLFE 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  555 HLFRGNLQILNLYGPTEAT---VCCtsYQYERDKEITtqnvpIGSPLLNTKIYILDSfhRLQPI-GVPGEICISG--IGL 628
Cdd:cd05968   380 TVGKGRNPIINYSGGTEISggiLGN--VLIKPIKPSS-----FNGPVPGMKADVLDE--SGKPArPEVGELVLLApwPGM 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  629 ARGYInRKEltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ 708
Cdd:cd05968   451 TRGFW-RDE---DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  709 REDE-SGEKYLCaYVVTEKDI-PIP----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd05968   527 VPHPvKGEAIVC-FVVLKPGVtPTEalaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRR 590
PRK07798 PRK07798
acyl-CoA synthetase; Validated
276-765 4.31e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 112.29  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTELPKQRVEYMLTDSGcSHVLTYQNSIIKGVA----------------------FQGSVINLMDI--------PFEEEQ 405
Cdd:PRK07798   84 NYRYVEDELRYLLDDSD-AVALVYEREFAPRVAevlprlpklrtlvvvedgsgndLLPGAVDYEDAlaagsperDFGERS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  406 VEDLqitmepqnlaYVIYTSGSTGQPKGVMIEH----RSLTNFLCAMYEDFSQDI-GITDNVLFS-SSISFDV------- 472
Cdd:PRK07798  163 PDDL----------YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEeELAKRAAAGpGMRRFPApplmhga 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  473 TIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTL------AYIPPtLLNEI-----YDyfvranqkisLNKLFV- 540
Cdd:PRK07798  233 GQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVitivgdAMARP-LLDALeargpYD----------LSSLFAi 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  541 ---GV---EPIKTELLakyDHLfrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSpllNTKIyILDSFHRLQP 614
Cdd:PRK07798  302 asgGAlfsPSVKEALL---ELL--PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV-LDEDGNPVEP 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  615 -IGVPGEICISG-IGLarGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:PRK07798  373 gSGEIGWIARRGhIPL--GYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  693 ASLLKYETIKTAVVIQREDESGEKYLCAyVVTEKDIPIP---EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK07798  448 EALKAHPDVADALVVGVPDERWGQEVVA-VVQLREGARPdlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
7-257 5.14e-25

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: 110.89  E-value: 5.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313     7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:pfam00668  182 LQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    87 LLSRYTDKDDVVIGMPVfkQGQEETVFQN------NFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:pfam00668  262 LLSRYTGQDDIVVGTPG--SGRPSPDIERmvgmfvNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLR 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   161 LDGESNNLPLLNTIVMLD---------DIHcYESTDKINSDMVIRFMKN----------EEQLKVQVDYNSTLYSEGLVS 221
Cdd:pfam00668  340 LPRDLSRHPLFDPMFSFQnylgqdsqeEEF-QLSELDLSVSSVIEEEAKydlsltaserGGGLTIKIDYNTSLFDEETIE 418
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 446807313   222 RIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQIL 257
Cdd:pfam00668  419 RFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
261-769 7.08e-25

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 112.05  E-value: 7.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  261 NHTTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIV 340
Cdd:PRK06710   10 SYPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  341 GILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGS-------VINLMD-IPF----------- 401
Cdd:PRK06710   90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSAtkiehviVTRIADfLPFpknllypfvqk 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  402 ---------------------EEEQVEDLQITMEPQN-LAYVIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEDFsqdigi 458
Cdd:PRK06710  170 kqsnlvvkvsesetihlwnsvEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLY------ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  459 tdNVLFSSSISFDVTIFEIFVPLVCGARMTIYQG------EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK 532
Cdd:PRK06710  244 --NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGykmvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  533 I-SLNKLFVGVEPIKTELLAKYDHLFRGNLqiLNLYGPTEAT-VCCTSYQYERdkeittqNVP--IGSPLLNTKIYI--L 606
Cdd:PRK06710  322 IsSIRACISGSAPLPVEVQEKFETVTGGKL--VEGYGLTESSpVTHSNFLWEK-------RVPgsIGVPWPDTEAMImsL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  607 DSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:PRK06710  393 ETGEALPP-GEIGEIVVKGPQIMKGYWNKPEETAAVLQD-------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE------VRAYLATklpyYMIPQQIISIQNIPLTQ 760
Cdd:PRK06710  465 YPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEeelnqfARKYLAA----YKVPKVYEFRDELPKTT 540

                  ....*....
gi 446807313  761 NGKIDRKKL 769
Cdd:PRK06710  541 VGKILRRVL 549
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1324-1812 7.90e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 111.79  E-value: 7.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK12583   24 FDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVLVHQNsiIKGIEFQGNVIDLMDMSFEEEPGEDMH-----------MMIE--PHNLAY----- 1463
Cdd:PRK12583  104 YRASELEYALGQSGVRWVICADA--FKTSDYHAMLQELLPGLAEGQPGALACerlpelrgvvsLAPAppPGFLAWhelqa 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 ------------------------VIYTSGSTGQPKGVMIEHRSLTN--FLCAmyedfsQDIGITDnvlfSSSISFDVTI 1517
Cdd:PRK12583  182 rgetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNngYFVA------ESLGLTE----HDRLCVPVPL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIF-------VPLIYGARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGV---EP 1587
Cdd:PRK12583  252 YHCFgmvlanlGCMTVGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFD--LSSLRTGImagAP 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1588 IKTELLAK-YDHLFRGNLQIlnGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICI 1666
Cdd:PRK12583  329 CPIEVMRRvMDEMHMAEVQI--AYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKV--VDPDGATVPRGEIGELCT 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1667 SGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIK 1745
Cdd:PRK12583  405 RGYSVMKGYWNNPEATA-ESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREIEEFLFTHPAVA 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1746 TAVVIDQEDEA-GEKyLCAYVVTE--KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12583  478 DVQVFGVPDEKyGEE-IVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
PLN02574 PLN02574
4-coumarate--CoA ligase-like
298-781 8.96e-25

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 111.47  E-value: 8.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYL---PIDTELP-KQRVeymltdSG 372
Cdd:PLN02574   64 GFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnPSSSLGEiKKRV------VD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  373 CSHVLTYQ--NSIIKGVAFQGSVINLMD-----------IPFEEEQVEDLQITMEP----QNLAYVIYTSGSTGQPKGVM 435
Cdd:PLN02574  138 CSVGLAFTspENVEKLSPLGVPVIGVPEnydfdskriefPKFYELIKEDFDFVPKPvikqDDVAAIMYSSGTTGASKGVV 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  436 IEHRsltNFLcAMYEDF-----SQ-DIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQV 509
Cdd:PLN02574  218 LTHR---NLI-AMVELFvrfeaSQyEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKV 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  510 T-LAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCT-SYQYERDKE 586
Cdd:PLN02574  294 ThFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-PHVDFIQGYGMTESTAVGTrGFNTEKLSK 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  587 ITTqnVPIGSPLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 666
Cdd:PLN02574  373 YSS--VGLLAPNMQAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTGDIAYFDED 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLPYY 744
Cdd:PLN02574  444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPY 523
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446807313  745 MIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHL 781
Cdd:PLN02574  524 KKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1328-1812 1.16e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 110.85  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI------DTD 1401
Cdd:PRK06188   22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgslDDH 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LpkqrveYMLTDSGCSHVLVHQN-------------SIIKGIEFQGNVIDLMDM-----SFEEEPGEDMHmmiEPHNLAY 1463
Cdd:PRK06188  102 A------YVLEDAGISTLIVDPApfveralallarvPSLKHVLTLGPVPDGVDLlaaaaKFGPAPLVAAA---LPPDIAG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFS--QDIgitdNVLFSSSISFDVTIFeiFVP-LIYGArmTIYQGEKFDV 1540
Cdd:PRK06188  173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEwpADP----RFLMCTPLSHAGGAF--FLPtLLRGG--TVIVLAKFDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPIK----TELLAKYDHLFrgnLQIlngYGPTEA 1615
Cdd:PRK06188  245 AEVLRAIEEQRITATFLVPTMIYALLDHpDLRTRDLSSLETVYYGASPMSpvrlAEAIERFGPIF---AQY---YGQTEA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1616 TVCCTsyrYESNKEITTQNVPI----GSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpf 1691
Cdd:PRK06188  319 PMVIT---YLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1692 eRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKD 1770
Cdd:PRK06188  391 -RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEA-VTAVVVLRPG 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 446807313 1771 IPI--PEVRAYL-ATKLPHYMiPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06188  468 AAVdaAELQAHVkERKGSVHA-PKQVDFVDSLPLTALGKPDKKAL 511
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1461-1815 1.22e-24

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 113.10  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRS-LTNFlcamyEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLIYGARMtIY 1533
Cdd:PRK08633  784 TATIIFSSGSEGEPKGVMLSHHNiLSNI-----EQISDVFNLRndDVILsslpFFHSFGLTVT---LWLPLLEGIKV-VY 854
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QGEKFDVTKLVQVILEEQVTLSYIPPTLLNeIYdyfVRdNQKI------VLNKLLVGVEPIKTELLAKYDHLFrgNLQIL 1607
Cdd:PRK08633  855 HPDPTDALGIAKLVAKHRATILLGTPTFLR-LY---LR-NKKLhplmfaSLRLVVAGAEKLKPEVADAFEEKF--GIRIL 927
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTE----ATVCCTSYRYESNKEIT-TQNVPIGSPLLNTKIYILD--SFHRIqPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK08633  928 EGYGATEtspvASVNLPDVLAADFKRQTgSKEGSVGMPLPGVAVRIVDpeTFEEL-PPGEDGLILIGGPQVMKGYLGDPE 1006
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTAD--KFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK--YETIKTAVVIDQEDEA 1756
Cdd:PRK08633 1007 KTAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1757 -GEKylCAYVVTEKDIPIPEVRAYLA-TKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK08633 1082 kGEK--LVVLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1329-1815 1.26e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 111.29  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK06178   44 RERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCShVLVHQNSIIKGIE-------------------------------------FQGNVIDLMDmSFEEEPGED 1451
Cdd:PRK06178  124 YELNDAGAE-VLLALDQLAPVVEqvraetslrhvivtsladvlpaeptlplpdslraprlAAAGAIDLLP-ALRACTAPV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnFLCAMYEDFSQDIGiTDNVLfsssISFdVTIFEI-------FVPL 1524
Cdd:PRK06178  202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGG-EDSVF----LSF-LPEFWIagenfglLFPL 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQgeKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY--FVRDNqkivLNKL-LVGVEPIKTELLAKYDHLFR 1601
Cdd:PRK06178  275 FSGATLVLLA--RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHprFAEYD----LSSLrQVRVVSFVKKLNPDYRQRWR 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 ---GNLQILNGYGPTEATVC--CTSYRYESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK06178  349 altGSVLAEAAWGMTETHTCdtFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGY 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK06178  429 WNKPEATAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1756 AGEKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIpIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK06178  502 DKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQAL 562
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1345-1812 1.37e-24

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: 110.41  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 --SIIKGIE-----FQGNVIDLMDMSFEEEPGEDMHM---MIEPH-----------NLAYVI-YTSGSTGQPKGVMIEHR 1482
Cdd:cd12119   107 flPLLEAIAprlptVEHVVVMTDDAAMPEPAGVGVLAyeeLLAAEspeydwpdfdeNTAAAIcYTSGTTGNPKGVVYSHR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLtnFLCAMyedfsqDIGITDNVLFSSSisfDVtiFEIFVP--------LIYGARMT----IYQGEKFDVTKLVQVILEE 1550
Cdd:cd12119   187 SL--VLHAM------AALLTDGLGLSES---DV--VLPVVPmfhvnawgLPYAAAMVgaklVLPGPYLDPASLAELIERE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrgnLQILNGYGPTEATVCCTSYRY----- 1624
Cdd:cd12119   254 GVTFAAGVPTVWQGLLDHLEANGRDLSsLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTETSPLGTVARPpsehs 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1625 -ESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPI-GVP-GEICISGIGLARGYINRKELTADKFIDHPFergeklyKTG 1701
Cdd:cd12119   331 nLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTG 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLcAYVV-------TEKdipi 1773
Cdd:cd12119   404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPL-AVVVlkegatvTAE---- 478
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313 1774 pEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd12119   479 -ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1322-1812 2.35e-24

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 110.23  E-value: 2.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK06155   25 AMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGcSHVLVHQNSIIKGIEfqgnVIDLMDMSFEE------------EPGEDMHMM-----------IEP 1458
Cdd:PRK06155  105 LRGPQLEHILRNSG-ARLLVVEAALLAALE----AADPGDLPLPAvwlldapasvsvPAGWSTAPLppldapapaaaVQP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1459 HNLAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEdfSQDIGIT-DNVLFSSSISFDVTIFEIFVP-LIYGARMTIyqGE 1536
Cdd:PRK06155  180 GDTAAILYTSGTTGPSKGVCCPHAQF--YWWGRNS--AEDLEIGaDDVLYTTLPLFHTNALNAFFQaLLAGATYVL--EP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1537 KFDVTKLVQVILEEQVTLSYipptLLNEIYDYFV------RDNQKIVLNKLLVGVEPiktELLAKYDHLFrgNLQILNGY 1610
Cdd:PRK06155  254 RFSASGFWPAVRRHGATVTY----LLGAMVSILLsqpareSDRAHRVRVALGPGVPA---ALHAAFRERF--GVDLLDGY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1611 GPTEATVCCTsyryesnkeittqnVPIGSPLLNTKIYILDSFH-RIQ-------PIGVPGEICISG---IGLARGYINRK 1679
Cdd:PRK06155  325 GSTETNFVIA--------------VTHGSQRPGSMGRLAPGFEaRVVdehdqelPDGEPGELLLRAdepFAFATGYFGMP 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 ELTADKFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEK 1759
Cdd:PRK06155  391 EKTVEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGED 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1760 YLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06155  464 EVMAAVVLRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1461-1815 3.79e-24

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: 105.88  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGItdnVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDv 1540
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD---SWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 tkLVQVILEEQVT-LSYIPPTLLNEIYDYFVRDNQKiVLNKLLVGVEPIKTELLAKYdhLFRGnLQILNGYGPTEATVCC 1619
Cdd:cd17630    78 --LAEDLAPPGVThVSLVPTQLQRLLDSGQGPAALK-SLRAVLLGGAPIPPELLERA--ADRG-IPLYTTYGMTETASQV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESNKEITtqnvpIGSPLLNTKIYILDsfhriqpigvPGEICISGIGLARGYINRKEltadkfIDHPFERGekLYK 1699
Cdd:cd17630   152 ATKRPDGFGRGG-----VGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG--WFT 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPIPEVRA 1778
Cdd:cd17630   209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQR-PVAVIVGRGPADPAELRA 287
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd17630   288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
283-771 6.99e-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: 108.38  E-value: 6.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  283 EQVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd17642    25 KRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDS----------GCSHVLTYQ--NSIIKGVAFQGSVINLM-------------DIPFEEEQVEDLQITMEP 415
Cdd:cd17642   105 ERELDHSLNISkptivfcskkGLQKVLNVQkkLKIIKTIIILDSKEDYKgyqclytfitqnlPPGFNEYDFKPPSFDRDE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  416 QnLAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIgitdnvlFSSSISFDVTIFEIfVP-------------LV 482
Cdd:cd17642   185 Q-VALIMNSSGSTGLPKGVQLTHKNI----VARFSHARDPI-------FGNQIIPDTAILTV-IPfhhgfgmfttlgyLI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  483 CGARMTIYQgeKFDVPKLVQVILEEQVTLAYIPPTLL-----NEIYDYFVRANqkisLNKLFVGVEPIKTELLAKYDHLF 557
Cdd:cd17642   252 CGFRVVLMY--KFEEELFLRSLQDYKVQSALLVPTLFaffakSTLVDKYDLSN----LHEIASGGAPLSKEVGEAVAKRF 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  558 RGNLqILNLYGPTEATVCCTSYQYERDKEITTQNVpigSPLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKE 637
Cdd:cd17642   326 KLPG-IRQGYGLTETTSAILITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  638 LTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKY 717
Cdd:cd17642   401 ATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGEL 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313  718 LCAYVVTE--KDIPIPEVRAYLATKL-PYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:cd17642   475 PAAVVVLEagKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
PLN02246 PLN02246
4-coumarate--CoA ligase
1345-1812 7.11e-24

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 108.53  E-value: 7.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA-------YLPidTDLPKQrveymLTDSGCS 1417
Cdd:PLN02246   52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTP--AEIAKQ-----AKASGAK 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQNSI--IKGIEFQGNV----ID-----------LMDMSFEEEPGEDMHmmiePHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:PLN02246  125 LIITQSCYVdkLKGLAEDDGVtvvtIDdppegclhfseLTQADENELPEVEIS----PDDVVALPYSSGTTGLPKGVMLT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNflcamyeDFSQDI-GITDNVLFSSSisfDVTIfeIFVPL--IY------------GARMTIYQgeKFDVTKLVQ 1545
Cdd:PLN02246  201 HKGLVT-------SVAQQVdGENPNLYFHSD---DVIL--CVLPMfhIYslnsvllcglrvGAAILIMP--KFEIGALLE 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLS-YIPPTLL----NEIYDYFVRDNQKIVLNkllvGVEPIKTELlakyDHLFRGNL--QIL-NGYGPTEA-T 1616
Cdd:PLN02246  267 LIQRHKVTIApFVPPIVLaiakSPVVEKYDLSSIRMVLS----GAAPLGKEL----EDAFRAKLpnAVLgQGYGMTEAgP 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 VCCTSYRYEsnKE-ITTQNVPIGSPLLNTKIYILD-----SFHRIQPigvpGEICISGIGLARGYINRKELTAdKFIDHp 1690
Cdd:PLN02246  339 VLAMCLAFA--KEpFPVKSGSCGTVVRNAELKIVDpetgaSLPRNQP----GEICIRGPQIMKGYLNDPEATA-NTIDK- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 fergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD 1770
Cdd:PLN02246  411 ----DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNG 486
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446807313 1771 IPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02246  487 SEITEdeIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
418-767 8.10e-24

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: 104.72  E-value: 8.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGItdnVLFSSSISFDVTIFEIFVP-LVCGARMTIYQGEkfd 496
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD---SWLLSLPLYHVGGLAILVRsLLAGAELVLLERN--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  497 vPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAkydhlfRGNLQILNL---YGPTE-- 571
Cdd:cd17630    76 -QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLE------RAADRGIPLyttYGMTEta 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  572 ATVCCTSYQYERDKEIttqnvpiGSPLLNTKIYILDsfhrlqpigvPGEICISGIGLARGYINRKEltadkfIDHPFERG 651
Cdd:cd17630   149 SQVATKRPDGFGRGGV-------GVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  652 ekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKyLCAYVVTEKDIPI 730
Cdd:cd17630   206 --WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQR-PVAVIVGRGPADP 282
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446807313  731 PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd17630   283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
300-769 9.34e-24

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 108.22  E-value: 9.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGcSHVL-- 377
Cdd:PRK13295   55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLvv 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 ---------------------TYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITME----PQNLAYVIYTSGSTGQPK 432
Cdd:PRK13295  134 pktfrgfdhaamarrlrpelpALRHVVVVGGDGADSFEALLITPAWEQEPDAPAILARlrpgPDDVTQLIYTSGTTGEPK 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  433 GVMieHRSltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLVCGARMtIYQgEKFDVPKLVQVILEEQV 509
Cdd:PRK13295  214 GVM--HTA--NTLMANIVPYAERLGLGaDDVILMASPMAHQTgfMYGLMMPVMLGATA-VLQ-DIWDPARAAELIRTEGV 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  510 TLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTE-ATVCCTSYQYERDKEI 587
Cdd:PRK13295  288 TFTMASTPFLTDLTRAVKESGRPVsSLRTFLCAGAPIPGALVERARAAL--GAKIVSAWGMTEnGAVTLTKLDDPDERAS 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  588 TTQnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfergEKLYKTGDIARWLPDG 667
Cdd:PRK13295  366 TTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADG 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  668 NIEYLGRvDHQVKIRG-YRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE--KDIPIPEVRAYLATK--- 740
Cdd:PRK13295  434 YIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERlGER-ACAFVVPRpgQSLDFEEMVEFLKAQkva 511
                         490       500
                  ....*....|....*....|....*....
gi 446807313  741 LPYymIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13295  512 KQY--IPERLVVRDALPRTPSGKIQKFRL 538
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
278-769 1.26e-23

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 107.80  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:PRK07059   26 ADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  358 ELPKQRVEYMLTDSGCSHVLTYQN-----------SIIKGV---------AFQGSVINLM-----------DIP----FE 402
Cdd:PRK07059  106 LYTPRELEHQLKDSGAEAIVVLENfattvqqvlakTAVKHVvvasmgdllGFKGHIVNFVvrrvkkmvpawSLPghvrFN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  403 EEQVEDLQITMEPQNL-----AYVIYTSGSTGQPKGVMIEHRS-LTNFL--CAMYEDFSQDIGITDNVLFSSSISfdvtI 474
Cdd:PRK07059  186 DALAEGARQTFKPVKLgpddvAFLQYTGGTTGVSKGATLLHRNiVANVLqmEAWLQPAFEKKPRPDQLNFVCALP----L 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  475 FEIFVPLVCGArMTIYQG-------EKFDVPKLVQVILEEQVTLayIPPtlLNEIYDYFVRAN--QKISLNKLFVGV--- 542
Cdd:PRK07059  262 YHIFALTVCGL-LGMRTGgrnilipNPRDIPGFIKELKKYQVHI--FPA--VNTLYNALLNNPdfDKLDFSKLIVANggg 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 ----EPIKTELLAKYdhlfrgNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:PRK07059  337 mavqRPVAERWLEMT------GCPITEGYGLSETSPVATCNPVDATEFSGT----IGLPLPSTEVSIRDDDGNDLPLGEP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  619 GEICISGIGLARGYINRKE-----LTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 693
Cdd:PRK07059  407 GEICIRGPQVMAGYWNRPDetakvMTADGF-----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313  694 SLLKYETIKTAVVIQREDE-SGEKyLCAYVVtEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07059  476 VVASHPGVLEVAAVGVPDEhSGEA-VKLFVV-KKDPALTEedVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
PRK09088 PRK09088
acyl-CoA synthetase; Validated
284-769 1.85e-23

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 106.81  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  284 QVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  362 QRVEYMLTDSgcshvltyQNSIIKG----VAFQGSVINLMDIPFEEEQVE-DLQITMEPQNLAYVIYTSGSTGQPKGVMI 436
Cdd:PRK09088   84 SELDALLQDA--------EPRLLLGddavAAGRTDVEDLAAFIASADALEpADTPSIPPERVSLILFTSGTSGQPKGVML 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  437 EHRSL----TNFlcamyedfsqdiGITDNVLFSSSISFDVTIFEIfVPLVCGARMTIYQGEKFdvpkLVQVILEEQVTLA 512
Cdd:PRK09088  156 SERNLqqtaHNF------------GVLGRVDAHSSFLCDAPMFHI-IGLITSVRPVLAVGGSI----LVSNGFEPKRTLG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  513 YIP-PTLlnEIYDYF--------VRANQKI------SLNKLFVGVEP-IKTELLAKYDHlfrgNLQILNLYGPTEA-TVC 575
Cdd:PRK09088  219 RLGdPAL--GITHYFcvpqmaqaFRAQPGFdaaalrHLTALFTGGAPhAAEDILGWLDD----GIPMVDGFGMSEAgTVF 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  576 CTSYQYERdkeITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLY 655
Cdd:PRK09088  293 GMSVDCDV---IRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  656 KTGDIARWLPDGnieYLGRVDHQVKI---RGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIP 731
Cdd:PRK09088  364 RTGDIARRDADG---FFWVVDRKKDMfisGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGAPLDL 440
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313  732 E-VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK09088  441 ErIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1319-1809 3.03e-23

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: 107.19  E-value: 3.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEEQVKRNPNQIAVVC-NEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGG 1393
Cdd:cd05968    62 IVEQLLDKWLADTRTRPALRWeGEDGtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1394 AYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFqgNVIDLMDMSFEEEPGEDmHMMIE--------PHNLAY-- 1463
Cdd:cd05968   142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREV--NLKEEADKACAQCPTVE-KVVVVrhlgndftPAKGRDls 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 ----------------------VIYTSGSTGQPKGVMIEHrslTNFLCAMYED--FSQDIGITDNVLFSSSISFDVTIFE 1519
Cdd:cd05968   219 ydeeketagdgaertesedplmIIYTSGTTGKPKGTVHVH---AGFPLKAAQDmyFQFDLKPGDLLTWFTDLGWMMGPWL 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1520 IFVPLIYGARMTIYQG--EKFDVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKTE-LL 1593
Cdd:cd05968   296 IFGGLILGATMVLYDGapDHPKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEpWN 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1594 AKYDHLFRGNLQILNGYGPTEAT---VCCtsYRYESNKEITtqnvpIGSPLLNTKIYILDSfhRIQPI-GVPGEICISG- 1668
Cdd:cd05968   376 WLFETVGKGRNPIINYSGGTEISggiLGN--VLIKPIKPSS-----FNGPVPGMKADVLDE--SGKPArPEVGELVLLAp 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1669 -IGLARGYInRKEltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:cd05968   447 wPGMTRGFW-RDE---DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1748 VVIDQEDEA-GEKYLCaYVVTEKDI-PIP----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd05968   523 AAIGVPHPVkGEAIVC-FVVLKPGVtPTEalaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1344-1814 3.04e-23

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: 105.29  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVhq 1423
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSG-ARLVV-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlMDMSFEEEPGEDMHMMIephnlayviYTSGSTGQPKGVMIEHRSLTNFlcAMYEDFSQDIGITD 1503
Cdd:cd05973    78 ----------------TDAANRHKLDSDPFVMM---------FTSGTTGLPKGVPVPLRALAAF--GAYLRDAVDLRPED 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSISFDVTIF-EIFVPLIYGARMTIYQGeKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDNQ------KI 1576
Cdd:cd05973   131 SFWNAADPGWAYGLYyAITGPLALGHPTILLEG-GFSVESTWRVIERLGVTNLAGSPT----AYRLLMAAGAevparpKG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGVEPIKTELLakydHLFRGNL--QILNGYGPTE-ATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFH 1653
Cdd:cd05973   206 RLRRVSSAGEPLTPEVI----RWFDAALgvPIHDHYGQTElGMVLANHHALEHPVHAGS----AGRAMPGWRVAVLDDDG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1654 RIQPIGVPGEICI----SGIGLARGYINRKELTADKfidhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd05973   278 DELGPGEPGRLAIdianSPLMWFRGYQLPDTPAIDG----------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-TEKDIPIPEVRAYLA----TKLPHYMIPQQLIPIHNIPLTQN 1804
Cdd:cd05973   348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPS 427
                         490
                  ....*....|
gi 446807313 1805 GKIDRSKLPK 1814
Cdd:cd05973   428 GKIQRFLLRR 437
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
287-780 3.39e-23

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 105.34  E-value: 3.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK09029   15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  367 MLTDSGCSHVLTYQNsiikgvafQGSVINLMDIPfEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRS-LTN-- 443
Cdd:PRK09029   95 LLPSLTLDFALVLEG--------ENTFSALTSLH-LQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhLASae 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  444 -FLCAMyeDFSQDigitDNVLFSssisfdvtifeifVP-------------LVCGARMTIYQGEKFDvpklvQVIleEQV 509
Cdd:PRK09029  166 gVLSLM--PFTAQ----DSWLLS-------------LPlfhvsgqgivwrwLYAGATLVVRDKQPLE-----QAL--AGC 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  510 TLAYIPPTLLNEIYDYfvrANQKISLNKLFVGVEPIKTEL---LAKYD-HLFRGnlqilnlYGPTEA--TVCCtsyqyer 583
Cdd:PRK09029  220 THASLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELteqAEQQGiRCWCG-------YGLTEMasTVCA------- 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  584 dKEI-TTQNVpiGSPLLNTKIYILDsfhrlqpigvpGEICISGIGLARGYINRKELTadkfidhPFERGEKLYKTGDIAR 662
Cdd:PRK09029  283 -KRAdGLAGV--GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGE 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  663 WLpDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLcAYVVTEKDIPIPEVRAYLATKL 741
Cdd:PRK09029  342 WQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaEFGQRPV-AVVESDSEAAVVNLAEWLQDKL 419
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446807313  742 -----P--YYMIPQQiisiqnipLTQNG-KIDRKKLPQPINNLKSSH 780
Cdd:PRK09029  420 arfqqPvaYYLLPPE--------LKNGGiKISRQALKEWVAQQLGNN 458
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
289-764 8.47e-23

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 105.24  E-value: 8.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK07786   31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLT-----------------YQNSIIKGVAFQGSVINLMDIPFEEEqvEDLQITMEPQNL-AYVIYTSGSTGQ 430
Cdd:PRK07786  111 SDCGAHVVVTeaalapvatavrdivplLSTVVVAGGSSDDSVLGYEDLLAEAG--PAHAPVDIPNDSpALIMYTSGTTGR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  431 PKGVMIEHRSLT----NFLCAMYEDFSQDIGitdnvlFSSSISFDVTIFEIFVP-LVCGARMTIYQGEKFDVPKLVQVIL 505
Cdd:PRK07786  189 PKGAVLTHANLTgqamTCLRTNGADINSDVG------FVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVLE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  506 EEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEAT-VCCTSYQYERD 584
Cdd:PRK07786  263 AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEA-QILAAFGQTEMSpVTCMLLGEDAI 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  585 KEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 664
Cdd:PRK07786  342 RKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVRQD 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVT--EKDIPIPEVRAYLATKL 741
Cdd:PRK07786  411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRndDAALTLEDLAEFLTDRL 490
                         490       500
                  ....*....|....*....|...
gi 446807313  742 PYYMIPQQIISIQNIPLTQNGKI 764
Cdd:PRK07786  491 ARYKHPKALEIVDALPRNPAGKV 513
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
298-769 1.29e-22

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: 103.33  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKRE-FIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05958     8 EREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LtyqnsiikgvafqgsvinlmdIPFEEEQVEDLQItmepqnlayVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDI 456
Cdd:cd05958    88 L---------------------CAHALTASDDICI---------LAFTSGTTGAPKATMHFHRDPL----ASADRYAVNV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  457 -GITDNVLFSSS----ISFDVTIFEIFvPLVCGARMTIYqgEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ 531
Cdd:cd05958   134 lRLREDDRFVGSpplaFTFGLGGVLLF-PFGVGASGVLL--EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  532 KIS-LNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFH 610
Cdd:cd05958   211 DLSsLRKCVSAGEALPAALHRAWKEAT--GIPIIDGIGSTEMFHIFISARPGDARPGAT-----GKPVPGYEAKVVDDEG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  611 RLQPIGVPGEICISGIGLARGyiNRKELTADKFidhpfeRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:cd05958   284 NPVPDGTIGRLAVRGPTGCRY--LADKRQRTYV------QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  691 IEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05958   355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434

                  ....
gi 446807313  766 RKKL 769
Cdd:cd05958   435 RFAL 438
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
421-766 1.33e-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: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  421 VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFS-SSISFDVTIFEIFVPLVCGARMTIYqGEKFDVPK 499
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTF--FAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVTG-GENTTYKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  500 LVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVE-PIKTEllaKYDHLFRGNLQILNLYGPTE-ATVCC 576
Cdd:cd17635    83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVpSLRLIGYGGSrAIAAD---VRFIEATGLTNTAQVYGLSEtGTALC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  577 TsyQYERD-KEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergekly 655
Cdd:cd17635   160 L--PTDDDsIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV------- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIP--IPE 732
Cdd:cd17635   227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDEnaIRA 306
                         330       340       350
                  ....*....|....*....|....*....|....
gi 446807313  733 VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17635   307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
288-779 1.69e-22

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 104.30  E-value: 1.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAylPIDTELPKQRVE-- 365
Cdd:PRK10946   36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSEln 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 -Y--------MLTDSgcSHVLTYQNSIIKgvAFQGSVINLMDIPFEEEQVE-DLQITMEPQNLAYVIYTS---------- 425
Cdd:PRK10946  114 aYasqiepalLIADR--QHALFSDDDFLN--TLVAEHSSLRVVLLLNDDGEhSLDDAINHPAEDFTATPSpadevaffql 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  426 --GSTGQPKGVMIEH--------RSL--------TNFLCAmyedfsqdIGITDNVLFSSSISFDVTIFEIFV-------P 480
Cdd:PRK10946  190 sgGSTGTPKLIPRTHndyyysvrRSVeicgftpqTRYLCA--------LPAAHNYPMSSPGALGVFLAGGTVvlapdpsA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  481 LVCgarmtiyqgekfdvpklVQVILEEQVTL-AYIPPTL---LNEIYDYFVRAnQKISLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK10946  262 TLC-----------------FPLIEKHQVNVtALVPPAVslwLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  557 FRGNLQilNLYGPTEATVCCTSYQYERDKEITTQNVPIgSPllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK10946  324 LGCQLQ--QVFGMAEGLVNYTRLDDSDERIFTTQGRPM-SP--DDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  637 ELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GE 715
Cdd:PRK10946  399 QHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGE 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  716 KYlCAYVVTEKDIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSS 779
Cdd:PRK10946  473 KS-CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1336-1812 2.69e-22

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: 102.56  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1336 AVVCNEKGITYNELNIKANQLARRLLDQGVKRE-SIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDS 1414
Cdd:cd05958     3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1415 GCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYED 1494
Cdd:cd05958    83 RITVALC------------------------------AHALTASDDICILAFTSGTTGAPKATMHFHRDPL----ASADR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FSQDI-GITDNVLFSSS----ISFDVTIFEIFvPLIYGARMTIYQGEKFDvtKLVQVILEEQVTLSYIPPTLLNEIYDYF 1569
Cdd:cd05958   129 YAVNVlRLREDDRFVGSpplaFTFGLGGVLLF-PFGVGASGVLLEEATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATvcctsYRYESNKEITTQNVPIGSPLLNTKIYI 1648
Cdd:cd05958   206 DAAGPDLSsLRKCVSAGEALPAALHRAWKEAT--GIPIIDGIGSTEMF-----HIFISARPGDARPGATGKPVPGYEAKV 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGyiNRKELTADKFidhpfeRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYR 1728
Cdd:cd05958   279 VDDEGNPVPDGTIGRLAVRGPTGCRY--LADKRQRTYV------QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1729 IELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:cd05958   350 IAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429

                  ....*....
gi 446807313 1804 NGKIDRSKL 1812
Cdd:cd05958   430 TGKLQRFAL 438
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
299-728 2.75e-22

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: 102.82  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCShVLT 378
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV-ALV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  379 YQNSiikgvafqgsvinlmdipfeeeqvedlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGi 458
Cdd:cd17640    83 VEND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  459 tDNVLfssSI-----SFDvTIFEIFVpLVCGARMtIYQGEKF--DVPKLVQVILEEQVTLAYIppTLLNEIYDYFV---R 528
Cdd:cd17640   130 -DRFL---SIlpiwhSYE-RSAEYFI-FACGCSQ-AYTSIRTlkDDLKRVKPHYIVSVPRLWE--SLYSGIQKQVSkssP 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 ANQKISLNKLFVGVepIKTEL-----LAKY-DHLFRG-NLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNT 601
Cdd:cd17640   201 IKQFLFLFFLSGGI--FKFGIsgggaLPPHvDTFFEAiGIEVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGT 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  602 KIYILDSFHR-LQPIGVPGEICISGIGLARGYINRKELTAdKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRV-DHQV 679
Cdd:cd17640   274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATS-KVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIV 347
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 446807313  680 KIRGYRIELGEIEASLLKYETIKTAVVIQREdesgEKYLCAYVVTEKDI 728
Cdd:cd17640   348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNFEE 392
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1344-1812 3.16e-22

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 103.38  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID-----TDLPKQRVE------YML 1411
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpssslGEIKKRVVDcsvglaFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDS-------GCSHVLVHQNSII--KGIEFQGNvidLMDMSFEEEPGedMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:PLN02574  147 PENveklsplGVPVIGVPENYDFdsKRIEFPKF---YELIKEDFDFV--PKPVIKQDDVAAIMYSSGTTGASKGVVLTHR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 sltNFLcAMYEDF-----SQ-DIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVT-LS 1555
Cdd:PLN02574  222 ---NLI-AMVELFvrfeaSQyEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVThFP 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPPTLLNeiydyFVRDNQKIV------LNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSyRYESNKE 1629
Cdd:PLN02574  298 VVPPILMA-----LTKKAKGVCgevlksLKQVSCGAAPLSGKFIQDFVQTL-PHVDFIQGYGMTESTAVGTR-GFNTEKL 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVPIGSPLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 1709
Cdd:PLN02574  371 SKYSSVGLLAPNMQAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTGDIAYFDED 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE--VRAYLATKLPHY 1787
Cdd:PLN02574  444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPY 523
                         490       500
                  ....*....|....*....|....*
gi 446807313 1788 MIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02574  524 KKVRKVVFVQSIPKSPAGKILRREL 548
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1344-1812 4.25e-22

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: 101.88  E-value: 4.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSiikgiefqgnvidlmdmsfeeepGEDMHMMIephnlayvIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEdfsqdIGIT 1502
Cdd:cd05974    81 NT-----------------------HADDPMLL--------YFTSGTTSKPKLVEHTHRSYpVGHLSTMYW-----IGLK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 --DNVLFSSSISFDVTIFE-IFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDNQ---KI 1576
Cdd:cd05974   125 pgDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT----VWRMLIQQDLasfDV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCtsyryeSNKeiTTQNVPIGS---PLLNTKIYILDsfh 1653
Cdd:cd05974   201 KLREVVGAGEPLNPEVIEQVRRAW--GLTIRDGYGQTETTALV------GNS--PGQPVKAGSmgrPLPGYRVALLD--- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1654 riqPIGVP---GEICIS-----GIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:cd05974   268 ---PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-TEKDIPIPE----VRAYLATKLPHYMIPQQLiPIHNIP 1800
Cdd:cd05974   338 DYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlRAGYEPSPEtaleIFRFSRERLAPYKRIRRL-EFAELP 416
                         490
                  ....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd05974   417 KTISGKIRRVEL 428
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
421-766 4.48e-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: 99.65  E-value: 4.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  421 VIYTSGSTGQPKGVMIEHRsltNFLCAMYEdFSQDIGITDNvlfsssisfDV--TIFEIF-VPLVCGARMTIYQG----- 492
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHG---NLIAANLQ-LIHAMGLTEA---------DVylNMLPLFhIAGLNLALATFHAGganvv 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 -EKFDVPKLVQVILEEQVTL-AYIPPTLLNeIYDYFVRANQKISLNKLFVGVE-PiktELLAKYDHLFRGNLQILnlYGP 569
Cdd:cd17637    72 mEKFDPAEALELIEEEKVTLmGSFPPILSN-LLDAAEKSGVDLSSLRHVLGLDaP---ETIQRFEETTGATFWSL--YGQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  570 TEaTVCCTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAdkfidHPFE 649
Cdd:cd17637   146 TE-TSGLVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA-----YTFR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  650 RGekLYKTGDIARWLPDGNIEYLGRVDHQ--VKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGE--KYLCA---- 720
Cdd:cd17637   215 NG--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpKWGEgiKAVCVlkpg 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 446807313  721 YVVTEKdipipEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17637   293 ATLTAD-----ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1330-1815 6.85e-22

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 102.38  E-value: 6.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAylPIDTDLPKQRVE- 1408
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSEl 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 --Y--------MLTDSgcSHVLVHQNSIIKgiEFQGNVIDLMDMSFEEEPGE-DMHMMIEPHNLAYVIYTS--------- 1468
Cdd:PRK10946  113 naYasqiepalLIADR--QHALFSDDDFLN--TLVAEHSSLRVVLLLNDDGEhSLDDAINHPAEDFTATPSpadevaffq 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 ---GSTGQPKGVMIEH--------RSL--------TNFLCAmyedfsqdIGITDNVLFSSSISFDVtiFEifvpliygAR 1529
Cdd:PRK10946  189 lsgGSTGTPKLIPRTHndyyysvrRSVeicgftpqTRYLCA--------LPAAHNYPMSSPGALGV--FL--------AG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQGEKFDVTKLVQVILEEQVTL-SYIPPTL---LNEIYDYFVRDnQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQ 1605
Cdd:PRK10946  251 GTVVLAPDPSATLCFPLIEKHQVNVtALVPPAVslwLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAELGCQLQ 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILngYGPTEATVCCTSYRYESNKEITTQNVPIgSPllNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADK 1685
Cdd:PRK10946  330 QV--FGMAEGLVNYTRLDDSDERIFTTQGRPM-SP--DDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1686 FIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYlCAY 1764
Cdd:PRK10946  405 FDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKS-CAF 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1765 VVTEKDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK10946  478 LVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1340-1812 8.11e-22

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: 102.22  E-value: 8.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDS----- 1414
Cdd:cd17642    41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISkptiv 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1415 -----GCSHVLVHQ--NSIIKGIEFQGNVIDLM----DMSFEEE---PGEDMHMMIEP-----HNLAYVIYTSGSTGQPK 1475
Cdd:cd17642   121 fcskkGLQKVLNVQkkLKIIKTIIILDSKEDYKgyqcLYTFITQnlpPGFNEYDFKPPsfdrdEQVALIMNSSGSTGLPK 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLtnflCAMYEDFSQDIgitdnvlFSSSISFDVTIFEIfVPLIYGARMTIYQG-----------EKFDVTKLV 1544
Cdd:cd17642   201 GVQLTHKNI----VARFSHARDPI-------FGNQIIPDTAILTV-IPFHHGFGMFTTLGylicgfrvvlmYKFEEELFL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1545 QVILEEQVTLSYIPPTLL-----NEIYDYFVRDNqkivLNKLLVGVEPIKTELLAKYDHLFRGNLqILNGYGPTEATVCC 1619
Cdd:cd17642   269 RSLQDYKVQSALLVPTLFaffakSTLVDKYDLSN----LHEIASGGAPLSKEVGEAVAKRFKLPG-IRQGYGLTETTSAI 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESNKEITTQNVpigSPLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYK 1699
Cdd:cd17642   344 LITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKALIDK------DGWLH 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE--KDIPIPEVR 1777
Cdd:cd17642   414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEagKTMTEKEVM 493
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 446807313 1778 AYLATKL-PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd17642   494 DYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1330-1812 8.87e-22

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 101.10  E-value: 8.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:PRK09029   15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGCSHVLVhqnsiikgIEFQGNVIDLMDMSFEEEPGEDMHMMiEPHNLAYVIYTSGSTGQPKGVMIEHRS-LTN-- 1486
Cdd:PRK09029   95 LLPSLTLDFALV--------LEGENTFSALTSLHLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQAhLASae 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 -FLCAMyeDFSQDigitDNVLFSssisfdvtifeifVPLIY-------------GARMTIYQGEKFDvtklvQVIleEQV 1552
Cdd:PRK09029  166 gVLSLM--PFTAQ----DSWLLS-------------LPLFHvsgqgivwrwlyaGATLVVRDKQPLE-----QAL--AGC 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNEIYDYfvrDNQKIVLNKLLVGVEPIKTELLAKYDHlfRGnLQILNGYGPTEA--TVCCtsyryesnKEI 1630
Cdd:PRK09029  220 THASLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELTEQAEQ--QG-IRCWCGYGLTEMasTVCA--------KRA 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1631 -TTQNVpiGSPLLNTKIYILDsfhriqpigvpGEICISGIGLARGYINRKELTadkfidhPFERGEKLYKTGDIARWLpD 1709
Cdd:PRK09029  286 dGLAGV--GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-N 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGEKYLcAYVVTEKDIPIPEVRAYLATKL---- 1784
Cdd:PRK09029  345 GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaEFGQRPV-AVVESDSEAAVVNLAEWLQDKLarfq 423
                         490       500       510
                  ....*....|....*....|....*....|...
gi 446807313 1785 -P--HYMIPQQLipihnipltQNG--KIDRSKL 1812
Cdd:PRK09029  424 qPvaYYLLPPEL---------KNGgiKISRQAL 447
PRK07638 PRK07638
acyl-CoA synthetase; Validated
287-775 1.09e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 101.01  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  287 QNPNQIAIVCNGKEITYKQLNIKANQLARrLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK07638   13 LQPNKIAIKENDRVLTYKDWFESVCKVAN-WLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  367 MLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDI-PFEEEQVEDLQITMEPQNLA-YVIYTSGSTGQPKGVMIEHRS-LTN 443
Cdd:PRK07638   92 RLAISNADMIVTERYKLNDLPDEEGRVIEIDEWkRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQSwLHS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  444 FLCAMyEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiy 523
Cdd:PRK07638  172 FDCNV-HDFH--MKREDSVLIAGTLVHSLFLYGAISTLYVGQ--TVHLMRKFIPNQVLDKLETENISVMYTVPTML---- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  524 DYFVRANQKISlNKLFVGVEPIKTELLAK------YDHLfrgnlQILNLYGPTEATVccTSYQYERDKEITTQNVpiGSP 597
Cdd:PRK07638  243 ESLYKENRVIE-NKMKIISSGAKWEAEAKekikniFPYA-----KLYEFYGASELSF--VTALVDEESERRPNSV--GRP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  598 LLNTKIYILDSfhrlqpigvPGEICISG-IG--------LARGYINRKELtadkfidhPFERGEKLYKT-GDIARWLPDG 667
Cdd:PRK07638  313 FHNVQVRICNE---------AGEEVQKGeIGtvyvkspqFFMGYIIGGVL--------ARELNADGWMTvRDVGYEDEEG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  668 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKylcAYVVTEKDIPIPEVRAYLATKLPYYMI 746
Cdd:PRK07638  376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEK---PVAIIKGSATKQQLKSFCLQRLSSFKI 452
                         490       500
                  ....*....|....*....|....*....
gi 446807313  747 PQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:PRK07638  453 PKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
PRK06164 PRK06164
acyl-CoA synthetase; Validated
280-771 1.39e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 101.36  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  360 PKQRVEYMLTDSGCShVLTYQNSIiKGVAFQGsVINLMD-----------------------IPFEEEQVEDLQITMEPQ 416
Cdd:PRK06164   95 RSHEVAHILGRGRAR-WLVVWPGF-KGIDFAA-ILAAVPpdalpplraiavvddaadatpapAPGARVQLFALPDPAPPA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  417 ---------NLAYVIYT-SGSTGQPKGVMieHRSLTnfLCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLVCG 484
Cdd:PRK06164  172 aageraadpDAGALLFTtSGTTSGPKLVL--HRQAT--LLRHARAIARAYGYDPGavLLAALPFCGVFGFSTLLGALAGG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  485 ArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKL-FVGVEPIKTELLAKYdhLFRGnLQI 563
Cdd:PRK06164  248 A--PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFgFASFAPALGELAALA--RARG-VPL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  564 LNLYGPTE--ATVCCtsyqYERDKEITTQNVPIGSPLL-NTKIYILDSFH-RLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK06164  323 TGLYGSSEvqALVAL----QPATDPVSVRIEGGGRPASpEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  640 ADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDEsGEKYLC 719
Cdd:PRK06164  399 ARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD-GKTVPV 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313  720 AYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNG---KIDRKKLPQ 771
Cdd:PRK06164  472 AFVIPTDGASPdeAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1344-1720 1.89e-21

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: 101.14  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKR--ESIVGVMMKRSIEMVIGILGVLKAGGAYLPI-DTdLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLyDT-LGPEAIEYILNHAEISIVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VHqnsiiKGIEFqgnvidlmdMSFEEEpgEDM-------HMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05927    85 CD-----AGVKV---------YSLEEF--EKLgkknkvpPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 DFSQDIGITDN-VLFSssisfdvtifeiFVPL--IY-----------GARMTIYQGekfDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd05927   149 ILEILNKINPTdVYIS------------YLPLahIFervvealflyhGAKIGFYSG---DIRLLLDDIKALKPTVFPGVP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDNQ---------------------------------KIVLNK-----------LLVGVEPIKTELLAK 1595
Cdd:cd05927   214 RVLNRIYDKIFNKVQakgplkrklfnfalnyklaelrsgvvraspfwdKLVFNKikqalggnvrlMLTGSAPLSPEVLEF 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1596 ydhlFRGNL--QILNGYGPTEAT-VCCTSYRYESNkeITTqnvpIGSPLLNTKIYILDsfhriqpigVP----------- 1661
Cdd:cd05927   294 ----LRVALgcPVLEGYGQTECTaGATLTLPGDTS--VGH----VGGPLPCAEVKLVD---------VPemnydakdpnp 354
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 -GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDH 1720
Cdd:cd05927   355 rGEVCIRGPNVFSGYYKDPEKTAEALDE------DGWLHTGDIGEWLPNGTLKIIDRKKN 408
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1464-1809 1.93e-21

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: 98.10  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFS-SSISFDVTIFEIFVPLIYGARMTIYqGEKFDVTK 1542
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTF--FAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVTG-GENTTYKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1543 LVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVE-PIKTEllaKYDHLFRGNLQILNGYGPTE-ATVCC 1619
Cdd:cd17635    83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVpSLRLIGYGGSrAIAAD---VRFIEATGLTNTAQVYGLSEtGTALC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESnKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyK 1699
Cdd:cd17635   160 LPTDDDS-IEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------N 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTEKDIP--IPEV 1776
Cdd:cd17635   228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDEnaIRAL 307
                         330       340       350
                  ....*....|....*....|....*....|...
gi 446807313 1777 RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17635   308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
414-768 2.65e-21

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 100.84  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 EPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNflCAMYEDFSQDIGITDNVLFSSSISFD---VTIFEIFVPLvCGARMTI 489
Cdd:PRK05605  217 TPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAWVPGLGDGPERVLAALPMFHaygLTLCLTLAVS-IGGELVL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  490 YqgEKFDVPKLVQVILEEQVT-LAYIPPtllneIYDYFVRANQK--ISLNKL---FVGVEPIKTELLAKYDHLFRGNLqi 563
Cdd:PRK05605  294 L--PAPDIDLILDAMKKHPPTwLPGVPP-----LYEKIAEAAEErgVDLSGVrnaFSGAMALPVSTVELWEKLTGGLL-- 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  564 LNLYGPTEAT--VCCTSyqyerdkeITTQNVP--IGSPLLNTKIYILD--SFHRLQPIGVPGEICISGIGLARGYINRKE 637
Cdd:PRK05605  365 VEGYGLTETSpiIVGNP--------MSDDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPE 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  638 LTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKY 717
Cdd:PRK05605  437 ETAKSFLD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446807313  718 LCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:PRK05605  510 VVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
PRK07788 PRK07788
acyl-CoA synthetase; Validated
287-770 4.78e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 99.62  E-value: 4.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK----- 361
Cdd:PRK07788   61 RAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGpqlae 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  362 ----QRVEYMLTDSGCSHVLTY-QNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNL-------AYVIYTSGSTG 429
Cdd:PRK07788  141 vaarEGVKALVYDDEFTDLLSAlPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLpkppkpgGIVILTSGTTG 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  430 QPKGVMIEH----RSLTNFLCAMyeDFSQDigitDNVLFSSSIsFDVTIFEIFVpLVCGARMTIYQGEKFDVPKLVQVIL 505
Cdd:PRK07788  221 TPKGAPRPEpsplAPLAGLLSRV--PFRAG----ETTLLPAPM-FHATGWAHLT-LAMALGSTVVLRRRFDPEATLEDIA 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  506 EEQVTLAYIPPTLLNEIYDYFVRANQKI---SLNKLFVGVEPIKTELLAKYDHLFrGNLqILNLYGPTEATVCCTSYQYE 582
Cdd:PRK07788  293 KHKATALVVVPVMLSRILDLGPEVLAKYdtsSLKIIFVSGSALSPELATRALEAF-GPV-LYNLYGSTEVAFATIATPED 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  583 RDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINrkelTADKfidhpfERGEKLYKTGDIAR 662
Cdd:PRK07788  371 LAEAPGT----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDK------QIIDGLLSSGDVGY 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATK 740
Cdd:PRK07788  437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEdaIKDYVRDN 516
                         490       500       510
                  ....*....|....*....|....*....|
gi 446807313  741 LPYYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK07788  517 LARYKVPRDVVFLDELPRNPTGKVLKRELR 546
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1332-1812 5.03e-21

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 99.47  E-value: 5.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK07786   31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVH-----------------QNSIIKGIEFQGNVIDLMDMSfeEEPGEDMHMMIEPHNL-AYVIYTSGSTGQ 1473
Cdd:PRK07786  111 SDCGAHVVVTEaalapvatavrdivpllSTVVVAGGSSDDSVLGYEDLL--AEAGPAHAPVDIPNDSpALIMYTSGTTGR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSLT----NFLCAMYEDFSQDIGitdnvlFSSSISFDVTIFEIFVP-LIYGARMTIYQGEKFDVTKLVQVIL 1548
Cdd:PRK07786  189 PKGAVLTHANLTgqamTCLRTNGADINSDVG------FVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVLE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEAT-VCCTSYRYESN 1627
Cdd:PRK07786  263 AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEA-QILAAFGQTEMSpVTCMLLGEDAI 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 1707
Cdd:PRK07786  342 RKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVRQD 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVT--EKDIPIPEVRAYLATKL 1784
Cdd:PRK07786  411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRndDAALTLEDLAEFLTDRL 490
                         490       500
                  ....*....|....*....|....*...
gi 446807313 1785 PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07786  491 ARYKHPKALEIVDALPRNPAGKVLKTEL 518
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1331-1814 6.18e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 98.70  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVVCNEKGITYNELNIKANQLARrLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYM 1410
Cdd:PRK07638   14 QPNKIAIKENDRVLTYKDWFESVCKVAN-WLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1411 LTDSGCSHVLVHQNSIIKGIEFQGNVIDL---MDMSFEEEP----GEDMHmmiepHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PRK07638   93 LAISNADMIVTERYKLNDLPDEEGRVIEIdewKRMIEKYLPtyapIENVQ-----NAPFYMGFTSGSTGKPKAFLRAQQS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 -LTNFLCAMyEDFSqdIGITDNVLFSSSIsfdvtIFEIFvplIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSY 1556
Cdd:PRK07638  168 wLHSFDCNV-HDFH--MKREDSVLIAGTL-----VHSLF---LYGAISTLYVGqtvhlmRKFIPNQVLDKLETENISVMY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIY--DYFVRDNQKIVLNKLLVGVEPiKTELLAKYDHLfrgnlQILNGYGPTEATVCCTSYRYESNKEITTqn 1634
Cdd:PRK07638  237 TVPTMLESLYkeNRVIENKMKIISSGAKWEAEA-KEKIKNIFPYA-----KLYEFYGASELSFVTALVDEESERRPNS-- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 vpIGSPLLNTKIYILDSF-HRIQPiGVPGEICISGIGLARGYINRKELtadkfidhPFERGEKLYKT-GDIARWLPDGNI 1712
Cdd:PRK07638  309 --VGRPFHNVQVRICNEAgEEVQK-GEIGTVYVKSPQFFMGYIIGGVL--------ARELNADGWMTvRDVGYEDEEGFI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKylcAYVVTEKDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK07638  378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEK---PVAIIKGSATKQQLKSFCLQRLSSFKIPK 454
                         490       500
                  ....*....|....*....|...
gi 446807313 1792 QLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:PRK07638  455 EWHFVDEIPYTNSGKIARMEAKS 477
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1336-1812 6.21e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 98.52  E-value: 6.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1336 AVVCNEKGITYNELNIKANQLARRLLdqGVKResiVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSG 1415
Cdd:PRK07787   18 AVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1416 CSHVLVHQNSIIKGIEfqgNV-IDLMDMSFEEEPGEDmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 1494
Cdd:PRK07787   93 AQAWLGPAPDDPAGLP---HVpVRLHARSWHRYPEPD------PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FsqdiGIT-DNVLFSSSISFDV--TIFEIFVPLIYGARMtIYQGeKFDVTKLVQViLEEQVTLSYIPPTllneIYDYFVR 1571
Cdd:PRK07787  164 W----QWTaDDVLVHGLPLFHVhgLVLGVLGPLRIGNRF-VHTG-RPTPEAYAQA-LSEGGTLYFGVPT----VWSRIAA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 DN---QKIVLNKLLV-GVEPIKTELLAKYDHLfrGNLQILNGYGPTEaTVCCTSYRYESNKEITTqnvpIGSPLLNTKIY 1647
Cdd:PRK07787  233 DPeaaRALRGARLLVsGSAALPVPVFDRLAAL--TGHRPVERYGMTE-TLITLSTRADGERRPGW----VGLPLAGVETR 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ILDSfhriqpIGVP--------GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGR-- 1717
Cdd:PRK07787  306 LVDE------DGGPvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGRes 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1718 VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPI 1796
Cdd:PRK07787  374 TD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQR-IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFV 451
                         490
                  ....*....|....*.
gi 446807313 1797 HNIPLTQNGKIDRSKL 1812
Cdd:PRK07787  452 DALPRNAMGKVLKKQL 467
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1460-1807 7.31e-21

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: 96.03  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1460 NLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLIYGArmTIY 1533
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTedDRYLiinpFFHTFGYKAG---IVACLLTGA--TVV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLV-GVEPIKTELLAKYdHLFRGNLQILNGYGP 1612
Cdd:cd17638    72 PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELVRRM-RSELGFETVLTAYGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1613 TEAtVCCTSYRYESNKEITTQNVpiGSPLLNTKIYILDsfhriqpigvPGEICISGIGLARGYINRKELTAdKFIDhpfE 1692
Cdd:cd17638   151 TEA-GVATMCRPGDDAETVATTC--GRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATA-EAID---A 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 RGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIP 1772
Cdd:cd17638   214 DG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT 291
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446807313 1773 IPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd17638   292 LTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
276-769 1.67e-20

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 97.91  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK06155   22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTELPKQRVEYMLTDSGC------SHVLTYQNSIIKGV-------AFQGSVINLMDIPFEEEQVEDLQ-----ITMEPQN 417
Cdd:PRK06155  102 NTALRGPQLEHILRNSGArllvveAALLAALEAADPGDlplpavwLLDAPASVSVPAGWSTAPLPPLDapapaAAVQPGD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEdfSQDIGIT-DNVLFSSSISFDVTIFEIFVP-LVCGARMTIyqGEKF 495
Cdd:PRK06155  182 TAAILYTSGTTGPSKGVCCPHAQF--YWWGRNS--AEDLEIGaDDVLYTTLPLFHTNALNAFFQaLLAGATYVL--EPRF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  496 DVPKLVQVILEEQVTLAYipptLLNEIYDYFVR--ANQKISLNKLFVGVEP-IKTELLAKYDHLFrgNLQILNLYGPTEA 572
Cdd:PRK06155  256 SASGFWPAVRRHGATVTY----LLGAMVSILLSqpARESDRAHRVRVALGPgVPAALHAAFRERF--GVDLLDGYGSTET 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  573 TVCCTsyqyerdkeittqnVPIGSPLLNTKIYILDSFH--------RLQPIGVPGEICISG---IGLARGYINRKELTAD 641
Cdd:PRK06155  330 NFVIA--------------VTHGSQRPGSMGRLAPGFEarvvdehdQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  642 KFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAY 721
Cdd:PRK06155  396 AWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAA 468
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 446807313  722 VVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06155  469 VVLRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
417-764 1.86e-20

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: 94.88  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  417 NLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLVCGArmTIY 490
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTedDRYLiinpFFHTFGYKAG---IVACLLTGA--TVV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  491 QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLAKydhlFRGNLQILNL--- 566
Cdd:cd17638    72 PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELVRR----MRSELGFETVlta 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  567 YGPTEA---TVCctsyqyERDKEITTQNVPIGSPLLNTKIYILDsfhrlqpigvPGEICISGIGLARGYINRKELTAdKF 643
Cdd:cd17638   148 YGLTEAgvaTMC------RPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATA-EA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  644 IDhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd17638   211 ID---ADG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVV 285
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 446807313  724 TEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17638   286 ARPGVTLTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
417-766 3.55e-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: 94.01  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  417 NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGaRMTIYQGeKFD 496
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN--ISGEDAILAPGPLSHSLFLYGAISALYLG-GTFIGQR-KFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  497 VPKLVQVILEEQVTLAYIPPTLLNEIYdyfvRANQKISLNK-LFVGVEPIKTELLAKYDHLFRgNLQILNLYGPTEAT-V 574
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKsIFSSGQKLFESTKKKLKNIFP-KANLIEFYGTSELSfI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  575 CCTSYQYERDKEittqnvPIGSPLLNTKIYILDSFHrlqpiGVPGEICISGIGLARGYINRKELTADKFidhpfergekl 654
Cdd:cd17633   152 TYNFNQESRPPN------SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW----------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  655 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAyVVTEKDIPIPEVR 734
Cdd:cd17633   210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGDKLTYKQLK 288
                         330       340       350
                  ....*....|....*....|....*....|..
gi 446807313  735 AYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17633   289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1315-1812 3.59e-20

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 97.01  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1315 SNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA 1394
Cdd:PRK07059   20 SQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1395 YLPIDTDLPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQGNVIDLM-DM------------------------- 1442
Cdd:PRK07059  100 VVNVNPLYTPRELEHQLKDSGAEAIVVLENfattvqQVLAKTAVKHVVVASMgDLlgfkghivnfvvrrvkkmvpawslp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1443 ---SFEEEPGEDMHMMIEPHNL-----AYVIYTSGSTGQPKGVMIEHRSLT-----------------------NFLCAM 1491
Cdd:PRK07059  180 ghvRFNDALAEGARQTFKPVKLgpddvAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawlqpafekkprpdqlNFVCAL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 --YEDFSqdigITDNVLFSSSISfDVTIfeifvpLIYGARmtiyqgekfDVTKLVQVILEEQVTLsyIPP--TLLNEIYD 1567
Cdd:PRK07059  260 plYHIFA----LTVCGLLGMRTG-GRNI------LIPNPR---------DIPGFIKELKKYQVHI--FPAvnTLYNALLN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1568 YfvRDNQKIVLNKLLVGV-------EPIKTELLAKYdhlfrgNLQILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSP 1640
Cdd:PRK07059  318 N--PDFDKLDFSKLIVANgggmavqRPVAERWLEMT------GCPITEGYGLSETSPVATCNPVDATEFSGT----IGLP 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKE-----LTADKFidhpfergeklYKTGDIARWLPDGNIEYL 1715
Cdd:PRK07059  386 LPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDetakvMTADGF-----------FRTGDVGVMDERGYTKIV 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVtEKDIPIPE--VRAYLATKLPHYMIPQQL 1793
Cdd:PRK07059  455 DRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEedVKAFCKERLTNYKRPKFV 533
                         570
                  ....*....|....*....
gi 446807313 1794 IPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07059  534 EFRTELPKTNVGKILRREL 552
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1460-1809 3.71e-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: 94.01  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1460 NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLiYGARMTIYQGeKFD 1539
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN--ISGEDAILAPGPLSHSLFLYGAISAL-YLGGTFIGQR-KFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1540 VTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQ-KIVLNkllvGVEPIKTELLAKYDHLFRgNLQILNGYGPTEAtvc 1618
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTMLQALARTLEPESKiKSIFS----SGQKLFESTKKKLKNIFP-KANLIEFYGTSEL--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 ctSY-RYESNKEITTQNvPIGSPLLNTKIYILDSFHriqpiGVPGEICISGIGLARGYINRKELTADKFidhpfergekl 1697
Cdd:cd17633   149 --SFiTYNFNQESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW----------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAyVVTEKDIPIPEVR 1777
Cdd:cd17633   210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGDKLTYKQLK 288
                         330       340       350
                  ....*....|....*....|....*....|..
gi 446807313 1778 AYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17633   289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
301-769 4.53e-20

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: 95.71  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVeymltdsgcshvltyQ 380
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL---------------R 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  381 NSIIKGVAFQGSVinlmdipfeeeqvEDLQITMEPQnLAYviYTSGSTGQPKGVMIEHRSL-TNFLCAMYEdfsqdIGIT 459
Cdd:cd05974    66 DRVDRGGAVYAAV-------------DENTHADDPM-LLY--FTSGTTSKPKLVEHTHRSYpVGHLSTMYW-----IGLK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  460 --DNVLFSSSISFDVTIFE-IFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRANQ---KI 533
Cdd:cd05974   125 pgDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT----VWRMLIQQDLasfDV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  534 SLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYqyerdkeiTTQNVPIGS---PLLNTKIYILDsfh 610
Cdd:cd05974   201 KLREVVGAGEPLNPEVIEQVRRAW--GLTIRDGYGQTETTALVGNS--------PGQPVKAGSmgrPLPGYRVALLD--- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  611 rlqPIGVP---GEICIS-----GIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 682
Cdd:cd05974   268 ---PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  683 GYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-TEKDIPIPE----VRAYLATKL-PYYMIPQqiISIQNI 756
Cdd:cd05974   338 DYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlRAGYEPSPEtaleIFRFSRERLaPYKRIRR--LEFAEL 415
                         490
                  ....*....|...
gi 446807313  757 PLTQNGKIDRKKL 769
Cdd:cd05974   416 PKTISGKIRRVEL 428
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
276-769 2.08e-19

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 94.56  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLP 354
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  355 IDTELPKQRVEYMLTDSGCSHVL-------TYQNSI----IKGVAF----------QGSVINLMdIPFEEEQVEDLQIT- 412
Cdd:PRK08751  106 VNPLYTPRELKHQLIDSGASVLVvidnfgtTVQQVIadtpVKQVITtglgdmlgfpKAALVNFV-VKYVKKLVPEYRINg 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  413 --------------------MEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSISFD- 471
Cdd:PRK08751  185 airfrealalgrkhsmptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV----ANMQQAHQWLAGTGKLEEGCEVVITa 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  472 VTIFEIFVPLVCGARMTIYQG------EKFDVPKLVQVILEEQVTLAYIPPTLLNEI-----YDYFVRANQKISLNKLFV 540
Cdd:PRK08751  261 LPLYHIFALTANGLVFMKIGGcnhlisNPRDMPGFVKELKKTRFTAFTGVNTLFNGLlntpgFDQIDFSSLKMTLGGGMA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  541 gVEPIKTELLAKYDHLfrgnlQILNLYGPTEAT--VCCTSYqyerdkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:PRK08751  341 -VQRSVAERWKQVTGL-----TLVEAYGLTETSpaACINPL------TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEI 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  619 GEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK08751  409 GELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313  699 E-TIKTAVVIQREDESGEkyLCAYVVTEKD--IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08751  483 PgVLEVAAVGVPDEKSGE--IVKVVIVKKDpaLTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1464-1809 2.27e-19

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: 91.56  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRsltNFLCAMYEdFSQDIGITD-----NVLfsssisfdvtifeifvPL--IYGARM---TIY 1533
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHG---NLIAANLQ-LIHAMGLTEadvylNML----------------PLfhIAGLNLalaTFH 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVE-PiktELLAKYDHLFRGNLQI 1606
Cdd:cd17637    65 AGganvvmEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDaP---ETIQRFEETTGATFWS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 lnGYGPTEaTVCCTSYRYESNKEITTqnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAdkf 1686
Cdd:cd17637   142 --LYGQTE-TSGLVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA--- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 idHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQ--VKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGE--KYL 1761
Cdd:cd17637   211 --YTFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpKWGEgiKAV 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1762 CA----YVVTEKdipipEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17637   287 CVlkpgATLTAD-----ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
301-677 3.00e-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: 94.20  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKR--EFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTeLPKQRVEYMLTDSGCSHVL 377
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLyDT-LGPEAIEYILNHAEISIVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 tyqnsIIKGVAFQgSVINLMDIpfEEEQVEDLqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 457
Cdd:cd05927    85 -----CDAGVKVY-SLEEFEKL--GKKNKVPP-PPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 ITDNvlfSSSISF--DVTIFEIFVPLVC---GARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK 532
Cdd:cd05927   156 INPT---DVYISYlpLAHIFERVVEALFlyhGAKIGFYSG---DIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  533 IS--LNKLFvgvepiKTELLAKYDHLFRGNL----------------------------------------------QIL 564
Cdd:cd05927   230 KGplKRKLF------NFALNYKLAELRSGVVraspfwdklvfnkikqalggnvrlmltgsaplspevleflrvalgcPVL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  565 NLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDsfhrlqpigVP------------GEICISGIGLARGY 632
Cdd:cd05927   304 EGYGQTE-CTAGATLTLPGDTSVGH----VGGPLPCAEVKLVD---------VPemnydakdpnprGEVCIRGPNVFSGY 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 446807313  633 INRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd05927   370 YKDPEKTAEALDE------DGWLHTGDIGEWLPNGTLKIIDRKKN 408
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
7-238 3.58e-19

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: 92.76  E-value: 3.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd20484   175 EQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKL 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFkqGQEETVFQN------NFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:cd20484   255 LLHRYTGQEDIIVGMPTM--GRPEERFDSligyfiNMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  161 LDGESNNLPLLNTIVML-----------------DDIHCyESTDKINS----DMVIRFMKNEEQLKVQVDYNSTLYSEGL 219
Cdd:cd20484   333 IPRSQANSPVFQVAFFYqnflqstslqqflaeyqDVLSI-EFVEGIHQegeyELVLEVYEQEDRFTLNIKYNPDLFDAST 411
                         250
                  ....*....|....*....
gi 446807313  220 VSRIVNHLYNILDILMKDP 238
Cdd:cd20484   412 IERMMEHYVKLAEELIANP 430
PRK08315 PRK08315
AMP-binding domain protein; Validated
1322-1812 4.86e-19

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 93.34  E-value: 4.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK08315   20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCShVLVHQNSIiKGIEFQGNVIDLMDMSFEEEPGE-------DMHMMI----EPHNLAY----- 1463
Cdd:PRK08315  100 PAYRLSELEYALNQSGCK-ALIAADGF-KDSDYVAMLYELAPELATCEPGQlqsarlpELRRVIflgdEKHPGMLnfdel 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 -----------------------VI---YTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLfsssisfdv 1515
Cdd:PRK08315  178 lalgravddaelaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFIGEAMKLTEE----DRLC--------- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 tifeIFVPLIY--------------GARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTL----LNEI----YDyfvrdn 1573
Cdd:PRK08315  245 ----IPVPLYHcfgmvlgnlacvthGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMfiaeLDHPdfarFD------ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 qkivLNKLLVGV---EPIKTELLAKYD---HLfrgnLQILNGYGPTEAT-VCCTSYRYES-NKEITTqnvpIGSPLLNTK 1645
Cdd:PRK08315  314 ----LSSLRTGImagSPCPIEVMKRVIdkmHM----SEVTIAYGMTETSpVSTQTRTDDPlEKRVTT----VGRALPHLE 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSF-HRIQPIGVPGEICISGIGLARGYINRKELTADKfID-----HpfergeklykTGDIARWLPDGNIEYLGRVD 1719
Cdd:PRK08315  382 VKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDadgwmH----------TGDLAVMDEEGYVNIVGRIK 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVkIRG----Y-RielgEIEASLLKYETIKTAVVIDQEDeagEKY---LCAYVVTEKDIPIP--EVRAYLATKLPHYMI 1789
Cdd:PRK08315  451 DMI-IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPD---EKYgeeVCAWIILRPGATLTeeDVRDFCRGKIAHYKI 522
                         570       580
                  ....*....|....*....|...
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08315  523 PRYIRFVDEFPMTVTGKIQKFKM 545
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1453-1809 6.09e-19

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 93.14  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TNflCAMYEDFSQDIGITDNVLFSSSISFD---VTIFEIFVPLIyGA 1528
Cdd:PRK05605  213 HPRPTPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAWVPGLGDGPERVLAALPMFHaygLTLCLTLAVSI-GG 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMTIYqgEKFDVTKLVQVILEEQVTlsYIP--PTLLNEIYDYFVRDNQKI--VLNKLlVGVEPIKTELLAKYDHLFRGNL 1604
Cdd:PRK05605  290 ELVLL--PAPDIDLILDAMKKHPPT--WLPgvPPLYEKIAEAAEERGVDLsgVRNAF-SGAMALPVSTVELWEKLTGGLL 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 qiLNGYGPTEatvccTSYRYESNKeITTQNVP--IGSPLLNTKIYILD--SFHRIQPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK05605  365 --VEGYGLTE-----TSPIIVGNP-MSDDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPE 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKY 1760
Cdd:PRK05605  437 ETAKSFLD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1761 LCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK05605  510 VVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1341-1790 1.12e-18

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: 91.26  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1341 EKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHR---SLTNFLCAMYEDFSQ 1497
Cdd:cd05940    81 V--------------------------------------DAALYIYTSGTTGLPKAAIISHRrawRGGAFFAGSGGALPS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIGITDNVLFSSSISfdvtIFEIFVPLIYGArmTIYQGEKFDVTKLVQVILEEQVTL-SYIPPT---LLN---EIYDyfv 1570
Cdd:cd05940   123 DVLYTCLPLYHSTAL----IVGWSACLASGA--TLVIRKKFSASNFWDDIRKYQATIfQYIGELcryLLNqppKPTE--- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQ--KIVLNkllvGVEP-IKTELLAKYdhlfrGNLQILNGYGPTEATVCCTSY--------------RYESNKEITTQ 1633
Cdd:cd05940   194 RKHKvrMIFGN----GLRPdIWEEFKERF-----GVPRIAEFYAATEGNSGFINFfgkpgaigrnpsllRKVAPLALVKY 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTkiyilDSFHRIQPIGVPGEiCISGIG-LAR--GYINRKELTADKFIDhPFERGEKLYKTGDIARWLPDG 1710
Cdd:cd05940   265 DLESGEPIRDA-----EGRCIKVPRGEPGL-LISRINpLEPfdGYTDPAATEKKILRD-VFKKGDAWFNTGDLMRLDGEG 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1711 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekylCAYVVT--EKDIPIPEVRAYLATK 1783
Cdd:cd05940   338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYgvqvpGTDGRAG----MAAIVLqpNEEFDLSALAAHLEKN 413

                  ....*..
gi 446807313 1784 LPHYMIP 1790
Cdd:cd05940   414 LPGYARP 420
PRK08315 PRK08315
AMP-binding domain protein; Validated
276-769 1.12e-18

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 92.18  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  276 TAPQLFEEQVKQNPNQIAIVCNGKEI--TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYL 353
Cdd:PRK08315   17 TIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  354 PIDTELPKQRVEYMLTDSGCSHVLT--------YQNSI----------------------IKGVAFQGSVINLMDIPFEE 403
Cdd:PRK08315   97 TINPAYRLSELEYALNQSGCKALIAadgfkdsdYVAMLyelapelatcepgqlqsarlpeLRRVIFLGDEKHPGMLNFDE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  404 ----------EQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLfsssisfd 471
Cdd:PRK08315  177 llalgravddAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngYFIGEAMKLTEE----DRLC-------- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  472 vtifeIFVP-----------LVC---GARMtIYQGEKFDvPKLV-QVILEEQVTLAYIPPTL----LNEI----YDyfvr 528
Cdd:PRK08315  245 -----IPVPlyhcfgmvlgnLACvthGATM-VYPGEGFD-PLATlAAVEEERCTALYGVPTMfiaeLDHPdfarFD---- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 anqkisLNKLFVGV---EPIKTELLAKYD---HLfrgnLQILNLYGPTEAT-VcctSYQYERD----KEITTqnvpIGSP 597
Cdd:PRK08315  314 ------LSSLRTGImagSPCPIEVMKRVIdkmHM----SEVTIAYGMTETSpV---STQTRTDdpleKRVTT----VGRA 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  598 LLNTKIYILDSF-HRLQPIGVPGEICISGIGLARGYINRKELTADKfID-----HpfergeklykTGDIARWLPDGNIEY 671
Cdd:PRK08315  377 LPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDadgwmH----------TGDLAVMDEEGYVNI 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  672 LGRVDHQVkIRG----Y-RielgEIEASLLKYETIKTAVVIQREDEsgeKY---LCAYVVTEKDIPIP--EVRAYLATKL 741
Cdd:PRK08315  446 VGRIKDMI-IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDE---KYgeeVCAWIILRPGATLTeeDVRDFCRGKI 517
                         570       580
                  ....*....|....*....|....*...
gi 446807313  742 PYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08315  518 AHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1344-1767 1.41e-18

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: 91.51  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGgayLPIDT---DLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyaTLGEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VHQNsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 1500
Cdd:cd17639    83 TDGK---------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNVLFSSSISFdvtIFEI---FVPLIYGARM----------TIYQGEKFDV-----TKLVQV----------ILEEQV 1552
Cdd:cd17639   130 PDDRYLAYLPLAH---IFELaaeNVCLYRGGTIgygsprtltdKSKRGCKGDLtefkpTLMVGVpaiwdtirkgVLAKLN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTL-----------LNEIYDYFVRDnqKIVLNK-----------LLVGVEPIKTEllakyDHLFRGNL--QILN 1608
Cdd:cd17639   207 PMGGLKRTLfwtayqsklkaLKEGPGTPLLD--ELVFKKvraalggrlryMLSGGAPLSAD-----TQEFLNIVlcPVIQ 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1609 GYGPTEaTVCCTsyryesnkeiTTQNVP------IGSPLLNTKIYILD------SFHRIQPigvPGEICISGIGLARGYI 1676
Cdd:cd17639   280 GYGLTE-TCAGG----------TVQDPGdletgrVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYY 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1677 NRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:cd17639   346 KNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK 419
                         490
                  ....*....|..
gi 446807313 1756 AgekYLCAYVVT 1767
Cdd:cd17639   420 S---YPVAIVVP 428
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1324-1791 1.41e-18

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 92.24  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLV------------------HQNSIIKGIEFQ--GNVIDLMDMSFE---EEPGEDMHMMIEphN 1460
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVgeelveafeearadlarpPRLWVAGGDTLDdpEGYEDLAAAAAGaptTNPASRSGVTAK--D 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPK-GVMIEHRSLTnflcaMYEDFSQDIGITDNvlfsssisfDVtifeIFVPL-IY------------ 1526
Cdd:PRK08279  201 TAFYIYTSGTTGLPKaAVMSHMRWLK-----AMGGFGGLLRLTPD---------DV----LYCCLpLYhntggtvawssv 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 ---GARMTIyqGEKFDVTKLVQVILEEQVTL-SYIpptllNEIYDYFV--------RDNQ--KIVLNkllvGVEP-IKTE 1591
Cdd:PRK08279  263 laaGATLAL--RRKFSASRFWDDVRRYRATAfQYI-----GELCRYLLnqppkptdRDHRlrLMIGN----GLRPdIWDE 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1592 LLAKYdhlfrGNLQILNGYGPTEATVcctSYRYESNKEITTQNVPI---------------GSPLLNTKiyildsfHRIQ 1656
Cdd:PRK08279  332 FQQRF-----GIPRILEFYAASEGNV---GFINVFNFDGTVGRVPLwlahpyaivkydvdtGEPVRDAD-------GRCI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1657 PIGvPGEI--CISGIGLAR---GYiNRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:PRK08279  397 KVK-PGEVglLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVAT 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1732 GEIEASLLKYETIKTAVVI-----DQEDEAGekyLCAYVVTE-KDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK08279  475 TEVENALSGFPGVEEAVVYgvevpGTDGRAG---MAAIVLADgAEFDLAALAAHLYERLPAYAVPL 537
PRK07787 PRK07787
acyl-CoA synthetase; Validated
293-772 2.06e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 90.82  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  293 AIVCNGKEITYKQLNIKANQLARRLLdqGVKRefiVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG 372
Cdd:PRK07787   18 AVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  373 CSHVLtyqnsiikgVAFQGSVINLMDIPFEEEQVEDLQI-TMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 451
Cdd:PRK07787   93 AQAWL---------GPAPDDPAGLPHVPVRLHARSWHRYpEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  452 FsqdiGIT-DNVLFSSSISFDV--TIFEIFVPLVCGARMtIYQGeKFDvPKLVQVILEEQVTLAYIPPTLLNEIYDYFVR 528
Cdd:PRK07787  164 W----QWTaDDVLVHGLPLFHVhgLVLGVLGPLRIGNRF-VHTG-RPT-PEAYAQALSEGGTLYFGVPTVWSRIAADPEA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 AnQKISLNKLFV-GVEPIKTELLAKYDHLfrGNLQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD 607
Cdd:PRK07787  237 A-RALRGARLLVsGSAALPVPVFDRLAAL--TGHRPVERYGMTE-TLITLSTRADGERRPGW----VGLPLAGVETRLVD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  608 SfhrlqpIGVP--------GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGR--VDh 677
Cdd:PRK07787  309 E------DGGPvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNI 756
Cdd:PRK07787  376 LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlGQR-IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDAL 454
                         490
                  ....*....|....*.
gi 446807313  757 PLTQNGKIDRKKLPQP 772
Cdd:PRK07787  455 PRNAMGKVLKKQLLSE 470
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1325-1814 3.42e-18

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: 90.60  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1325 EEQVKRNPNQIAVVCNEKGI----TYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd05928    19 EKAGKRPPNPALWWVNGKGDevkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLtdsgcshvlvhQNSIIKGIEFQGNVIDLMD-----------------------MSFEE---EPGEDMH 1453
Cdd:cd05928    99 IQLTAKDILYRL-----------QASKAKCIVTSDELAPEVDsvasecpslktkllvseksrdgwLNFKEllnEASTEHH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1454 MMIEPHNLAYVIY-TSGSTGQPKgvMIEHR----SLTNFLCAMY--EDFSQDI--GITDNVLFSSSISfdvtifEIFVPL 1524
Cdd:cd05928   168 CVETGSQEPMAIYfTSGTTGSPK--MAEHShsslGLGLKVNGRYwlDLTASDImwNTSDTGWIKSAWS------SLFEPW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDN----QKIVLNKLLVGVEPIKTELLAKYDHlf 1600
Cdd:cd05928   240 IQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPT----VYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKA-- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1601 RGNLQILNGYGPTEATVCCTSYRyesNKEITTQNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICIS-----GIGLARGY 1675
Cdd:cd05928   314 QTGLDIYEGYGQTETGLICANFK---GMKIKPGSMGKASPPYDVQI--IDDNGNVLPPGTEGDIGIRvkpirPFGLFSGY 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKfidhpfERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:cd05928   389 VDNPEKTAAT------IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1756 AGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05928   462 IRGEVVKAFVVlapqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
907-1184 3.67e-18

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: 89.47  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  907 DICKDKFENIFQSLIERHEILRTSFQIlDGElvQKIEPNV-DFNIEyVH----VNEKDAD--------YLIHEFISP--- 970
Cdd:cd19535    36 DLDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVpWYGIT-VHdlrgLSEEEAEaaleelreRLSHRVLDVerg 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  971 --FDLSkppllrvlLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNE--LPKLRVQYKDYVMWQNgPYYKNLI 1046
Cdd:cd19535   112 plFDIR--------LSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGepLPPLELSFRDYLLAEQ-ALRETAY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1047 SEQKNYW---LTTLKG--ELPVLNFPTDFQRPTIQSFkgnvcSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRY 1121
Cdd:cd19535   183 ERARAYWqerLPTLPPapQLPLAKDPEEIKEPRFTRR-----EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1122 TGQEDIIVGSPIAGR--SHSDTNHMIGMFIN-TLV-MRNylENDDEFIEFLSRLKLNTLEAYENQDY 1184
Cdd:cd19535   258 SGQPRFLLNLTLFNRlpLHPDVNDVVGDFTSlLLLeVDG--SEGQSFLERARRLQQQLWEDLDHSSY 322
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
298-747 5.50e-18

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: 89.34  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 TyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHR---SLTNFLCAMYEDFSQ 454
Cdd:cd05940    81 V--------------------------------------DAALYIYTSGTTGLPKAAIISHRrawRGGAFFAGSGGALPS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  455 DIGITDNVLFSSSISfdvtIFEIFVPLVCGArmTIYQGEKFDVPKLVQVILEEQVTL-AYIPPT---LLN---EIYDyfv 527
Cdd:cd05940   123 DVLYTCLPLYHSTAL----IVGWSACLASGA--TLVIRKKFSASNFWDDIRKYQATIfQYIGELcryLLNqppKPTE--- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  528 RANQ--KISLNklfvGVEP-IKTELLAKYdhlfrGNLQILNLYGPTEATvcCTSYQYERDKEITTQNVPIGSPLLNTKI- 603
Cdd:cd05940   194 RKHKvrMIFGN----GLRPdIWEEFKERF-----GVPRIAEFYAATEGN--SGFINFFGKPGAIGRNPSLLRKVAPLALv 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  604 -YILDS---------FHRLQPIGVPGEiCISGIG-LAR--GYINRKELTADKFIDhPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:cd05940   263 kYDLESgepirdaegRCIKVPRGEPGL-LISRINpLEPfdGYTDPAATEKKILRD-VFKKGDAWFNTGDLMRLDGEGFWY 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV--IQREDESGEKYLCAYVV-TEKDIPIPEVRAYLATKLPYYMIP 747
Cdd:cd05940   341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLqPNEEFDLSALAAHLEKNLPGYARP 420
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
284-769 5.79e-18

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: 90.31  E-value: 5.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  284 QVKQNPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG-------G 350
Cdd:cd05966    62 HLKERGDKVAIIWEGDEpdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  351 AYLPidtELPKQRVEymltDSGCSHVLTyqnsiIKGVAFQGSVINL--------------------------------MD 398
Cdd:cd05966   142 GFSA---ESLADRIN----DAQCKLVIT-----ADGGYRGGKVIPLkeivdealekcpsvekvlvvkrtggevpmtegRD 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  399 IPFEEEqVEDLQITMEPQNLA-----YVIYTSGSTGQPKGVMieHRS--------LT-----------NFLCAmyedfsQ 454
Cdd:cd05966   210 LWWHDL-MAKQSPECEPEWMDsedplFILYTSGSTGKPKGVV--HTTggyllyaaTTfkyvfdyhpddIYWCT------A 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  455 DIG-ITDNvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPT---LLNEIYD 524
Cdd:cd05966   281 DIGwITGH----SYI--------VYGPLANGATTVMFEG----TPtypdpgRYWDIVEKHKVTIFYTAPTairALMKFGD 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  525 YFVRANQKISLNKL-FVGvEPIKTEL-LAKYDHLFRGNLQILNLYGPTEATVCCtsyqyerdkeIT-----TQNVPiGS- 596
Cdd:cd05966   345 EWVKKHDLSSLRVLgSVG-EPINPEAwMWYYEVIGKERCPIVDTWWQTETGGIM----------ITplpgaTPLKP-GSa 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  597 --PLLNTKIYILDSFHRLQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd05966   413 trPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWIT 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVV-----TEKDIPIPEVRAYLATKLPYYMI 746
Cdd:cd05966   489 GRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEA-IYAFVTlkdgeEPSDELRKELRKHVRKEIGPIAT 567
                         570       580
                  ....*....|....*....|...
gi 446807313  747 PQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05966   568 PDKIQFVPGLPKTRSGKIMRRIL 590
PRK09274 PRK09274
peptide synthase; Provisional
286-680 7.25e-18

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 89.57  E-value: 7.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIVCNG----------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK09274   17 QERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  356 DTEL--------------------PKQRVEYMLTDSGCS---HVLTYQNSIIKGVAFQGSVinLMDIPFEEEQVEDLQit 412
Cdd:PRK09274   97 DPGMgiknlkqclaeaqpdafigiPKAHLARRLFGWGKPsvrRLVTVGGRLLWGGTTLATL--LRDGAAAPFPMADLA-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  413 mePQNLAYVIYTSGSTGQPKGVMIEHRSltnfLCAMYEDFSQDIGITDNvlfsssiSFDVTIFEIFV--PLVCGARMTIy 490
Cdd:PRK09274  173 --PDDMAAILFTSGSTGTPKGVVYTHGM----FEAQIEALREDYGIEPG-------EIDLPTFPLFAlfGPALGMTSVI- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  491 qgekfdvP-------------KLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK09274  239 -------PdmdptrpatvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERFRAM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  557 FRGNLQILNLYGPTEATVCCT---SYQYERDKEITTQN--VPIGSPLLNTKIYI----------LDSFHRLqPIGVPGEI 621
Cdd:PRK09274  312 LPPDAEILTPYGATEALPISSiesREILFATRAATDNGagICVGRPVDGVEVRIiaisdapipeWDDALRL-ATGEIGEI 390
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  622 CISGIGLARGYINRKELTA-DKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 680
Cdd:PRK09274  391 VVAGPMVTRSYYNRPEATRlAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
PLN03102 PLN03102
acyl-activating enzyme; Provisional
271-769 8.58e-18

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 89.69  E-value: 8.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  271 LCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGIL 346
Cdd:PLN03102    6 LCEANNVPltpiTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  347 KAGGAYLPIDTELPKQRVEYMLTDSG-------------CSHVL----TYQNSIIKGVAFqgsvINLMDIP----FEEEQ 405
Cdd:PLN03102   86 MAGAVLNPINTRLDATSIAAILRHAKpkilfvdrsfeplAREVLhllsSEDSNLNLPVIF----IHEIDFPkrpsSEELD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  406 VEDLQITMEPQNLAY--------------VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSI--- 468
Cdd:PLN03102  162 YECLIQRGEPTPSLVarmfriqdehdpisLNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCPVYLWTLPMfhc 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  469 ---SFDVTIFEIFVPLVCGARMTiyqgekfdVPKLVQVILEEQVTLAYIPPTLLNeiydYFVRANQ-----KISLNKLFV 540
Cdd:PLN03102  240 ngwTFTWGTAARGGTSVCMRHVT--------APEIYKNIEMHNVTHMCCVPTVFN----ILLKGNSldlspRSGPVHVLT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  541 GVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT--VCCTSYQYERDKEITTQNVPIGSP--LLNTKIYILDSFHRLQPIG 616
Cdd:PLN03102  308 GGSPPPAALVKKVQRL---GFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKARqgVSILGLADVDVKNKETQES 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  617 VP------GEICISGIGLARGYINRKELTADKFiDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:PLN03102  385 VPrdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVE 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  691 IEASLLKY-ETIKTAVVIQREDESGEKyLCAYVVTEK-DIPIPEVRAYLATK-----------LPYYMIPQQIISIQNIP 757
Cdd:PLN03102  458 VENVLYKYpKVLETAVVAMPHPTWGET-PCAFVVLEKgETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELP 536
                         570
                  ....*....|..
gi 446807313  758 LTQNGKIDRKKL 769
Cdd:PLN03102  537 KNGNGKILKPKL 548
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
289-764 1.16e-17

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 88.86  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:PRK08314   24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  368 LTDSGCSHVLTYQNSIIKGVAFQGS-------VINLMD----------------------------IPFEE---EQVEDL 409
Cdd:PRK08314  104 VTDSGARVAIVGSELAPKVAPAVGNlrlrhviVAQYSDylpaepeiavpawlraepplqalapggvVAWKEalaAGLAPP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDfsqdiGITDNVLFSSSISFDVTIFE--IFVPLVCGA 485
Cdd:PRK08314  184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmaNAVGSVLWSN-----STPESVVLAVLPLFHVTGMVhsMNAPIYAGA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  486 rmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiYDYFvrANQKIS---LNKL-FVG------VEPIKTELLAKYdh 555
Cdd:PRK08314  259 --TVVLMPRWDREAAARLIERYRVTHWTNIPTMV---VDFL--ASPGLAerdLSSLrYIGgggaamPEAVAERLKELT-- 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  556 lfrgNLQILNLYGPTEatvccTSYQyerdkeiTTQNVP-------IGSPLLNTKIYILD--SFHRLqPIGVPGEICISGI 626
Cdd:PRK08314  330 ----GLDYVEGYGLTE-----TMAQ-------THSNPPdrpklqcLGIPTFGVDARVIDpeTLEEL-PPGEVGEIVVHGP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  627 GLARGYINRKELTADKFIDhpFErGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 706
Cdd:PRK08314  393 QVFKGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACV 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  707 IQREDE-SGE--KylcAYVV---------TEKDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKI 764
Cdd:PRK08314  470 IATPDPrRGEtvK---AVVVlrpeargktTEEEI-IAWAREHMAA----YKYPRIVEFVDSLPKSGSGKI 531
PRK07470 PRK07470
acyl-CoA synthetase; Validated
286-767 1.23e-17

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 88.94  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK07470   18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 YMLTDSGCS----------HV-------LTYQNSIIKGVAFQGS-----VINLMDIPFEEEQVE-DlqitmEPqnlAYVI 422
Cdd:PRK07470   98 YLAEASGARamichadfpeHAaavraasPDLTHVVAIGGARAGLdyealVARHLGARVANAAVDhD-----DP---CWFF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  423 YTSGSTGQPKGVMIEHRSL----TNFLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIfVPLVCGARMTIYQGEKFDVP 498
Cdd:PRK07470  170 FTSGTTGRPKAAVLTHGQMafviTNHLADLMPGTTEQ----DASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  499 KLVQVILEEQVTLAYIPPTLLN--------EIYD-----YFV-------RANQKISLNKLfvgvepikTELLAKYdhlfr 558
Cdd:PRK07470  245 EVWALVERHRVTNLFTVPTILKmlvehpavDRYDhsslrYVIyagapmyRADQKRALAKL--------GKVLVQY----- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  559 gnlqilnlYGPTEATVCCT---SYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:PRK07470  312 --------FGLGEVTGNITvlpPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNN 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  636 KELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED---- 711
Cdd:PRK07470  384 PEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwg 456
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  712 ESGekylCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:PRK07470  457 EVG----VAVCVARDGAPVdeAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1344-1810 1.30e-17

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: 88.83  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESiVGVMMKRSIEMVIGILGVLKAGG----AYLPidtDLPKQ--RVEYMLTDSGCS 1417
Cdd:cd05931    25 LTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAiavpLPPP---TPGRHaeRLAAILADAGPR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLV----------HQNSIIKGIEFQGNVIDLMDmsfEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TN 1486
Cdd:cd05931   101 VVLTtaaalaavraFAASRPAAGTPRLLVVDLLP---DTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlAN 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 FLCAM--YEDFSQDIGIT------DNVLfsssisfdvtIFEIFVPLIYGARMTIYQGEKFdVTK---LVQVILEEQVTLS 1555
Cdd:cd05931   178 VRQIRraYGLDPGDVVVSwlplyhDMGL----------IGGLLTPLYSGGPSVLMSPAAF-LRRplrWLRLISRYRATIS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPptllNEIYDYFVR-----DNQKIVLNKL---LVGVEPIKTELLAKYDHLFRG-NLQ---ILNGYGPTEATV------ 1617
Cdd:cd05931   247 AAP----NFAYDLCVRrvrdeDLEGLDLSSWrvaLNGAEPVRPATLRRFAEAFAPfGFRpeaFRPSYGLAEATLfvsggp 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 -----CCTSYRYESNK----------EITTQNVPIGSPLLNTKIYILDSFHRIQ-PIGVPGEICISGIGLARGYINRKEL 1681
Cdd:cd05931   323 pgtgpVVLRVDRDALAgravavaaddPAARELVSCGRPLPDQEVRIVDPETGRElPDGEVGEIWVRGPSVASGYWGRPEA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1682 TADKFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASlLKYETIKT------AVVIDQEDE 1755
Cdd:cd05931   403 TAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEAT-AEEAHPALrpgcvaAFSVPDDGE 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1756 AGEKYLCAYV--VTEKDIP--IPEVRAYLATKlpHYMIPQQ--LIPIHNIPLTQNGKIDRS 1810
Cdd:cd05931   481 ERLVVVAEVErgADPADLAaiAAAIRAAVARE--HGVAPADvvLVRPGSIPRTSSGKIQRR 539
PLN03102 PLN03102
acyl-activating enzyme; Provisional
1332-1812 1.31e-17

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 88.92  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL--------- 1402
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLdatsiaail 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 ----PK------------QRVEYML-TDSGCSH---VLVHQNSIIKGIEFQGNVIDLMDMSFEEEPG--EDMHMMIEPHN 1460
Cdd:PLN03102  108 rhakPKilfvdrsfeplaREVLHLLsSEDSNLNlpvIFIHEIDFPKRPSSEELDYECLIQRGEPTPSlvARMFRIQDEHD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSI----------------SFDVTIFEIFVPL 1524
Cdd:PLN03102  188 PISLNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCPVYLWTLPMfhcngwtftwgtaargGTSVCMRHVTAPE 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGarmtiyQGEKFDVTKLVQVileeqvtlsyipPTLLNeiydyFVRDNQKIVLN------KLLVGVEPIKTELLAKYDH 1598
Cdd:PLN03102  266 IYK------NIEMHNVTHMCCV------------PTVFN-----ILLKGNSLDLSprsgpvHVLTGGSPPPAALVKKVQR 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1599 LfrgNLQILNGYGPTEAT--VCCTSYRYESNKEITTQNVPIGSP--LLNTKIYILDSFHRIQPIGVP------GEICISG 1668
Cdd:PLN03102  323 L---GFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKARqgVSILGLADVDVKNKETQESVPrdgktmGEIVIKG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1669 IGLARGYINRKELTADKFiDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY-ETIKTA 1747
Cdd:PLN03102  400 SSIMKGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYpKVLETA 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1748 VVIDQEDEAGEKyLCAYVVTEK-DIPIPEVRAYLATK-----------LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN03102  473 VVAMPHPTWGET-PCAFVVLEKgETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
301-724 1.33e-17

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: 88.43  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGgayLPIDT---ELPKQRVEYMLTDSGCSHVL 377
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyaTLGEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 TYQNsiikgvafqgsvinlmdipfeeeqvedlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 457
Cdd:cd17639    83 TDGK---------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 ITDNVLFSSSISFdvtIFEIFVPLVC---GARM----------TIYQGEKFD-----------VPKLVQVI---LEEQV- 509
Cdd:cd17639   130 PDDRYLAYLPLAH---IFELAAENVClyrGGTIgygsprtltdKSKRGCKGDltefkptlmvgVPAIWDTIrkgVLAKLn 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  510 TLAYIPPTLLNEIYDYFVRANQKIS----LNKLFVGvePIKTEL-------------LAKYDHLFRGNL--QILNLYGPT 570
Cdd:cd17639   207 PMGGLKRTLFWTAYQSKLKALKEGPgtplLDELVFK--KVRAALggrlrymlsggapLSADTQEFLNIVlcPVIQGYGLT 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  571 EaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD------SFHRLQPigvPGEICISGIGLARGYINRKELTADKFi 644
Cdd:cd17639   285 E-TCAGGTVQDPGDLETGR----VGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAF- 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  645 dhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIQREDESgekYLCAYVV 723
Cdd:cd17639   356 -----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS---YPVAIVV 427

                  .
gi 446807313  724 T 724
Cdd:cd17639   428 P 428
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1327-1815 1.44e-17

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: 89.16  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAV------VCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILG---------VLKA 1391
Cdd:cd05966    62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1392 G-------------GAYLPIDTD--------LP-KQRVEYMLTDSGC-SHVLVHQNSiikgiefqGNVIDLM---DMSFE 1445
Cdd:cd05966   142 GfsaesladrindaQCKLVITADggyrggkvIPlKEIVDEALEKCPSvEKVLVVKRT--------GGEVPMTegrDLWWH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1446 EE-PGEDMHMMIEP----HNLaYVIYTSGSTGQPKGVMieHRS--------LT-----------NFLCAmyedfsQDIG- 1500
Cdd:cd05966   214 DLmAKQSPECEPEWmdseDPL-FILYTSGSTGKPKGVV--HTTggyllyaaTTfkyvfdyhpddIYWCT------ADIGw 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNvlfsSSIsfdvtifeIFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEiydyFVRDNQKIVL 1578
Cdd:cd05966   285 ITGH----SYI--------VYGPLANGATTVMFEGTPTypDPGRYWDIVEKHKVTIFYTAPTAIRA----LMKFGDEWVK 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 N------KLL--VGvEPIKTEL-LAKYDHLFRGNLQILNGYGPTEatvccTSYRYESNKEITTQNVPiGS---PLLNTKI 1646
Cdd:cd05966   349 KhdlsslRVLgsVG-EPINPEAwMWYYEVIGKERCPIVDTWWQTE-----TGGIMITPLPGATPLKP-GSatrPFFGIEP 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1647 YILDSFHRIQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 1724
Cdd:cd05966   422 AILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINV 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1725 RGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:cd05966   498 SGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGL 577
                         570
                  ....*....|....*.
gi 446807313 1800 PLTQNGKIDRSKLPKL 1815
Cdd:cd05966   578 PKTRSGKIMRRILRKI 593
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
281-748 1.45e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 89.16  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  361 KQRVEYMLTDSGCSHVL-------TYQnSIIKGVAFQGSVINLMDIPFEEEQ-VEDL----------------QITMEpq 416
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIvgeelveAFE-EARADLARPPRLWVAGGDTLDDPEgYEDLaaaaagapttnpasrsGVTAK-- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  417 NLAYVIYTSGSTGQPK-GVMIEHRSLTnflcaMYEDFSQDIGITDNvlfsssisfDVtiFEIFVPL-------VC----- 483
Cdd:PRK08279  200 DTAFYIYTSGTTGLPKaAVMSHMRWLK-----AMGGFGGLLRLTPD---------DV--LYCCLPLyhntggtVAwssvl 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  484 --GARMTIyqGEKFDVPKLVQVILEEQVTL-AYIpptllNEIYDYFV--------RANqkiSLNKLF-VGVEP-IKTELL 550
Cdd:PRK08279  264 aaGATLAL--RRKFSASRFWDDVRRYRATAfQYI-----GELCRYLLnqppkptdRDH---RLRLMIgNGLRPdIWDEFQ 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  551 AKYdhlfrGNLQILNLYGPTEATVCCTSYqYERDKeiTTQNVPI---------------GSPLLNTKiyildsfHRLQPI 615
Cdd:PRK08279  334 QRF-----GIPRILEFYAASEGNVGFINV-FNFDG--TVGRVPLwlahpyaivkydvdtGEPVRDAD-------GRCIKV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  616 GvPGEI--CISGIGLAR---GYiNRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:PRK08279  399 K-PGEVglLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTE 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313  691 IEASLLKYETIKTAVV--IQREDESGEKYLCAYVVTE-KDIPIPEVRAYLATKLPYYMIPQ 748
Cdd:PRK08279  477 VENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVPL 537
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1323-1812 1.98e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 88.26  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShVLVHQNSIiKGIEFQGNV-------------IDLMDMSFEEEPGE---------DMHMMIE--- 1457
Cdd:PRK06164   95 RSHEVAHILGRGRAR-WLVVWPGF-KGIDFAAILaavppdalpplraIAVVDDAADATPAPapgarvqlfALPDPAPpaa 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 -------PHNLAYVIYTSGSTGQPKGVMieHRSLTnfLCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLIYGA 1528
Cdd:PRK06164  173 ageraadPDAGALLFTTSGTTSGPKLVL--HRQAT--LLRHARAIARAYGYDPGavLLAALPFCGVFGFSTLLGALAGGA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 rmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKLLVGV---EPIKTELLAkydhLFRGNLQ 1605
Cdd:PRK06164  249 --PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILD--TAGERADFPSARLFGFasfAPALGELAA----LARARGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILNG-YGPTE--ATVCC------TSYRYESNkeittqNVPIgSPllNTKIYILDSFH-RIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK06164  321 PLTGlYGSSEvqALVALqpatdpVSVRIEGG------GRPA-SP--EARVRARDPQDgALLPDGESGEIEIRAPSLMRGY 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK06164  392 LDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1756 aGEKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNG---KIDRSKL 1812
Cdd:PRK06164  466 -GKTVPVAFVIPTDGASPdeAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1329-1807 3.37e-17

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 87.40  E-value: 3.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK07470   18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCSHVLV------HQNSIIKGIEFQGNVIDLMDMSFEEEPG----EDMHMMIEPHNLAY-----VIYTSGSTGQ 1473
Cdd:PRK07470   98 YLAEASGARAMIChadfpeHAAAVRAASPDLTHVVAIGGARAGLDYEalvaRHLGARVANAAVDHddpcwFFFTSGTTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSL----TNFLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIfVPLIYGARMTIYQGEKFDVTKLVQVILE 1549
Cdd:PRK07470  178 PKAAVLTHGQMafviTNHLADLMPGTTEQ----DASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAEVWALVER 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1550 EQVTLSYIPPTLLN--------EIYD-----YFV-------RDNQKIVLNKLlvgvepikTELLAKYdhlfrgnlqilng 1609
Cdd:PRK07470  253 HRVTNLFTVPTILKmlvehpavDRYDhsslrYVIyagapmyRADQKRALAKL--------GKVLVQY------------- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1610 YGPTEATVCCTSYRYESNKEITTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK07470  312 FGLGEVTGNITVLPPALHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLcAYV 1765
Cdd:PRK07470  392 RDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwGEVGV-AVC 463
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446807313 1766 VTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK07470  464 VARDGAPVdeAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
567-769 5.22e-17

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 87.18  E-value: 5.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  567 YGPTEATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidh 646
Cdd:PRK12492  365 YGLTETSPVASTNPYGELARLGT----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL--- 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  647 pfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKYLCAYVVTE 725
Cdd:PRK12492  438 ---DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErSGEAVKLFVVARD 514
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446807313  726 KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK12492  515 PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1634-1899 5.97e-17

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 83.65  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGN 1711
Cdd:COG3433    17 PPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpaQPGRQADDLRLLLRRGLGPG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEkDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:COG3433    97 GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAAL-DGLAAAAALAALDKVPPDVVAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1792 QLIPIHNIPLTQNGKIDRSKLPKL-NTLGNSNYVPPRNEIDSSLI-----DIWSSILGV--NNIGINDNFFELGGHSLKG 1863
Cdd:COG3433   176 SAVVALDALLLLALKVVARAAPALaAAEALLAAASPAPALETALTeeelrADVAELLGVdpEEIDPDDNLFDLGLDSIRL 255
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 446807313 1864 LKLFENIKRMfNVQLPLSLLFQKATIEQLSDVISRN 1899
Cdd:COG3433   256 MQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAA 290
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1458-1815 6.33e-17

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 84.84  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKgvMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIsFDV--TIFEIFVPLIYGARMTI--- 1532
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLagp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1533 --YQG-----------EKFDVTKLVQVileeqvtlsyipPTLLNEIYDyfVRDNQKI-VLNKLLVGVEPIKTELLAKY-D 1597
Cdd:cd05944    78 agYRNpglfdnfwklvERYRITSLSTV------------PTVYAALLQ--VPVNADIsSLRFAMSGAAPLPVELRARFeD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 HLfrgNLQILNGYGPTEATvcCTSYRYESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVP--GEICISGIGLARG 1674
Cdd:cd05944   144 AT---GLPVVEGYGLTEAT--CLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1675 YINrKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:cd05944   219 YLY-TEGNKNAFVA------DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQP 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1754 D-EAGEkYLCAYVVTEKDIPIP--EVRAYLATKLPHY-MIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05944   291 DaHAGE-LPVAYVQLKPGAVVEeeELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRAD 355
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
290-769 6.60e-17

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 86.87  E-value: 6.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  290 NQIAIVCNGKE----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG-------AYLPidtE 358
Cdd:PRK04319   59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAivgplfeAFME---E 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEymltDSGCSHVLT----YQNSIIKGVAFQGSVInLMDIPFEE-EQVEDLQITME------------PQNLAYV 421
Cdd:PRK04319  136 AVRDRLE----DSEAKVLITtpalLERKPADDLPSLKHVL-LVGEDVEEgPGTLDFNALMEqasdefdiewtdREDGAIL 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  422 IYTSGSTGQPKGVMIEHRS-LTNFLCAMYE-DFSQDigitdnvlfsssisfDV------------TIFEIFVPLVCGARM 487
Cdd:PRK04319  211 HYTSGSTGKPKGVLHVHNAmLQHYQTGKYVlDLHED---------------DVywctadpgwvtgTSYGIFAPWLNGATN 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  488 TIYQGEkFDVPKLVQVILEEQVTLAYIPPTLLNeiydYFVRAN----QKISLNKL----FVGvEPIKTELLAKYDHLFrg 559
Cdd:PRK04319  276 VIDGGR-FSPERWYRILEDYKVTVWYTAPTAIR----MLMGAGddlvKKYDLSSLrhilSVG-EPLNPEVVRWGMKVF-- 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  560 NLQILNLYGPTE--ATVCCTSYqyerdkeitTQNVPIGS---PLLNTKIYILDSFHRLQPIGVPGEICI-----SgigLA 629
Cdd:PRK04319  348 GLPIHDNWWMTEtgGIMIANYP---------AMDIKPGSmgkPLPGIEAAIVDDQGNELPPNRMGNLAIkkgwpS---MM 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  630 RGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQR 709
Cdd:PRK04319  416 RGIWNNPEKYESYFAG-------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  710 EDE-SGE--KylcAYV-----VTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK04319  489 PDPvRGEiiK---AFValrpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1606-1812 8.63e-17

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 86.41  E-value: 8.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADK 1685
Cdd:PRK12492  361 IVEGYGLTETSPVASTNPYGELARLGT----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1686 FidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKYLCAY 1764
Cdd:PRK12492  437 L------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErSGEAVKLFV 510
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313 1765 VVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12492  511 VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
301-695 1.07e-16

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: 86.14  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREfIVGVMMERSIEMIVGILGILKAGG----AYLPIDTELpKQRVEYMLTDSGCSHV 376
Cdd:cd05931    25 LTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAiavpLPPPTPGRH-AERLAAILADAGPRVV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTyQNSIIKGVAFQGSVINLMDIP--FEEEQVED------LQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNFLCA 447
Cdd:cd05931   103 LT-TAAALAAVRAFAASRPAAGTPrlLVVDLLPDtsaadwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlANVRQI 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  448 M--YEDFSQDIGIT------DNVLfsssisfdvtIFEIFVPLVCGARMTIYQGEKFdV--PKL-VQVILEEQVTLAYIPp 516
Cdd:cd05931   182 RraYGLDPGDVVVSwlplyhDMGL----------IGGLLTPLYSGGPSVLMSPAAF-LrrPLRwLRLISRYRATISAAP- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  517 tllNEIYDYFVRanqKI-----------SLNKLFVGVEPIKTELLAKYDHLFRGnlqiLNL--------YGPTEATV--- 574
Cdd:cd05931   250 ---NFAYDLCVR---RVrdedlegldlsSWRVALNGAEPVRPATLRRFAEAFAP----FGFrpeafrpsYGLAEATLfvs 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  575 --------CCTSYQYE----------RDKEITTQNVPIGSPLLNTKIYILDS-FHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:cd05931   320 ggppgtgpVVLRVDRDalagravavaADDPAARELVSCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYWGR 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  636 KELTADKFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASL 695
Cdd:cd05931   400 PEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
421-769 1.15e-16

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: 85.60  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  421 VIYTSGSTGQPKgvMIEHR----SLTNFLCAMY--EDFSQDI--GITDNVLFSSSISfdvtifEIFVPLVCGARMTIYQG 492
Cdd:cd05928   179 IYFTSGTTGSPK--MAEHShsslGLGLKVNGRYwlDLTASDImwNTSDTGWIKSAWS------SLFEPWIQGACVFVHHL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 EKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN----QKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILNLYG 568
Cdd:cd05928   251 PRFDPLVILKTLSSYPITTFCGAPT----VYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKA--QTGLDIYEGYG 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  569 PTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICIS-----GIGLARGYINRKELTADKf 643
Cdd:cd05928   325 QTETGLICANFKGMKIKPGS-----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAAT- 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  644 idhpfERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd05928   399 -----IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV 472
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446807313  724 -------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05928   473 lapqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1320-1812 2.18e-16

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 84.93  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:PRK08751   27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTDLPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQgNVI-----DLMD-------------------------- 1441
Cdd:PRK08751  107 NPLYTPRELKHQLIDSGASVLVVIDNfgttvqQVIADTPVK-QVIttglgDMLGfpkaalvnfvvkyvkklvpeyringa 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1442 MSFEEEPGE-DMHMM----IEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSISFD-V 1515
Cdd:PRK08751  186 IRFREALALgRKHSMptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV----ANMQQAHQWLAGTGKLEEGCEVVITaL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TIFEIFVPLIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEI-----YDYFVRDNQKIVLNKLLVg 1584
Cdd:PRK08751  262 PLYHIFALTANGLVFMKIGGcnhlisNPRDMPGFVKELKKTRFTAFTGVNTLFNGLlntpgFDQIDFSSLKMTLGGGMA- 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 VEPIKTELLAKYDHLfrgnlQILNGYGPTEAT--VCCTSYryesnkEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPG 1662
Cdd:PRK08751  341 VQRSVAERWKQVTGL-----TLVEAYGLTETSpaACINPL------TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIG 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1663 EICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:PRK08751  410 ELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313 1743 TIKTAVVIDQEDE-AGEkyLCAYVVTEKD--IPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08751  484 GVLEVAAVGVPDEkSGE--IVKVVIVKKDpaLTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
415-769 2.36e-16

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 83.30  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKgvMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIsFDV--TIFEIFVPLVCGARMTIYQG 492
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 EKFDVPKLVQVI--LEEQVTLAYIP--PTLLNEIYDYFVRANQKiSLNKLFVGVEPIKTELLAKY-DHLfrgNLQILNLY 567
Cdd:cd05944    78 AGYRNPGLFDNFwkLVERYRITSLStvPTVYAALLQVPVNADIS-SLRFAMSGAAPLPVELRARFeDAT---GLPVVEGY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  568 GPTEATvCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILD-SFHRLQPIGVP--GEICISGIGLARGYINrKELTADKFI 644
Cdd:cd05944   154 GLTEAT-CLVAVNP-PDGPKRPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGGYLY-TEGNKNAFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  645 DhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd05944   231 A------DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 446807313  724 TEKDIPIP--EVRAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05944   304 LKPGAVVEeeELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK08308 PRK08308
acyl-CoA synthetase; Validated
337-770 2.43e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 83.93  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  337 EMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCsHVLTYQNSiikgvafqgsvinlmDIPFEEEQVEDLqitmEPQ 416
Cdd:PRK08308   44 DIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGC-HGLLYGES---------------DFTKLEAVNYLA----EEP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  417 NLayVIYTSGSTGQPKgvMIEhRSLTNF---LCAMYEDFSQDIGITDNVLFSSSISFDvtifeifvpLVCGARMTIYQGE 493
Cdd:PRK08308  104 SL--LQYSSGTTGEPK--LIR-RSWTEIdreIEAYNEALNCEQDETPIVACPVTHSYG---------LICGVLAALTRGS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  494 KFDV-----PK-LVQVILEEQVTLAYIPPTLLNeIYDYFVRANQKIslNKLFVGVEPIKTELLAKydhlFRGN-LQILNL 566
Cdd:PRK08308  170 KPVIitnknPKfALNILRNTPQHILYAVPLMLH-ILGRLLPGTFQF--HAVMTSGTPLPEAWFYK----LRERtTYMMQQ 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  567 YGPTEATVCCTSYQYERDKEIttqnvpiGSPLLNTKIYILDSFHRlqpigvPGEICISgiglargyINRKELtadkfidh 646
Cdd:PRK08308  243 YGCSEAGCVSICPDMKSHLDL-------GNPLPHVSVSAGSDENA------PEEIVVK--------MGDKEI-------- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  647 pfergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTE 725
Cdd:PRK08308  294 ---------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGER-VKAKVISH 363
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 446807313  726 KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK08308  364 EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
873-1285 2.63e-16

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: 83.90  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  873 YLASTSQKRMFIVDQFEDGTNTTYNMpTILKVEGDICKDKFENIFQSLIERHEILRTSFQILD-GELVQKIEPNVDFNIE 951
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQ-NVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  952 YVHVNEKDAD--------YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDG--LSM--GILIKEFVELYK 1019
Cdd:cd19547    81 LLDWSGEDPDrraellerLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGwcLSLiwGDVFRVYEELAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1020 GNElPKLRV--QYKDYVMWQNGPYYKNliSEQKNYWLTTLKgELPvlnfPTDF-QRPTIQSFKGNVCSFNLGTDLTFKVN 1096
Cdd:cd19547   161 GRE-PQLSPcrPYRDYVRWIRARTAQS--EESERFWREYLR-DLT----PSPFsTAPADREGEFDTVVHEFPEQLTRLVN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1097 KLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd19547   233 EAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRdTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFK-QSVSKFDLSLVATEIDnNIHL 1253
Cdd:cd19547   313 LATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHaQEKTEYPIGLIVLPLQ-KLAF 390
                         410       420       430
                  ....*....|....*....|....*....|..
gi 446807313 1254 KVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19547   391 HFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1463-1808 3.12e-16

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 82.82  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHR-----SLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTifeifvPLIYGARM------- 1530
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEdifrmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAP------PLMHGTGSwtafggl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1531 -----TIYQGEKFDVTKLVQVILEEQVTLSYI-------PptLLNEIYDYFVRD--NQKIVLNKLLVGVEPIKTELLaky 1596
Cdd:cd05924    81 lggqtVVLPDDRFDPEEVWRTIEKHKVTSMTIvgdamarP--LIDALRDAGPYDlsSLFAISSGGALLSPEVKQGLL--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1597 DHLfrGNLQILNGYGPTEATVCCTSYRYES-NKEITTQNVPIGSPLLNtkiyilDSFHRIQP-IGVPGEICISGIgLARG 1674
Cdd:cd05924   156 ELV--PNITLVDAFGSSETGFTGSGHSAGSgPETGPFTRANPDTVVLD------DDGRVVPPgSGGVGWIARRGH-IPLG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1675 YINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED 1754
Cdd:cd05924   227 YYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1755 EAGEKYLCAYVVTEK--DIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd05924   304 ERWGQEVVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1344-1814 3.80e-16

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: 84.26  E-value: 3.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVK-RESIVgVMMKRSIEMVIGILGVLKAGGAYLP----IDTDLPKQRVEYM-----LTD 1413
Cdd:cd05906    40 QSYQDLLEDARRLAAGLRQLGLRpGDSVI-LQFDDNEDFIPAFWACVLAGFVPAPltvpPTYDEPNARLRKLrhiwqLLG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGcsHVLVHQNSI--IKGIE--FQGNVIDLMDMSFEEEPGEDMHMMI-EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL 1488
Cdd:cd05906   119 SP--VVLTDAELVaeFAGLEtlSGLPGIRVLSIEELLDTAADHDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 ---CAMYEDFSQDIGIT----DNVlfsSSISFdvtiFEIFvPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd05906   197 agkIQHNGLTPQDVFLNwvplDHV---GGLVE----LHLR-AVYLGCQQVHVPTEEIlaDPLRWLDLIDRYRVTITWAPN 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDNQK----IVLNKLLVGVEPIKT-------ELLAKYdhlfrgNLQ---ILNGYGPTE----ATVCCTS 1621
Cdd:cd05906   269 FAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAktirrllRLLEPY------GLPpdaIRPAFGMTEtcsgVIYSRSF 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1622 YRYESNKEITTqnVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTG 1701
Cdd:cd05906   343 PTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE------DGWFRTG 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLlkyETIK------TAVVIDQEDEAGEKYLCAYVVTEKDIP--- 1772
Cdd:cd05906   415 DLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV---EEVPgvepsfTAAFAVRDPGAETEELAIFFVPEYDLQdal 490
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313 1773 ---IPEVRAYLATKL---PHYMIPqqlIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05906   491 setLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLKA 535
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
576-853 4.06e-16

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 81.33  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  576 CTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEK 653
Cdd:COG3433     2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpaQPGRQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  654 LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEkDIPIPEV 733
Cdd:COG3433    82 ADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAAL-DGLAAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  734 RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEP------TNSTERKLVEIWKDVLGI--QRIG 805
Cdd:COG3433   161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASpapaleTALTEEELRADVAELLGVdpEEID 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313  806 IRDNFFEIGGHSLKAARLISIVNKEfNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:COG3433   241 PDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALL 287
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
288-775 4.91e-16

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: 84.29  E-value: 4.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  288 NPNQIAIVC------NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG-------GAYLP 354
Cdd:cd05967    64 RGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  355 ------IDTELPK------------QRVEYM------LTDSGCS--HVLTYQNSIIKGVAFQGsvinLMDIPFEEE--QV 406
Cdd:cd05967   144 kelasrIDDAKPKlivtascgiepgKVVPYKplldkaLELSGHKphHVLVLNRPQVPADLTKP----GRDLDWSELlaKA 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  407 EDLQ-ITMEPQNLAYVIYTSGSTGQPKGVMiehRSLTNFLCAMYEDFSQDIGI-TDNVLFSSSisfDVT-----IFEIFV 479
Cdd:cd05967   220 EPVDcVPVAATDPLYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIkPGDVWWAAS---DVGwvvghSYIVYG 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  480 PLVCGARMTIYQGEKFDVPKLVQ---VILEEQVTLAYIPPTLLNEIYDY-----FVRANQKISLNKLFVGVEPIKTELLA 551
Cdd:cd05967   294 PLLHGATTVLYEGKPVGTPDPGAfwrVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSLRTLFLAGERLDPPTLE 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  552 KYDHLFrgNLQILNLYGPTEA--TVCCTSyqyerdKEITTQNVPIGS---PLLNTKIYILDSFHRLQPIGVPGEICISGi 626
Cdd:cd05967   374 WAENTL--GVPVIDHWWQTETgwPITANP------VGLEPLPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVIKL- 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  627 GLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 706
Cdd:cd05967   445 PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  707 IQREDESGEKYLCAYVVTEKDIPI------PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:cd05967   525 VGVRDELKGQVPLGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1345-1750 6.05e-16

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: 83.29  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV--- 1421
Cdd:cd05932     8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgkl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 -HQNSIIKGIEfqGNVIDLMDMSFEEEPGED-------MHMMIE------PHNLAYVIYTSGSTGQPKGVMIEHRSLTNF 1487
Cdd:cd05932    88 dDWKAMAPGVP--EGLISISLPPPSAANCQYqwddliaQHPPLEerptrfPEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFsqDIGITDNVL--------------FSSSISFDVTIF-----EIFVPLIYGARMTIYqgekFDVTKLvqVIL 1548
Cdd:cd05932   166 AQAGIEHI--GTEENDRMLsylplahvtervfvEGGSLYGGVLVAfaeslDTFVEDVQRARPTLF----FSVPRL--WTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDnqKIVLNKLLVGV------------EPIKTELLAKYDHLfrgNLQILNGYGPTEat 1616
Cdd:cd05932   238 FQQGVQDKIPQQKLNLLLKIPVVN--SLVKRKVLKGLgldqcrlagcgsAPVPPALLEWYRSL---GLNILEAYGMTE-- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 vcctSYRYES-NKEITTQNVPIGSPLLNTKIYILDSfhriqpigvpGEICISGIGLARGYINRKELTADKFIDHPFERge 1695
Cdd:cd05932   311 ----NFAYSHlNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLR-- 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1696 klykTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVI 1750
Cdd:cd05932   375 ----TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1330-1815 8.34e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 83.05  E-value: 8.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK-QRVE 1408
Cdd:PRK07788   61 RAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGpQLAE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSgcSHVLVHQNsiikgiEFQGNVIDL-----------MDMSFEEEPG------EDMHMMIEPHNL-------AYV 1464
Cdd:PRK07788  141 VAAREG--VKALVYDD------EFTDLLSALppdlgrlrawgGNPDDDEPSGstdetlDDLIAGSSTAPLpkppkpgGIV 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1465 IYTSGSTGQPKGVMIEH----RSLTNFLCAMyeDFSQDigitDNVLFSSSIsFDVTIFEIFVpLIYGARMTIYQGEKFDV 1540
Cdd:PRK07788  213 ILTSGTTGTPKGAPRPEpsplAPLAGLLSRV--PFRAG----ETTLLPAPM-FHATGWAHLT-LAMALGSTVVLRRRFDP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLLNEIYDyfvrdnqkivlnkllvgVEPiktELLAKYD----------------HLFRGNL 1604
Cdd:PRK07788  285 EATLEDIAKHKATALVVVPVMLSRILD-----------------LGP---EVLAKYDtsslkiifvsgsalspELATRAL 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 Q-----ILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINrk 1679
Cdd:PRK07788  345 EafgpvLYNLYGSTEVAFATIATPEDLAEAPGT----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD-- 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 elTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEK 1759
Cdd:PRK07788  419 --GRDK------QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1760 YLCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07788  491 RLRAFVVKAPGAALDEdaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
420-765 9.12e-16

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 81.27  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  420 YVIYTSGSTGQPKGVMIEHR-----SLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTifeifvPLVCGARM------- 487
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEdifrmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAP------PLMHGTGSwtafggl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  488 -----TIYQGEKFDVPKLVQVILEEQVTL------AYIPPtLLNEIydyfvRANQKISLNKLFV----GV---EPIKTEL 549
Cdd:cd05924    81 lggqtVVLPDDRFDPEEVWRTIEKHKVTSmtivgdAMARP-LIDAL-----RDAGPYDLSSLFAissgGAllsPEVKQGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  550 LakyDHLfrGNLQILNLYGPTEATVCCTSYQYERDKEITT-QNVPIGSPLLNtkiyilDSFHRLQP-IGVPGEICISGIg 627
Cdd:cd05924   155 L---ELV--PNITLVDAFGSSETGFTGSGHSAGSGPETGPfTRANPDTVVLD------DDGRVVPPgSGGVGWIARRGH- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  628 LARGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:cd05924   223 IPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  708 QREDESGEKYLCAYVVTEK--DIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05924   300 GRPDERWGQEVVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
300-707 1.02e-15

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: 82.52  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV--- 376
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfvg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 -LTYQNSIIKGVAfqGSVINLMDIPFEE----EQVEDLQ---------ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLT 442
Cdd:cd05932    86 kLDDWKAMAPGVP--EGLISISLPPPSAancqYQWDDLIaqhppleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  443 NFLCAMYEDFsqDIGITDNVL--------------FSSSISFDVTIF-----EIFVPLVCGARMTIYqgekFDVPKLvqV 503
Cdd:cd05932   164 WAAQAGIEHI--GTEENDRMLsylplahvtervfvEGGSLYGGVLVAfaeslDTFVEDVQRARPTLF----FSVPRL--W 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  504 ILEEQVTLAYIPPTLLN-----EIYDYFVRAN--QKISLNK---LFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT 573
Cdd:cd05932   236 TKFQQGVQDKIPQQKLNlllkiPVVNSLVKRKvlKGLGLDQcrlAGCGSAPVPPALLEWYRSL---GLNILEAYGMTENF 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  574 VCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSfhrlqpigvpGEICISGIGLARGYINRKELTADKFIDHPFERgek 653
Cdd:cd05932   313 AYSHLNYPGRDKIGT-----VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLR--- 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  654 lykTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:cd05932   375 ---TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
280-769 1.21e-15

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 82.79  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  359 LPKQRVEYMLTDSGCSHVLTYQN--SIIKGVAFQ-------------------GSVINLM-----------DIPFEEEQV 406
Cdd:PRK08974  108 YTPRELEHQLNDSGAKAIVIVSNfaHTLEKVVFKtpvkhviltrmgdqlstakGTLVNFVvkyikrlvpkyHLPDAISFR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  407 EDLQI---------TMEPQNLAYVIYTSGSTGQPKGVMIEHRS-LTNFLcamyedfsQDIGITDNVLFSSSiSFDVT--- 473
Cdd:PRK08974  188 SALHKgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLE--------QAKAAYGPLLHPGK-ELVVTalp 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  474 IFEIFVpLVCGARMTIYQGEK-------FDVPKLVQVILEEQVTLAyippTLLNEIYDYFVRANQKISLN----KLFVGV 542
Cdd:PRK08974  259 LYHIFA-LTVNCLLFIELGGQnllitnpRDIPGFVKELKKYPFTAI----TGVNTLFNALLNNEEFQELDfsslKLSVGG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  543 -EPIKTELLAKYDHLFRGNLqiLNLYGPTEATVCCTSYQYERDKeittQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEI 621
Cdd:PRK08974  334 gMAVQQAVAERWVKLTGQYL--LEGYGLTECSPLVSVNPYDLDY----YSGSIGLPVPSTEIKLVDDDGNEVPPGEPGEL 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  622 CISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE-ASLLKYET 700
Cdd:PRK08974  408 WVKGPQVMLGYWQRPEATDEVIKD-------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEdVVMLHPKV 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313  701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08974  481 LEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
393-773 1.26e-15

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: 82.15  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  393 VINLMDIPF---EEEQVEDLqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEdfSQDIGITDNVLFSSSIS 469
Cdd:cd05908    85 VWNTLKNPYlitEEEVLCEL-----ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN--STEWKTKDRILSWMPLT 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  470 FDVTIFEI-FVPLVCGARMTIYQGEKFDV-PKL-VQVILEEQVTLAYIPptllNEIYDYFVRA--NQKI------SLNKL 538
Cdd:cd05908   158 HDMGLIAFhLAPLIAGMNQYLMPTRLFIRrPILwLKKASEHKATIVSSP----NFGYKYFLKTlkPEKAndwdlsSIRMI 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  539 FVGVEPIKTELLAKY-DHLFRGNLQ---ILNLYGPTEATVCCTS-----------------YQYERDKEITTQN------ 591
Cdd:cd05908   234 LNGAEPIDYELCHEFlDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvTHGEPEPEVDKKDsecltf 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  592 VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEY 671
Cdd:cd05908   314 VEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTD------DGWLKTGDLG-FIRNGRLVI 386
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  672 LGRVDHQVKIRGYRIELGEIEASLLKYETI---KTAVVIQREDESGEKYLCAYVVTEKDIpipEVRAYLATKLPYYMIP- 747
Cdd:cd05908   387 TGREKDIIFVNGQNVYPHDIERIAEELEGVelgRVVACGVNNSNTRNEEIFCFIEHRKSE---DDFYPLGKKIKKHLNKr 463
                         410       420       430
                  ....*....|....*....|....*....|.
gi 446807313  748 -----QQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:cd05908   464 ggwqiNEVLPIRRIPKTTSGKVKRYELAQRY 494
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1329-1807 1.36e-15

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 82.32  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK08314   21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCS----------------------HVLVHQ-------NSIIKGIEF-----------QGNVIDLMDMSFE-E 1446
Cdd:PRK08314  101 AHYVTDSGARvaivgselapkvapavgnlrlrHVIVAQysdylpaEPEIAVPAWlraepplqalaPGGVVAWKEALAAgL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1447 EPGEdmhMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDfsqdiGITDNVLFSSSISFDVTIFE--IFV 1522
Cdd:PRK08314  181 APPP---HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmaNAVGSVLWSN-----STPESVVLAVLPLFHVTGMVhsMNA 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1523 PLIYGArmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLneiYDYFVRDN-QKIVLNKLLV----GV---EPIKTELLA 1594
Cdd:PRK08314  253 PIYAGA--TVVLMPRWDREAAARLIERYRVTHWTNIPTMV---VDFLASPGlAERDLSSLRYigggGAampEAVAERLKE 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1595 KYdhlfrgNLQILNGYGPTEaTVCCTsyryESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLAR 1673
Cdd:PRK08314  328 LT------GLDYVEGYGLTE-TMAQT----HSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDhpFErGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK08314  397 GYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1754 DE-AGE--KylcAYVV---------TEKDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK08314  474 DPrRGEtvK---AVVVlrpeargktTEEEI-IAWAREHMAA----YKYPRIVEFVDSLPKSGSGKI 531
PRK07529 PRK07529
AMP-binding domain protein; Validated
1582-1812 1.54e-15

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 82.70  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LVGVEPIKTELLAKYDHlfRGNLQILNGYGPTEAT-VCCTSYRYESNKeittqnvpIGS-----PLLNTKIYILDSFHRI 1655
Cdd:PRK07529  339 LCGAAPLPVEVFRRFEA--ATGVRIVEGYGLTEATcVSSVNPPDGERR--------IGSvglrlPYQRVRVVILDDAGRY 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1656 Q---PIGVPGEICISGIGLARGYinrkeLTADKFIDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIEL 1731
Cdd:PRK07529  409 LrdcAVDEVGVLCIAGPNVFSGY-----LEAAHNKGLWLEDG--WLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDP 480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDE-AGEkyL-CAYV--VTEKDIPIPEVRAYLATKLPH-YMIPQQLIPIHNIPLTQNGK 1806
Cdd:PRK07529  481 AAIEEALLRHPAVALAAAVGRPDAhAGE--LpVAYVqlKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGK 558

                  ....*.
gi 446807313 1807 IDRSKL 1812
Cdd:PRK07529  559 IFKPAL 564
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1331-1837 3.61e-15

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: 81.21  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVVC------NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG-------GAYLP 1397
Cdd:cd05967    64 RGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 ------IDTDLPK------------QRVEYM------LTDSGCS--HVLVHQNSIIKGIEFQGnvidLMDMSFEEEpged 1451
Cdd:cd05967   144 kelasrIDDAKPKlivtascgiepgKVVPYKplldkaLELSGHKphHVLVLNRPQVPADLTKP----GRDLDWSEL---- 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMmIEPHNLA--------YVIYTSGSTGQPKGVMiehRSLTNFLCAMYEDFSQDIGI-TDNVLFSSSisfDVT-----I 1517
Cdd:cd05967   216 LAK-AEPVDCVpvaatdplYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIkPGDVWWAAS---DVGwvvghS 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKF---DVTKLVQVILEEQVTLSYIPPTLLNEIYDY-----FVRDNQKIVLNKLLVGVEPIK 1589
Cdd:cd05967   289 YIVYGPLLHGATTVLYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSLRTLFLAGERLD 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1590 TELLAKYDHLFrgNLQILNGYGPTEATVCCTSyryeSNKEITTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICI 1666
Cdd:cd05967   369 PPTLEWAENTL--GVPVIDHWWQTETGWPITA----NPVGLEPLPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVI 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1667 SGiGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT 1746
Cdd:cd05967   443 KL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1747 AVVIDQEDEAGEKYLCAYVVTEKDIPI------PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLntLGN 1820
Cdd:cd05967   522 CAVVGVRDELKGQVPLGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI--ADG 599
                         570
                  ....*....|....*...
gi 446807313 1821 SNY-VPPRNEIDSSLIDI 1837
Cdd:cd05967   600 EDYtIPSTIEDPSVLDEI 617
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
415-765 4.56e-15

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 81.55  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMYEdfsqdigITDNVLFSSS-ISFDV-TIFEIFvPLVCGARMTIYQG 492
Cdd:PRK06814  792 PDDPAVILFTSGSEGTPKGVVLSHR---NLLANRAQ-------VAARIDFSPEdKVFNAlPVFHSF-GLTGGLVLPLLSG 860
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 EKF----------DVPKLVQVIleeQVTLAYIPPTLLN------EIYDYFvranqkiSLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK06814  861 VKVflypsplhyrIIPELIYDT---NATILFGTDTFLNgyaryaHPYDFR-------SLRYVFAGAEKVKEETRQTWMEK 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  557 FRgnLQILNLYGPTEAtvcctsyqyerdkeittqnvpigSPLL--NTKIY--------ILDSFH-RLQPI-GVP--GEIC 622
Cdd:PRK06814  931 FG--IRILEGYGVTET-----------------------APVIalNTPMHnkagtvgrLLPGIEyRLEPVpGIDegGRLF 985
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  623 ISGIGLARGYinrkeLTADK-FIDHPFERGEklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK06814  986 VRGPNVMLGY-----LRAENpGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPD 1058
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  702 KTAVVIQREDES-GEKYLcaYVVTEKDIPIPEVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK06814 1059 ALHAAVSIPDARkGERII--LLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
PRK09274 PRK09274
peptide synthase; Provisional
1329-1723 4.82e-15

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 80.71  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVC----------NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPI 1398
Cdd:PRK09274   17 QERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA--VPV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTD----------------------LPKQRVEYMLTDSGCSH----VLVHQNSIIKGIEFQGNVIDLMDMSFEeepgedM 1452
Cdd:PRK09274   95 LVDpgmgiknlkqclaeaqpdafigIPKAHLARRLFGWGKPSvrrlVTVGGRLLWGGTTLATLLRDGAAAPFP------M 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMiEPHNLAYVIYTSGSTGQPKGVMIEHRSltnfLCAMYEDFSQDIGITDNvlfsssiSFDVTIFEIFV--PLIYGARM 1530
Cdd:PRK09274  169 ADL-APDDMAAILFTSGSTGTPKGVVYTHGM----FEAQIEALREDYGIEPG-------EIDLPTFPLFAlfGPALGMTS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1531 TIyqgEKFDVTK--------LVQVILEEQVTLSYIPPTLLNEIYDYFVrdNQKIVLNKL---LVGVEPIKTELLAKYDHL 1599
Cdd:PRK09274  237 VI---PDMDPTRpatvdpakLFAAIERYGVTNLFGSPALLERLGRYGE--ANGIKLPSLrrvISAGAPVPIAVIERFRAM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1600 FRGNLQILNGYGPTEAT-VCCTSYR--YESNKEITTQN--VPIGSPLLNTKIYI-------LDSFHRIQ--PIGVPGEIC 1665
Cdd:PRK09274  312 LPPDAEILTPYGATEALpISSIESReiLFATRAATDNGagICVGRPVDGVEVRIiaisdapIPEWDDALrlATGEIGEIV 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1666 ISGIGLARGYINRKELTA-DKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:PRK09274  392 VAGPMVTRSYYNRPEATRlAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
298-766 5.77e-15

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: 79.79  E-value: 5.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05914     5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 tyqnsiikgvafqgsvinlmdipfeeeqvedlqiTMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNflcAMYEDFSQDI 456
Cdd:cd05914    85 ----------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIvSN---VDGVKEVVLL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  457 GITDNVLfsSSISFDVT---IFEIFVPLVCGArmTIYQGEKFDVPKLVqVILEEQVTLAYIPPTLLnEIYDYFVRANQ-K 532
Cdd:cd05914   128 GKGDKIL--SILPLHHIyplTFTLLLPLLNGA--HVVFLDKIPSAKII-ALAFAQVTPTLGVPVPL-VIEKIFKMDIIpK 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  533 ISLNKLF------VGVEPIKTELLAKYDHLFRGNLQI-------LNL----------------YGPTEATVCCTSYQYER 583
Cdd:cd05914   202 LTLKKFKfklakkINNRKIRKLAFKKVHEAFGGNIKEfviggakINPdveeflrtigfpytigYGMTETAPIISYSPPNR 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  584 DKEITTqnvpiGSPLLNTKIYILDSfhrlQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARW 663
Cdd:cd05914   282 IRLGSA-----GKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHTGDLGKI 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  664 LPDGNIEYLGRVDHQ-VKIRGYRIELGEIEASLLKYETIKTAVVIQREDES---------GEKYLCAYVVTEKDIPIPEV 733
Cdd:cd05914   347 DAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLvalayidpdFLDVKALKQRNIIDAIKWEV 426
                         490       500       510
                  ....*....|....*....|....*....|....
gi 446807313  734 RAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd05914   427 RDKVNQKVPnYKKISKVKIVKEEFEKTPKGKIKR 460
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
300-769 6.64e-15

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: 79.81  E-value: 6.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDsgcshvlty 379
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQE--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  380 qnsiIKGVAFQGsvinlmdIPFEEEQvedlqitmepqnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT 459
Cdd:cd05910    73 ----AEPDAFIG-------IPKADEP-------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  460 DNVLFSssisfdvtIFEIFVPLVCGAR----MTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-S 534
Cdd:cd05910   129 DLATFP--------LFALFGPALGLTSvipdMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLpS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  535 LNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEA-TVCCTSyqyERDKEITTQNVP-------IGSPLLNTKIYIL 606
Cdd:cd05910   201 LRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlPVSSIG---SRELLATTTAATsggagtcVGRPIPGVRVRII 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  607 ----------DSFHRLqPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERgeKLYKTGDIARWLPDGNIEYLGRVD 676
Cdd:cd05910   278 eiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG--FWHRMGDLGYLDDEGRLWFCGRKA 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  677 HQVKIRGYRIELGEIEASLLKYETIK-TAVVIQREDESGEKYLCayVVTEKDIPIPEVRAY-----LATKLPYYMIPQQI 750
Cdd:cd05910   355 HRVITTGGTLYTEPVERVFNTHPGVRrSALVGVGKPGCQLPVLC--VEPLPGTITPRARLEqelraLAKDYPHTQRIGRF 432
                         490       500
                  ....*....|....*....|.
gi 446807313  751 ISIQNIP--LTQNGKIDRKKL 769
Cdd:cd05910   433 LIHPSFPvdIRHNAKIFREKL 453
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1458-1717 9.46e-15

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 80.14  E-value: 9.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGITDNVLFSSS---ISF--DVTIFE---IFVPLIYGAR 1529
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNL----------IANVAGSSLSTKFYPSdvhISYlpLAHIYErvnQIVMLHYGVA 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQGekfDVTKLVQVILEEQVTLSYIPPTLLNEIYDY---------FVRDN-----------------------QKIV 1577
Cdd:PLN02736  290 VGFYQG---DNLKLMDDLAALRPTIFCSVPRLYNRIYDGitnavkesgGLKERlfnaaynakkqalengknpspmwDRLV 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKL-----------LVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEaTVCCTSYRYESNKeiTTQNVpiGSPLLNTKI 1646
Cdd:PLN02736  367 FNKIkaklggrvrfmSSGASPLSPDVMEFLRICFGG--RVLEGYGMTE-TSCVISGMDEGDN--LSGHV--GSPNPACEV 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1647 YILDsfhriqpigVP-------------GEICISGIGLARGYInRKELTADKFIDhpferGEKLYKTGDIARWLPDGNIE 1713
Cdd:PLN02736  440 KLVD---------VPemnytsedqpyprGEICVRGPIIFKGYY-KDEVQTREVID-----EDGWLHTGDIGLWLPGGRLK 504

                  ....
gi 446807313 1714 YLGR 1717
Cdd:PLN02736  505 IIDR 508
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1344-1809 1.06e-14

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: 79.02  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHq 1423
Cdd:cd05914     8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TNflcAMYEDFSQDIGIT 1502
Cdd:cd05914    87 ---------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIvSN---VDGVKEVVLLGKG 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 DNVLfsSSISFDVT---IFEIFVPLIYGArmTIYQGEKFDvTKLVQVILEEQVTLSYIPPTLLnEIYDYFVRDNQ-KIVL 1578
Cdd:cd05914   131 DKIL--SILPLHHIyplTFTLLLPLLNGA--HVVFLDKIP-SAKIIALAFAQVTPTLGVPVPL-VIEKIFKMDIIpKLTL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NKLL------VGVEPIKTELLAKYDHLFRGNLQIL-----------------------NGYGPTEATVCCTSYRYESNKE 1629
Cdd:cd05914   205 KKFKfklakkINNRKIRKLAFKKVHEAFGGNIKEFviggakinpdveeflrtigfpytIGYGMTETAPIISYSPPNRIRL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTqnvpiGSPLLNTKIYILDSfhriQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 1709
Cdd:cd05914   285 GSA-----GKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHTGDLGKIDAE 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQ-VKIRGYRIELGEIEASLLKYETIKTAVVIDQE---------DEAGEKYLCAYVVTEKDIPIPEVRAY 1779
Cdd:cd05914   350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEkklvalayiDPDFLDVKALKQRNIIDAIKWEVRDK 429
                         490       500       510
                  ....*....|....*....|....*....|....
gi 446807313 1780 LATKLPHYmipQQL--IPIHNIPL--TQNGKIDR 1809
Cdd:cd05914   430 VNQKVPNY---KKIskVKIVKEEFekTPKGKIKR 460
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
414-769 1.37e-14

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: 79.25  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL---CAMYEDFSQDIGIT----DNVlfsSSISFdvtiFEIFvPLVCGAR 486
Cdd:cd05906   165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSagkIQHNGLTPQDVFLNwvplDHV---GGLVE----LHLR-AVYLGCQ 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  487 MTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK----ISLNKLFVGVEPIKT-------ELLAKY 553
Cdd:cd05906   237 QVHVPTEEIlaDPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAktirrllRLLEPY 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  554 dhlfrgNLQ---ILNLYGPTE----ATVCCTSYQYERDKEITTqnVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGI 626
Cdd:cd05906   317 ------GLPpdaIRPAFGMTEtcsgVIYSRSFPTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  627 GLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLlkyETIK---- 702
Cdd:cd05906   389 VVTKGYYNNPEANAEAFTE------DGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV---EEVPgvep 458
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  703 --TAVVIQREDESGEKYLCAYVVTEKDIP------IPEVRAYLATKL---PYYMIPqqiISIQNIPLTQNGKIDRKKL 769
Cdd:cd05906   459 sfTAAFAVRDPGAETEELAIFFVPEYDLQdalsetLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1323-1812 1.57e-14

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 78.96  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKG-----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:PRK08008   12 MWDDLADVYGHKTALIFESSGgvvrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLVHQN-------------SIIKGIEFQGNVIDLMD--MSFE----EEPGE-DMHMMIE 1457
Cdd:PRK08008   92 INARLLREESAWILQNSQASLLVTSAQfypmyrqiqqedaTPLRHICLTRVALPADDgvSSFTqlkaQQPATlCYAPPLS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSL------TNFLCAMYEDfsqDIGITdnVLFSSSISFDVTIfeIFVPLIYGARMT 1531
Cdd:PRK08008  172 TDDTAEILFTSGTTSRPKGVVITHYNLrfagyySAWQCALRDD---DVYLT--VMPAFHIDCQCTA--AMAAFSAGATFV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1532 IYqgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIY---------DYFVRDnqkiVLNKLLVGVEpiktellAKYDHLFRG 1602
Cdd:PRK08008  245 LL--EKYSARAFWGQVCKYRATITECIPMMIRTLMvqppsandrQHCLRE----VMFYLNLSDQ-------EKDAFEERF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1603 NLQILNGYGPTEATVCCT------SYRYESnkeittqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGI---GLAR 1673
Cdd:PRK08008  312 GVRLLTSYGMTETIVGIIgdrpgdKRRWPS----------IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFK 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK08008  382 EYYLDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1754 DEAGEKYLCAYVV-TE-KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08008  456 DSIRDEAIKAFVVlNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1458-1812 1.62e-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: 78.68  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEdfSQDIGITDNVLFSSSISFDVTIFEI-FVPLIYGARMTIYQGE 1536
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN--STEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTR 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1537 KFDV--TKLVQVILEEQVTLSYIPptllNEIYDYFVR--DNQKI------VLNKLLVGVEPIKTELLAKY-DHLFRGNLQ 1605
Cdd:cd05908   183 LFIRrpILWLKKASEHKATIVSSP----NFGYKYFLKtlKPEKAndwdlsSIRMILNGAEPIDYELCHEFlDHMSKYGLK 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ---ILNGYGPTEATVCCTSYRYESN-----------------KEITTQN------VPIGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05908   259 rnaILPVYGLAEASVGASLPKAQSPfktitlgrrhvthgepePEVDKKDsecltfVEVGKPIDETDIRICDEDNKILPDG 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLL 1739
Cdd:cd05908   339 YIGHIQIRGKNVTPGYYNNPEATAKVFTD------DGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAE 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1740 KYETI---KTAVVIDQEDEAGEKYLCAYVVTEKDIpipEVRAYLATKLPHYMIP------QQLIPIHNIPLTQNGKIDRS 1810
Cdd:cd05908   412 ELEGVelgRVVACGVNNSNTRNEEIFCFIEHRKSE---DDFYPLGKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKRY 488

                  ..
gi 446807313 1811 KL 1812
Cdd:cd05908   489 EL 490
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
300-771 1.63e-14

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 79.06  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG-----C 373
Cdd:PRK05620   38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEdevivA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  374 SHVLTYQ-NSIIKGVAFQGSVINLMDIPFEEEQVEDL-QIT-------------------MEPQNLAYVIYTSGSTGQPK 432
Cdd:PRK05620  118 DPRLAEQlGEILKECPCVRAVVFIGPSDADSAAAHMPeGIKvysyealldgrstvydwpeLDETTAAAICYSTGTTGAPK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  433 GVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIF---VPLvcGARMT----IYQGEKFDVPKLVQVIL 505
Cdd:PRK05620  198 GVVYSHRSL--YLQSLSLRTTDSLAVTHGESFLCC----VPIYHVLswgVPL--AAFMSgtplVFPGPDLSAPTLAKIIA 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  506 EEQVTLAYIPPTLLNEIYDYFVRAN-QKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILNLYGPTEATVCCT------- 577
Cdd:PRK05620  270 TAMPRVAHGVPTLWIQLMVHYLKNPpERMSLQEIYVGGSAVPPILIKAWEE--RYGVDVVHVWGMTETSPVGTvarppsg 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  578 -SYQYERDKEITTQNVPIGsplLNTKI----YILDSFHRLQpigvpGEICISGIGLARGYIN----RKELTADKFIDHPF 648
Cdd:PRK05620  348 vSGEARWAYRVSQGRFPAS---LEYRIvndgQVMESTDRNE-----GEIQVRGNWVTASYYHspteEGGGAASTFRGEDV 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  649 ERGEKLY------KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAY 721
Cdd:PRK05620  420 EDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVT 499
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446807313  722 VVTEKDIPIPE----VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK05620  500 VLAPGIEPTREtaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1390-1815 1.70e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 78.15  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1390 KAGGAYLPIDTDLPKQRVEYMLTDSGCsHVLVHQNsiikgIEFqgnVIDLMDMSFEEEPGedmhmmiephnlaYVIYTSG 1469
Cdd:PRK08308   54 EKGASVLPIHPDTPKEAAIRMAKRAGC-HGLLYGE-----SDF---TKLEAVNYLAEEPS-------------LLQYSSG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1470 STGQPKgvMIEhRSLTNF---LCAMYEDFSQDIGITDNVLFSSSISFDvtifeifvpLIYGARMTIYQGEKFDV--TK-- 1542
Cdd:PRK08308  112 TTGEPK--LIR-RSWTEIdreIEAYNEALNCEQDETPIVACPVTHSYG---------LICGVLAALTRGSKPVIitNKnp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1543 --LVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQkivLNKLLVGVEPIKTELLAKydhlFRGN-LQILNGYGPTEATvcC 1619
Cdd:PRK08308  180 kfALNILRNTPQHILYAVPLMLHILGRLLPGTFQ---FHAVMTSGTPLPEAWFYK----LRERtTYMMQQYGCSEAG--C 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYryesNKEITTQNvPIGSPLLNTKIYILDSFHRiqpigvPGEICISgiglargyINRKELtadkfidhpfergeklyK 1699
Cdd:PRK08308  251 VSI----CPDMKSHL-DLGNPLPHVSVSAGSDENA------PEEIVVK--------MGDKEI-----------------F 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPIPEVRA 1778
Cdd:PRK08308  295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGER-VKAKVISHEEIDPVQLRE 373
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRsKLPKL 1815
Cdd:PRK08308  374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSR-KLLEL 409
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1344-1809 3.04e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 78.40  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCS------ 1417
Cdd:PRK04319   74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKvlittp 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 ---------------HVLVhqnsIIKGIEFQGNVID---LMDMSFEEEPGEDMHmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:PRK04319  154 allerkpaddlpslkHVLL----VGEDVEEGPGTLDfnaLMEQASDEFDIEWTD----REDGAILHYTSGSTGKPKGVLH 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRS-LTNFLCAMYE-DFSQDigitdnvlfsssisfDV------------TIFEIFVPLIYGARMTIYQGEkFDVTKLVQ 1545
Cdd:PRK04319  226 VHNAmLQHYQTGKYVlDLHED---------------DVywctadpgwvtgTSYGIFAPWLNGATNVIDGGR-FSPERWYR 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLSYIPPTLLneiydyfvrdnqkivlnKLLVGVEPiktELLAKYD--HLfR-----G---------------N 1603
Cdd:PRK04319  290 ILEDYKVTVWYTAPTAI-----------------RMLMGAGD---DLVKKYDlsSL-RhilsvGeplnpevvrwgmkvfG 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1604 LQILNGYGPTE--ATVCCTSYryesnkeitTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICI-----SgigLAR 1673
Cdd:PRK04319  349 LPIHDNWWMTEtgGIMIANYP---------AMDIKPGSmgkPLPGIEAAIVDDQGNELPPNRMGNLAIkkgwpS---MMR 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK04319  417 GIWNNPEKYESYFAG-------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1754 DE-AGE--KylcAYV-----VTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK04319  490 DPvRGEiiK---AFValrpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1344-1812 3.61e-14

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 78.15  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLpkQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL--HRDDHALAARNTEPALVVT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNVIDLMDMSFEE---EPGEdmHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED----FS 1496
Cdd:PRK06060  109 SDALRDRFQPSRVAEAAELMSEAarvAPGG--YEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKalrlTP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1497 QDIGITdnvlfSSSISFDVTI-FEIFVPLIYGARMTIYQgekfdvtklVQVILEEQVTLS-YIPPTLLNEIYDYFVR--- 1571
Cdd:PRK06060  187 EDTGLC-----SARMYFAYGLgNSVWFPLATGGSAVINS---------APVTPEAAAILSaRFGPSVLYGVPNFFARvid 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 ----DNQKIVLNKLLVG--VEPIKTELLAKydhlFRGNLQILNGYGPTEatvccTSYRYESNKEITTQNVPIGSPLLNTK 1645
Cdd:PRK06060  253 scspDSFRSLRCVVSAGeaLELGLAERLME----FFGGIPILDGIGSTE-----VGQTFVSNRVDEWRLGTLGRVLPPYE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKEltadkfidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:PRK06060  324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE-----VRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:PRK06060  395 GVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLP 474
                         490
                  ....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:PRK06060  475 RTPNGKLVRGAL 486
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
310-849 3.81e-14

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: 78.59  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAF 389
Cdd:COG3319    36 AAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALALALL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  390 QGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIS 469
Cdd:COG3319   116 ALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  470 FDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTEL 549
Cdd:COG3319   196 AALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALL 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  550 LAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLA 629
Cdd:COG3319   276 LLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAG 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  630 RGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKyETIKTAVVIQR 709
Cdd:COG3319   356 GLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAE-AAAVAAAVAAA 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  710 EDESGEKYLCAYVVTEKDIPIPEVRAYLATK--LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEPTNST 787
Cdd:COG3319   435 AAAAAAAAALAAAVVAAAALAAAALLLLLLLllLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAAL 514
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313  788 ERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDF 849
Cdd:COG3319   515 ELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAAL 576
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
289-770 4.22e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 77.73  E-value: 4.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK13383   49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 TDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNlAYVIYTSGSTGQPKGVmiehrsltnflcAM 448
Cdd:PRK13383  129 RAHHISTVVA-DNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGV------------PR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  449 YEDFSQDIGITDNVL------FSSSISFDVTIFE------IFVPLVCGArmTIYQGEKFDV-PKLVQVILEEQVTLAYIP 515
Cdd:PRK13383  195 APQLRSAVGVWVTILdrtrlrTGSRISVAMPMFHglglgmLMLTIALGG--TVLTHRHFDAeAALAQASLHRADAFTAVP 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  516 pTLLNEIYDYFVRANQKISLNKLFVGV---EPIKTELLAKYDHLFrGNLqILNLYGPTEATVCCTSYQYE-RDKEITtqn 591
Cdd:PRK13383  273 -VVLARILELPPRVRARNPLPQLRVVMssgDRLDPTLGQRFMDTY-GDI-LYNGYGSTEVGIGALATPADlRDAPET--- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  592 vpIGSPLLNTKIYILDSFHRlqPIG--VPGEICISGiglargyinrkELTADKFIDHpferGEK-----LYKTGDIARWL 664
Cdd:PRK13383  347 --VGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMGYLD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEK--DIPIPEVRAYLATKLP 742
Cdd:PRK13383  408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKDRVS 487
                         490       500
                  ....*....|....*....|....*...
gi 446807313  743 YYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK13383  488 RFEQPRDINIVSSIPRNPTGKVLRKELP 515
PLN02614 PLN02614
long-chain acyl-CoA synthetase
1345-1717 5.66e-14

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 77.75  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGiLGVLKAGGAY-LPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGLYcVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIK-------GIEFQGNVIDLMDMSFEE-EPGEDMHMMI--------------------EPHNLAYVIYTSGSTGQPK 1475
Cdd:PLN02614  160 KKISElfktcpnSTEYMKTVVSFGGVSREQkEEAETFGLVIyawdeflklgegkqydlpikKKSDICTIMYTSGTTGDPK 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDF-SQDIGITDNVLFSSSIS----FDVTIFEIFVPliYGARMTIYQGekfDVTKLVQVILEE 1550
Cdd:PLN02614  240 GVMISNESIVTLIAGVIRLLkSANAALTVKDVYLSYLPlahiFDRVIEECFIQ--HGAAIGFWRG---DVKLLIEDLGEL 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLLNEIYD-------------YFVRDN----------------------QKIVLNK-----------LLVG 1584
Cdd:PLN02614  315 KPTIFCAVPRVLDRVYSglqkklsdggflkKFVFDSafsykfgnmkkgqshveasplcDKLVFNKvkqglggnvriILSG 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 VEPIKTELlakyDHLFR--GNLQILNGYGPTEAtvcCTSYRYESNKEITTQNVpIGSPLLNTKIYiLDSFHRIQPIGVP- 1661
Cdd:PLN02614  395 AAPLASHV----ESFLRvvACCHVLQGYGLTES---CAGTFVSLPDELDMLGT-VGPPVPNVDIR-LESVPEMEYDALAs 465
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1662 ---GEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGR 1717
Cdd:PLN02614  466 tprGEICIRGKTLFSGYYKREDLTKEVLID-------GWLHTGDVGEWQPNGSMKIIDR 517
PRK07529 PRK07529
AMP-binding domain protein; Validated
414-769 5.71e-14

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 77.69  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLVCGARMTI- 489
Cdd:PRK07529  211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEV----ANAWLGALLLGLGpGDTVFCGLPLFHVNalLVTGLAPLARGAHVVLa 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  490 ----YQGEKFdVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILN 565
Cdd:PRK07529  287 tpqgYRGPGV-IANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEA--ATGVRIVE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  566 LYGPTEAT-VCCTSYqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQ---PIGVPGEICISGIGLARGYinrkeLTAD 641
Cdd:PRK07529  364 GYGLTEATcVSSVNP---PDGERRIGSVGLRLPYQRVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-----LEAA 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  642 KFIDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIQREDE-SGEkyL- 718
Cdd:PRK07529  436 HNKGLWLEDG--WLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGE--Lp 510
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446807313  719 CAYV--VTEKDIPIPEVRAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07529  511 VAYVqlKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1323-1812 7.35e-14

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 77.02  E-value: 7.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL---PI 1398
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTdlPKQrVEYMLTDSGCSHVLVHQN--SIIKGIEFQGNV---------------------------------IDLMD-M 1442
Cdd:PRK08974  108 YT--PRE-LEHQLNDSGAKAIVIVSNfaHTLEKVVFKTPVkhviltrmgdqlstakgtlvnfvvkyikrlvpkYHLPDaI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1443 SFEEEPGEDMHMM-----IEPHNLAYVIYTSGSTGQPKGVMIEHRS-LTNFLCA--MYEDF---SQDIGITDNVLFSssi 1511
Cdd:PRK08974  185 SFRSALHKGRRMQyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAkaAYGPLlhpGKELVVTALPLYH--- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1512 sfdvtIFEIFVP------------LIYGARmtiyqgekfDVTKLVQVILEEQVTLSyippTLLNEIYDYFVRDNQKIVLN 1579
Cdd:PRK08974  262 -----IFALTVNcllfielggqnlLITNPR---------DIPGFVKELKKYPFTAI----TGVNTLFNALLNNEEFQELD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 ----KLLVGV-EPIKTELLAKYDHLFRGNLqiLNGYGPTEATVCCTSYRYESNKeittQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:PRK08974  324 fsslKLSVGGgMAVQQAVAERWVKLTGQYL--LEGYGLTECSPLVSVNPYDLDY----YSGSIGLPVPSTEIKLVDDDGN 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEI 1734
Cdd:PRK08974  398 EVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKD-------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1735 E-ASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08974  471 EdVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1330-1813 7.67e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 76.57  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:PRK13383   47 RWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGCShVLVHQNSIIKGIEFQGN---VIDLMDMSFEEEPGEDMhmMIEPHNLayVIYTSGSTGQPKGVmiehrsltn 1486
Cdd:PRK13383  127 ALRAHHIS-TVVADNEFAERIAGADDavaVIDPATAGAEESGGRPA--VAAPGRI--VLLTSGTTGKPKGV--------- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 flcAMYEDFSQDIGITDNVLFSSSISFDVTIfEIFVPLIYGARM-----------TIYQGEKFDV-TKLVQVILEEQVTL 1554
Cdd:PRK13383  193 ---PRAPQLRSAVGVWVTILDRTRLRTGSRI-SVAMPMFHGLGLgmlmltialggTVLTHRHFDAeAALAQASLHRADAF 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPpTLLNEIYDYFVRDNQKIVLNKLLVGV---EPIKTELLAKYDHLFrGNLqILNGYGPTEATVCCTSyryeSNKEIT 1631
Cdd:PRK13383  269 TAVP-VVLARILELPPRVRARNPLPQLRVVMssgDRLDPTLGQRFMDTY-GDI-LYNGYGSTEVGIGALA----TPADLR 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1632 TQNVPIGSPLLNTKIYILDSFHRiqPIG--VPGEICISGiglargyinrkELTADKFIDHpferGEK-----LYKTGDIA 1704
Cdd:PRK13383  342 DAPETVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1705 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEK--DIPIPEVRAYLAT 1782
Cdd:PRK13383  405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKD 484
                         490       500       510
                  ....*....|....*....|....*....|.
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:PRK13383  485 RVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK07514 PRK07514
malonyl-CoA synthase; Validated
287-692 9.18e-14

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 76.45  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  287 QNPNQIAI-VCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK07514   14 ADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  366 YMLTDS----------------------GCSHVLTYqnsiikGVAFQGSVINL-MDIPFEEEQVEdlqitMEPQNLAYVI 422
Cdd:PRK07514   94 YFIGDAepalvvcdpanfawlskiaaaaGAPHVETL------DADGTGSLLEAaAAAPDDFETVP-----RGADDLAAIL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  423 YTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDigitdnvlfsssisfDVTI--FEIF----------VPLVCGARMt 488
Cdd:PRK07514  163 YTSGTTGRSKGAMLSHGNLLSNALTLvdYWRFTPD---------------DVLIhaLPIFhthglfvatnVALLAGASM- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  489 IYQgEKFDVPKLVQviLEEQVTLAYIPPTllneiydYFVRANQKISLNK-------LFV-GVEPikteLLAKYDHLF--R 558
Cdd:PRK07514  227 IFL-PKFDPDAVLA--LMPRATVMMGVPT-------FYTRLLQEPRLTReaaahmrLFIsGSAP----LLAETHREFqeR 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  559 GNLQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD--SFHRLqPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK07514  293 TGHAILERYGMTE-TNMNTSNPYDGERRAGT----VGFPLPGVSLRVTDpeTGAEL-PPGEIGMIEVKGPNVFKGYWRMP 366
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  637 ELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:PRK07514  367 EKTAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
421-765 1.48e-13

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: 74.26  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  421 VIYTSGSTGQPKGVMIEHRSL-TNFLCAMYedfSQDIGiTDNVLFSSSISFDV-TIFEIFVPLVCGARMTIYQgeKFDVP 498
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlAQALVLAV---LQAID-EGTVFLNSGPLFHIgTLMFTLATFHAGGTNVFVR--RVDAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  499 KLVQVILEEQVTLAYI-PPTL-----LNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYdhlFRGnlqilnlYGPTEA 572
Cdd:cd17636    79 EVLELIEAERCTHAFLlPPTIdqiveLNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRK---PGG-------YGQTEV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  573 TVCCTSYQYERdKEITTQNVPigSPLLntKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpferge 652
Cdd:cd17636   149 MGLATFAALGG-GAIGGAGRP--SPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  653 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TE 725
Cdd:cd17636   217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkpgasvTE 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 446807313  726 KDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd17636   297 AEL-IEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
PRK13382 PRK13382
bile acid CoA ligase;
273-772 2.23e-13

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 75.18  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  273 ETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAY 352
Cdd:PRK13382   41 EGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  353 LPIDTELPKQRVEYMLTDSGcSHVLTYQNSIIKGV--AFQG--SVINLMDIPFEEEQVEDLQITMEPQNLA--------- 419
Cdd:PRK13382  121 LLLNTSFAGPALAEVVTREG-VDTVIYDEEFSATVdrALADcpQATRIVAWTDEDHDLTVEVLIAAHAGQRpeptgrkgr 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  420 YVIYTSGSTGQPKG--------------VM----IEHRSLTNFLCAMYE--DFSQdigitdnVLFSSSIsfdvtifeifv 479
Cdd:PRK13382  200 VILLTSGTTGTPKGarrsgpggigtlkaILdrtpWRAEEPTVIVAPMFHawGFSQ-------LVLAASL----------- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  480 plvcgaRMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGV---EPIKTELLAKYDHL 556
Cdd:PRK13382  262 ------ACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAasgSRMRPDVVIAFMDQ 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  557 FrGNLqILNLYGPTEATVCCTSYQYERDKEITTQnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK13382  336 F-GDV-IYNNYNATEAGMIATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  637 eltadkfiDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEK 716
Cdd:PRK13382  410 --------TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQ 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313  717 YLCAYVVTEKDIP-IPE-----VRAYLATklpyYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:PRK13382  480 RLAAFVVLKPGASaTPEtlkqhVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1344-1812 2.58e-13

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 74.94  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK08276   12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 ------NSIIKGIEfQGNVIDLMD-------MSFEEE-------------PGEDMHmmiephnlayviYTSGSTGQPKGV 1477
Cdd:PRK08276   92 aladtaAELAAELP-AGVPLLLVVagpvpgfRSYEEAlaaqpdtpiadetAGADML------------YSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 MIE------HRSLTNFLCAMYEDFsqdIGITDNVLFSSSisfdvtifeifvPLIYGA----RMTIYQG-------EKFDV 1540
Cdd:PRK08276  159 KRPlpgldpDEAPGMMLALLGFGM---YGGPDSVYLSPA------------PLYHTAplrfGMSALALggtvvvmEKFDA 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLlneiydyFVRdnqkivLNKLlvgvePikTELLAKYD----------------HLFRgnl 1604
Cdd:PRK08276  224 EEALALIERYRVTHSQLVPTM-------FVR------MLKL-----P--EEVRARYDvsslrvaihaaapcpvEVKR--- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPteatvccTSYRYESNKE------ITTQNV---P--IGSPLLnTKIYILDSFHRIQPIGVPGEICISGIGLAR 1673
Cdd:PRK08276  281 AMIDWWGP-------IIHEYYASSEgggvtvITSEDWlahPgsVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPF 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDHPFergeklYKTGDIArWL-PDGnieYL---GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 1749
Cdd:PRK08276  353 EYHNDPEKTAAARNPHGW------VTVGDVG-YLdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1750 I---DqeDEAGEKYLCayVVTEKDIPIP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08276  423 FgvpD--EEMGERVKA--VVQPADGADAgdalaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
297-771 3.68e-13

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: 74.39  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  297 NGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDtelpkqrveYMLTDSGCSH 375
Cdd:cd05937     2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLIH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  376 VLTYQNSiikgvafqgsvinlmdipfeeeqvedLQITMEPQNLAYVIYTSGSTGQPKGVMIE-HRSLTNFLCamyedFSQ 454
Cdd:cd05937    73 CLKLSGS--------------------------RFVIVDPDDPAILIYTSGTTGLPKAAAISwRRTLVTSNL-----LSH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  455 DIGITDNVLFSSSIS-FDVTIFEIFVPLVCGARMTIYQGEKFDVPKL-VQVILEEQVTLAYIPPT---LLN---EIYDyf 526
Cdd:cd05937   122 DLNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKFSASQFwKDVRDSGATIIQYVGELcryLLStppSPYD-- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  527 vrANQKISL---NklfvGVEPiktELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQ-------------------YERD 584
Cdd:cd05937   200 --RDHKVRVawgN----GLRP---DIWERFRERF-NVPEIGEFYAATEGVFALTNHNvgdfgagaighhglirrwkFENQ 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  585 KEITTQNVPIGSPLLNTKiyilDSFHRLQPIGVPGEICI----SGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDI 660
Cdd:cd05937   270 VVLVKMDPETDDPIRDPK----TGFCVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  661 ARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV--IQREDESGEKYLCAYVVTEKDIPIPEVRAYLA 738
Cdd:cd05937   346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPTEFTKSLL 425
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446807313  739 TK-----LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:cd05937   426 ASlarknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1345-1812 3.69e-13

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: 74.42  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDsgcshvlvhqn 1424
Cdd:cd05910     4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQE----------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgIEFQGnvidlmdmsFEEEPGEDmhmmiEPhnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDN 1504
Cdd:cd05910    73 -----AEPDA---------FIGIPKAD-----EP---AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSssisfdvtIFEIFVPLIYGAR----MTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLN 1579
Cdd:cd05910   131 ATFP--------LFALFGPALGLTSvipdMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLpSLR 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 KLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEA-TVCCTSYRyesNKEITTQNVP-------IGSPLLNTKIYIL-- 1649
Cdd:cd05910   203 RVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlPVSSIGSR---ELLATTTAATsggagtcVGRPIPGVRVRIIei 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 --------DSFHRIqPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERgeKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd05910   280 ddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG--FWHRMGDLGYLDDEGRLWFCGRKAHR 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIK-TAVVIDQEDEAGEKYLCayVVTEKDIPIPEVRAY-----LATKLPH-YMIPQQLI 1794
Cdd:cd05910   357 VITTGGTLYTEPVERVFNTHPGVRrSALVGVGKPGCQLPVLC--VEPLPGTITPRARLEqelraLAKDYPHtQRIGRFLI 434
                         490
                  ....*....|....*....
gi 446807313 1795 -PIHNIPLTQNGKIDRSKL 1812
Cdd:cd05910   435 hPSFPVDIRHNAKIFREKL 453
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
1344-1718 8.64e-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: 73.55  E-value: 8.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSgCSHVLVHQ 1423
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANILVVE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 N-------SIIKG--------IEFQG-------NVI---DLMDMSFEEePGEDMHMMIE---PHNLAYVIYTSGSTGQPK 1475
Cdd:cd05933    88 NqkqlqkiLQIQDklphlkaiIQYKEplkekepNLYswdEFMELGRSI-PDEQLDAIISsqkPNQCCTLIYTSGTTGMPK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMyedfSQDIGITDN-VLFSSSISF------DVTIFEIFVPLIYGA-------------------- 1528
Cdd:cd05933   167 GVMLSHDNITWTAKAA----SQHMDLRPAtVGQESVVSYlplshiAAQILDIWLPIKVGGqvyfaqpdalkgtlvktlre 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 -RMTIYQG-----EKFDvTKLVQVI------------------LEEQVTL--SYIPPTLLNEIYDYFV--RDNQKIVLN- 1579
Cdd:cd05933   243 vRPTAFMGvprvwEKIQ-EKMKAVGaksgtlkrkiaswakgvgLETNLKLmgGESPSPLFYRLAKKLVfkKVRKALGLDr 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 --KLLVGVEPIKTELLakydHLFRG-NLQILNGYGPTEATVCCT-----SYR-YESNKEIttqnvpigsPLLNTKIyild 1650
Cdd:cd05933   322 cqKFFTGAAPISRETL----EFFLSlNIPIMELYGMSETSGPHTisnpqAYRlLSCGKAL---------PGCKTKI---- 384
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1651 sfHRIQPIGVpGEICISGIGLARGYINRKELTADKFIDHPFERgeklykTGDIARWLPDGNIEYLGRV 1718
Cdd:cd05933   385 --HNPDADGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH------SGDLGKLDEDGFLYITGRI 443
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
301-779 1.15e-12

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 73.53  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyq 380
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  381 NSIIKGVAFQGSVINLMDIPFEEEQVE--DLQItMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED----FSQ 454
Cdd:PRK06060  109 SDALRDRFQPSRVAEAAELMSEAARVApgGYEP-MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKalrlTPE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  455 DIGITdnvlfSSSISFDVTI-FEIFVPLVCGARMTIYQgekfdvpklVQVILEEQVTL-AYIPPTLLNEIYDYFVR---- 528
Cdd:PRK06060  188 DTGLC-----SARMYFAYGLgNSVWFPLATGGSAVINS---------APVTPEAAAILsARFGPSVLYGVPNFFARvids 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 --ANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYIL 606
Cdd:PRK06060  254 csPDSFRSLRCVVSAGEALELGLAERLMEFF-GGIPILDGIGSTEVGQTFVSNRVDEWRLGT-----LGRVLPPYEIRVV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  607 DSFHRLQPIGVPGEICISGIGLARGYINRKEltadkfidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:PRK06060  328 APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE-----VRAYLATKLPYYMIPQQIISIQNIPLTQN 761
Cdd:PRK06060  399 DPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPN 478
                         490       500
                  ....*....|....*....|...
gi 446807313  762 GKIDRKKL-----PQPINNLKSS 779
Cdd:PRK06060  479 GKLVRGALrkqspTKPIWELSLT 501
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
269-771 1.24e-12

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 73.00  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  269 TLLCETVTAPQLF---EEQVKQNPNQIAIVCNGKEI--TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGIL 343
Cdd:PRK05852    7 AAPMASDFGPRIAdlvEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  344 GILKAGGAYLPIDTELPKQ-----------RVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDI--PFEEEQVEDLQ 410
Cdd:PRK05852   87 AASRADLVVVPLDPALPIAeqrvrsqaagaRVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTlsVHLDAATEPTP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  411 ITMEPQNL----AYVIYTSGSTGQPKGVMIEHRSLT---NFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIFVPLVC 483
Cdd:PRK05852  167 ATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIAssvRAIITGYRLSPRDATVAVMPLYHGH----GLIAALLATLAS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  484 GARMTIYQGEKFD------------------VPKLVQVILEEQVT--LAYIPPTLlneiydYFVRAnqkISLNKLFVGVE 543
Cdd:PRK05852  243 GGAVLLPARGRFSahtfwddikavgatwytaVPTIHQILLERAATepSGRKPAAL------RFIRS---CSAPLTAETAQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  544 PIKTELLAKydhlfrgnlqILNLYGPTEATVCCTSYQYE---RDKEITTQNVPIGSPLlNTKIYILDSFHRLQPIGVPGE 620
Cdd:PRK05852  314 ALQTEFAAP----------VVCAFGMTEATHQVTTTQIEgigQTENPVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  621 ICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:PRK05852  383 VWLRGTTVVRGYLGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313  701 IKTAVVIQREDES-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK05852  456 VMEAAVFGVPDQLyGEAVAAVIVPRESAPPTAeELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
PLN02614 PLN02614
long-chain acyl-CoA synthetase
280-713 2.21e-12

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 72.36  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  280 LFEEQVKQNPNQIAI----VCNGKE-----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG 350
Cdd:PLN02614   50 VFRMSVEKYPNNPMLgrreIVDGKPgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  351 AYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIK-------GVAFQGSVINLMDI-PFEEEQVEDLQITM--------- 413
Cdd:PLN02614  130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISElfktcpnSTEYMKTVVSFGGVsREQKEEAETFGLVIyawdeflkl 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 -----------EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF-SQDIGITDNVLFSSSIS----FDVTIFEI 477
Cdd:PLN02614  210 gegkqydlpikKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLkSANAALTVKDVYLSYLPlahiFDRVIEEC 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  478 FVPLvcGARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFvraNQKISLNKLF------------------ 539
Cdd:PLN02614  290 FIQH--GAAIGFWRG---DVKLLIEDLGELKPTIFCAVPRVLDRVYSGL---QKKLSDGGFLkkfvfdsafsykfgnmkk 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  540 ----VGVEPIKTELL-AKYDHLFRGNLQ-ILNLYGPTEATV--------CC---TSYQYERDKEITTQNVP--------I 594
Cdd:PLN02614  362 gqshVEASPLCDKLVfNKVKQGLGGNVRiILSGAAPLASHVesflrvvaCChvlQGYGLTESCAGTFVSLPdeldmlgtV 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  595 GSPLLNTKIYiLDSFHRLQPIGVP----GEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIE 670
Cdd:PLN02614  442 GPPVPNVDIR-LESVPEMEYDALAstprGEICIRGKTLFSGYYKREDLTKEVLID-------GWLHTGDVGEWQPNGSMK 513
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446807313  671 YLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIQREDES 713
Cdd:PLN02614  514 IIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWVYGNSFES 557
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1462-1808 2.33e-12

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 72.69  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHRsltNFLCAMYE-----DFS-QDIGItdNVL--FSSsisFDVTIFEIfVPLIYGARMTIY 1533
Cdd:PRK06814  796 AVILFTSGSEGTPKGVVLSHR---NLLANRAQvaariDFSpEDKVF--NALpvFHS---FGLTGGLV-LPLLSGVKVFLY 866
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QgEKFDVTKLVQVILEEQVTLSYIPPTLLN------EIYDYFVrdnqkivLNKLLVGVEPIKTELLAKYDHLFRgnLQIL 1607
Cdd:PRK06814  867 P-SPLHYRIIPELIYDTNATILFGTDTFLNgyaryaHPYDFRS-------LRYVFAGAEKVKEETRQTWMEKFG--IRIL 936
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTEAtvcctsyryesnkeittqnvpigSPLL--NTKIY--------ILDSFH-RIQPI-GVP--GEICISGIGLAR 1673
Cdd:PRK06814  937 EGYGVTET-----------------------APVIalNTPMHnkagtvgrLLPGIEyRLEPVpGIDegGRLFVRGPNVML 993
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYinrkeLTADK-FIDHPFERGEklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE--ASLLkYETIKTAVVI 1750
Cdd:PRK06814  994 GY-----LRAENpGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelAAEL-WPDALHAAVS 1065
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1751 DQEDEAGEKYLcaYVVTEKDIPIPEVRAYLATK-LPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK06814 1066 IPDARKGERII--LLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
298-769 3.15e-12

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 71.47  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG----- 372
Cdd:PRK08276    9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGakvli 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  373 CSHVLTYQNSIIKGVAFQGSVINLMD-------IPFEEE--QVEDLQITMEPQNlAYVIYTSGSTGQPKGVMIE------ 437
Cdd:PRK08276   89 VSAALADTAAELAAELPAGVPLLLVVagpvpgfRSYEEAlaAQPDTPIADETAG-ADMLYSSGTTGRPKGIKRPlpgldp 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  438 HRSLTNFLCAMYEDFsqdIGITDNVLFSSSisfdvtifeifvPLVCGA----RMTIYQG-------EKFDVPKLVQVILE 506
Cdd:PRK08276  168 DEAPGMMLALLGFGM---YGGPDSVYLSPA------------PLYHTAplrfGMSALALggtvvvmEKFDAEEALALIER 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  507 EQVTLAYIPPTLlneiydyFVRanqkisLNKLfvgvePikTELLAKYD----------------HLFRgnlQILNLYGP- 569
Cdd:PRK08276  233 YRVTHSQLVPTM-------FVR------MLKL-----P--EEVRARYDvsslrvaihaaapcpvEVKR---AMIDWWGPi 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  570 -------TEA---TVcCTSYQYERDKEittqnvPIGSPLLnTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK08276  290 iheyyasSEGggvTV-ITSEDWLAHPG------SVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKT 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  640 ADKFIDHPFergeklYKTGDIArWL-PDGnieYL---GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ-REDESG 714
Cdd:PRK08276  362 AAARNPHGW------VTVGDVG-YLdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGvPDEEMG 431
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313  715 EKYLCayVVTEKDIPIP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08276  432 ERVKA--VVQPADGADAgdalaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1340-1812 3.65e-12

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


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 71.31  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDtdlpkqrveYMLTDSGCSH 1418
Cdd:cd05937     2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLIH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVhqnsiIKGIEFqgnvidlmdmsfeeepgedmhMMIEPHNLAYVIYTSGSTGQPKGVMIE-HRSLTNFLCamyedFSQ 1497
Cdd:cd05937    73 CLK-----LSGSRF---------------------VIVDPDDPAILIYTSGTTGLPKAAAISwRRTLVTSNL-----LSH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIGITDNVLFSSSIS-FDVTIFEI-FVPLIYGARmTIYQGEKFDVTKL-VQVILEEQVTLSYIPPT---LLN---EIYDy 1568
Cdd:cd05937   122 DLNLKNGDRTYTCMPlYHGTAAFLgACNCLMSGG-TLALSRKFSASQFwKDVRDSGATIIQYVGELcryLLStppSPYD- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 fvRDNQKIVL--NKL----------LVGVEPIK-----TELLAKYDHLFRGNLQI--LNGYGPTeatvcctSYRYESNKE 1629
Cdd:cd05937   200 --RDHKVRVAwgNGLrpdiwerfreRFNVPEIGefyaaTEGVFALTNHNVGDFGAgaIGHHGLI-------RRWKFENQV 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVP-IGSPLLNTKiyilDSFHRIQPIGVPGEICI----SGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIA 1704
Cdd:cd05937   271 VLVKMDPeTDDPIRDPK----TGFCVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLL 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1705 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekylCAYV-VTEKDIPIPEVRA 1778
Cdd:cd05937   347 RQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYgvkvpGHDGRAG----CAAItLEESSAVPTEFTK 422
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446807313 1779 YLATK-----LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05937   423 SLLASlarknLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
782-855 3.74e-12

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: 63.72  E-value: 3.74e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313  782 EPTNSTERKLVEIWKDVLGI--QRIGIRDNFF-EIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILE 855
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1826-1901 1.19e-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: 62.18  E-value: 1.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1826 PRNEIDSSLIDIWSSILGVN--NIGINDNFF-ELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKG 1901
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1605-1812 1.20e-11

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 69.79  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAD 1684
Cdd:PRK05677  353 AICEGYGMTETSPVVSVNPSQAIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1685 KFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAY 1764
Cdd:PRK05677  428 ILDS------DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVF 501
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 446807313 1765 VVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK05677  502 VVVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
789-848 1.31e-11

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: 61.43  E-value: 1.31e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313   789 RKLVEIWKDVLGI--QRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVD 848
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1344-1735 1.34e-11

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 69.52  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV-- 1421
Cdd:PRK07514   29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCdp 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 HQNSIIKGIEFQGNVIDL-----------------MDMSFEEEP-GEDmhmmiephNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PRK07514  109 ANFAWLSKIAAAAGAPHVetldadgtgslleaaaaAPDDFETVPrGAD--------DLAAILYTSGTTGRSKGAMLSHGN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLCAM--YEDFSQDigitdnvlfsssisfDVTI--FEIF----------VPLIYGARMtIYQgEKFDvtkLVQVI-L 1548
Cdd:PRK07514  181 LLSNALTLvdYWRFTPD---------------DVLIhaLPIFhthglfvatnVALLAGASM-IFL-PKFD---PDAVLaL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTllneiydYFVRDNQKIVLNKLLV--------GVEPikteLLAKYDHLF--RGNLQILNGYGPTEaTVC 1618
Cdd:PRK07514  241 MPRATVMMGVPT-------FYTRLLQEPRLTREAAahmrlfisGSAP----LLAETHREFqeRTGHAILERYGMTE-TNM 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFH-RIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKL 1697
Cdd:PRK07514  309 NTSNPYDGERRAGT----VGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF------RADGF 378
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 1735
Cdd:PRK07514  379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
PLN02736 PLN02736
long-chain acyl-CoA synthetase
415-674 1.46e-11

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 69.74  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGITDNVLFSSS---ISF--DVTIFE---IFVPLVCGAR 486
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNL----------IANVAGSSLSTKFYPSdvhISYlpLAHIYErvnQIVMLHYGVA 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  487 MTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ--------------------------------KIS 534
Cdd:PLN02736  290 VGFYQG---DNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKesgglkerlfnaaynakkqalengknpspmwdRLV 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  535 LNKL-----------FVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEaTVCCTSYQYERDKeiTTQNVpiGSPLLNTKI 603
Cdd:PLN02736  367 FNKIkaklggrvrfmSSGASPLSPDVMEFLRICFGG--RVLEGYGMTE-TSCVISGMDEGDN--LSGHV--GSPNPACEV 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  604 YILDsfhrlqpigVP-------------GEICISGIGLARGYInRKELTADKFIDhpferGEKLYKTGDIARWLPDGNIE 670
Cdd:PLN02736  440 KLVD---------VPemnytsedqpyprGEICVRGPIIFKGYY-KDEVQTREVID-----EDGWLHTGDIGLWLPGGRLK 504

                  ....
gi 446807313  671 YLGR 674
Cdd:PLN02736  505 IIDR 508
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
302-769 1.47e-11

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 69.40  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  302 TYKQLNIKANQLARRLLDQGVKREFIVGVM---MERSIEMIVGILGIlkagGA--------------------------- 351
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI----GAichtvnprlfpeqiawiinhaedrvvi 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  352 ----YLP----IDTELPkqRVEYMLTDSGCSHVLtyQNSIIKGVAFQGSVinlmdipfeEEQVEDLQITMEPQNLAYVI- 422
Cdd:PRK06018  117 tdltFVPilekIADKLP--SVERYVVLTDAAHMP--QTTLKNAVAYEEWI---------AEADGDFAWKTFDENTAAGMc 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  423 YTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDnvlfSSSISFDVTIFEI------FVPLVCGARMtIYQGEKFD 496
Cdd:PRK06018  184 YTSGTTGDPKGVLYSHRS--NVLHALMANNGDALGTSA----ADTMLPVVPLFHAnswgiaFSAPSMGTKL-VMPGAKLD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  497 VPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTE---- 571
Cdd:PRK06018  257 GASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLpHLKMVVCGGSAMPRSMIKAFEDM---GVEVRHAWGMTEmspl 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  572 ATVCCTSYQYER---DKEItTQNVPIGSPLLNTKIYILDSFHRLQPIG--VPGEICISGIGLARGY--INRKELTADKFI 644
Cdd:PRK06018  334 GTLAALKPPFSKlpgDARL-DVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYyrVDGEILDDDGFF 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  645 DhpfergeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVV 723
Cdd:PRK06018  413 D-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgVYHPKWDERPLLIVQL 481
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446807313  724 TEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06018  482 KPGETATReEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
7-238 1.77e-11

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: 68.54  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDclslnnIQASK-ESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVK 85
Cdd:cd19531   179 QREWLQGEVLERQLAYWREQLAGAPPVLELPTDrpr-paVQSFRgARVRFTLPAELTAALRALARREGATLFMTLLAAFQ 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   86 YLLSRYTDKDDVVIGMPVFKQGQEET-------VfqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQ- 157
Cdd:cd19531   258 VLLHRYSGQDDIVVGTPVAGRNRAELegligffV---NTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEa 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  158 ------------------LLSLDGESNNLPLLNTIVMLDDIHcyesTDKinSDMVIRFMKNEEQLKVQVDYNSTLYSEGL 219
Cdd:cd19531   335 lqperdlsrsplfqvmfvLQNAPAAALELPGLTVEPLEVDSG----TAK--FDLTLSLTETDGGLRGSLEYNTDLFDAAT 408
                         250
                  ....*....|....*....
gi 446807313  220 VSRIVNHLYNILDILMKDP 238
Cdd:cd19531   409 IERMAGHFQTLLEAIVADP 427
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1464-1808 4.02e-11

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: 66.94  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSL-TNFLCAMYedfSQDIGiTDNVLFSSSISFDV-TIFEIFVPLIYGARMTIYQgeKFDVT 1541
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlAQALVLAV---LQAID-EGTVFLNSGPLFHIgTLMFTLATFHAGGTNVFVR--RVDAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1542 KLVQVILEEQVTLSYI-PPTL-----LNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYdhlfrgnlqiLNGYGPTEa 1615
Cdd:cd17636    79 EVLELIEAERCTHAFLlPPTIdqiveLNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRK----------PGGYGQTE- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1616 TVCCTSYRYESNKEITTQNVPigSPLLntKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpferge 1695
Cdd:cd17636   148 VMGLATFAALGGGAIGGAGRP--SPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1696 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-------TE 1768
Cdd:cd17636   217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkpgasvTE 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 446807313 1769 KDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd17636   297 AEL-IEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
562-769 5.59e-11

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 67.87  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  562 QILNLYGPTEAT--VCCTSYQYerdkeitTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK05677  353 AICEGYGMTETSpvVSVNPSQA-------IQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEAT 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  640 ADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLC 719
Cdd:PRK05677  426 DEILDS------DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIK 499
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446807313  720 AYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK05677  500 VFVVVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1345-1815 5.95e-11

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 67.45  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd05939     5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 SiikgiefqgnviDLMDMSFEEEPGEDmhmMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQDIGI 1501
Cdd:cd05939    85 D------------PLLTQSSTEPPSQD---DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFgmrPEDVVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 TDNVLFSSSISfdvtIFEIFVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLS-YIpptllNEIYDYF----VRDNQKI 1576
Cdd:cd05939   150 DCLPLYHSAGG----IMGVGQALLHG--STVVIRKKFSASNFWDDCVKYNCTIVqYI-----GEICRYLlaqpPSEEEQK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGvEPIKTELLAKYDHLFRGNlQILNGYGPTEatvcCTSyryeSNKEITTQNVPIG-SPLLNTKIY-------- 1647
Cdd:cd05939   219 HNVRLAVG-NGLRPQIWEQFVRRFGIP-QIGEFYGATE----GNS----SLVNIDNHVGACGfNSRILPSVYpirlikvd 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ------ILDSFHRIQPIGvPGEiciSGIGLAR-----------GYINRKElTADKFIDHPFERGEKLYKTGDIARWLPDG 1710
Cdd:cd05939   289 edtgelIRDSDGLCIPCQ-PGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELG 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1711 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekyLCAYVVTEKDIPIPEVRAYLATKLP 1785
Cdd:cd05939   364 YLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgvevpGVEGRAG---MAAIVDPERKVDLDRFSAVLAKSLP 440
                         490       500       510
                  ....*....|....*....|....*....|
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05939   441 PYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
7-238 6.67e-11

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: 67.02  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGdVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd19539   179 QREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFKQGQ---EETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:cd19539   258 LLRRYTGQTDIVVGTPVAGRNHprfESTVgFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELPVD 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  163 GESNNLPLL-------NTIVMLDDIHCYES-------TDKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLY 228
Cdd:cd19539   338 RDAGRHPLVqivfqvtNAPAGELELAGGLSytegsdiPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYL 417
                         250
                  ....*....|
gi 446807313  229 NILDILMKDP 238
Cdd:cd19539   418 QVLRQLLANP 427
PRK13382 PRK13382
bile acid CoA ligase;
1329-1813 6.92e-11

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 67.48  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVcNEKGI-TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK13382   54 QRCPDRPGLI-DELGTlTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLVHQnsiikgiEFqgnvIDLMDMSFEEEPG---------EDMHMMIE--------------PHNLAYV 1464
Cdd:PRK13382  133 AEVVTREGVDTVIYDE-------EF----SATVDRALADCPQatrivawtdEDHDLTVEvliaahagqrpeptGRKGRVI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1465 IYTSGSTGQPKGVmieHRSLtnflcamyedfSQDIGITDNVLFSSSISFDVTIFEI--------FVPLIYGARM--TIYQ 1534
Cdd:PRK13382  202 LLTSGTTGTPKGA---RRSG-----------PGGIGTLKAILDRTPWRAEEPTVIVapmfhawgFSQLVLAASLacTIVT 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1535 GEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYF--VRDNQKIVLNKLLVGV-EPIKTELLAKYDHLFrGNLqILNGYG 1611
Cdd:PRK13382  268 RRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASgSRMRPDVVIAFMDQF-GDV-IYNNYN 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1612 PTEATVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKeltadkfiDHPF 1691
Cdd:PRK13382  346 ATEAGMIATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS--------TKDF 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1692 ERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDI 1771
Cdd:PRK13382  414 HDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313 1772 P-IPE-----VRAYLAtklpHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:PRK13382  492 SaTPEtlkqhVRDNLA----NYKVPRDIVVLDELPRGATGKILRRELQ 535
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
293-772 7.13e-11

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 67.03  E-value: 7.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  293 AIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG 372
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  373 cSHVLTYQNSIIKGVAFQ-GSVINLMDIPFEEEQVEDLQI----------------------------TMEPQNLayvIY 423
Cdd:PRK12406   84 -ARVLIAHADLLHGLASAlPAGVTVLSVPTPPEIAAAYRIspalltppagaidwegwlaqqepydgppVPQPQSM---IY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  424 TSGSTGQPKGV-----MIEHRSLTNFLCAMYEDFSQDIG--ITDNVLFSSSISFDVTIFEIFVPLVCGARmtiyqgekFD 496
Cdd:PRK12406  160 TSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGIRalLTGPLYHSAPNAYGLRAGRLGGVLVLQPR--------FD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  497 VPKLVQVILEEQVTLAYIPPTLLNEIYDY--FVRANQKIS-LNKLFVGVEP----IKTELLAKYDHLfrgnlqILNLYGP 569
Cdd:PRK12406  232 PEELLQLIERHRITHMHMVPTMFIRLLKLpeEVRAKYDVSsLRHVIHAAAPcpadVKRAMIEWWGPV------IYEYYGS 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  570 TE--ATVCCTSYQYERdKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLAR-GYINRKELTADkfidh 646
Cdd:PRK12406  306 TEsgAVTFATSEDALS-HPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE----- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  647 pFERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEK 726
Cdd:PRK12406  375 -IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 446807313  727 DIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:PRK12406  453 GATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
313-786 7.19e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 67.52  E-value: 7.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  313 LARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPID----TELPKQRVEY----ML-TDSGCSH-VLTYQNS 382
Cdd:PLN02860   45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsFEEAKSAMLLvrpvMLvTDETCSSwYEELQND 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  383 IIKGVAFQgsviNLMDIPFEEEQVEDLQI-TME-----------------PQNLAYVIYTSGSTGQPKGVMIEHRSLTNF 444
Cdd:PLN02860  125 RLPSLMWQ----VFLESPSSSVFIFLNSFlTTEmlkqralgtteldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQ 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  445 LCAmyedfsqDIGI----TDNVLFSSS-------ISFDVTIF-----EIFVPlvcgarmtiyqgeKFDVPKLVQVILEEQ 508
Cdd:PLN02860  201 SLA-------KIAIvgygEDDVYLHTAplchiggLSSALAMLmvgacHVLLP-------------KFDAKAALQAIKQHN 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  509 VTLAYIPPTLLNEIydyfVRANQKI-------SLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEAtvcCTSYQY 581
Cdd:PLN02860  261 VTSMITVPAMMADL----ISLTRKSmtwkvfpSVRKILNGGGSLSSRLLPDAKKLF-PNAKLFSAYGMTEA---CSSLTF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  582 ERDKEITTQNvPIGSPLLNTKIYiLDSFHRLQP--IGVPG---EICISGIGLAR-GYI-NRKELTADKFIDHPFERGEKL 654
Cdd:PLN02860  333 MTLHDPTLES-PKQTLQTVNQTK-SSSVHQPQGvcVGKPAphvELKIGLDESSRvGRIlTRGPHVMLGYWGQNSETASVL 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  655 YK-----TGDIArWLPD-GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI--------------------- 707
Cdd:PLN02860  411 SNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgvpdsrltemvvacvrlrdgw 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  708 QREDESGEKYLCAYVVTEKDIpipevRAYLATK-LPYYMIPQQIISIQN-IPLTQNGKIDRKKLPQPInnlkSSHLEPTN 785
Cdd:PLN02860  490 IWSDNEKENAKKNLTLSSETL-----RHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV----LSHLQSLP 560

                  .
gi 446807313  786 S 786
Cdd:PLN02860  561 S 561
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1318-1812 7.20e-11

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 67.08  E-value: 7.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1318 LLVHKMFEEQVKRNPNQIAVVCNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVM---MKRSIEMVIGILGVlk 1390
Cdd:PRK06018   10 LLCHRIIDHAARIHGNREVVTRSVEGpivrTTYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1391 agGA-------------------------------YLPIDTDLPKQ--RVEYMLTDSGCSHVlvHQNSIIKGIEFQGNVi 1437
Cdd:PRK06018   88 --GAichtvnprlfpeqiawiinhaedrvvitdltFVPILEKIADKlpSVERYVVLTDAAHM--PQTTLKNAVAYEEWI- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 dlmdmsfEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITdnvlfSSSISFDVti 1517
Cdd:PRK06018  163 -------AEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRS--NVLHALMANNGDALGTS-----AADTMLPV-- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 feifVPLIY-------------GARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLV 1583
Cdd:PRK06018  227 ----VPLFHanswgiafsapsmGTKL-VMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLpHLKMVVC 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1584 GVEPIKTELLAKYDHLfrgNLQILNGYGPTE----ATVCCTSYRYE--SNKEITTQNVPIGSPLLNTKIYILDSFHRIQP 1657
Cdd:PRK06018  302 GGSAMPRSMIKAFEDM---GVEVRHAWGMTEmsplGTLAALKPPFSklPGDARLDVLQKQGYPPFGVEMKITDDAGKELP 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IG--VPGEICISGIGLARGY--INRKELTADKFIDhpfergeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 1733
Cdd:PRK06018  379 WDgkTFGRLKVRGPAVAAAYyrVDGEILDDDGFFD-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSID 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1734 IEASLLKYETIKTAVVIDQ-EDEAGEKYLCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK06018  448 LENLAVGHPKVAEAAVIGVyHPKWDERPLLIVQLKPGETATReEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTA 527

                  .
gi 446807313 1812 L 1812
Cdd:PRK06018  528 L 528
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
285-769 7.78e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 67.02  E-value: 7.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  285 VKQNPNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQ 362
Cdd:PRK13391    7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  363 RVEYMLTDSGCSHVLTY--QNSIIKGVAFQGSVINL---MDIPFEEEQVEDLQ----------ITMEPQNLAyVIYTSGS 427
Cdd:PRK13391   87 EAAYIVDDSGARALITSaaKLDVARALLKQCPGVRHrlvLDGDGELEGFVGYAeavaglpatpIADESLGTD-MLYSSGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  428 TGQPKGVM--------IEHRSLTNFLCAMYedfsqdiGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK 499
Cdd:PRK13391  166 TGRPKGIKrplpeqppDTPLPLTAFLQRLW-------GFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  500 LVQVILEEQVTLAYIPPTLlneiydyFVR-------ANQKISLNKLFVGVEP-------IKTELLAKYDHLfrgnlqILN 565
Cdd:PRK13391  239 YLALIEEYGVTHTQLVPTM-------FSRmlklpeeVRDKYDLSSLEVAIHAaapcppqVKEQMIDWWGPI------IHE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  566 LYGPTEA--TVCCTSYQYERDKEittqnvPIGSPLLNtKIYILDSFHRLQPIGVPGEICISGiGLARGYINRKELTADKF 643
Cdd:PRK13391  306 YYAATEGlgFTACDSEEWLAHPG------TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEAR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  644 IDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKylCAYV 722
Cdd:PRK13391  378 HPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEE--VKAV 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446807313  723 VTEKDIPIP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13391  451 VQPVDGVDPgpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1323-1809 8.14e-11

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 67.22  E-value: 8.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVC--NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK05852   21 LVEVAATRLPEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVHQNSI----------------IKGIEFQGNVIDLMDMSFEEEPgedMHMMIEPHNL--- 1461
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLIDADGPhdraepttrwwpltvnVGGDSGPSGGTLSVHLDAATEP---TPATSTPEGLrpd 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 -AYVIYTSGSTGQPKGVMIEHRSLT---NFLCAMYEDFSQDIGITD----------NVLFSSSISFDVTIF--------E 1519
Cdd:PRK05852  178 dAMIMFTGGTTGLPKMVPWTHANIAssvRAIITGYRLSPRDATVAVmplyhghgliAALLATLASGGAVLLpargrfsaH 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1520 IFVPLIYGARMTIYQGekfdVTKLVQVILEEQVTLSY--IPPTLlneiydYFVRDNQKIVLNKllvGVEPIKTELLAKyd 1597
Cdd:PRK05852  258 TFWDDIKAVGATWYTA----VPTIHQILLERAATEPSgrKPAAL------RFIRSCSAPLTAE---TAQALQTEFAAP-- 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 hlfrgnlqILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNT--KIYILDSFHRIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK05852  323 --------VVCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK05852  395 LGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQ 467
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1756 A-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK05852  468 LyGEAVAAVIVPRESAPPTAeELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
PRK09192 PRK09192
fatty acyl-AMP ligase;
1346-1811 8.23e-11

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 67.34  E-value: 8.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1346 YNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGG--AYLPIDTDLpKQRVEY------MLTDSGCS 1417
Cdd:PRK09192   52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGF-GGRESYiaqlrgMLASAQPA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQ------NSIIKGiefQGNVIDLMDMSFEEEPGEDMHM-MIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-- 1488
Cdd:PRK09192  131 AIITPDellpwvNEATHG---NPLLHVLSHAWFKALPEADVALpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLra 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 -------------CAMYEDFSQDIGITDNVL--FSSSISFDVTIFEIFV--PLIYgarmtiyqgekfdvtklVQVILEEQ 1551
Cdd:PRK09192  208 ishdglkvrpgdrCVSWLPFYHDMGLVGFLLtpVATQLSVDYLPTRDFArrPLQW-----------------LDLISRNR 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1552 VTLSYIPPTLlneiYDYFVRDNQKIVLNKL-L-------VGVEPIKTELLAKYDHLFRGN----LQILNGYGPTEATVCC 1619
Cdd:PRK09192  271 GTISYSPPFG----YELCARRVNSKDLAELdLscwrvagIGADMIRPDVLHQFAEAFAPAgfddKAFMPSYGLAEATLAV 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 T-----------------------SYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYI 1676
Cdd:PRK09192  347 SfsplgsgivveevdrdrleyqgkAVAPGAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1677 NRKE----LTADKFIDhpfergeklykTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT----AV 1748
Cdd:PRK09192  427 RDEEsqdvLAADGWLD-----------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdaaAF 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1749 VIDQEDeaGEKYLcayVVTEKDIPIPEVRAYLATKLPHYMIPQ-------QLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK09192  495 SIAQEN--GEKIV---LLVQCRISDEERRGQLIHALAALVRSEfgveaavELVPPHSLPRTSSGKLSRAK 559
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
301-675 1.07e-10

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: 67.00  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSgCSHVLTYQ 380
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANILVVE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  381 N-------SIIKG--------VAFQGSV----INL------MDIPFE--EEQVEDLQITMEPQNLAYVIYTSGSTGQPKG 433
Cdd:cd05933    88 NqkqlqkiLQIQDklphlkaiIQYKEPLkekePNLyswdefMELGRSipDEQLDAIISSQKPNQCCTLIYTSGTTGMPKG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  434 VMIEHRSLTNFLCAMyedfSQDIGITDN-VLFSSSISF------DVTIFEIFVPLVCGA--------------------- 485
Cdd:cd05933   168 VMLSHDNITWTAKAA----SQHMDLRPAtVGQESVVSYlplshiAAQILDIWLPIKVGGqvyfaqpdalkgtlvktlrev 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  486 RMTIYQG-----EKFDvPKLVQVI------------------LEEQVTL--AYIPPTLLNEIYDYFV--RANQKISLN-- 536
Cdd:cd05933   244 RPTAFMGvprvwEKIQ-EKMKAVGaksgtlkrkiaswakgvgLETNLKLmgGESPSPLFYRLAKKLVfkKVRKALGLDrc 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  537 -KLFVGVEPIKTELLakydHLFRG-NLQILNLYGPTEATVCCTSYQyerdkeitTQNVPIGS-----PLLNTKIYILDSf 609
Cdd:cd05933   323 qKFFTGAAPISRETL----EFFLSlNIPIMELYGMSETSGPHTISN--------PQAYRLLScgkalPGCKTKIHNPDA- 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  610 hrlqpIGVpGEICISGIGLARGYINRKELTADKFIDHPFERgeklykTGDIARWLPDGNIEYLGRV 675
Cdd:cd05933   390 -----DGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH------SGDLGKLDEDGFLYITGRI 443
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1356-1809 2.10e-10

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 65.98  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1356 LARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID----TDLPKQRVEY----ML-TDSGCS--------- 1417
Cdd:PLN02860   45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsFEEAKSAMLLvrpvMLvTDETCSswyeelqnd 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 -------HVLVHQNSIIKGIEFqgNVIDLMDMSFEEEPGE-DMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLC 1489
Cdd:PLN02860  125 rlpslmwQVFLESPSSSVFIFL--NSFLTTEMLKQRALGTtELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSL 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1490 AmyedfsqDIGI----TDNVLFSSS-------ISFDVTIF-----EIFVPliygarmtiyqgeKFDVTKLVQVILEEQVT 1553
Cdd:PLN02860  203 A-------KIAIvgygEDDVYLHTAplchiggLSSALAMLmvgacHVLLP-------------KFDAKAALQAIKQHNVT 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1554 LSYIPPTLLNEIYDY----FVRDNQKIVLnKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEAtvcCTSYRYesnke 1629
Cdd:PLN02860  263 SMITVPAMMADLISLtrksMTWKVFPSVR-KILNGGGSLSSRLLPDAKKLF-PNAKLFSAYGMTEA---CSSLTF----- 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ittqnVPIGSPLLNTKIYILDSFHRI--QPIGVPGEICIS--------GIGLAR----GYI-NRKELTADKFIDHPFERG 1694
Cdd:PLN02860  333 -----MTLHDPTLESPKQTLQTVNQTksSSVHQPQGVCVGkpaphvelKIGLDEssrvGRIlTRGPHVMLGYWGQNSETA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1695 EKLYK-----TGDIArWLPD-GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI------------------ 1750
Cdd:PLN02860  408 SVLSNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgvpdsrltemvvacvrlr 486
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1751 --------DQEDEAGEKYLCAyvvtekdipiPEVRAYLATK-LPHYMIPQQLI----PihnIPLTQNGKIDR 1809
Cdd:PLN02860  487 dgwiwsdnEKENAKKNLTLSS----------ETLRHHCREKnLSRFKIPKLFVqwrkP---FPLTTTGKIRR 545
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
289-769 2.26e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 65.42  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK13390   11 PDRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  367 MLTDSGCSHVLTyqNSIIKGVAFQGSVINLMDIPF--EEEQVEDLQITM--------EPQNLAYVIYTSGSTGQPKGVM- 435
Cdd:PRK13390   91 IVGDSGARVLVA--SAALDGLAAKVGADLPLRLSFggEIDGFGSFEAALagagprltEQPCGAVMLYSSGTTGFPKGIQp 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  436 -IEHRSLT---NFLCAMYEDFsqdIGITD-NVLFSSSISFDVTIFEiFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVT 510
Cdd:PRK13390  169 dLPGRDVDapgDPIVAIARAF---YDISEsDIYYSSAPIYHAAPLR-WCSMVHALGGTVVLAKRFDAQATLGHVERYRIT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  511 LAYIPPTLLNEI--YDYFVRANQKI-SLNKLFVGVEPIKTEL-LAKYDHLfrGNLqILNLYGPTEA---TVCCTSyqyer 583
Cdd:PRK13390  245 VTQMVPTMFVRLlkLDADVRTRYDVsSLRAVIHAAAPCPVDVkHAMIDWL--GPI-VYEYYSSTEAhgmTFIDSP----- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  584 dkEITTQNVPIGSPLLNTkIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAD-KFIDHPFergekLYKTGDIAR 662
Cdd:PRK13390  317 --DWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPF-----WTTVGDLGS 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLCAYVVTEKDIPIPEVRA----YL 737
Cdd:PRK13390  389 VDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpEMGEQVKAVIQLVEGIRGSDELARelidYT 468
                         490       500       510
                  ....*....|....*....|....*....|..
gi 446807313  738 ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13390  469 RSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
298-769 2.62e-10

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: 65.14  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  378 TYQNSIIKgvafqgsvinlmdipfeeEQVEDLQITMEPQN----LAYvIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF- 452
Cdd:cd05939    81 FNLLDPLL------------------TQSSTEPPSQDDVNfrdkLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFg 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  453 --SQDIGITDNVLFSSSISfdvtIFEIFVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLA-YIpptllNEIYDYFVRA 529
Cdd:cd05939   142 mrPEDVVYDCLPLYHSAGG----IMGVGQALLHG--STVVIRKKFSASNFWDDCVKYNCTIVqYI-----GEICRYLLAQ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  530 NQKISLNKLFV------GVEP-IKTELLAKYdhlfrGNLQILNLYGPTEatvcCTSYQYERDKEITTqnvpIG-SPLLNT 601
Cdd:cd05939   211 PPSEEEQKHNVrlavgnGLRPqIWEQFVRRF-----GIPQIGEFYGATE----GNSSLVNIDNHVGA----CGfNSRILP 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  602 KIY--------------ILDSFHRLQPIGvPGEiciSGIGLAR-----------GYINRKElTADKFIDHPFERGEKLYK 656
Cdd:cd05939   278 SVYpirlikvdedtgelIRDSDGLCIPCQ-PGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFL 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  657 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----QREDESGekyLCAYVVTEKDIPIP 731
Cdd:cd05939   353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgvevpGVEGRAG---MAAIVDPERKVDLD 429
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446807313  732 EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05939   430 RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1834-1891 2.80e-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: 2.80e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1834 LIDIWSSILGVNN--IGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQ 1891
Cdd:pfam00550    3 LRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1344-1785 4.70e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 64.45  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKResiVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK06334   46 LSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNVI----DLMDM-------SFEEEPGEDMHMMI--------------EPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:PRK06334  123 QLMQHLAQTHGEDAeypfSLIYMeevrkelSFWEKCRIGIYMSIpfewlmrwfgvsdkDPEDVAVILFTSGTEKLPKGVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1479 IEHRSLTNFLCAMYEDFSQdigITDNVLFSSSISFDVTIFE--IFVPLIYGARMtIYQGEKFDVTKLVQVILEEQVTLSY 1556
Cdd:PRK06334  203 LTHANLLANQRACLKFFSP---KEDDVMMSFLPPFHAYGFNscTLFPLLSGVPV-VFAYNPLYPKKIVEMIDEAKVTFLG 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRgNLQILNGYGPTEATVCCTsyryesnkeITTQNV 1635
Cdd:PRK06334  279 STPVFFDYILKTAKKQESCLpSLRFVVIGGDAFKDSLYQEALKTFP-HIQLRQGYGTTECSPVIT---------INTVNS 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 P-----IGSPLLNTKIYIL-DSFHRIQPIGVPGEICISGIGLARGYINRKEltadkfiDHPFER--GEKLYKTGDIARWL 1707
Cdd:PRK06334  349 PkhescVGMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLGEDF-------GQGFVElgGETWYVTGDLGYVD 421
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETiktavvIDQEDEAGEKYLCAyvvtekdIPIPEVRAYLATKLP 1785
Cdd:PRK06334  422 RHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFG------QNAADHAGPLVVCG-------LPGEKVRLCLFTTFP 486
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
420-769 6.43e-10

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: 63.94  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  420 YVIYTSGSTGQPKGVM--IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSsisfdvtifeifVPLVCGA-----RMTIYQG 492
Cdd:cd05929   129 KMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGA--DSVYLSP------------APLYHAApfrwsMTALFMG 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 ------EKFDVPKLVQVILEEQVTLAYIPPTLLNEI----------YDYfvranqkISLNKLFVGVEPIKTELLAKYDHL 556
Cdd:cd05929   195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFVRLlklpeavrnaYDL-------SSLKRVIHAAAPCPPWVKEQWIDW 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  557 frGNLQILNLYGPTEAT--VCCTSYQYerdkeiTTQNVPIGSPLLNtKIYILDSFHRLQPIGVPGEICISGiGLARGYIN 634
Cdd:cd05929   268 --GGPIIWEYYGGTEGQglTIINGEEW------LTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTN 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  635 RKELTADKFIDHPFErgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESG 714
Cdd:cd05929   338 DPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  715 EKYLCAYVVTEKD-----IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05929   412 GQRVHAVVQPAPGadagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1346-1812 7.84e-10

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 63.95  E-value: 7.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1346 YNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQNS 1425
Cdd:PRK12406   14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG-ARVLIAHAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1426 IIKGIEfqGNVIDLMDMSFEEEPGE--------DMHMMIEPHNLAY--------------------VIYTSGSTGQPKGV 1477
Cdd:PRK12406   93 LLHGLA--SALPAGVTVLSVPTPPEiaaayrisPALLTPPAGAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHPKGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 miEHRSLTNFLCAMYEDFSQDI-GITDNV-------LFSSSisfdvtifeifvPLIYGaRMTIYQGE------KFDVTKL 1543
Cdd:PRK12406  171 --RRAAPTPEQAAAAEQMRALIyGLKPGIralltgpLYHSA------------PNAYG-LRAGRLGGvlvlqpRFDPEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1544 VQVILEEQVTLSYIPPTLlneiydyFVRdnqkivLNKLlvgvepiKTELLAKYD-----HLFRGNLQ------------- 1605
Cdd:PRK12406  236 LQLIERHRITHMHMVPTM-------FIR------LLKL-------PEEVRAKYDvsslrHVIHAAAPcpadvkramieww 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ---ILNGYGPTE--ATVCCTSYRYeSNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLAR-GYINRK 1679
Cdd:PRK12406  296 gpvIYEYYGSTEsgAVTFATSEDA-LSHPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 ELTADkfidhpFERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGE 1758
Cdd:PRK12406  370 EKRAE------IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDaEFGE 442
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1759 KyLCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12406  443 A-LMAVVEPQPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1405-1738 7.88e-10

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 64.37  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGCSHVLVHQNSIIKGIEFqgnvidlmdmSFEEEPGEDMHM---MIEPHNLAYVIYTSGSTGQPKGVMIEH 1481
Cdd:PLN02387  203 KRVIYMDDEGVDSDSSLSGSSNWTVSSF----------SEVEKLGKENPVdpdLPSPNDIAVIMYTSGSTGLPKGVMMTH 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1482 RSLTNFLCAMYEDFSqDIGITD---------NVLfssSISFDVTIFEIFVPLIYGARMT-------IYQGEKFDVTKLvq 1545
Cdd:PLN02387  273 GNIVATVAGVMTVVP-KLGKNDvylaylplaHIL---ELAAESVMAAVGAAIGYGSPLTltdtsnkIKKGTKGDASAL-- 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 vileeQVTLSYIPPTLLNEIYDYfVRD--NQKIVLNKLLV-------------------GVEPIKTELLA--KYDHLFRG 1602
Cdd:PLN02387  347 -----KPTLMTAVPAILDRVRDG-VRKkvDAKGGLAKKLFdiaykrrlaaiegswfgawGLEKLLWDALVfkKIRAVLGG 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1603 NLQ------------------------ILNGYGPTEAtvcCTSYRYESNKEITTQNVpiGSPLLNTKIYILD---SFHRI 1655
Cdd:PLN02387  421 RIRfmlsggaplsgdtqrfiniclgapIGQGYGLTET---CAGATFSEWDDTSVGRV--GPPLPCCYVKLVSweeGGYLI 495
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1656 QPIGVP-GEICISGIGLARGYINRKELTADKF-IDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELG 1732
Cdd:PLN02387  496 SDKPMPrGEIVIGGPSVTLGYFKNQEKTDEVYkVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLG 572

                  ....*.
gi 446807313 1733 EIEASL 1738
Cdd:PLN02387  573 KVEAAL 578
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1323-1812 8.77e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 63.56  E-value: 8.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQ-VKRNPNQIAVVCNEKG--ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK13391    1 MYPGIhAQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSG--------------------CSHV----LVHQNSIIKGIE-FQGNVIDLMDMSFEEEP-GEDMh 1453
Cdd:PRK13391   81 SHLTPAEAAYIVDDSGaralitsaakldvarallkqCPGVrhrlVLDGDGELEGFVgYAEAVAGLPATPIADESlGTDM- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1454 mmiephnlayvIYTSGSTGQPKGVM--------IEHRSLTNFLCAMYedfsqdiGITDNVLFSSSISFDVTIFEIFVPLI 1525
Cdd:PRK13391  160 -----------LYSSGTTGRPKGIKrplpeqppDTPLPLTAFLQRLW-------GFRSDMVYLSPAPLYHSAPQRAVMLV 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1526 YGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLlneiydyFVR-------DNQKIVLNKLLVGVEP-------IKTE 1591
Cdd:PRK13391  222 IRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTM-------FSRmlklpeeVRDKYDLSSLEVAIHAaapcppqVKEQ 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1592 LLAKYDHLfrgnlqILNGYGPTEA--TVCCTSYRYESNKEittqnvPIGSPLLNtKIYILDSFHRIQPIGVPGEICISGi 1669
Cdd:PRK13391  295 MIDWWGPI------IHEYYAATEGlgFTACDSEEWLAHPG------TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG- 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1670 GLARGYINRKELTADKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 1749
Cdd:PRK13391  361 GRPFEYLNDPAKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAV 435
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1750 ID-QEDEAGEKylCAYVVTEKDIPIP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK13391  436 FGvPNEDLGEE--VKAVVQPVDGVDPgpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
265-697 9.10e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 63.68  E-value: 9.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  265 RVHKTLLC-------ETVTAPQLFEEQVkqnpnqiaivcnGKeITYKQLNIKANQLARRLLDQGVKRefiVGVMMERSIE 337
Cdd:PRK06334   16 RSGKTVLEsflklcsEMTTATVCWDEQL------------GK-LSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  338 MIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIK-------GVAFQGSVINLMDIPFEEEQVEDLQ 410
Cdd:PRK06334   80 AYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqthgeDAEYPFSLIYMEEVRKELSFWEKCR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  411 ITM------------------EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQdigITDNVLFSSSISFDV 472
Cdd:PRK06334  160 IGIymsipfewlmrwfgvsdkDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSP---KEDDVMMSFLPPFHA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  473 TIFE--IFVPLVCGARMtIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiyDYFVRANQKI-----SLNKLFVGVEPI 545
Cdd:PRK06334  237 YGFNscTLFPLLSGVPV-VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFF----DYILKTAKKQesclpSLRFVVIGGDAF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  546 KTELLAKYDHLFRgNLQILNLYGPTEATVCCTsyqyerdkeITTQNVP-----IGSPLLNTKIYIL-DSFHRLQPIGVPG 619
Cdd:PRK06334  312 KDSLYQEALKTFP-HIQLRQGYGTTECSPVIT---------INTVNSPkhescVGMPIRGMDVLIVsEETKVPVSSGETG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  620 EICISGIGLARGYINRKEltadkfiDHPFER--GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK 697
Cdd:PRK06334  382 LVLTRGTSLFSGYLGEDF-------GQGFVElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
690-763 9.64e-10

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


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 56.78  E-value: 9.64e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313   690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGK 763
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
20-238 1.01e-09

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: 62.99  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   20 KEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVI 99
Cdd:cd19543   188 EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVF 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  100 GM-----PVFKQGQEETV--FQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGEsnnlpLLN 172
Cdd:cd19543   268 GTtvsgrPAELPGIETMVglFINT-LPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLYEIQAWSEGKQA-----LFD 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  173 TIVMLDD--IHCYESTDKINSDMVIRFMKNEEQ--------------LKVQVDYNSTLYSEGLVSRIVNHLYNILDILMK 236
Cdd:cd19543   342 HLLVFENypVDESLEEEQDEDGLRITDVSAEEQtnypltvvaipgeeLTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421

                  ..
gi 446807313  237 DP 238
Cdd:cd19543   422 NP 423
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1344-1812 2.07e-09

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 62.49  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSG-----CS 1417
Cdd:PRK05620   39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEdevivAD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQ-NSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMM--------------------IEPHNLAYVIYTSGSTGQPKG 1476
Cdd:PRK05620  119 PRLAEQlGEILKECPCVRAVVFIGPSDADSAAAHMPEGIkvysyealldgrstvydwpeLDETTAAAICYSTGTTGAPKG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1477 VMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIF---VPLiyGARMT----IYQGEKFDVTKLVQVILE 1549
Cdd:PRK05620  199 VVYSHRSL--YLQSLSLRTTDSLAVTHGESFLCC----VPIYHVLswgVPL--AAFMSgtplVFPGPDLSAPTLAKIIAT 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1550 EQVTLSYIPPTLLNEIYDYFVRDN-QKIVLNKLLVGVEPIKTELLAKYDHlfRGNLQILNGYGPTEATVCCTSYRYES-- 1626
Cdd:PRK05620  271 AMPRVAHGVPTLWIQLMVHYLKNPpERMSLQEIYVGGSAVPPILIKAWEE--RYGVDVVHVWGMTETSPVGTVARPPSgv 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 ------NKEITTQNVPIGsplLNTKI----YILDSFHRIQpigvpGEICISGIGLARGYIN----RKELTADKFIDHPFE 1692
Cdd:PRK05620  349 sgearwAYRVSQGRFPAS---LEYRIvndgQVMESTDRNE-----GEIQVRGNWVTASYYHspteEGGGAASTFRGEDVE 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 RGEKLY------KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYV 1765
Cdd:PRK05620  421 DANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVTV 500
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1766 VTEKDIPIPE----VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK05620  501 LAPGIEPTREtaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1444-1805 2.48e-09

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: 62.47  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1444 FEEEPGEDmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNF--LCAMYEDFSQDIGITDN-----------VLF--- 1507
Cdd:cd17632   216 FRPEPDDD--------PLALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQDIRPPASITLNfmpmshiagriSLYgtl 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1508 ----------SSSISfdvTIFE----------IFVPLIYGARMTIYQGE--KFDVTKLVQVILEEQVTLSyipptllnei 1565
Cdd:cd17632   288 arggtayfaaASDMS---TLFDdlalvrptelFLVPRVCDMLFQRYQAEldRRSVAGADAETLAERVKAE---------- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1566 ydyfVRDNqkiVLNKLL----VGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVcctsyryesnkeITTQNVPIGSPL 1641
Cdd:cd17632   355 ----LRER---VLGGRLlaavCGSAPLSAEMKAFMESLL--DLDLHDGYGSTEAGA------------VILDGVIVRPPV 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1642 LNTKI-------YIL-DSFHriqpigvP-GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDI-ARWLPDgN 1711
Cdd:cd17632   414 LDYKLvdvpelgYFRtDRPH-------PrGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD-R 479
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIDQEDEAgekYLCAYVVTEKD----IPIPEVRAYLATKLPH 1786
Cdd:cd17632   480 LVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGNSERA---YLLAVVVPTQDalagEDTARLRAALAESLQR 556
                         410       420
                  ....*....|....*....|....*....
gi 446807313 1787 ---------YMIPQQLIpIHNIPLTQ-NG 1805
Cdd:cd17632   557 iareaglqsYEIPRDFL-IETEPFTIaNG 584
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
7-238 2.84e-09

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: 61.66  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd19066   177 LEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFAL 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   87 LLSRYTDKDDVVIGMPVFKQ---GQEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS-- 160
Cdd:cd19066   257 ALKRLTASIDVVIGLTFLNRpdeAVEDTIgLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGvv 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  161 ------------LDGESNNLPLLNTIVMLDDIHCYESTDKINSDMVIRFMKNEE-QLKVQVDYNSTLYSEGLVSRIVNHL 227
Cdd:cd19066   337 peapkhplfepvFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDgDLLLRLEYSRGVYDERTIDRFAERY 416
                         250
                  ....*....|.
gi 446807313  228 YNILDILMKDP 238
Cdd:cd19066   417 MTALRQLIENP 427
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1462-1815 4.20e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 60.83  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYedfsQDIGITDNVLFSSSiSFDVTIFEIFV-PLIYGARMTIYQ-GEKFD 1539
Cdd:PRK07824   38 ALVVATSGTTGTPKGAMLTAAALTASADATH----DRLGGPGQWLLALP-AHHIAGLQVLVrSVIAGSEPVELDvSAGFD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1540 VTKLVQVILE---EQVTLSYIPPTLLNEIYDyfvrdnqkivlnkllvgvePIKTELLAKYDhlfrgnlQILNGYGPTEAT 1616
Cdd:PRK07824  113 PTALPRAVAElggGRRYTSLVPMQLAKALDD-------------------PAATAALAELD-------AVLVGGGPAPAP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 VcctsyrYESNKE-----ITTQN--------VPIGSPLLNTKIYILDsfhriqpigvpGEICISGIGLARGYINrkelta 1683
Cdd:PRK07824  167 V------LDAAAAaginvVRTYGmsetsggcVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRN------ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1684 dkFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLC 1762
Cdd:PRK07824  224 --PVDPDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVA 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1763 AYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07824  301 AVVGDGGPAPTLeALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
13-238 5.37e-09

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: 60.85  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   13 SEKFKKEKEYWLDKLSGDVE---LSRfPCDCLSLNNIQASKEsyycqFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLS 89
Cdd:cd19533   182 SERFERDRAFWTEQFEDLPEpvsLAR-RAPGRSLAFLRRTAE-----LPPELTRTLLEAAEAHGASWPSFFIALVAAYLH 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   90 RYTDKDDVVIGMPVFKQG----QEETVFQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGES 165
Cdd:cd19533   256 RLTGANDVVLGVPVMGRLgaaaRQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGEL 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  166 NNL--PLLNTIVM---LDDIHCYESTDKINS----DMVIRFMK--NEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDIL 234
Cdd:cd19533   336 HPLfgPTVNYMPFdygLDFGGVVGLTHNLSSgptnDLSIFVYDrdDESGLRIDFDANPALYSGEDLARHQERLLRLLEEA 415

                  ....
gi 446807313  235 MKDP 238
Cdd:cd19533   416 AADP 419
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
415-762 6.05e-09

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: 61.32  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNF--LCAMYEDFSQDIGITDN-----------VLF-------------SSSI 468
Cdd:cd17632   222 DDPLALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQDIRPPASITLNfmpmshiagriSLYgtlarggtayfaaASDM 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  469 SfdvTIFE----------IFVPLVCGARMTIYQGE--KFDVPKLVQVILEEQVTlAYIPPTLLNEiydyfvranqkiSLN 536
Cdd:cd17632   302 S---TLFDdlalvrptelFLVPRVCDMLFQRYQAEldRRSVAGADAETLAERVK-AELRERVLGG------------RLL 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  537 KLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVcctsyqyerdkeITTQNVPIGSPLLNTKI-------YIL-DS 608
Cdd:cd17632   366 AAVCGSAPLSAEMKAFMESLL--DLDLHDGYGSTEAGA------------VILDGVIVRPPVLDYKLvdvpelgYFRtDR 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  609 FHrlqpigvP-GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDI-ARWLPDgNIEYLGRVDHQVKI-RGYR 685
Cdd:cd17632   432 PH-------PrGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD-RLVYVDRRNNVLKLsQGEF 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  686 IELGEIEASLLKYETIKTAVViqrEDESGEKYLCAYVVTEKD----IPIPEVRAYLATKLPY---------YMIPQQIIs 752
Cdd:cd17632   498 VTVARLEAVFAASPLVRQIFV---YGNSERAYLLAVVVPTQDalagEDTARLRAALAESLQRiareaglqsYEIPRDFL- 573
                         410
                  ....*....|.
gi 446807313  753 IQNIPLTQ-NG 762
Cdd:cd17632   574 IETEPFTIaNG 584
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1662-1815 1.00e-08

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 60.01  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYInrkeltaDKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:PRK07445  302 GNITIQAQSLALGYY-------PQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1742 ETIKTAVVIDQED-EAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07445  370 GLVQDVCVLGLPDpHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
1921-2007 1.35e-08

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 57.55  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQsigYD--DSRF---PNLSVEEMAVRYIEEIKQvKKEGPYTLLGWSFGGIV 1995
Cdd:COG3208    10 FCFPYAGGSASAYRPWAAALPPDIEVLAVQ---LPgrGDRLgepPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALL 85
                          90
                  ....*....|..
gi 446807313 1996 AFEMARKLEELG 2007
Cdd:COG3208    86 AFELARRLERRG 97
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
7-238 1.39e-08

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: 59.59  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    7 QQVLLSSEK-----FKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILL 81
Cdd:cd19538   174 QQELLGDESdpdslIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQ 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   82 SGVKYLLSRYTDKDDVVIGMPVFKQGQEETV-----FQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLT 156
Cdd:cd19538   254 AGFAALLTRLGAGTDIPIGSPVAGRNDDSLEdlvgfFVNT-LVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLV 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  157 QLLSLDGESNNLPLLNtiVMLD---------DIHCYESTDKINS------DMVI-----RFMKNEEQLKVQVDYNSTLYS 216
Cdd:cd19538   333 EALNPTRSRSRHPLFQ--IMLAlqntpqpslDLPGLEAKLELRTvgsakfDLTFelreqYNDGTPNGIEGFIEYRTDLFD 410
                         250       260
                  ....*....|....*....|..
gi 446807313  217 EGLVSRIVNHLYNILDILMKDP 238
Cdd:cd19538   411 HETIEALAQRYLLLLESAVENP 432
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
895-1155 1.90e-08

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


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 58.99  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  895 TYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF---------QIldgelVQKiepNVDFNIEYVHVNEKD--ADYL 963
Cdd:cd19544    23 PYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAIlweglsepvQV-----VWR---QAELPVEELTLDPGDdaLAQL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  964 IHEFIS---PFDLSKppllrvlllRIAEE----RHILVVDMHHIISDGLSMGILIKEfVELY---KGNELPKLrVQYKDY 1033
Cdd:cd19544    95 RARFDPrryRLDLRQapl---lraHVAEDpangRWLLLLLFHHLISDHTSLELLLEE-IQAIlagRAAALPPP-VPYRNF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1034 VM--WQNGPyyknlISEQKNYWLTTLKgelpvlnfptDFQRPT----IQSFKGNVCSFN-----LGTDLTFKVNKLATET 1102
Cdd:cd19544   170 VAqaRLGAS-----QAEHEAFFREMLG----------DVDEPTapfgLLDVQGDGSDITearlaLDAELAQRLRAQARRL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1103 GTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMR 1155
Cdd:cd19544   235 GVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLR 289
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1441-1812 2.11e-08

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: 59.31  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1441 DMSFEEEPGEDMHMMIEPH-NLAYVIYTSGSTGQPKGVM--IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSsisfdvti 1517
Cdd:cd05929   106 LEDYEAAEGGSPETPIEDEaAGWKMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGA--DSVYLSP-------- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 feifVPLIYGA-----RMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYF--VRDNQKIVLNKLLVG 1584
Cdd:cd05929   176 ----APLYHAApfrwsMTALFMGgtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPeaVRNAYDLSSLKRVIH 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 V-EPIKTELLAKYDHLfrGNLQILNGYGPTEAT--VCCTSyryesnKEITTQNVPIGSPLLNtKIYILDSFHRIQPIGVP 1661
Cdd:cd05929   252 AaAPCPPWVKEQWIDW--GGPIIWEYYGGTEGQglTIING------EEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEI 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGiGLARGYINRKELTADKFIDHPFErgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:cd05929   323 GEVYFAN-GPGFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1742 ETIKTAVVIDQED-EAGEKyLCAYVVTEKD-----IPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05929   396 PKVLDAAVVGVPDeELGQR-VHAVVQPAPGadagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1733-1806 2.14e-08

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: 52.93  E-value: 2.14e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313  1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
284-769 3.23e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 59.00  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  284 QVKQNPNQIAIVCNG------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILG------------- 344
Cdd:PRK00174   76 HLKTRGDKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsvvfg 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  345 ----------ILKA-------------GGAYLPIdtelpKQRVEYMLTDSGC-SHVLTYQNSIIKgVAFQGSvinlMDIP 400
Cdd:PRK00174  156 gfsaealadrIIDAgaklvitadegvrGGKPIPL-----KANVDEALANCPSvEKVIVVRRTGGD-VDWVEG----RDLW 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  401 FEEE-QVEDLQITMEPQN----LaYVIYTSGSTGQPKGVM------IEHRSLTN-----------FLCamyedfSQDIG- 457
Cdd:PRK00174  226 WHELvAGASDECEPEPMDaedpL-FILYTSGSTGKPKGVLhttggyLVYAAMTMkyvfdykdgdvYWC------TADVGw 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 ITDNvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPTL---LNEIYDYFVR 528
Cdd:PRK00174  299 VTGH----SYI--------VYGPLANGATTLMFEG----VPnypdpgRFWEVIDKHKVTIFYTAPTAiraLMKEGDEHPK 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  529 ANQKISLNKL-FVGvEPIKTEllA---KYDHLFRGNLQILNLYGPTE--ATVcctsyqyerdkeIT-----TQNVPiGS- 596
Cdd:PRK00174  363 KYDLSSLRLLgSVG-EPINPE--AwewYYKVVGGERCPIVDTWWQTEtgGIM------------ITplpgaTPLKP-GSa 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  597 --PLLNTKIYILDSFHRLQPIGVPGEICI--SGIGLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:PRK00174  427 trPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWIT 502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIP-----IPEVRAYLATKLPYYMI 746
Cdd:PRK00174  503 GRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDiKGQG-IYAFVTLKGGEEpsdelRKELRNWVRKEIGPIAK 581
                         570       580
                  ....*....|....*....|...
gi 446807313  747 PQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK00174  582 PDVIQFAPGLPKTRSGKIMRRIL 604
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
595-769 3.73e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 57.75  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  595 GSPLLNTKIYILDsfhrlqpigvpGEICISGIGLARGYINrkeltadkFIDHPFERGEKLYKTGDIARwLPDGNIEYLGR 674
Cdd:PRK07824  195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRN--------PVDPDPFAEPGWFRTDDLGA-LDDGVLTVLGR 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  675 VDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIIS 752
Cdd:PRK07824  255 ADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVVGDGGPAPTLeALRAHVARTLDRTAAPRELHV 334
                         170
                  ....*....|....*..
gi 446807313  753 IQNIPLTQNGKIDRKKL 769
Cdd:PRK07824  335 VDELPRRGIGKVDRRAL 351
PRK05850 PRK05850
acyl-CoA synthetase; Validated
278-484 4.15e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 58.42  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  278 PQLFEEQVKQNPNQIAIVCNGKE---------ITYKQLNIKANQLARRLLDQGVKREFIVgVMMERSIEMIVGILGILKA 348
Cdd:PRK05850    4 PSLLRERASLQPDDAAFTFIDYEqdpagvaetLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  349 GGAYLPIDTELPKQ---RVEYMLTDSGCSHVLTyQNSIIKGV-----AFQGSV------INLMDIPFEEEQVEDLQitmE 414
Cdd:PRK05850   83 GLIAVPLSVPQGGAhdeRVSAVLRDTSPSVVLT-TSAVVDDVteyvaPQPGQSappvieVDLLDLDSPRGSDARPR---D 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRSLT-NFLCAMYEDFsqdiGITDNV--LFSSSISF-----DV-TIFEIFVPLVCG 484
Cdd:PRK05850  159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMSDYF----GDTGGVppPDTTVVSWlpfyhDMgLVLGVCAPILGG 233
PLN02479 PLN02479
acetate-CoA ligase
423-769 5.79e-08

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 57.93  E-value: 5.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  423 YTSGSTGQPKGVMIEHR-----SLTNFLCamyedFSQDIGI----TDNVLFSSSISFDVTIFEIFVPLVCGARMT---IY 490
Cdd:PLN02479  202 YTSGTTASPKGVVLHHRgaylmALSNALI-----WGMNEGAvylwTLPMFHCNGWCFTWTLAALCGTNICLRQVTakaIY 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  491 QGekfdvpklvqvILEEQVTLAYIPPTLLNEIYDyfVRANQKI-----SLNKLFVGVEPIKTELLAKYDHLFRgnlqILN 565
Cdd:PLN02479  277 SA-----------IANYGVTHFCAAPVVLNTIVN--APKSETIlplprVVHVMTAGAAPPPSVLFAMSEKGFR----VTH 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  566 LYGPTE----ATVCctSYQYERDKEittqnVPIGSPLLNTKI---YI----LDSFHRLQPIGVP------GEICISGIGL 628
Cdd:PLN02479  340 TYGLSEtygpSTVC--AWKPEWDSL-----PPEEQARLNARQgvrYIglegLDVVDTKTMKPVPadgktmGEIVMRGNMV 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  629 ARGYINRKELTADKFidhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ 708
Cdd:PLN02479  413 MKGYLKNPKANEEAF-----ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313  709 REDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIIsIQNIPLTQNGKIDRKKL 769
Cdd:PLN02479  486 RPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVL 552
PLN02654 PLN02654
acetate-CoA ligase
288-769 7.38e-08

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 57.60  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  288 NPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PLN02654  102 NGDKIAIYWEGNEpgfdasLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  362 QRVEYMLTDSGCSHVLTyQNSIIKGVafqgSVINLMDI------PFEEEQVE-DLQITMEPQNLA--------------- 419
Cdd:PLN02654  182 ESLAQRIVDCKPKVVIT-CNAVKRGP----KTINLKDIvdaaldESAKNGVSvGICLTYENQLAMkredtkwqegrdvww 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  420 ----------------------YVIYTSGSTGQPKGVMieHR-------SLTNFLCAMYEDFSQDIGITDNVLFSSSISF 470
Cdd:PLN02654  257 qdvvpnyptkcevewvdaedplFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTDVYWCTADCGWITGHSY 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  471 dVTifeiFVPLVCGARMTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPI 545
Cdd:PLN02654  335 -VT----YGPMLNGATVLVFEGAPNypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPI 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  546 KTELLAKYdhlfrgnlqiLNLYGPTEATVCCTSYQYERDKEITTqnvPI--------GS---PLLNTKIYILDSFHRLQP 614
Cdd:PLN02654  410 NPSAWRWF----------FNVVGDSRCPISDTWWQTETGGFMIT---PLpgawpqkpGSatfPFFGVQPVIVDEKGKEIE 476
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  615 IGVPGEICI--SGIGLAR---GYINRKELTADKfidhPFErgeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:PLN02654  477 GECSGYLCVkkSWPGAFRtlyGDHERYETTYFK----PFA---GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTA 549
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP-EVRAYLA----TKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:PLN02654  550 EVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKI 629

                  ....*
gi 446807313  765 DRKKL 769
Cdd:PLN02654  630 MRRIL 634
PRK08162 PRK08162
acyl-CoA synthetase; Validated
289-764 9.47e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 57.26  E-value: 9.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  369 tDSGCSHVL----TYQNSIIKGVA-FQGSVINLMDI---------PFEEEQVEDLQITMEPqNLAYVI-----------Y 423
Cdd:PRK08162  112 -RHGEAKVLivdtEFAEVAREALAlLPGPKPLVIDVddpeypggrFIGALDYEAFLASGDP-DFAWTLpadewdaialnY 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  424 TSGSTGQPKGVMIEHRSltNFLCAMyedfsqdigitdnvlfSSSISFDVTIFEIF---VPLV-CGA-----RMTIYQG-- 492
Cdd:PRK08162  190 TSGTTGNPKGVVYHHRG--AYLNAL----------------SNILAWGMPKHPVYlwtLPMFhCNGwcfpwTVAARAGtn 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 ---EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQKISLN---KLFVGVEPIKTELLAKYDHLfrgNLQILNL 566
Cdd:PRK08162  252 vclRKVDPKLIFDLIREHGVTHYCGAPIVLSALIN--APAEWRAGIDhpvHAMVAGAAPPAAVIAKMEEI---GFDLTHV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  567 YGPTE----ATVCCTSYQY------ERDKEITTQNVPIgsPLLNTkIYILDSfHRLQPigVP------GEICISGIGLAR 630
Cdd:PRK08162  327 YGLTEtygpATVCAWQPEWdalpldERAQLKARQGVRY--PLQEG-VTVLDP-DTMQP--VPadgetiGEIMFRGNIVMK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  631 GYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIeylgrvdhQVKIR--------GYRIELGEIEASLLKYETIK 702
Cdd:PRK08162  401 GYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVL 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313  703 TAVVIQREDESGEKYLCAYV-------VTEKDIpIPEVRAYLATklpyYMIPQQIIsIQNIPLTQNGKI 764
Cdd:PRK08162  466 VAAVVAKPDPKWGEVPCAFVelkdgasATEEEI-IAHCREHLAG----FKVPKAVV-FGELPKTSTGKI 528
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
619-771 1.29e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 56.54  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  619 GEICISGIGLARGYInrkeltaDKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK07445  302 GNITIQAQSLALGYY-------PQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313  699 ETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK07445  370 GLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5-237 1.51e-07

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: 56.11  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313    5 FT--QQVLLSSEKFKKEKEYWLDKLSGDVELS---------RFPCDCLSLNNIQASkesyycqFPSDIAKRAVAISNNSD 73
Cdd:cd20483   174 FTlwHNALLQSPLVQPLLDFWKEKLEGIPDASkllpfakaeRPPVKDYERSTVEAT-------LDKELLARMKRICAQHA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   74 MLLYTILLSGVKYLLSRYTDKDDVVIGM-------PVFkqgqEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESN 145
Cdd:cd20483   247 VTPFMFLLAAFRAFLYRYTEDEDLTIGMvdgdrphPDF----DDLVgFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAY 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  146 EHCHFPFNKLTQLLSLDGESNNLPLLNTIV-------MLD------DIHCYESTD-KINSDMVIRFMKNEE-QLKVQVDY 210
Cdd:cd20483   323 EHSAVPFDYIVDALDVPRSTSHFPIGQIAVnyqvhgkFPEydtgdfKFTDYDHYDiPTACDIALEAEEDPDgGLDLRLEF 402
                         250       260
                  ....*....|....*....|....*..
gi 446807313  211 NSTLYSEGLVSRIVNHLYNILDILMKD 237
Cdd:cd20483   403 STTLYDSADMERFLDNFVTFLTSVIRD 429
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1463-1834 1.60e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 56.67  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDNVLFSSS----ISFDVTIFEIfvpLIYGARMTIYQGekf 1538
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFSHSsigwVSFHGFLYGS---LSLGNTFVMFEG--- 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTK-------LVQVILEEQVTLSYIPPTLLNeiydYFVRD--NQKIV--------LNKLLVGVEPIKtELLAKYdhlFR 1601
Cdd:PTZ00237  330 GIIKnkhieddLWNTIEKHKVTHTLTLPKTIR----YLIKTdpEATIIrskydlsnLKEIWCGGEVIE-ESIPEY---IE 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 GNLQI--LNGYGPTEaTVCCTSYRYES-NKEITTQNVPigSPLLNTKIYILDSfhRIQPIGVPGEICIS---GIGLARGY 1675
Cdd:PTZ00237  402 NKLKIksSRGYGQTE-IGITYLYCYGHiNIPYNATGVP--SIFIKPSILSEDG--KELNVNEIGEVAFKlpmPPSFATTF 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PTZ00237  477 YKNDEKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1756 AGEKYLCAYVVTEKDIPIP---------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLntLGNSNYVPP 1826
Cdd:PTZ00237  552 DCYNVPIGLLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKF--LNDSNYQLP 629

                  ....*...
gi 446807313 1827 RNEIDSSL 1834
Cdd:PTZ00237  630 DNVNDSEI 637
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
414-681 1.66e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 56.75  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDIGITDNVLFS----SSIsFDVTIFEIFvpLVCGARM 487
Cdd:PLN02430  218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlFMEQFEDKMTHDDVYLSflplAHI-LDRMIEEYF--FRKGASV 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  488 TIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELL---AKYDH--------- 555
Cdd:PLN02430  295 GYYHG---DLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAwmnRGYSHkkaspmadf 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  556 -LFR-------GNLQILNLYG---PTE------ATVCC---TSYQYERDKEITTQNVP--------IGSPLLNTKIyild 607
Cdd:PLN02430  372 lAFRkvkaklgGRLRLLISGGaplSTEieeflrVTSCAfvvQGYGLTETLGPTTLGFPdemcmlgtVGAPAVYNEL---- 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  608 sfhRLQ--------PIGVP--GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDH 677
Cdd:PLN02430  448 ---RLEevpemgydPLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKN 517

                  ....
gi 446807313  678 QVKI 681
Cdd:PLN02430  518 LIKL 521
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
410-765 1.99e-07

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 56.26  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSI----SFDVTIfEIFVPLVCGA 485
Cdd:PRK08043  359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALplfhSFGLTV-GLFTPLLTGA 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  486 RMTIYQG--EKFDVPKLVqviLEEQVTLAYIPPTLLNEI------YD-----YFVRANQKISlnklfvgvEPIKTELLAK 552
Cdd:PRK08043  434 EVFLYPSplHYRIVPELV---YDRNCTVLFGTSTFLGNYarfanpYDfarlrYVVAGAEKLQ--------ESTKQLWQDK 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  553 YdhlfrgNLQILNLYGPTEatvcCTSyqyerdkeITTQNVPIGspllnTKIYildSFHRLQP------IGVPG-----EI 621
Cdd:PRK08043  503 F------GLRILEGYGVTE----CAP--------VVSINVPMA-----AKPG---TVGRILPgmdarlLSVPGieqggRL 556
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  622 CISGIGLARGYI---NRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK08043  557 QLKGPNIMNGYLrveKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGV 636
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313  699 ETIKTAVVIQREDES-GEkylcAYVV--TEKDIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK08043  637 SPDKQHATAIKSDASkGE----ALVLftTDSELTREKLQQYArEHGVPELAVPRDIRYLKQLPLLGSGKPD 703
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
1922-2154 2.59e-07

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 54.05  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1922 IIHGQGGGILNYYDLARELGED-KTVYGLQSIGYDDSRFP----NLSVEEMAvRYIEEIKQVKKEGPYTLLGWSFGGIVA 1996
Cdd:pfam00561    5 LLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqdDYRTDDLA-EDLEYILEALGLEKVNLVGHSMGGLIA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1997 FEMARKLEELGDKVSFLG-LLDVHPIEQGREILSLNIKNAFEE--LEKFNDQLGIeKISFEQMSEEQLIESLLKKFTLNE 2073
Cdd:pfam00561   84 LAYAAKYPDRVKALVLLGaLDPPHELDEADRFILALFPGFFDGfvADFAPNPLGR-LVAKLLALLLLRLRLLKALPLLNK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  2074 NSCQQNFEDPMMNKL--KVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNEYTSGEVYALQVPGSHLSML 2151
Cdd:pfam00561  163 RFPSGDYALAKSLVTgaLLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242

                   ...
gi 446807313  2152 EKP 2154
Cdd:pfam00561  243 EGP 245
PLN02479 PLN02479
acetate-CoA ligase
1662-1812 3.07e-07

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 55.62  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYINRKELTADKFidhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:PLN02479  403 GEIVMRGNMVMKGYLKNPKANEEAF-----ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTH 475
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1742 ETIKTAVVIDQEDEAGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIpIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02479  476 PAVLEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVL 552
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
300-489 3.20e-07

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 55.52  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLlDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELP--KQRVEYMLTDSGCSHV 376
Cdd:PRK12476   68 ELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTYQ------NSIIKGV--AFQGSVINLMDIPfeEEQVEDLQ-ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNFLC 446
Cdd:PRK12476  147 LTTTaaaeavEGFLRNLprLRRPRVIAIDAIP--DSAGESFVpVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQ 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 446807313  447 AMYEdfsqdIGITDNVLFSSS---ISFDVTIFEIFVPLVCGARMTI 489
Cdd:PRK12476  225 MILS-----IDLLDRNTHGVSwlpLYHDMGLSMIGFPAVYGGHSTL 265
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
1457-1724 3.60e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 55.59  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDIGITDNVLFSssisfdvtifeiFVPLIY-------- 1526
Cdd:PLN02430  218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlFMEQFEDKMTHDDVYLS------------FLPLAHildrmiee 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 -----GARMTIYQGekfDVTKLVQVILEeqvtlsyIPPTLLNEIYDYFVRDNQKIvlNKLLVGVEPIKTELlakYDHLFR 1601
Cdd:PLN02430  286 yffrkGASVGYYHG---DLNALRDDLME-------LKPTLLAGVPRVFERIHEGI--QKALQELNPRRRLI---FNALYK 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 GNLQILN-GYGPTEA----------------------------------------TVCC---TSYRYESNKEITTQNVP- 1636
Cdd:PLN02430  351 YKLAWMNrGYSHKKAspmadflafrkvkaklggrlrllisggaplsteieeflrvTSCAfvvQGYGLTETLGPTTLGFPd 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 -------IGSPLLNTKIYILD-SFHRIQPIGVP--GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARW 1706
Cdd:PLN02430  431 emcmlgtVGAPAVYNELRLEEvPEMGYDPLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEI 503
                         330
                  ....*....|....*...
gi 446807313 1707 LPDGNIEYLGRVDHQVKI 1724
Cdd:PLN02430  504 LPNGVLKIIDRKKNLIKL 521
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
1324-1717 5.89e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 54.85  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIA----VVCNEKG-----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA 1394
Cdd:PLN02861   49 FSDAVKKYPNNQMlgrrQVTDSKVgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGIT 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1395 YLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSI-------------IKGIEFQGNVIDLMDM----------SFEEEP--G 1449
Cdd:PLN02861  129 YVPLYDTLGANAVEFIINHAEVSIAFVQESKIssilsclpkcssnLKTIVSFGDVSSEQKEeaeelgvscfSWEEFSlmG 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1450 EDMHMMIEPH--NLAYVIYTSGSTGQPKGVMIEHRSLtnflcaMYEDFSQD--IGITDNVLFSSSISFDvtifeiFVPLI 1525
Cdd:PLN02861  209 SLDCELPPKQktDICTIMYTSGTTGEPKGVILTNRAI------IAEVLSTDhlLKVTDRVATEEDSYFS------YLPLA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1526 Y-------------GARMTIYQGekfDVTKLVQVILEEQVTLSYIPPTLLNEIY------------------DY------ 1568
Cdd:PLN02861  277 HvydqvietyciskGASIGFWQG---DIRYLMEDVQALKPTIFCGVPRVYDRIYtgimqkissggmlrkklfDFaynykl 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 ------FVRDNQKIVLNKLLVgvEPIKTELLAKYDHLFRGN----------LQILN------GYGPTEATVCCTSYRYES 1626
Cdd:PLN02861  354 gnlrkgLKQEEASPRLDRLVF--DKIKEGLGGRVRLLLSGAaplprhveefLRVTScsvlsqGYGLTESCGGCFTSIANV 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITTQNVP---IGSPLLNTKIYILDSFHriqpiGVP-GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGD 1702
Cdd:PLN02861  432 FSMVGTVGVPmttIEARLESVPEMGYDALS-----DVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGD 499
                         490
                  ....*....|....*
gi 446807313 1703 IARWLPDGNIEYLGR 1717
Cdd:PLN02861  500 IGEWQPNGAMKIIDR 514
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
300-769 5.95e-07

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: 54.74  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCShvLTY 379
Cdd:cd05915    24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK--VLL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  380 QNSIIKGVAFQGSVI--NLMDIPFEE---EQVEDLQITMEPQ----------NLAYVIYTSGSTGQPKGVMIEHRSLtnF 444
Cdd:cd05915   102 FDPNLLPLVEAIRGElkTVQHFVVMDekaPEGYLAYEEALGEeadpvrvperAACGMAYTTGTTGLPKGVVYSHRAL--V 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  445 LCAMYedfsqdIGITDNVLFSSsisfdVTIFEIFVPLV-CGARMTIYQGEKF--------DVPK---LVQVILEEQVTLA 512
Cdd:cd05915   180 LHSLA------ASLVDGTALSE-----KDVVLPVVPMFhVNAWCLPYAATLVgakqvlpgPRLDpasLVELFDGEGVTFT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  513 YIPPTLLNEIydyfvrANQKISLNKLFV--------GVEPikTELLAKYDHLfrGNLQILNLYGPTE----ATVCCTSYQ 580
Cdd:cd05915   249 AGVPTVWLAL------ADYLESTGHRLKtlrrlvvgGSAA--PRSLIARFER--MGVEVRQGYGLTEtspvVVQNFVKSH 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  581 YER--DKEITTQNVPIGSPLLNTKIYILDSfhrlQPIGVPGE------ICISGIGLARGYINRKELT-ADKFidhpfeRG 651
Cdd:cd05915   319 LESlsEEEKLTLKAKTGLPIPLVRLRVADE----EGRPVPKDgkalgeVQLKGPWITGGYYGNEEATrSALT------PD 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  652 eKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYV-VTEKDIPI 730
Cdd:cd05915   389 -GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRGEKPTP 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 446807313  731 PEVRAYLATKL-PYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05915   468 EELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
300-489 6.01e-07

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 54.74  E-value: 6.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  300 EITYKQLNIKANQLARRLlDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELPKQ--RVEYMLTDSGCSHV 376
Cdd:PRK07769   55 DLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCTPSAI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  377 LTyQNSIIKGVA--FQG-------SVINLMDIPfeeEQVEDLQITMEPQ--NLAYVIYTSGSTGQPKGVMIEHRSL-TNF 444
Cdd:PRK07769  134 LT-TTDSAEGVRkfFRArpakerpRVIAVDAVP---DEVGATWVPPEANedTIAYLQYTSGSTRIPAGVQITHLNLpTNV 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 446807313  445 LcAMYEDFSQDIGitdnvlfSSSISF-----DVTIFEIFVPLVCGARMTI 489
Cdd:PRK07769  210 L-QVIDALEGQEG-------DRGVSWlpffhDMGLITVLLPALLGHYITF 251
PRK09192 PRK09192
fatty acyl-AMP ligase;
303-441 8.04e-07

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 54.24  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  303 YKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG--AYLPIDTELpKQRVEY------MLTDSGCS 374
Cdd:PRK09192   52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGF-GGRESYiaqlrgMLASAQPA 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  375 HVLT------YQNSIIKGVA--FQGSVINLMDIPfeeEQVEDLQiTMEPQNLAYVIYTSGSTGQPKGVMIEHRSL 441
Cdd:PRK09192  131 AIITpdellpWVNEATHGNPllHVLSHAWFKALP---EADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
279-726 9.08e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 54.08  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  279 QLFEEQVKQNPNQIAI----VCNGKE-----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG 349
Cdd:PLN02861   47 QFFSDAVKKYPNNQMLgrrqVTDSKVgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  350 GAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSI-------------IKGVAFQGSVINLMDIPFEE-----------EQ 405
Cdd:PLN02861  127 ITYVPLYDTLGANAVEFIINHAEVSIAFVQESKIssilsclpkcssnLKTIVSFGDVSSEQKEEAEElgvscfsweefSL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  406 VEDLQITMEPQ---NLAYVIYTSGSTGQPKGVMIEHRSLtnflcaMYEDFSQD--IGITDNVLFSSSISFD----VTIFE 476
Cdd:PLN02861  207 MGSLDCELPPKqktDICTIMYTSGTTGEPKGVILTNRAI------IAEVLSTDhlLKVTDRVATEEDSYFSylplAHVYD 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  477 IFVPLVC---GARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYdyfVRANQKIS-----LNKLF--------- 539
Cdd:PLN02861  281 QVIETYCiskGASIGFWQG---DIRYLMEDVQALKPTIFCGVPRVYDRIY---TGIMQKISsggmlRKKLFdfaynyklg 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  540 -----------------VGVEPIKTELLAKYDHLFRGN----------LQILNL------YGPTEATVCCTSYQYERDKE 586
Cdd:PLN02861  355 nlrkglkqeeasprldrLVFDKIKEGLGGRVRLLLSGAaplprhveefLRVTSCsvlsqgYGLTESCGGCFTSIANVFSM 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  587 ITTQNVP---IGSPLLNTKIYILDSFHrlqpiGVP-GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIAR 662
Cdd:PLN02861  435 VGTVGVPmttIEARLESVPEMGYDALS-----DVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGE 502
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313  663 WLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIqreDESGEKYLCAYVVTEK 726
Cdd:PLN02861  503 WQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASIWVY---GNSFESFLVAVVVPDR 564
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1332-1807 1.17e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 53.80  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 tDSGCSHVLvhqnsiIKGIEFQGN--------------VIDLMDMSFEE----------------EPGEDMHMmiePHNL 1461
Cdd:PRK08162  112 -RHGEAKVL------IVDTEFAEVarealallpgpkplVIDVDDPEYPGgrfigaldyeaflasgDPDFAWTL---PADE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVI---YTSGSTGQPKGVMIEHRSltNFLCAMyedfsqdigitdnvlfSSSISFDVTIFEIF---VPLI------YGAR 1529
Cdd:PRK08162  182 WDAIalnYTSGTTGNPKGVVYHHRG--AYLNAL----------------SNILAWGMPKHPVYlwtLPMFhcngwcFPWT 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQG-----EKFDVTKLVQVILEEQVT-LSYIPptllneiydyfvrdnqkIVLNKLLVGVEpiktELLAKYDHLFRGN 1603
Cdd:PRK08162  244 VAARAGtnvclRKVDPKLIFDLIREHGVThYCGAP-----------------IVLSALINAPA----EWRAGIDHPVHAM 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1604 ------------------LQILNGYGPTE----ATVCC---------TSYRYESNKEittQNVPIgsPLLNTkIYILDSf 1652
Cdd:PRK08162  303 vagaappaaviakmeeigFDLTHVYGLTEtygpATVCAwqpewdalpLDERAQLKAR---QGVRY--PLQEG-VTVLDP- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1653 HRIQPigVP------GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIeylgrvdhQVKIR- 1725
Cdd:PRK08162  376 DTMQP--VPadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYI--------KIKDRs 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 -------GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYV-------VTEKDIpIPEVRAYLAtklpHYMIPQ 1791
Cdd:PRK08162  439 kdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVelkdgasATEEEI-IAHCREHLA----GFKVPK 513
                         570
                  ....*....|....*.
gi 446807313 1792 QLIpIHNIPLTQNGKI 1807
Cdd:PRK08162  514 AVV-FGELPKTSTGKI 528
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
420-791 1.33e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 53.59  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  420 YVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDNVLFSSS----ISFDVTIFEIfvpLVCGARMTIYQG--- 492
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFSHSsigwVSFHGFLYGS---LSLGNTFVMFEGgii 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  493 -EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-----FVRANQKIS-LNKLFVGVEPIKtELLAKYdhlFRGNLQI-- 563
Cdd:PTZ00237  333 kNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSnLKEIWCGGEVIE-ESIPEY---IENKLKIks 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  564 LNLYGPTEaTVCCTSYQYerdKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICIS---GIGLARGYINRKELTA 640
Cdd:PTZ00237  409 SRGYGQTE-IGITYLYCY---GHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  641 DKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCA 720
Cdd:PTZ00237  485 QLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  721 YVVTEKDIPIP---------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNlkSSHLEPTNSTERKL 791
Cdd:PTZ00237  560 LLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLND--SNYQLPDNVNDSEI 637
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
415-695 1.39e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 53.58  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqDIGITD---------NVLfssSISFDVTIFEIFVPLVCGA 485
Cdd:PLN02387  249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVP-KLGKNDvylaylplaHIL---ELAAESVMAAVGAAIGYGS 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  486 RMT-------IYQGEKFDVPKLvqvileeQVTLAYIPPTLLNEIYD-YFVRANQKISLNK-LF----------------- 539
Cdd:PLN02387  325 PLTltdtsnkIKKGTKGDASAL-------KPTLMTAVPAILDRVRDgVRKKVDAKGGLAKkLFdiaykrrlaaiegswfg 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  540 -VGVEPIKTELLA--KYDHLFRGNLQIL---------------NL---------YGPTEATVCCTSYQYErdkEITTQNV 592
Cdd:PLN02387  398 aWGLEKLLWDALVfkKIRAVLGGRIRFMlsggaplsgdtqrfiNIclgapigqgYGLTETCAGATFSEWD---DTSVGRV 474
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  593 piGSPLLNTKIYILD---SFHRLQPIGVP-GEICISGIGLARGYINRKELTADKF-IDhpfERGEKLYKTGDIARWLPDG 667
Cdd:PLN02387  475 --GPPLPCCYVKLVSweeGGYLISDKPMPrGEIVIGGPSVTLGYFKNQEKTDEVYkVD---ERGMRWFYTGDIGQFHPDG 549
                         330       340
                  ....*....|....*....|....*....
gi 446807313  668 NIEYLGRVDHQVKIR-GYRIELGEIEASL 695
Cdd:PLN02387  550 CLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1691-1807 2.60e-06

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: 52.66  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 FERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD 1770
Cdd:cd05943   479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446807313 1771 IPIPE-----VRAYLATKL-PHYmIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd05943   559 VELDDelrkrIRSTIRSALsPRH-VPAKIIAVPDIPRTLSGKK 600
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1345-1487 2.70e-06

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 52.64  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVgVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQ---RVEYMLTDSGCSHVLV 1421
Cdd:PRK05850   37 TWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAhdeRVSAVLRDTSPSVVLT 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1422 hQNSIIKGI-----EFQGNV------IDLMDMSFEEEPGEDMHmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLT-NF 1487
Cdd:PRK05850  116 -TSAVVDDVteyvaPQPGQSappvieVDLLDLDSPRGSDARPR---DLPSTAYLQYTSGSTRTPAGVMVSHRNVIaNF 189
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
648-764 2.93e-06

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: 52.66  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  648 FERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD 727
Cdd:cd05943   479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446807313  728 IPIPE-----VRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd05943   559 VELDDelrkrIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
292-528 3.55e-06

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: 51.97  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  292 IAIVCNGKE---ITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQ----- 362
Cdd:cd05905     3 TLLDSKGKEattLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQqlgfl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  363 ----------RVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQN---LAYVIYTSGSTG 429
Cdd:cd05905    83 lgtckvrvalTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRdgdTAYIEYSFSSDG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  430 QPKGVMIEHRSLTNFL------CAMYE--------DFSQDIGitdnvlfsssisfdvtifeifvpLVCGARMTIYQGekf 495
Cdd:cd05905   163 SLSGVAVSHSSLLAHCralkeaCELYEsrplvtvlDFKSGLG-----------------------LWHGCLLSVYSG--- 216
                         250       260       270
                  ....*....|....*....|....*....|...
gi 446807313  496 dvpklVQVILEEQVTLAYIPPTLLNEIYDYFVR 528
Cdd:cd05905   217 -----HHTILIPPELMKTNPLLWLQTLSQYKVR 244
PLN02654 PLN02654
acetate-CoA ligase
1331-1831 4.61e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 51.82  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVV--CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PLN02654  102 NGDKIAIYweGNEPGfdasLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDsgCS-HVLVHQNSIIKGIEFQgNVIDLMDMSFEE---------------------------EPGEDMHMM- 1455
Cdd:PLN02654  182 ESLAQRIVD--CKpKVVITCNAVKRGPKTI-NLKDIVDAALDEsakngvsvgicltyenqlamkredtkwQEGRDVWWQd 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1456 -------------IEPHNLAYVIYTSGSTGQPKGVMieHR-------SLTNFLCAMYEDFSQDIGITDNVLFSSSISFdV 1515
Cdd:PLN02654  259 vvpnyptkcevewVDAEDPLFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTDVYWCTADCGWITGHSY-V 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TifeiFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKT 1590
Cdd:PLN02654  336 T----YGPMLNGATVLVFEGAPNypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPINP 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1591 ELLAKYdhlfrgnlqiLNGYGPTEATVCCTSYRYESNKEITTQnVPIGSPLLNTKIYIldSFHRIQPIGV---------- 1660
Cdd:PLN02654  412 SAWRWF----------FNVVGDSRCPISDTWWQTETGGFMITP-LPGAWPQKPGSATF--PFFGVQPVIVdekgkeiege 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1661 -PGEICI--SGIGLAR---GYINRKELTADKfidhPFErgeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEI 1734
Cdd:PLN02654  479 cSGYLCVkkSWPGAFRtlyGDHERYETTYFK----PFA---GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEV 551
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1735 EASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP-EVRAYLA----TKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PLN02654  552 ESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
                         570       580
                  ....*....|....*....|....*..
gi 446807313 1810 SKLPK-----LNTLGNSNYVPPRNEID 1831
Cdd:PLN02654  632 RILRKiasrqLDELGDTSTLADPGVVD 658
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1457-1808 5.47e-06

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 51.63  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSI----SFDVTIfEIFVPLIYGARMTI 1532
Cdd:PRK08043  363 QPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALplfhSFGLTV-GLFTPLLTGAEVFL 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1533 YQgekfdvTKLVQVILEEQV-----TLSYIPPTLLNEI------YDyFVRdnqkivLNKLLVGVEPIKTELLAKYDHLFr 1601
Cdd:PRK08043  438 YP------SPLHYRIVPELVydrncTVLFGTSTFLGNYarfanpYD-FAR------LRYVVAGAEKLQESTKQLWQDKF- 503
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 gNLQILNGYGPTEatvcCTSyryesnkeITTQNVPIGspllnTKIYildSFHRIQP------IGVPG-----EICISGIG 1670
Cdd:PRK08043  504 -GLRILEGYGVTE----CAP--------VVSINVPMA-----AKPG---TVGRILPgmdarlLSVPGieqggRLQLKGPN 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYI---NRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT- 1746
Cdd:PRK08043  563 IMNGYLrveKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQh 642
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1747 AVVIDQEDEAGEkylcAYVV--TEKDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK08043  643 ATAIKSDASKGE----ALVLftTDSELTREKLQQYArEHGVPELAVPRDIRYLKQLPLLGSGKPD 703
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
1928-2026 6.45e-06

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 49.15  E-value: 6.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   1928 GGILNYYDLARELGEDKTVYGLQSIGYDDS-RFPnlSVEEMAVRYI-EEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEE 2005
Cdd:smart00824   10 SGPHEYARLAAALRGRRDVSALPLPGFGPGePLP--ASADALVEAQaEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEA 87
                            90       100
                    ....*....|....*....|.
gi 446807313   2006 LGDKVSFLGLLDVHPIEQGRE 2026
Cdd:smart00824   88 RGIPPAAVVLLDTYPPGDPAP 108
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
1923-2017 6.49e-06

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 49.61  E-value: 6.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1923 IHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFP--NLSVEEMAVRYIEEIKQVKKEgPYTLLGWSFGGIVAFEMA 2000
Cdd:COG0596    29 LHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPagGYTLDDLADDLAALLDALGLE-RVVLVGHSMGGMVALELA 107
                          90
                  ....*....|....*..
gi 446807313 2001 RKleeLGDKVSFLGLLD 2017
Cdd:COG0596   108 AR---HPERVAGLVLVD 121
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
1461-1718 9.29e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 50.75  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG--------------------ITDNVLFS--SSISF----- 1513
Cdd:PTZ00216  266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGppeedetycsylplahimefGVTNIFLArgALIGFgsprt 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1514 ----------DVT----IFEIFVPLIygarmtiyqgekFD-VTKLVQvileeqvtlSYIPP--TLLNEIYD--YFVR--- 1571
Cdd:PTZ00216  346 ltdtfarphgDLTefrpVFLIGVPRI------------FDtIKKAVE---------AKLPPvgSLKRRVFDhaYQSRlra 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 -----D----NQKIV----------LNKLLVGVEPIKTELLAKYDHLFRGnlqILNGYGPTEaTVCCTSYRYESNkeITT 1632
Cdd:PTZ00216  405 lkegkDtpywNEKVFsapravlggrVRAMLSGGGPLSAATQEFVNVVFGM---VIQGWGLTE-TVCCGGIQRTGD--LEP 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 QNVpiGSPLLNTKIYILDS---FHRIQPigVP-GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLP 1708
Cdd:PTZ00216  479 NAV--GQLLKGVEMKLLDTeeyKHTDTP--EPrGEILLRGPFLFKGYYKQEELTREVLDE------DGWFHTGDVGSIAA 548
                         330
                  ....*....|
gi 446807313 1709 DGNIEYLGRV 1718
Cdd:PTZ00216  549 NGTLRIIGRV 558
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
418-675 9.29e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 50.75  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  418 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG--------------------ITDNVLFS--SSISF----- 470
Cdd:PTZ00216  266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGppeedetycsylplahimefGVTNIFLArgALIGFgsprt 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  471 ----------DVT----IFEIFVPLVcgarmtiyqgekFD-VPKLVQvileeqvtlAYIPP--TLLNEIYDYF----VRA 529
Cdd:PTZ00216  346 ltdtfarphgDLTefrpVFLIGVPRI------------FDtIKKAVE---------AKLPPvgSLKRRVFDHAyqsrLRA 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  530 ----------NQKI----------SLNKLFVGVEPIKTELLAKYDHLFRGnlqILNLYGPTEaTVCCTSYQyeRDKEITT 589
Cdd:PTZ00216  405 lkegkdtpywNEKVfsapravlggRVRAMLSGGGPLSAATQEFVNVVFGM---VIQGWGLTE-TVCCGGIQ--RTGDLEP 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  590 QNVpiGSPLLNTKIYILDS---FHRLQPigVP-GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLP 665
Cdd:PTZ00216  479 NAV--GQLLKGVEMKLLDTeeyKHTDTP--EPrGEILLRGPFLFKGYYKQEELTREVLDE------DGWFHTGDVGSIAA 548
                         330
                  ....*....|
gi 446807313  666 DGNIEYLGRV 675
Cdd:PTZ00216  549 NGTLRIIGRV 558
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1327-1809 1.30e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 50.52  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAVV------CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG-------- 1392
Cdd:PRK00174   76 HLKTRGDKVAIIwegddpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfg 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1393 --------------GAYLPIDTD--------LP-KQRVEYMLTDSGC-SHVLVHQNSiikgiefqGNVI----------- 1437
Cdd:PRK00174  156 gfsaealadriidaGAKLVITADegvrggkpIPlKANVDEALANCPSvEKVIVVRRT--------GGDVdwvegrdlwwh 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 DLMDMSFEEEPGEDM---HMMiephnlaYVIYTSGSTGQPKGVM------IEHRSLTN-----------FLCamyedfSQ 1497
Cdd:PRK00174  228 ELVAGASDECEPEPMdaeDPL-------FILYTSGSTGKPKGVLhttggyLVYAAMTMkyvfdykdgdvYWC------TA 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIG-ITDNvlfsSSIsfdvtifeIFVPLIYGARMTIYQG--EKFDVTKLVQVILEEQVTLSYIPPTLLNEiydyFVRDNQ 1574
Cdd:PRK00174  295 DVGwVTGH----SYI--------VYGPLANGATTLMFEGvpNYPDPGRFWEVIDKHKVTIFYTAPTAIRA----LMKEGD 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1575 KIVLN------KLL--VGvEPIKTEllA---KYDHLFRGNLQILNGYGPTE--ATVcctsyryesnkeIT-----TQNVP 1636
Cdd:PRK00174  359 EHPKKydlsslRLLgsVG-EPINPE--AwewYYKVVGGERCPIVDTWWQTEtgGIM------------ITplpgaTPLKP 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 iGS---PLLNTKIYILDSFHRIQPIGVPGEICI--SGIGLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGN 1711
Cdd:PRK00174  424 -GSatrPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGY 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIP-----IPEVRAYLATKLP 1785
Cdd:PRK00174  499 YWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDiKGQG-IYAFVTLKGGEEpsdelRKELRNWVRKEIG 577
                         570       580
                  ....*....|....*....|....
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK00174  578 PIAKPDVIQFAPGLPKTRSGKIMR 601
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
879-1129 1.62e-05

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: 49.56  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  879 QKRMFivDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVD--FNIEYVHVN 956
Cdd:cd19534     8 QRWFF--EQNLAGRHH-FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVVDLS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  957 EKDADYLIHEFISP----FDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNELPK-LR 1027
Cdd:cd19534    85 SLAQAAAIEALAAEaqssLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYeqalAGEPIPLpSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1028 VQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLnfPTDFQRptiqsFKGNV--CSFNLGTDLTfkvNKLATET--- 1102
Cdd:cd19534   165 TSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGL--PKDPEQ-----TYGDArtVSFTLDEEET---EALLQEAnaa 234
                         250       260
                  ....*....|....*....|....*...
gi 446807313 1103 -GTTPYMILLAIYNILLSRYTGQEDIIV 1129
Cdd:cd19534   235 yRTEINDLLLAALALAFQDWTGRAPPAI 262
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1341-1484 2.34e-05

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 49.60  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1341 EKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAG--GAYLP-------------------- 1397
Cdd:cd05938     3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 -IDTDLPK--QRVEYMLTDSGCSHVLVHQNSIIKGIEfqgNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQP 1474
Cdd:cd05938    83 vVAPELQEavEEVLPALRADGVSVWYLSHTSNTEGVI---SLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLP 159
                         170
                  ....*....|
gi 446807313 1475 KGVMIEHRSL 1484
Cdd:cd05938   160 KAARISHLRV 169
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
21-179 2.64e-05

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


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 49.02  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   21 EYWLDKLSGDVELSRFPCDclSLNNIQASKE--SYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVV 98
Cdd:cd19546   196 AYWRDALAGAPDELELPTD--RPRPVLPSRRagAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVT 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   99 IGMpVFKQGQEETVFQ------NNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLN 172
Cdd:cd19546   274 VGT-VLPRDDEEGDLEgmvgpfARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQ 352

                  ....*..
gi 446807313  173 TIVMLDD 179
Cdd:cd19546   353 VALDVRD 359
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
22-238 7.41e-05

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: 47.44  E-value: 7.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   22 YWLDKLsGDVELSRFPCDCLSLNniQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGM 101
Cdd:cd19536   190 YWREYL-AGATLATLPALSEAVG--GGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGT 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  102 PVFKQGQEETVFQN------NFLLLRTQINQEDnFKEIIYKIKETILESNEHCHFPfnkltqLLSLDGESNNLPLLNTIV 175
Cdd:cd19536   267 VVHGRSEETTGAERllglflNTLPLRVTLSEET-VEDLLKRAQEQELESLSHEQVP------LADIQRCSEGEPLFDSIV 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  176 MLDDIHCYEST---------------DKINSDMVIRFMKN--EEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDP 238
Cdd:cd19536   340 NFRHFDLDFGLpewgsdegmrrgllfSEFKSNYDVNLSVLpkQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1664-1814 8.48e-05

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: 47.43  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISGIGLARGYINRKELT-ADKFidhpfeRGeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:cd05915   363 VQLKGPWITGGYYGNEEATrSALT------PD-GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHP 435
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1743 TIKTAVVIDQEDEAGEKYLCAYV-VTEKDIPIPEVRAYLATKLPHY-MIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05915   436 KVKEAAVVAIPHPKWQERPLAVVvPRGEKPTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
17-238 1.44e-04

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: 46.53  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   17 KKEKEYWLDKLSGdVELSRFPCdcLSlnnIQASKESYYCQFPSDIAK-RAVAISNNSDMLlyTILLSGVKYLLSRYTDKD 95
Cdd:cd19542   170 EESLQYWRKYLQG-ASPCAFPS--LS---PKRPAERSLSSTRRSLAKlEAFCASLGVTLA--SLFQAAWALVLARYTGSR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313   96 DVVIG---------MPvfkqGQEETV---FqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDG 163
Cdd:cd19542   242 DVVFGyvvsgrdlpVP----GIDDIVgpcI--NTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWP 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  164 ESnnlPLLNTIV----------MLDDIHCYESTDKINS----DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYN 229
Cdd:cd19542   316 SG---TLFNTLVsyqnfeaspeSELSGSSVFELSAAEDpteyPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDD 392

                  ....*....
gi 446807313  230 ILDILMKDP 238
Cdd:cd19542   393 ILEALLANP 401
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
1457-1730 2.89e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 46.25  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-----CAMYEDFSQDIG--------ITDNVLFSSSISFDVTI------ 1517
Cdd:PTZ00342  302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTHlsylpishIYERVIAYLSFMLGGTIniwskd 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyFVRDNQKIVLNKLLVGVEPIKTELLAKYD 1597
Cdd:PTZ00342  382 INYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILS-LRKSNNNGGFSKFLEGITHISSKIKDKVN 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 hlfrGNLQ-ILNGYGPTEATVC-----------CTSYRY-ESNKEITTQNV------PIGSPLLNTKIYILDSFHRIQPI 1658
Cdd:PTZ00342  461 ----PNLEvILNGGGKLSPKIAeelsvllnvnyYQGYGLtETTGPIFVQHAddnnteSIGGPISPNTKYKVRTWETYKAT 536
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1659 GVP--GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIE 1730
Cdd:PTZ00342  537 DTLpkGELLIKSDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
1922-2001 6.88e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 43.23  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  1922 IIHGQGggiLNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAvRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMAR 2001
Cdd:pfam12697    3 LVHGAG---LSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLA-DLAALLDELGAARPVVLVGHSLGGAVALAAAA 78
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
414-687 1.04e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 44.32  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-----CAMYEDFSQDIG--------ITDNVLFSSSISFDVTI------ 474
Cdd:PTZ00342  302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTHlsylpishIYERVIAYLSFMLGGTIniwskd 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  475 FEIFVPLVCGARMTIYQGekfdVPKLVQVILEEQVT-LAYIPPT---LLNEIYDyFVRANQKISLNKLFVGV----EPIK 546
Cdd:PTZ00342  382 INYFSKDIYNSKGNILAG----VPKVFNRIYTNIMTeINNLPPLkrfLVKKILS-LRKSNNNGGFSKFLEGIthisSKIK 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  547 TELLAKYDHLFRG----------------NLQILNLYGPTEATvCCTSYQYERDKEITTQNVPIgSPllNTKiYILDSFH 610
Cdd:PTZ00342  457 DKVNPNLEVILNGggklspkiaeelsvllNVNYYQGYGLTETT-GPIFVQHADDNNTESIGGPI-SP--NTK-YKVRTWE 531
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  611 RLQPIGVP--GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIE 687
Cdd:PTZ00342  532 TYKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PRK07867 PRK07867
acyl-CoA synthetase; Validated
315-769 1.40e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 43.52  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  315 RRLLDQGvkREFIVGVMMERSIEMIV-----GILGILKAG------GAYLPIDTELPKQRVeyMLTDSGCSHVLtyqNSI 383
Cdd:PRK07867   46 RARLDPT--RPPHVGVLLDNTPEFSLllgaaALSGIVPVGlnptrrGAALARDIAHADCQL--VLTESAHAELL---DGL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  384 IKGVafqgSVINLmDIPFEEEQVEDLQ------ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiG 457
Cdd:PRK07867  119 DPGV----RVINV-DSPAWADELAAHRdaeppfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRF----G 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  458 IT-DNVLFSSSISF--DVTIFEIFVPLVCGARMTIYQgeKFDVPKLVQVILEEQVT--------LAYI---PPtllneiy 523
Cdd:PRK07867  190 LGpDDVCYVSMPLFhsNAVMAGWAVALAAGASIALRR--KFSASGFLPDVRRYGATyanyvgkpLSYVlatPE------- 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  524 dyfvRANQKISLNKLFVGVE--PIKTELLAKydhlfRGNLQILNLYGPTEATVCCTSyqyerdkeitTQNVPIGS--PLL 599
Cdd:PRK07867  261 ----RPDDADNPLRIVYGNEgaPGDIARFAR-----RFGCVVVDGFGSTEGGVAITR----------TPDTPPGAlgPLP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  600 -NTKIY-----------ILDSFHRLQPIGVPGEIC-ISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPD 666
Cdd:PRK07867  322 pGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRG-------GVYWSGDLAYRDAD 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLCAYVVTEKDIPIPE-VRAYLATK--LP 742
Cdd:PRK07867  395 GYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQVMAALVLAPGAKFDPDaFAEFLAAQpdLG 474
                         490       500
                  ....*....|....*....|....*..
gi 446807313  743 YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07867  475 PKQWPSYVRVCAELPRTATFKVLKRQL 501
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1834-1894 3.79e-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: 38.39  E-value: 3.79e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313   1834 LIDIWSSILGVNN---IGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSD 1894
Cdd:smart00823   17 VREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
298-441 4.53e-03

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: 41.89  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  298 GKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAG--GAYLP-------------------- 354
Cdd:cd05938     3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313  355 -IDTELPK--QRVEYMLTDSGCSHVLTYQNSIIKGVafqGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQP 431
Cdd:cd05938    83 vVAPELQEavEEVLPALRADGVSVWYLSHTSNTEGV---ISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLP 159
                         170
                  ....*....|
gi 446807313  432 KGVMIEHRSL 441
Cdd:cd05938   160 KAARISHLRV 169
 
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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