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Conserved domains on  [gi|557786167|ref|NP_001273600|]
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beta-alanine-activating enzyme isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
15-533 0e+00

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: 666.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  15 MDRVAVCFDEcnNQLPVYYTYKTVVNAASELSNFLLLHCDFqGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPP 94
Cdd:cd17654    1 PDRPALIIDQ--TTSDTTVSYADLAEKISNLSNFLRKKFQT-EERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  95 SLSTHFMKKCNLKYILVEKKQINKFKSFHetllnydtftvehndlvlfrlhwkntevnlmlndgkekyekekiksisseh 174
Cdd:cd17654   78 QRSLTVMKKCHVSYLLQNKELDNAPLSFT--------------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 175 vneeKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALS 254
Cdd:cd17654  107 ----PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 255 SGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGE 334
Cdd:cd17654  183 SGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGK 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 335 GNKTQIFNVYGITEVSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTNGFtiqEGSGQVFLGGRNRVCFLDD 414
Cdd:cd17654  263 GNRTRIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPLLGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDD 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 415 EVTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKdaSVK 494
Cdd:cd17654  332 EVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSS 409
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 557786167 495 EYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17654  410 SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
552-608 7.50e-05

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


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 41.76  E-value: 7.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 552 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:COG0236    3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
PQQ super family cl34291
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
735-830 2.25e-03

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG1520:

Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 41.34  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 735 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 811
Cdd:COG1520    9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86
                         90
                 ....*....|....*....
gi 557786167 812 DRIesSACVSKCGNFIVVG 830
Cdd:COG1520   87 EPL--SGGVGADGGLVVVG 103
 
Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
15-533 0e+00

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: 666.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  15 MDRVAVCFDEcnNQLPVYYTYKTVVNAASELSNFLLLHCDFqGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPP 94
Cdd:cd17654    1 PDRPALIIDQ--TTSDTTVSYADLAEKISNLSNFLRKKFQT-EERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  95 SLSTHFMKKCNLKYILVEKKQINKFKSFHetllnydtftvehndlvlfrlhwkntevnlmlndgkekyekekiksisseh 174
Cdd:cd17654   78 QRSLTVMKKCHVSYLLQNKELDNAPLSFT--------------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 175 vneeKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALS 254
Cdd:cd17654  107 ----PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 255 SGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGE 334
Cdd:cd17654  183 SGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGK 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 335 GNKTQIFNVYGITEVSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTNGFtiqEGSGQVFLGGRNRVCFLDD 414
Cdd:cd17654  263 GNRTRIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPLLGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDD 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 415 EVTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKdaSVK 494
Cdd:cd17654  332 EVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSS 409
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 557786167 495 EYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17654  410 SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
68-474 8.51e-61

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: 211.74  E-value: 8.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   68 GIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEkkqinkfkSFHETLLNYDTFTVEHNDLVLfrlhwk 147
Cdd:TIGR01733  35 SAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD--------SALASRLAGLVLPVILLDPLE------ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  148 ntevNLMLNDGKekyekekiksiSSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD 227
Cdd:TIGR01733 101 ----LAALDDAP-----------APPPPDAPSGPDD--------LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  228 ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLrrfgsQLIKSTVLS 307
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL-----ALLAAALPP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  308 ATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVR 387
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDR-WRARGPGARLINLYGPTETTVWSTATLVDPDDAPR----ESPVPIGRPLANTRLYVL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  388 DTNGFTIQEG-------SG-QVFLG-----GRNRVCFLDDE-VTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGK 452
Cdd:TIGR01733 308 DDDLRPVPVGvvgelyiGGpGVARGylnrpELTAERFVPDPfAGGDGARLYRTGDLVRYlPDGNLEFLGRIDDQVKIRGY 387
                         410       420
                  ....*....|....*....|....
gi 557786167  453 RlnIEL--VQQVAEELQQVESCAV 474
Cdd:TIGR01733 388 R--IELgeIEAALLRHPGVREAVV 409
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2-475 2.60e-55

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: 208.17  E-value: 2.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    2 TLQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLhcdfQGIRE---IGLYCQPGIDLPSWILGI 78
Cdd:COG1020   477 TLHELFEAQAARTPDAVAVVFGD--QSL----TYAELNARANRLAHHLRA----LGVGPgdlVGVCLERSLEMVVALLAV 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   79 LQVPAAYVPIEPDSPPS-LstHFM-KKCNLKYILVEKKQINKFKSFHETLLNYDTFTVEHNDlvlfrlhwkntevnlmln 156
Cdd:COG1020   547 LKAGAAYVPLDPAYPAErL--AYMlEDAGARLVLTQSALAARLPELGVPVLALDALALAAEP------------------ 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  157 dgkekyEKEKIKSISSEHvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFL 236
Cdd:COG1020   607 ------ATNPPVPVTPDD-----------------LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ 663
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  237 ASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIkSTVLSATTSLRVLA 316
Cdd:COG1020   664 FASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL-ARHRVTVLNLTPSLLR----ALL-DAAPEALPSLRLVL 737
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  317 LGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGftiQ- 395
Cdd:COG1020   738 VGGEALP-PELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGG-----SVPIGRPIANTRVYVLDAHL---Qp 808
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  396 --EG-SGQVFLGG----------------RnrvcFLDDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRln 455
Cdd:COG1020   809 vpVGvPGELYIGGaglargylnrpeltaeR----FVADPFGFPGARLYRTGDLARWlPDGNLEFLGRADDQVKIRGFR-- 882
                         490       500
                  ....*....|....*....|..
gi 557786167  456 IEL--VQQVAEELQQVESCAVT 475
Cdd:COG1020   883 IELgeIEAALLQHPGVREAVVV 904
PRK12467 PRK12467
peptide synthase; Provisional
6-637 1.28e-48

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 188.06  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    6 LVHKAASCYMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAY 85
Cdd:PRK12467  517 LIEAQARQHPERPALVFGE------QVLSYAELNRQANRLAHVLIAAGVGPDVL-VGIAVERSIEMVVGLLAVLKAGGAY 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   86 VPIEPDSPPSLSTHFMKKCNLKYILvekkqinkfksfhetllnydtftveHNDLVLFRLHWKNTEVNLMLNDGKEKYeke 165
Cdd:PRK12467  590 VPLDPEYPQDRLAYMLDDSGVRLLL-------------------------TQSHLLAQLPVPAGLRSLCLDEPADLL--- 641
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  166 kiksissehvnEEKAEEHMDLRLK-HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDP 244
Cdd:PRK12467  642 -----------CGYSGHNPEVALDpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDL 710
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  245 SVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAFPs 324
Cdd:PRK12467  711 GVTELFGALASGATLHLLPPDCARDAEAFAALM-ADQGVTVLKIVPSHLQ----ALLQASRVALPRPQRALVCGGEALQ- 784
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  325 LTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL 403
Cdd:PRK12467  785 VDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-----NVPIGQPLANLGLYILDHYLNPVPVGVvGELYI 859
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  404 GGR--------------NRvcFLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRL---NIELVQQVAEE 465
Cdd:PRK12467  860 GGAglargyhrrpaltaER--FVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIelgEIEARLLAQPG 937
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  466 LQQVESCAVTWYNQEKLILFMV-------SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiyl 538
Cdd:PRK12467  938 VREAVVLAQPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK--- 1014
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  539 NYINLKSENKLSGKEDLWEKLQYLWKSTLnlpeDLLRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVPglLEIILSSS 618
Cdd:PRK12467 1015 PDASAVQATFVAPQTELEKRLAAIWADVL----KVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQ 1088
                         650
                  ....*....|....*....
gi 557786167  619 ILEIYnhiLQTVVPDEDVT 637
Cdd:PRK12467 1089 TLAGF---AQAVAAQQQGA 1104
AMP-binding pfam00501
AMP-binding enzyme;
7-449 4.92e-39

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 150.16  E-value: 4.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    7 VHKAASCYMDRVAVCFDEcnnqlPVYYTYKTVVNAASELSNFLLLHcdfqGIRE---IGLYCQPGIDLPSWILGILQVPA 83
Cdd:pfam00501   1 LERQAARTPDKTALEVGE-----GRRLTYRELDERANRLAAGLRAL----GVGKgdrVAILLPNSPEWVVAFLACLKAGA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   84 AYVPIEPDSPPSLSTHFMKKCNLKYILV-EKKQINKFKSFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNlmlndgkeky 162
Cdd:pfam00501  72 VYVPLNPRLPAEELAYILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP---------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  163 ekekikSISSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL----FDITQEDVLFLAS 238
Cdd:pfam00501 142 ------ADVPPPPPPPPDPDD--------LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  239 PLTFDPSVV-EIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLA 316
Cdd:pfam00501 208 PLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLELI-ERYKVTVLYGVPTLLNMLlEAGAPKRALLS---SLRLVL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  317 LGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTLKCelpvqlGFPLLGTVVEVRD--TNGFTI 394
Cdd:pfam00501 284 SGGAPLPP-ELARRFR-ELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGSV------GRPLPGTEVKIVDdeTGEPVP 355
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167  395 QEGSGQVFLGGRNrV--CFLDD-----EVTVPLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKR 449
Cdd:pfam00501 356 PGEPGELCVRGPG-VmkGYLNDpeltaEAFDEDGWYR-TGDLGRRdEDGYLEIVGRKKDQIKL 416
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
552-608 7.50e-05

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 41.76  E-value: 7.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 552 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:COG0236    3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
557-608 3.92e-04

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: 39.08  E-value: 3.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557786167  557 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
735-830 2.25e-03

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 41.34  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 735 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 811
Cdd:COG1520    9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86
                         90
                 ....*....|....*....
gi 557786167 812 DRIesSACVSKCGNFIVVG 830
Cdd:COG1520   87 EPL--SGGVGADGGLVVVG 103
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
750-830 3.95e-03

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 40.30  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  750 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 829
Cdd:TIGR03300  35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110

                  .
gi 557786167  830 G 830
Cdd:TIGR03300 111 G 111
 
Name Accession Description Interval E-value
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
15-533 0e+00

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: 666.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  15 MDRVAVCFDEcnNQLPVYYTYKTVVNAASELSNFLLLHCDFqGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPP 94
Cdd:cd17654    1 PDRPALIIDQ--TTSDTTVSYADLAEKISNLSNFLRKKFQT-EERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  95 SLSTHFMKKCNLKYILVEKKQINKFKSFHetllnydtftvehndlvlfrlhwkntevnlmlndgkekyekekiksisseh 174
Cdd:cd17654   78 QRSLTVMKKCHVSYLLQNKELDNAPLSFT--------------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 175 vneeKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALS 254
Cdd:cd17654  107 ----PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 255 SGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGE 334
Cdd:cd17654  183 SGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGK 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 335 GNKTQIFNVYGITEVSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTNGFtiqEGSGQVFLGGRNRVCFLDD 414
Cdd:cd17654  263 GNRTRIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPLLGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDD 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 415 EVTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKdaSVK 494
Cdd:cd17654  332 EVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSS 409
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 557786167 495 EYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17654  410 SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
16-533 1.92e-98

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: 314.08  E-value: 1.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDecNNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd05930    2 DAVAVVDG--DQSL----TYAELDARANRLARYLRERGVGPGDL-VAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  96 LSTHFMKKCNLKYILVEkkqinkfksfhetllnydtftveHNDLvlfrlhwkntevnlmlndgkekyekekiksissehv 175
Cdd:cd05930   75 RLAYILEDSGAKLVLTD-----------------------PDDL------------------------------------ 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 176 neekaeehmdlrlkhclAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd05930   96 -----------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLA 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsatTSLRVLALGGEAFPSlTVLRSWRGEG 335
Cdd:cd05930  159 GATLVVLPEEVRKDPEALAD-LLAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLVGGEALPP-DLVRRWRELL 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 336 NKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN--RVCFL 412
Cdd:cd05930  233 PGARLVNLYGPTEATVDATYYRVPPDDEEDG-----RVPIGRPIPNTRVYVLDENLRPVPPGvPGELYIGGAGlaRGYLN 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DDEVT---------VPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYN---- 478
Cdd:cd05930  308 RPELTaerfvpnpfGPGERMYRTGDLVRWLpDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdgdg 387
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 479 QEKLILFMVSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05930  388 EKRLVAYVVPDEGGEldEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
68-474 8.51e-61

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: 211.74  E-value: 8.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   68 GIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEkkqinkfkSFHETLLNYDTFTVEHNDLVLfrlhwk 147
Cdd:TIGR01733  35 SAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD--------SALASRLAGLVLPVILLDPLE------ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  148 ntevNLMLNDGKekyekekiksiSSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD 227
Cdd:TIGR01733 101 ----LAALDDAP-----------APPPPDAPSGPDD--------LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  228 ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLrrfgsQLIKSTVLS 307
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL-----ALLAAALPP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  308 ATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVR 387
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDR-WRARGPGARLINLYGPTETTVWSTATLVDPDDAPR----ESPVPIGRPLANTRLYVL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  388 DTNGFTIQEG-------SG-QVFLG-----GRNRVCFLDDE-VTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGK 452
Cdd:TIGR01733 308 DDDLRPVPVGvvgelyiGGpGVARGylnrpELTAERFVPDPfAGGDGARLYRTGDLVRYlPDGNLEFLGRIDDQVKIRGY 387
                         410       420
                  ....*....|....*....|....
gi 557786167  453 RlnIEL--VQQVAEELQQVESCAV 474
Cdd:TIGR01733 388 R--IELgeIEAALLRHPGVREAVV 409
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2-475 2.60e-55

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: 208.17  E-value: 2.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    2 TLQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLhcdfQGIRE---IGLYCQPGIDLPSWILGI 78
Cdd:COG1020   477 TLHELFEAQAARTPDAVAVVFGD--QSL----TYAELNARANRLAHHLRA----LGVGPgdlVGVCLERSLEMVVALLAV 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   79 LQVPAAYVPIEPDSPPS-LstHFM-KKCNLKYILVEKKQINKFKSFHETLLNYDTFTVEHNDlvlfrlhwkntevnlmln 156
Cdd:COG1020   547 LKAGAAYVPLDPAYPAErL--AYMlEDAGARLVLTQSALAARLPELGVPVLALDALALAAEP------------------ 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  157 dgkekyEKEKIKSISSEHvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFL 236
Cdd:COG1020   607 ------ATNPPVPVTPDD-----------------LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ 663
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  237 ASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIkSTVLSATTSLRVLA 316
Cdd:COG1020   664 FASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL-ARHRVTVLNLTPSLLR----ALL-DAAPEALPSLRLVL 737
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  317 LGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGftiQ- 395
Cdd:COG1020   738 VGGEALP-PELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGG-----SVPIGRPIANTRVYVLDAHL---Qp 808
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  396 --EG-SGQVFLGG----------------RnrvcFLDDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRln 455
Cdd:COG1020   809 vpVGvPGELYIGGaglargylnrpeltaeR----FVADPFGFPGARLYRTGDLARWlPDGNLEFLGRADDQVKIRGFR-- 882
                         490       500
                  ....*....|....*....|..
gi 557786167  456 IEL--VQQVAEELQQVESCAVT 475
Cdd:COG1020   883 IELgeIEAALLQHPGVREAVVV 904
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
16-533 5.23e-50

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: 183.26  E-value: 5.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVcfdECNNQLpvyYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd12116    2 DATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDR-VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  96 LSTHFMKKCNLKYILVEkkqinkfksfhetllnydtftvehnDLVLFRLHWKNTEVNLMLNDGkekyekekiksisseHV 175
Cdd:cd12116   75 RLRYILEDAEPALVLTD-------------------------DALPDRLPAGLPVLLLALAAA---------------AA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 176 NEEKAEEHMDLRLkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd12116  115 APAAPRTPVSPDD---LAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLA 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLAlGGEAFPS-------LTVL 328
Cdd:cd12116  192 GARVVIAPRETQRDPEALAR-LIEAHSITVMQATPATWR-----MLLDAGWQGRAGLTALC-GGEALPPdlaarllSRVG 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 329 RSWrgegnktqifNVYGITEVSSWATIYRI-PEKTlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG- 405
Cdd:cd12116  265 SLW----------NLYGPTETTIWSTAARVtAAAG---------PIPIGRPLANTQVYVLDAALRPVPPGvPGELYIGGd 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 406 ------RNR-----VCFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12116  326 gvaqgyLGRpaltaERFVPDPFAGPGSRLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHR--IELgeIEAALAAHPGVAQ 403
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 472 CAVTWYNQE---KLILFMVSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12116  404 AAVVVREDGgdrRLVAYVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
192-533 5.71e-50

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: 182.83  E-value: 5.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:cd05945   99 NAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPK 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 KLASVLfSHHRVTVLQATPTLLRR-FGSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:cd05945  179 QLFRFL-AEHGITVWVSTPSFAAMcLLSPTFTPESLP---SLRHFLFCGEVLP-HKTARALQQRFPDARIYNTYGPTEAT 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 351 SWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG------GRNRVCFLDDEV 416
Cdd:cd05945  254 VAVTYIEVTPEVLDG----YDRLPIGYAKPGAKLVILDEDGRPVPPGekgelvisGPSVSKGylnnpeKTAAAFFPDEGQ 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 417 TVplgtmRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC-AVTWYNQEK---LILFMVSKDA 491
Cdd:cd05945  330 RA-----YRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAvVVPKYKGEKvteLIAFVVPKPG 404
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 557786167 492 S----VKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05945  405 AeaglTKA-IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
16-533 9.28e-50

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: 183.17  E-value: 9.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHcdfqGIRE---IGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd12117   12 DAVAVVYGDRS------LTYAELNERANRLARRLRAA----GVGPgdvVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  93 PPSLSTHFMKKCNLKyilvekkqinkfksfheTLLNYDTFTVEHNDLVLFRLHwkntevnlmLNDGKEKYEKEKIKSISS 172
Cdd:cd12117   82 PAERLAFMLADAGAK-----------------VLLTDRSLAGRAGGLEVAVVI---------DEALDAGPAGNPAVPVSP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 173 EHvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVpniqhfRVLFD-----ITQEDVLFLASPLTFDPSVV 247
Cdd:cd12117  136 DD-----------------LAYVMYTSGSTGRPKGVAVTHRGVV------RLVKNtnyvtLGPDDRVLQTSPLAFDASTF 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 248 EIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLALGGEAFPSLTV 327
Cdd:cd12117  193 EIWGALLNGARLVLAPKGTLLDPDALGALI-AEEGVTVLWLTAALFN-----QLADEDPECFAGLRELLTGGEVVSPPHV 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 328 lRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG- 405
Cdd:cd12117  267 -RRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEV-----AGSIPIGRPIANTRVYVLDEDGRPVPPGvPGELYVGGd 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 406 ------RNRVCfLDDEVTVPL-----GTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12117  341 glalgyLNRPA-LTAERFVADpfgpgERLYRTGDLARWLpDGRLEFLGRIDDQVKIRGFR--IELgeIEAALRAHPGVRE 417
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 472 CAVTWYNQE----KLILFMVSK----DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12117  418 AVVVVREDAggdkRLVAYVVAEgaldAAELRAF----LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
5-533 1.84e-49

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: 182.14  E-value: 1.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   5 ELVHKAASCYMDRVAVCFDecNNQLpvyyTYKTVVNAASELSNFLLLhcdfQGIRE---IGLYCQPGIDLPSWILGILQV 81
Cdd:cd17655    1 ELFEEQAEKTPDHTAVVFE--DQTL----TYRELNERANQLARTLRE----KGVGPdtiVGIMAERSLEMIVGILGILKA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  82 PAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKfKSFHETLLNYDTFTVEHNDlvlfrlhwkntevnlmlndgkek 161
Cdd:cd17655   71 GGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDLLDEDTIYHEE----------------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 162 yekekikSISSEHVNeeKAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT 241
Cdd:cd17655  127 -------SENLEPVS--KSDD---------LAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 242 FDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVlFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATTSLRVLALGGEA 321
Cdd:cd17655  189 FDASVTEIFASLLSGNTLYIVRKETVLDGQALTQY-IRQNRITIIDLTPAHL-----KLLDAADDSEGLSLKHLIVGGEA 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 322 FPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQ 400
Cdd:cd17655  263 LSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-----SVPIGKPLGNTRIYILDQYGRPQPVGVaGE 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 401 VFLGGR-------NR-----VCFLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQ 467
Cdd:cd17655  338 LYIGGEgvargylNRpeltaEKFVDDPF-VPGERMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557786167 468 QVESCAVTWY----NQEKLILFMVS-KDASVKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17655  417 DIKEAVVIARkdeqGQNYLCAYIVSeKELPVAQ-LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
PRK12467 PRK12467
peptide synthase; Provisional
6-637 1.28e-48

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 188.06  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    6 LVHKAASCYMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAY 85
Cdd:PRK12467  517 LIEAQARQHPERPALVFGE------QVLSYAELNRQANRLAHVLIAAGVGPDVL-VGIAVERSIEMVVGLLAVLKAGGAY 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   86 VPIEPDSPPSLSTHFMKKCNLKYILvekkqinkfksfhetllnydtftveHNDLVLFRLHWKNTEVNLMLNDGKEKYeke 165
Cdd:PRK12467  590 VPLDPEYPQDRLAYMLDDSGVRLLL-------------------------TQSHLLAQLPVPAGLRSLCLDEPADLL--- 641
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  166 kiksissehvnEEKAEEHMDLRLK-HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDP 244
Cdd:PRK12467  642 -----------CGYSGHNPEVALDpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDL 710
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  245 SVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAFPs 324
Cdd:PRK12467  711 GVTELFGALASGATLHLLPPDCARDAEAFAALM-ADQGVTVLKIVPSHLQ----ALLQASRVALPRPQRALVCGGEALQ- 784
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  325 LTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL 403
Cdd:PRK12467  785 VDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-----NVPIGQPLANLGLYILDHYLNPVPVGVvGELYI 859
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  404 GGR--------------NRvcFLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRL---NIELVQQVAEE 465
Cdd:PRK12467  860 GGAglargyhrrpaltaER--FVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIelgEIEARLLAQPG 937
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  466 LQQVESCAVTWYNQEKLILFMV-------SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiyl 538
Cdd:PRK12467  938 VREAVVLAQPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK--- 1014
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  539 NYINLKSENKLSGKEDLWEKLQYLWKSTLnlpeDLLRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVPglLEIILSSS 618
Cdd:PRK12467 1015 PDASAVQATFVAPQTELEKRLAAIWADVL----KVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQ 1088
                         650
                  ....*....|....*....
gi 557786167  619 ILEIYnhiLQTVVPDEDVT 637
Cdd:PRK12467 1089 TLAGF---AQAVAAQQQGA 1104
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
61-529 2.22e-48

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: 178.27  E-value: 2.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  61 IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPslsthfmkkcnlkyilvekkqinkfksfhetllnydtftvEHNDLV 140
Cdd:cd17643   40 VALALPRSAELIVALLAILKAGGAYVPIDPAYPV----------------------------------------ERIAFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 141 LfrlhwKNTEVNLMLNDGkekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQ 220
Cdd:cd17643   80 L-----ADSGPSLLLTDP-------------------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 221 HFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQL 300
Cdd:cd17643  124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLL-RDEGVTVLNQTPSAFYQLVEAA 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 301 IKSTvlSATTSLRVLALGGEAFPsLTVLRSWRG--EGNKTQIFNVYGITEVSSWATIYRIpektLNSTLKCELPVQLGFP 378
Cdd:cd17643  203 DRDG--RDPLALRYVIFGGEALE-AAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPL----DAADLPAAAASPIGRP 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 379 LLGTVVEVRDTNGFTIQEGS-GQVFLGG---------RNRVC---FLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKD 444
Cdd:cd17643  276 LPGLRVYVLDADGRPVPPGVvGELYVSGagvargylgRPELTaerFVANPFGGPGSRMYRTGDLARrLPDGELEYLGRAD 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 445 SQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLILFMVSKD------ASVKEYIfKELqkyLPSHAVPD 512
Cdd:cd17643  356 EQVKIRGFR--IELgeIEAALATHPSVRDAAVIVREDEpgdtRLVAYVVADDgaaadiAELRALL-KEL---LPDYMVPA 429
                        490
                 ....*....|....*..
gi 557786167 513 ELVLIDSLPFTSHGKID 529
Cdd:cd17643  430 RYVPLDALPLTVNGKLD 446
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
59-529 9.72e-44

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: 165.98  E-value: 9.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  59 REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKkqinkfksfhetllnydtftvEHND 138
Cdd:cd17651   46 DLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHP---------------------ALAG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 139 LVLFRLHWkntevnlmlndGKEKYEKEKIKSISSEHVNEEKAeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPN 218
Cdd:cd17651  105 ELAVELVA-----------VTLLDQPGAAAGADAEPDPALDA---------DDLAYVIYTSGSTGRPKGVVMPHRSLANL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 219 IQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRFGS 298
Cdd:cd17651  165 VAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWL-DEQRISRVFLPTVALRALAE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 299 QLIKSTVLSAttSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEvSSWATIYRIPektlNSTLKCELPVQLGFP 378
Cdd:cd17651  244 HGRPLGVRLA--ALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLP----GDPAAWPAPPPIGRP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 379 LLGTVVEVRDTNGFTIQEG-SGQVFLGG-------RNR-----VCFLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKD 444
Cdd:cd17651  317 IDNTRVYVLDAALRPVPPGvPGELYIGGaglargyLNRpeltaERFVPDPF-VPGARMYRTGDLARwLPDGELEFLGRAD 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 445 SQIKRHGKRlnIEL--VQQVAEELQQVESCAVT----WYNQEKLILFMVSKDASVK--EYIFKELQKYLPSHAVPDELVL 516
Cdd:cd17651  396 DQVKIRGFR--IELgeIEAALARHPGVREAVVLaredRPGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVL 473
                        490
                 ....*....|...
gi 557786167 517 IDSLPFTSHGKID 529
Cdd:cd17651  474 LDALPLTPNGKLD 486
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
187-538 1.14e-43

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: 164.60  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 187 RLKHCL----------AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-PSVVEIFLALSS 255
Cdd:COG0318   87 ELAYILedsgaralvtALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLA 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 256 GASLLIVPtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRfgsqLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRG 333
Cdd:COG0318  167 GATLVLLP---RFDPERVLE-LIERERVTVLFGVPTMLAR----LLRHPEFARYdlSSLRLVVSGGAPLPP-ELLERFEE 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 334 EGNkTQIFNVYGITEvSSWATIYRIPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG- 404
Cdd:COG0318  238 RFG-VRIVEGYGLTE-TSPVVTVNPEDPGE------RRPGSVGRPLPGVEVRIVDEDGRELPPGevgeivvrGPNVMKGy 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 405 ----GRNRVCFLDdevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNIEL--VQQVAEELQQVESCAVT-- 475
Cdd:COG0318  310 wndpEATAEAFRD-------GWLR-TGDLGRLdEDGYLYIVGRKKDMIISGG--ENVYPaeVEEVLAAHPGVAEAAVVgv 379
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 476 ----WynQEKLILFMVSKD---ASVKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYL 538
Cdd:COG0318  380 pdekW--GERVVAFVVLRPgaeLDAEE-LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
192-529 5.95e-43

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: 163.10  E-value: 5.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIvpTSVKLLP 270
Cdd:cd05918  108 AAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLQFASY-TFDVSILEIFTTLAAGGCLCI--PSEEDRL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVLfSHHRVTVLQATPTLLRrfgsqLIKstvLSATTSLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITEvs 350
Cdd:cd05918  185 NDLAGFI-NRLRVTWAFLTPSVAR-----LLD---PEDVPSLRTLVLGGEA-LTQSDVDTW---ADRVRLINAYGPAE-- 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 351 swATIYRipekTLNSTLKCELPVQLGFPLLGT--VVEVRDTN-----GFTiqegsGQVFLGG------------RNRVCF 411
Cdd:cd05918  250 --CTIAA----TVSPVVPSTDPRNIGRPLGATcwVVDPDNHDrlvpiGAV-----GELLIEGpilargylndpeKTAAAF 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 412 LDDEVTVPLGTMRA------TGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------VQQVAEELQQVESCAVT--- 475
Cdd:cd05918  319 IEDPAWLKQEGSGRgrrlyrTGDLVRyNPDGSLEYVGRKDTQVKIRGQR--VELgeiehhLRQSLPGAKEVVVEVVKpkd 396
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167 476 WYNQEKLILFMVSKDASVK-------------------EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05918  397 GSSSPQLVAFVVLDGSSSGsgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKID 469
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
192-529 3.60e-42

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: 157.06  E-value: 3.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvKLLPS 271
Cdd:cd04433    2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 KLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVS 350
Cdd:cd04433   79 AALE-LIEREKVTILLGVPTLLARLLKAPeSAGYDLS---SLRALVSGGAPLPP-ELLERFE-EAPGIKLVNGYGLTETG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 351 SWATIYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVcFLDDEVTVPlGT 422
Cdd:cd04433  153 GTVATGPPDDDA-------RKPGSVGRPVPGVEVRIVDPDGGELPPGeigelvvrGPSVMKGYWNNP-EATAAVDED-GW 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 423 MRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIEL--VQQVAEELQQVESCAV------TWynQEKLILFMVSKDAS- 492
Cdd:cd04433  224 YR-TGDLGRLdEDGYLYIVGRLKDMIKSGGE--NVYPaeVEAVLLGHPGVAEAAVvgvpdpEW--GERVVAVVVLRPGAd 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 557786167 493 -----VKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd04433  299 ldaeeLRAH----VRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
5-533 1.65e-41

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: 157.86  E-value: 1.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   5 ELVHKAASCYMDRVAVcfDECNNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAA 84
Cdd:cd17653    1 DAFERIAAAHPDAVAV--ESLGGSL----TYGELDAASNALANRLLQLGVVPGDV-VPLLSDRSLEMLVAILAILKAGAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  85 YVPIEPDSPPSLSTHFMKKCNLKYILVEKKQinkfksfhetllnydtftvehndlvlfrlhwkntevnlmlndgkekyek 164
Cdd:cd17653   74 YVPLDAKLPSARIQAILRTSGATLLLTTDSP------------------------------------------------- 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 165 ekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFD 243
Cdd:cd17653  105 -------------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrVAQVLSI-AFD 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 244 PSVVEIFLALSSGASLLIVPTSvkllpSKLASVLFShhrVTVLQATPTLLrrfgsqliksTVLSATT--SLRVLALGGEA 321
Cdd:cd17653  159 ACIGEIFSTLCNGGTLVLADPS-----DPFAHVART---VDALMSTPSIL----------STLSPQDfpNLKTIFLGGEA 220
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 322 fPSLTVLRSWRGEgnkTQIFNVYGITEVSSWATIYRI-PEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SG 399
Cdd:cd17653  221 -VPPSLLDRWSPG---RRLYNAYGPTECTISSTMTELlPGQ----------PVTIGKPIPNSTCYILDADLQPVPEGvVG 286
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 400 QVFLGG------------RNRVCFLDDEVtVPLGTMRATGD--FVTvKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEE 465
Cdd:cd17653  287 EICISGvqvargylgnpaLTASKFVPDPF-WPGSRMYRTGDygRWT-EDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ 364
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786167 466 LQQVESCAVTWYNQEKLILFMVSKDASVkEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17653  365 SQPEVTQAAAIVVNGRLVAFVTPETVDV-DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
16-533 2.49e-41

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: 158.59  E-value: 2.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHcdfqGIREIGLYcqpGIDLP-SW-----ILGILQVPAAYVPIE 89
Cdd:cd12114    2 DATAVICGDGT------LTYGELAERARRVAGALKAA----GVRPGDLV---AVTLPkGPeqvvaVLGILAAGAAYVPVD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  90 PDSPPSLSTHFMKKCNLKYILVEKkqinkfksfHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDgkekyekekiks 169
Cdd:cd12114   69 IDQPAARREAILADAGARLVLTDG---------PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDD------------ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 170 issehvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEI 249
Cdd:cd12114  128 ----------------------LAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDI 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 250 FLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPsLT 326
Cdd:cd12114  186 FGALSAGATLVLPDEARRRDPAHWAELI-ERHGVTLWNSVPALL-----EMLLDVLEAAQAllpSLRLVLLSGDWIP-LD 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 327 VLRSWRGEGNKTQIFNVYGITEVSSWATIYRI--PEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFL 403
Cdd:cd12114  259 LPARLRALAPDARLISLGGATEASIWSIYHPIdeVPPDWRS-------IPYGRPLANQRYRVLDPRGRDCPDWvPGELWI 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 404 GGRN--RVCFLDDEVT----VPLGTMRA---TGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12114  332 GGRGvaLGYLGDPELTaarfVTHPDGERlyrTGDLGRYRpDGTLEFLGRRDGQVKVRGYR--IELgeIEAALQAHPGVAR 409
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557786167 472 CAVTWY---NQEKLILFMVSKD-------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12114  410 AVVVVLgdpGGKRLAAFVVPDNdgtpiapDALRAF----LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
61-533 7.83e-41

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: 156.32  E-value: 7.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  61 IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLsthfmkkcnLKYILvekkqinkfksfhetllnydtftvehndlv 140
Cdd:cd12115   52 VGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER---------LRFIL------------------------------ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 141 lfrlhwKNTEVNLMLNDGkekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQ 220
Cdd:cd12115   93 ------EDAQARLVLTDP-------------------------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 221 HFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPSklasvLFSHHRVTVLQATPTLLRrfgsQL 300
Cdd:cd12115  136 WAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-DNVLALPD-----LPAAAEVTLINTVPSAAA----EL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 301 IKSTVLSatTSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcelPVQLGFPLL 380
Cdd:cd12115  206 LRHDALP--ASVRVVNLAGEPLPR-DLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASG-------EVSIGRPLA 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 381 GTVVEVRDTNGFTIQEG-SGQVFLGGRN-RVCFLDDE-------VTVPLGT---MRATGDFVTVK-DGEIFFLGRKDSQI 447
Cdd:cd12115  276 NTQAYVLDRALQPVPLGvPGELYIGGAGvARGYLGRPgltaerfLPDPFGPgarLYRTGDLVRWRpDGLLEFLGRADNQV 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 448 KRHGKRLNIELVQQVAEELQQV-ESCAVTW---YNQEKLILFMVSKD--ASVKEYIFKELQKYLPSHAVPDELVLIDSLP 521
Cdd:cd12115  356 KVRGFRIELGEIEAALRSIPGVrEAVVVAIgdaAGERRLVAYIVAEPgaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALP 435
                        490
                 ....*....|..
gi 557786167 522 FTSHGKIDVSEL 533
Cdd:cd12115  436 LTPNGKIDRSAL 447
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
192-533 1.14e-40

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: 156.67  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:cd17646  140 LAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 KLASvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITE--- 348
Cdd:cd17646  220 YLAA-LIREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEaai 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 -VSSWAtiYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRVC-----FLDD 414
Cdd:cd17646  293 dVTHWP--VRGPAET--------PSVPIGRPVPNTRLYVLDDALRPVPVGvPGELYLGGVqlargylGRPAltaerFVPD 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 415 evtvPLGT---MRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFM 486
Cdd:cd17646  363 ----PFGPgsrMYRTGDLARWRpDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApagaARLVGYV 438
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557786167 487 VSK-------DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17646  439 VPAagaagpdTAALRAH----LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
192-533 3.50e-40

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: 153.95  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:cd17652   95 LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVLQFASP-SFDASVWELLMALLAGATLVLAPAEELLPG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVLfSHHRVTVLQATPTLLRrfgsqlikstVLSATT--SLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITE 348
Cdd:cd17652  174 EPLADLL-REHRITHVTLPPAALA----------ALPPDDlpDLRTLVVAGEA-CPAELVDRW---APGRRMINAYGPTE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 VSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTN------GFTiqegsGQVFLGGR-------NR-----VC 410
Cdd:cd17652  239 TTVCATMAGPLPG--------GGVPPIGRPVPGTRVYVLDARlrpvppGVP-----GELYIAGAglargylNRpgltaER 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 411 FLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLI 483
Cdd:cd17652  306 FVADPFGAPGSRMYRTGDLARwRADGQLEFLGRADDQVKIRGFR--IELgeVEAALTEHPGVAEAVVVVRDDRpgdkRLV 383
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 557786167 484 LFMV--SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17652  384 AYVVpaPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
AMP-binding pfam00501
AMP-binding enzyme;
7-449 4.92e-39

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 150.16  E-value: 4.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    7 VHKAASCYMDRVAVCFDEcnnqlPVYYTYKTVVNAASELSNFLLLHcdfqGIRE---IGLYCQPGIDLPSWILGILQVPA 83
Cdd:pfam00501   1 LERQAARTPDKTALEVGE-----GRRLTYRELDERANRLAAGLRAL----GVGKgdrVAILLPNSPEWVVAFLACLKAGA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   84 AYVPIEPDSPPSLSTHFMKKCNLKYILV-EKKQINKFKSFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNlmlndgkeky 162
Cdd:pfam00501  72 VYVPLNPRLPAEELAYILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP---------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  163 ekekikSISSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL----FDITQEDVLFLAS 238
Cdd:pfam00501 142 ------ADVPPPPPPPPDPDD--------LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  239 PLTFDPSVV-EIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLA 316
Cdd:pfam00501 208 PLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLELI-ERYKVTVLYGVPTLLNMLlEAGAPKRALLS---SLRLVL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  317 LGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTLKCelpvqlGFPLLGTVVEVRD--TNGFTI 394
Cdd:pfam00501 284 SGGAPLPP-ELARRFR-ELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGSV------GRPLPGTEVKIVDdeTGEPVP 355
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167  395 QEGSGQVFLGGRNrV--CFLDD-----EVTVPLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKR 449
Cdd:pfam00501 356 PGEPGELCVRGPG-VmkGYLNDpeltaEAFDEDGWYR-TGDLGRRdEDGYLEIVGRKKDQIKL 416
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
16-529 2.58e-38

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: 149.06  E-value: 2.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDECnnqlpvYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd17649    2 DAVALVFGDQ------SLSYAELDARANRLAHRLRALGVGPEVR-VGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  96 lsthfmkkcnlkyilvekkqinkfksfhetllnydtftvehndlvlfRLHWkntevnlMLNDGKEKYekekiksISSEHv 175
Cdd:cd17649   75 -----------------------------------------------RLRY-------MLEDSGAGL-------LLTHH- 92
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 176 neekaeehmdlrlKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd17649   93 -------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLIC 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFgSQLIKSTVLSATTSLRVLALGGEAfpsLTVLRSWRGEG 335
Cdd:cd17649  160 GACVVLRPDELWASADELAE-MVRELGVTVLDLPPAYLQQL-AEEADRTGDGRPPSLRLYIFGGEA---LSPELLRRWLK 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 336 NKTQIFNVYGITEVSSWATIYRIPEKtlNSTLKCELPvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------N 407
Cdd:cd17649  235 APVRLFNAYGPTEATVTPLVWKCEAG--AARAGASMP--IGRPLGGRSAYILDADLNPVPVGvTGELYIGGEglargylG 310
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 408 RVC-----FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYN 478
Cdd:cd17649  311 RPEltaerFVPDPFGAPGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVvalDGAG 390
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 479 QEKLILFMVSKDASV----KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17649  391 GKQLVAYVVLRAAAAqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
16-529 6.89e-38

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: 147.97  E-value: 6.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFdeCNNQLpvyyTYKTVVNAASELSNFLllhcDFQGIRE---IGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd17644   15 DAVAVVF--EDQQL----TYEELNTKANQLAHYL----QSLGVKSeslVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  93 PPSlsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDGkekyekekiksiss 172
Cdd:cd17644   85 PQE---------RLTYIL------------------------------------EDAQISVLLTQP-------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 173 ehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA 252
Cdd:cd17644  106 -----------------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVT 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 253 LSSGASLLIVPTsvKLLPSKLASVLFSHH-RVTVLQATPTLLRRFGSQLIKSTvLSATTSLRVLALGGEAF-PSLtvLRS 330
Cdd:cd17644  169 LLSGATLVLRPE--EMRSSLEDFVQYIQQwQLTVLSLPPAYWHLLVLELLLST-IDLPSSLRLVIVGGEAVqPEL--VRQ 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 331 WR-GEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-- 406
Cdd:cd17644  244 WQkNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITS----VPIGRPIANTQVYILDENLQPVPVGvPGELHIGGVgl 319
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 407 -----NRvcfldDEVTV-----------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQV 469
Cdd:cd17644  320 argylNR-----PELTAekfishpfnssESERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786167 470 ESCAVT----WYNQEKLILFMVSKdaSVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17644  395 KTAVVIvredQPGNKRLVAYIVPH--YEESPSTVELRQFlkakLPDYMIPSAFVVLEELPLTPNGKID 460
PRK12316 PRK12316
peptide synthase; Provisional
46-597 7.21e-38

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 154.34  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   46 SNFLLLHCDFQGI---REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSlsthfmkkcNLKYILvEKKQINkfksf 122
Cdd:PRK12316  546 ANRLAHALIERGVgpdVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE---------RLAYML-EDSGVQ----- 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  123 hetLLNYDTFTVEHNDLvlfrlhwkNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKaeehmdlrlkhcLAYVLHTSGTT 202
Cdd:PRK12316  611 ---LLLSQSHLGRKLPL--------AAGVQVLDLDRPAAWLEGYSEENPGTELNPEN------------LAYVIYTSGST 667
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  203 GIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASvLFSHHR 282
Cdd:PRK12316  668 GKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREG 746
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  283 VTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWrGEGNKTQIFNVYGITEVSSWATIYripekT 362
Cdd:PRK12316  747 VDTLHFVPSMLQAF----LQDEDVASCTSLRRIVCSGEALPADAQEQVF-AKLPQAGLYNLYGPTEAAIDVTHW-----T 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  363 LNSTLKCELPVqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN------RVCFLDDE--VTVPLGT---MRATGDFV 430
Cdd:PRK12316  817 CVEEGGDSVPI--GRPIANLACYILDANLEPVPVGvLGELYLAGRGlargyhGRPGLTAErfVPSPFVAgerMYRTGDLA 894
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  431 TVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKD--ASVKEYIFKELQKYLPS 507
Cdd:PRK12316  895 RYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESegGDWREALKAHLAASLPE 974
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  508 HAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGG 587
Cdd:PRK12316  975 YMVPAQWLALERLPLTPNGKLDRKALPAP---EASVAQQGYVAPRNALERTLAAIWQDVLGVE----RVGLDDNFFELGG 1047
                         570
                  ....*....|
gi 557786167  588 DSLKSIRLLS 597
Cdd:PRK12316 1048 DSIVSIQVVS 1057
PRK12467 PRK12467
peptide synthase; Provisional
192-597 8.40e-38

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 153.78  E-value: 8.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:PRK12467 1720 LAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPE 1799
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  272 KLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE--- 348
Cdd:PRK12467 1800 QLIQLI-ERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVCGGEALE-VEALRPWLERLPDTGLFNLYGPTEtav 1874
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  349 -VSSWATIYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEgSGQVFLGG-------RNRVC-----FLDDE 415
Cdd:PRK12467 1875 dVTHWTCRRKDLEGRDSV------PIGQPIANLSTYILDASLNPVPIGV-AGELYLGGvglargyLNRPAltaerFVADP 1947
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  416 VTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQVAEELQQ--VESCAVT---WYNQEKLILFMVSK 489
Cdd:PRK12467 1948 FGTVGSRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEIEARLREQggVREAVVIaqdGANGKQLVAYVVPT 2025
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  490 DASVKEY---------IFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKI--------DVSELNKIYlnyinlksenkLSG 551
Cdd:PRK12467 2026 DPGLVDDdeaqvalraILKNhLKASLPEYMVPAHLVFLARMPLTPNGKLdrkalpapDASELQQAY-----------VAP 2094
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 557786167  552 KEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12467 2095 QSELEQRLAAIWQDVLGLE----QVGLHDNFFELGGDSIISIQVVS 2136
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
192-533 8.95e-38

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: 147.55  E-value: 8.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED---VLFLASpLTFDPSVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd17648   96 LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeaVLFFSN-YVFDFFVEQMTLALLNGQKLVVPPDEMRF 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLASvLFSHHRVTVLQATPTLLRRFGsqlikstvLSATTSLRVLALGGEAF--PSLTVLRSwrgeGNKTQIFNVYGI 346
Cdd:cd17648  175 DPDRFYA-YINREKVTYLSGTPSVLQQYD--------LARLPHLKRVDAAGEEFtaPVFEKLRS----RFAGLIINAYGP 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSSWATIYRIP--EKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG-------RNRvcfldDEV 416
Cdd:cd17648  242 TETTVTNHKRFFPgdQRFDKS---------LGRPVRNTKCYVLNDAMKRVPVGAvGELYLGGdgvargyLNR-----PEL 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 417 T----VP-------------LGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---- 474
Cdd:cd17648  308 TaerfLPnpfqteqerargrNARLYKTGDLVRwLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvake 387
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 475 -----TWYNQEKLILFMVSKDASVKEY-IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17648  388 dasqaQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
PRK12316 PRK12316
peptide synthase; Provisional
3-608 2.73e-35

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 145.87  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    3 LQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVP 82
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVVFDE--EKL----TYAELNRRANRLAHALIARGVGPEVL-VGIAMERSAEMMVGLLAVLKAG 4625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   83 AAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKF---KSFHETLLNYD---TFTVEHNDLVlfRLHWKNtevnlmln 156
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipDGLASLALDRDedwEGFPAHDPAV--RLHPDN-------- 4695
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  157 dgkekyekekiksissehvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFL 236
Cdd:PRK12316 4696 -----------------------------------LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQ 4740
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  237 ASPLTFDPSVVEIFLALSSGASLLIVPTSVKlLPSKLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLA 316
Cdd:PRK12316 4741 FMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEI-HEHRVTVLVFPPVYLQQL---AEHAERDGEPPSLRVYC 4815
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  317 LGGEAFPSLTVLRSWRGEGNkTQIFNVYGITEVSSWATIYripeKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQE 396
Cdd:PRK12316 4816 FGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLW----KARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPV 4890
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  397 G-SGQVFLGGR--------------NRvcFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLnielvq 460
Cdd:PRK12316 4891 GvAGELYLGGEgvargylerpaltaER--FVPDPFGAPGGRLYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRI------ 4962
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  461 qvaeELQQVESC-------------AVTWYNQEKLILFMVSKDASVKEYIFKE----------LQKYLPSHAVPDELVLI 517
Cdd:PRK12316 4963 ----ELGEIEARlrehpavreavviAQEGAVGKQLVGYVVPQDPALADADEAQaelrdelkaaLRERLPEYMVPAHLVFL 5038
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  518 DSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12316 5039 ARMPLTPNGKLDRKALPQP---DASLLQQAYVAPRSELEQQVAAIWAEVLQLE----RVGLDDNFFELGGHSLLAIQVTS 5111
                         650
                  ....*....|.
gi 557786167  598 EIEKLVGTSVP 608
Cdd:PRK12316 5112 RIQLELGLELP 5122
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
192-529 3.02e-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: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 137.19  E-value: 3.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVklLPS 271
Cdd:cd05922  119 LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV--LDD 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 KLASvLFSHHRVTVLQATPT---LLRRFGSQLIKstvlsaTTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05922  197 AFWE-DLREHGATGLAGVPStyaMLTRLGFDPAK------LPSLRYLTQAGGRLPQETI-ARLRELLPGAQVYVMYGQTE 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 VSSWATiYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVpl 420
Cdd:cd05922  269 ATRRMT-YLPPERILEK------PGSIGLAIPGGEFEILDDDGTPTPPGepgeivhrGPNVMKGYWNDPPYRRKEGRG-- 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 421 GTMRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVT---WYNQEKLILFMVSKDASVKEY 496
Cdd:cd05922  340 GGVLHTGDLaRRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglpDPLGEKLALFVTAPDKIDPKD 419
                        330       340       350
                 ....*....|....*....|....*....|...
gi 557786167 497 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05922  420 VLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
PRK12316 PRK12316
peptide synthase; Provisional
59-597 7.01e-34

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 141.25  E-value: 7.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   59 REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILvekkqinkfksfhetllnydtfTVEHnd 138
Cdd:PRK12316 3108 VLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL----------------------SQSH-- 3163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  139 lvlFRLHWKNTEVNLMLNDGKekyekekiksissehvnEEKAEEHMDLR-LKHCLAYVLHTSGTTGIPKIVRVPHKCIVP 217
Cdd:PRK12316 3164 ---LRLPLAQGVQVLDLDRGD-----------------ENYAEANPAIRtMPENLAYVIYTSGSTGKPKGVGIRHSALSN 3223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  218 NIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFShHRVTVLQATPTLLRRFg 297
Cdd:PRK12316 3224 HLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINS-EGVDVLHAYPSMLQAF- 3301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  298 sqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEgnktQIFNVYGITEVSSWATIYRIPEKTlnstlkcELPVQLGF 377
Cdd:PRK12316 3302 ---LEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL----PLYNLYGPTEATITVTHWQCVEEG-------KDAVPIGR 3367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  378 PLLGTVVEVRDTNGFTIQEGS-GQVFLGGRN--RVCFLDDEVT---------VPLGTMRATGDFVTVK-DGEIFFLGRKD 444
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGAlGELYLGGEGlaRGYHNRPGLTaerfvpdpfVPGERLYRTGDLARYRaDGVIEYIGRVD 3447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  445 SQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPF 522
Cdd:PRK12316 3448 HQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAgdLREALKAHLKASLPEYMVPAHLLFLERMPL 3527
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167  523 TSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12316 3528 TPNGKLDRKALPRP---DAALLQQDYVAPVNELERRLAAIWADVLKLE----QVGLTDNFFELGGDSIISLQVVS 3595
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
190-607 4.42e-33

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 138.25  E-value: 4.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  190 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLL 269
Cdd:PRK10252  598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRD 677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  270 PSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRGEGNkTQIFNVYGITE- 348
Cdd:PRK10252  678 PLAMQQ-FFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPA-DLCREWQQLTG-APLHNLYGPTEa 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  349 ---VSSWATiyrIPEKTLNSTlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR--------------NRvc 410
Cdd:PRK10252  755 avdVSWYPA---FGEELAAVR---GSSVPIGYPVWNTGLRILDARMRPVPPGvAGDLYLTGIqlaqgylgrpdltaSR-- 826
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  411 FLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------------VQQVAEELQQVESCAVTWY 477
Cdd:PRK10252  827 FIADPF-APGERMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQR--IELgeidramqalpdVEQAVTHACVINQAAATGG 903
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  478 NQEKLILFMVSKD------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylnyINLKSENKLSG 551
Cdd:PRK10252  904 DARQLVGYLVSQSglpldtSALQAQ----LRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL-----PELKAQVPGRA 974
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167  552 KEDLWEK-LQYLWKSTLNLPEdllrVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSV 607
Cdd:PRK10252  975 PKTGTETiIAAAFSSLLGCDV----VDADADFFALGGHSLLAMKLAAQLSRQFARQV 1027
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
16-529 1.02e-32

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: 132.29  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFdecNNQlpvYYTYKTVVNAASELSNfLLLHCDFQGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd17645   13 DHVAVVD---RGQ---SLTYKQLNEKANQLAR-HLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  96 lsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDgkekyekekiksissehv 175
Cdd:cd17645   86 ---------RIAYML------------------------------------ADSSAKILLTN------------------ 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 176 neekAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd17645  103 ----PDD---------LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTA 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVlQATPTllrrfgsQLIKSTVLSATTSLRVLALGGEafpsltVLRswRGEG 335
Cdd:cd17645  170 GAALHVVPSERRLDLDALND-YFNQEGITI-SFLPT-------GAAEQFMQLDNQSLRVLLTGGD------KLK--KIER 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 336 NKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------N 407
Cdd:cd17645  233 KGYKLVNNYGPTENTVVATSFEIDKPYAN--------IPIGKPIDNTRVYILDEALQLQPIGvAGELCIAGEglargylN 304
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 408 RvcfldDEVT---------VPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY 477
Cdd:cd17645  305 R-----PELTaekfivhpfVPGERMYRTGDLAKfLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK 379
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557786167 478 NQEK----LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17645  380 EDADgrkyLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
PRK05691 PRK05691
peptide synthase; Validated
2-597 7.53e-31

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 131.44  E-value: 7.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    2 TLQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLlHCDFQGIREIGLYCQPGIDLPSWILGILQV 81
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVWDG--GSL----DYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKA 1204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   82 PAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKkqinkfkSFHETLLNYDTFTVehndLVLFRLH---WKNTEVNLMLNDg 158
Cdd:PRK05691 1205 GGAYVPLDPDYPAERLAYMLADSGVELLLTQS-------HLLERLPQAEGVSA----IALDSLHldsWPSQAPGLHLHG- 1272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  159 kekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLAS 238
Cdd:PRK05691 1273 -------------------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKA 1321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  239 PLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHrVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALG 318
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYG-VTTLHFVPPLLQLF----IDEPLAAACTSLRRLFSG 1396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  319 GEAFPS------LTVLrswrgegNKTQIFNVYGITEVSSWATIYRIP-EKTLNStlkcelPVqlGFPLLGTVVEVRDTNG 391
Cdd:PRK05691 1397 GEALPAelrnrvLQRL-------PQVQLHNRYGPTETAINVTHWQCQaEDGERS------PI--GRPLGNVLCRVLDAEL 1461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  392 FTIQEG-SGQVFLGGR-------NRVCFLDDE-VTVPLGTMRA----TGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIE 457
Cdd:PRK05691 1462 NLLPPGvAGELCIGGAglargylGRPALTAERfVPDPLGEDGArlyrTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPE 1541
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  458 LVQQVAEELQQVESCAV---TWYNQEKLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSE 532
Cdd:PRK05691 1542 EIQARLLAQPGVAQAAVlvrEGAAGAQLVGYYTGEAGQeaEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRA 1621
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167  533 LNKiylnyINLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRvpDEslFLNSGGDSLKSIRLLS 597
Cdd:PRK05691 1622 LPE-----PVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLR--DD--FFALGGHSLLATQIVS 1677
PRK12467 PRK12467
peptide synthase; Provisional
3-608 9.90e-31

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 131.05  E-value: 9.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    3 LQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLH---CDfqgiREIGLYCQPGIDLPSWILGIL 79
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGD--QQL----SYAELNRRANRLAHRLIAIgvgPD----VLVGVAVERSVEMIVALLAVL 3166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   80 QVPAAYVPIEPDSPPSlsthfmkkcNLKYILVEkkqinkfkSFHETLLnydtfTVEHndlVLFRLHWKNTEVNLMLNDGK 159
Cdd:PRK12467 3167 KAGGAYVPLDPEYPRE---------RLAYMIED--------SGVKLLL-----TQAH---LLEQLPAPAGDTALTLDRLD 3221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  160 EKYEKEKIKSISSEHVNeekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASP 239
Cdd:PRK12467 3222 LNGYSENNPSTRVMGEN---------------LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS 3286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  240 LTFDPSVVEIFLALSSGASLLIVPTSVKlLPSKLASVLFSHHrVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGG 319
Cdd:PRK12467 3287 FSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHR-ISIACFPPAYLQ----QFAEDAGGADCASLDIYVFGG 3360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  320 EAFPSLTVLRSWRGEGNKtQIFNVYGITEVSSWATIYRIPektlnSTLKCELP-VQLGFPLLGTVVEVRDTNGFTIQEG- 397
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTLWKCG-----GDAVCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGv 3434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  398 SGQVFLGGrnrVC---------------FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQ 461
Cdd:PRK12467 3435 AGELYIGG---VGlargyhqrpsltaerFVADPFSGSGGRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEI 3509
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  462 VAEELQQ--VESCAVTWYNQE---KLILFMVSKD--ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELN 534
Cdd:PRK12467 3510 EARLLQHpsVREAVVLARDGAggkQLVAYVVPADpqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALP 3589
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167  535 KIYLNyinlKSENKLSGKEDLWEKLQYLWkstlnlpEDLLRVPDESL---FLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK12467 3590 DPDAK----GSREYVAPRSEVEQQLAAIW-------ADVLGVEQVGVtdnFFELGGDSLLALQVLSRIRQSLGLKLS 3655
PRK12316 PRK12316
peptide synthase; Provisional
4-608 3.37e-30

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 129.69  E-value: 3.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167    4 QELVHKAASCyMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPA 83
Cdd:PRK12316 2007 QRIAEQAARA-PEAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVR-VAIAAERSFELVVALLAVLKAGG 2078
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   84 AYVPIEPDSPPSLSTHFMKKCNLKYILVEKKqinkfksfhetllnydtftvehndlVLFRLHWKNTEVNLMLNDgkekye 163
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRH-------------------------LLERLPLPAGVARLPLDR------ 2127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  164 KEKIKSISSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD 243
Cdd:PRK12316 2128 DAEWADYPDTAPAVQLAGEN--------LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD 2199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  244 PSVVEIFLALSSGASLLIVPTSVKLlPSKLASVLfSHHRVTVLQATPTLLRRFGSQLiksTVLSATTSLRVLALGGEAFP 323
Cdd:PRK12316 2200 GAHEQWFHPLLNGARVLIRDDELWD-PEQLYDEM-ERHGVTILDFPPVYLQQLAEHA---ERDGRPPAVRVYCFGGEAVP 2274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  324 SLTVLRSWRGEGnKTQIFNVYGITEVSSWATIYripektlnstlKC--ELPVQLGFPLLGTVVEVRDT----NGFTI--Q 395
Cdd:PRK12316 2275 AASLRLAWEALR-PVYLFNGYGPTEAVVTPLLW-----------KCrpQDPCGAAYVPIGRALGNRRAyildADLNLlaP 2342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  396 EGSGQVFLGGR-------NRVC-----FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQV 462
Cdd:PRK12316 2343 GMAGELYLGGEglargylNRPGltaerFVPDPFSASGERLYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEAR 2422
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  463 AEELQQVESCAVTwyNQE-----KLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK12316 2423 LQAHPAVREAVVV--AQDgasgkQLVAYVVPDDAAedLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167  536 IYLnyiNLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK12316 2501 PDV---SQLRQAYVAPQEGLEQRLAAIWQAVLKVE----QVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVP 2566
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
192-533 3.96e-30

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


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 124.50  E-value: 3.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKcivpNIQHF------RVLFDITQEDVLFLASpLTFDPSVVEIFLALSSGASLLIVPTS 265
Cdd:cd17650   95 LAYVIYTSGTTGKPKGVMVEHR----NVAHAahawrrEYELDSFPVRLLQMAS-FSFDVFAGDFARSLLNGGTLVICPDE 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 266 VKLLPSKLASVLFShHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYG 345
Cdd:cd17650  170 VKLDPAALYDLILK-SRITLMESTPALIRPVMAYVYRNGL--DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYG 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 346 ITEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRNrVC-------------F 411
Cdd:cd17650  247 VTEATIDSTYYEEGRDPLGDSAN----VPIGRPLPNTAMYVLDERLQPQPVGvAGELYIGGAG-VArgylnrpeltaerF 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 412 LDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY---NQEK-LILFM 486
Cdd:cd17650  322 VENPF-APGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRedkGGEArLCAYV 400
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557786167 487 VSKD----ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17650  401 VAAAtlntAELRAF----LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
16-533 4.11e-30

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: 125.28  E-value: 4.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLhcdfQGI---REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd17656    3 DAVAVVFENQK------LTYRELNERSNQLARFLRE----KGVkkdSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  93 PPSLSTHFMKKCNLKYILVEKKQINKFK-SFHETLLNYDTFTVEhndlvlfrlhwkntevnlmlndgkekyekekiksiS 171
Cdd:cd17656   73 PEERRIYIMLDSGVRVVLTQRHLKSKLSfNKSTILLEDPSISQE-----------------------------------D 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 172 SEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIF 250
Cdd:cd17656  118 TSNIDYINNSDD--------LLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDkVLQFATC-SFDVCYQEIF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 251 LALSSGASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEAFPSLTVLRS 330
Cdd:cd17656  189 STLLSGGTLYIIREETKRDVEQLFD-LVKRHNIEVVFLPVAFLKFIFSE--REFINRFPTCVKHIITAGEQLVITNEFKE 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 331 WRGEGNKTqIFNVYGITEvSSWATIYRI-PEKTLNstlkcELPvQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRN- 407
Cdd:cd17656  266 MLHEHNVH-LHNHYGPSE-THVVTTYTInPEAEIP-----ELP-PIGKPISNTWIYILDQEQQLQPQGIvGELYISGASv 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 408 -RVCFLDDEVTV---------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV-T 475
Cdd:cd17656  338 aRGYLNRQELTAekffpdpfdPNERMYRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVlD 417
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557786167 476 WYNQEK---LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17656  418 KADDKGekyLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
194-535 1.90e-27

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 117.30  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 194 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLA-SPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSK 272
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL-PEGPQFLNqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQ 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 273 LASVLFSHHrVTVLQATPT------LLRRFGSQLIkstvlsatTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGI 346
Cdd:PRK04813 226 LFETLPQLP-INVWVSTPSfadmclLDPSFNEEHL--------PNLTHFLFCGEELPHKTA-KKLLERFPSATIYNTYGP 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSSWATIYRIPEKTLNstlKCE-LPVqlGFPLLGTVVEVRDTNG---FTIQEG----SGQ-VFLGgrnrvcFLD---- 413
Cdd:PRK04813 296 TEATVAVTSIEITDEMLD---QYKrLPI--GYAKPDSPLLIIDEEGtklPDGEQGeiviSGPsVSKG------YLNnpek 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 414 -DEVTVPLGTMRA--TGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFM 486
Cdd:PRK04813 365 tAEAFFTFDGQPAyhTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqYLIAYV 444
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 557786167 487 VSKDASV-KEY-----IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDV----SELNK 535
Cdd:PRK04813 445 VPKEEDFeREFeltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRkaliEEVNK 503
PRK05691 PRK05691
peptide synthase; Validated
186-597 1.40e-22

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 104.87  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  186 LRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASllIVPTS 265
Cdd:PRK05691 2329 LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGAR--VVLRA 2406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  266 VKLLPSKLASVLFSHHRVTVLQATPTllrrFGSQLIKSTVLS-ATTSLRVLALGGEAfpsLTV--LRSWRGEGNKTQIFN 342
Cdd:PRK05691 2407 QGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWLAGQgEQLPVRMCITGGEA---LTGehLQRIRQAFAPQLFFN 2479
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  343 VYGITEVSSWATIYRIPEKtlnstlkceLPVQLGFPLLGTVVEVR-----DTN-GFTIQEGSGQVFLGGR---------- 406
Cdd:PRK05691 2480 AYGPTETVVMPLACLAPEQ---------LEEGAASVPIGRVVGARvayilDADlALVPQGATGELYVGGAglaqgyhdrp 2550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  407 ----NRvcFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE- 480
Cdd:PRK05691 2551 gltaER--FVADPFAADGGRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPs 2628
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  481 --KLILFMVSKDAS--------VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLS 550
Cdd:PRK05691 2629 gkQLAGYLVSAVAGqddeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQA 2705
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 557786167  551 GKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK05691 2706 PRSELEQQLAQIWREVLNVE----RVGLGDNFFELGGDSILSIQVVS 2748
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
193-539 1.52e-21

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 99.80  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVpnIQH---FRVLFDITQEDVLFLASPL---TFDPSVVeiFLALSSGASLLI---VP 263
Cdd:COG0365  187 LFILYTSGTTGKPKGVVHTHGGYL--VHAattAKYVLDLKPGDVFWCTADIgwaTGHSYIV--YGPLLNGATVVLyegRP 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 264 TSVKllPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQI 340
Cdd:COG0365  263 DFPD--PGRLWELI-EKYGVTVFFTAPTAIRalmKAGDEPLKKYDLS---SLRLLGSAGEPLNP-EVWEWWY-EAVGVPI 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 341 FNVYGITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----D 413
Cdd:COG0365  335 VDGWGQTETGGIfiSNLPGLPVK----------PGSMGKPVPGYDVAVVDEDGNPVPPGEeGELVIKGPWPGMFRgywnD 404
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 414 DEVTV------PLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQ--QVAEelqqvesCAVTWYNQ 479
Cdd:COG0365  405 PERYRetyfgrFPGWYR-TGDGARRdEDGYFWILGRSDDVINVSGHRIgtaEIEsaLVShpAVAE-------AAVVGVPD 476
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786167 480 E----KLILFMVSKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLN 539
Cdd:COG0365  477 EirgqVVKAFVVLKPgVEPSDELAKELQAHvreeLGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
PRK05691 PRK05691
peptide synthase; Validated
192-608 6.56e-21

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 99.47  E-value: 6.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  192 LAYVLHTSGTTGIPKIVRVPHKCIVPNiQHFRVLF-DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMVEQRGMLNN-QLSKVPYlALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDP 3949
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  271 SKLAsVLFSHHRVTVLQATPTLLRRFGSQlikstVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:PRK05691 3950 QGLL-AHVQAQGITVLESVPSLIQGMLAE-----DRQALDGLRWMLPTGEAMPPE-LARQWLQRYPQIGLVNAYGPAECS 4022
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  351 SWATIYRIpekTLNSTLKCELPVqlGFPL----------------LGTVVE--VRDTngftiqeGSGQVFLGG--RNRVC 410
Cdd:PRK05691 4023 DDVAFFRV---DLASTRGSYLPI--GSPTdnnrlylldealelvpLGAVGElcVAGT-------GVGRGYVGDplRTALA 4090
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  411 FLDDEVTVPLGTMRATGDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYNQEKLILFM 486
Cdd:PRK05691 4091 FVPHPFGAPGERLYRTGDLArRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVavqEGVNGKHLVGYL 4170
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  487 VSKDASVK-----EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNyiNLKSENKLSGKEDLWEKLQY 561
Cdd:PRK05691 4171 VPHQTVLAqgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIG--QLQSQAYLAPRNELEQTLAT 4248
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 557786167  562 LWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK05691 4249 IWADVLKVE----RVGVHDNFFELGGHSLLATQIASRVQKALQRNVP 4291
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
195-528 9.20e-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: 94.63  E-value: 9.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRV-LFDITQEDVLFLASPLTFDPSVVEIFLALSSGAsLLIVPTSVKLLPSKL 273
Cdd:cd17635    6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENTTYKSLF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 274 ASVLFshHRVTVLQATPTLLRRFGSqLIKSTvLSATTSLRVLALGGE-AFPSLTVLRSWRGegnKTQIFNVYGITEVSSW 352
Cdd:cd17635   85 KILTT--NAVTTTCLVPTLLSKLVS-ELKSA-NATVPSLRLIGYGGSrAIAADVRFIEATG---LTNTAQVYGLSETGTA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 353 ATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQ-VFLGGRNRVCFLDDEVTVP---LGTMRAT 426
Cdd:cd17635  158 LCLpTDDDSIEINA---------VGRPYPGVDVYLAATDGIAGPSASfGTiWIKSPANMLGYWNNPERTAevlIDGWVNT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 427 GDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVS---KDASVKEYIF 498
Cdd:cd17635  229 GDLGeRREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDeefgELVGLAVVAsaeLDENAIRALK 308
                        330       340       350
                 ....*....|....*....|....*....|
gi 557786167 499 KELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17635  309 HTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
194-529 1.52e-19

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: 90.54  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 194 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIvptSVKLLPSKL 273
Cdd:cd17633    4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 274 ASVLfSHHRVTVLQATPTLLRrfgsQLIKstVLSATTSLRVLALGGEAFPSLTvLRSWRGEGNKTQIFNVYGITEVSSWA 353
Cdd:cd17633   81 IRKI-NQYNATVIYLVPTMLQ----ALAR--TLEPESKIKSIFSSGQKLFEST-KKKLKNIFPKANLIEFYGTSELSFIT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 354 tiYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGF---TIQEGSGQVFLGgrnrvcFLDDEVTVPLGTMrATGDFV 430
Cdd:cd17633  153 --YNFNQES-------RPPNSVGRPFPNVEIEIRNADGGeigKIFVKSEMVFSG------YVRGGFSNPDGWM-SVGDIG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 431 TVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK---LILFMVSKDASVKEYIFKELQKYLP 506
Cdd:cd17633  217 YVDeEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALYSGDKLTYKQLKRFLKQKLS 296
                        330       340
                 ....*....|....*....|...
gi 557786167 507 SHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17633  297 RYEIPKKIIFVDSLPYTSSGKIA 319
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
192-535 2.58e-19

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: 92.01  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaSPLTFDPS---VVEIFLALSSGASLLIV--PTSV 266
Cdd:cd05909  149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVF--GALPFFHSfglTGCLWLPLLSGIKVVFHpnPLDY 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 267 KLLPSklasvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGI 346
Cdd:cd05909  227 KKIPE-----LIYDKKATILLGTPTFLRGY----ARAAHPEDFSSLRLVVAGAEKLKD-TLRQEFQ-EKFGIRILEGYGT 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSswatiyriPEKTLNSTLKCELPVQLGFPLLGT---VVEVRDTNGFTIQEGsGQVFLGGRNRVC-FLDDE---VTVP 419
Cdd:cd05909  296 TECS--------PVISVNTPQSPNKEGTVGRPLPGMevkIVSVETHEEVPIGEG-GLLLVRGPNVMLgYLNEPeltSFAF 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 420 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL--QQVESCAVTWYNQ---EKLILFMVSKDASV 493
Cdd:cd05909  367 GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGrkgEKIVLLTTTTDTDP 446
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 557786167 494 keyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05909  447 -----SSLNDILKNAgisnlAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
192-529 1.98e-18

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: 88.82  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPtsvKLLP 270
Cdd:cd17631  100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILR---KFDP 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASvLFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPSLtVLRSWRGEGnkTQIFNVYGIT 347
Cdd:cd17631  177 ETVLD-LIERHRVTSFFLVPTMI-----QALLQHPRFATTdlsSLRAVIYGGAPMPER-LLRALQARG--VKFVQGYGMT 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 348 EVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRvcfldDEVTVP 419
Cdd:cd17631  248 ETSPGVTFLS-PEDHR------RKLGSAGRPVFFVEVRIVDPDGREVPPGevgeivvrGPHVMAGYWNR-----PEATAA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 420 L---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ElVQQVAEELQQVESCAV------TWynQEKLILFM 486
Cdd:cd17631  316 AfrdGWFH-TGDLGRLdEDGYLYIVDRKKDMIISGGE--NVypaE-VEDVLYEHPAVAEVAVigvpdeKW--GEAVVAVV 389
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 557786167 487 VSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17631  390 VPRPGAEldEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
192-528 4.55e-18

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: 87.82  E-value: 4.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPTsvkLLP 270
Cdd:cd05903   95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKlASVLFSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITE 348
Cdd:cd05903  172 DK-ALALMREHGVTFMMGATPFL----TDLLNAVEEAGEplSRLRTFVCGGATVPRSLARRAAELLGAK--VCSAYGSTE 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 VSSWATIYRIPEKTLNSTLKcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-FLDDevtvPLGTMRA- 425
Cdd:cd05903  245 CPGAVTSITPAPEDRRLYTD-------GRPLPGVEIKVVDDTGATLAPGVeGELLSRGPSVFLgYLDR----PDLTADAa 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 426 ------TGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASvk 494
Cdd:cd05903  314 pegwfrTGDLaRLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLgeraCAVVVTKSGA-- 391
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 557786167 495 EYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 528
Cdd:cd05903  392 LLTFDELVAYLDRQGVakqywPERLVHVDDLPRTPSGKV 430
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
192-533 6.75e-18

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: 87.13  E-value: 6.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFLASPLTFDPSV-VEIFLALSSGASLLIVPTSVKll 269
Cdd:cd05919   93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPT-- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 PSKLASVLfSHHRVTVLQATPTLLRRfgsqLIKSTVLS--ATTSLRVLALGGEAFPsltvlrswRGEGNK------TQIF 341
Cdd:cd05919  171 AERVLATL-ARFRPTVLYGVPTFYAN----LLDSCAGSpdALRSLRLCVSAGEALP--------RGLGERwmehfgGPIL 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 342 NVYGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG--------RNRvcfl 412
Cdd:cd05919  238 DGIGATEVGHIFLSNRPGAWRLGST---------GRPVPGYEIRLVDEEGHTIPPGEeGDLLVRGpsaavgywNNP---- 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 487
Cdd:cd05919  305 EKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEStglsRLTAFVV 384
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557786167 488 SK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05919  385 LKspaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
193-529 1.51e-17

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: 86.65  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFlaspltfdpSVVEIFLALSSGASL---LIVPTSVKL 268
Cdd:cd05959  166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYaRNVLGIREDDVCF---------SAAKLFFAYGLGNSLtfpLSVGATTVL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLASVLFSH----HRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRgegNKT--QI 340
Cdd:cd05959  237 MPERPTPAAVFKrirrYRPTVFFGVPTLY----AAMLAAPNLPSRdlSSLRLCVSAGEALPA-EVGERWK---ARFglDI 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 341 FNVYGITEVsswATIY---RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFL-GGRNRVCFL--- 412
Cdd:cd05959  309 LDGIGSTEM---LHIFlsnRPGRVRYGTT---------GKPVPGYEVELRDEDGGDVADGePGELYVrGPSSATMYWnnr 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DDEVTVPLGTMRATGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 487
Cdd:cd05959  377 DKTRDTFQGEWTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgltKPKAFVV 456
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 557786167 488 SKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05959  457 LRPgYEDSEALEEELKEFvkdrLAPYKYPRWIVFVDELPKTATGKIQ 503
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
192-535 2.90e-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: 81.37  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-TFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:cd05944    4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLfHVNGSVVTLLTPLASGAHVVLAGPAGYRNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05944   84 GLFDNFwkLVERYRITSLSTVPTVY----AALLQVPVNADISSLRFAMSGAAPLP--VELRARFEDATGLPVVEGYGLTE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 VSSWATI-YRIPEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQE-GSGQVF---------LGG-----RNRVCFL 412
Cdd:cd05944  158 ATCLVAVnPPDGPKRPGS-------VGLRLPYARVRIKVLDGVGRLLRDcAPDEVGeicvagpgvFGGylyteGNKNAFV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFM- 486
Cdd:cd05944  231 AD------GWLN-TGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGqpdaHAGELPVAYVq 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557786167 487 VSKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05944  304 LKPGAVVEE---EELLAWARDHvperaAVPKHIEVLEELPVTAVGKVFKPALRA 354
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
192-533 4.96e-16

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


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 81.84  E-value: 4.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQ--HFRVLFDITQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPTSVk 267
Cdd:cd05936  127 VAVLQYTSGTTGVPKGAMLTHRNLVANALqiKAWLEDLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIPRFR- 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 llpSKLASVLFSHHRVTVLQATPTLLrrfgSQLI--KSTVLSATTSLRVLALGGEAFPsLTVLRSWRgegnktQIFNV-- 343
Cdd:cd05936  205 ---PIGVLKEIRKHRVTIFPGVPTMY----IALLnaPEFKKRDFSSLRLCISGGAPLP-VEVAERFE------ELTGVpi 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 344 ---YGITEVSSWATIYRIPEKTLNSTlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS--------GQVFLGGRNRvcfl 412
Cdd:cd05936  271 vegYGLTETSPVVAVNPLDGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEvgelwvrgPQVMKGYWNR---- 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 ddevtvPLGTMRA-------TGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ElVQQVAEELQQVESCAVTW----Y 477
Cdd:cd05936  339 ------PEETAEAfvdgwlrTGDIGYMdEDGYFFIVDRKKDMIIVGG--FNVyprE-VEEVLYEHPAVAEAAVVGvpdpY 409
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557786167 478 NQEKLILFMVSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05936  410 SGEAVKAFVVLKEgASLtEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2-535 3.72e-15

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 79.41  E-value: 3.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   2 TLQELVHKAASCYMDRVAVCFDECNNqlpvyYTYKTVVNAASELSNFLLLhcdfQGIreiglycQPG----IDLPSW--- 74
Cdd:PRK06087  24 SLADYWQQTARAMPDKIAVVDNHGAS-----YTYSALDHAASRLANWLLA----KGI-------EPGdrvaFQLPGWcef 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  75 ---ILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEK--KQINKFKSFHEtlLNYDTFTVEHndLVLF-RLHWKN 148
Cdd:PRK06087  88 tiiYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfKQTRPVDLILP--LQNQLPQLQQ--IVGVdKLAPAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 149 TEVNL--MLNDGKekyekekikSISSE---HVNEekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFR 223
Cdd:PRK06087 164 SSLSLsqIIADYE---------PLTTAittHGDE--------------LAAVLFTSGTEGLPKGVMLTHNNILASERAYC 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 224 VLFDITQEDVLFLASPLT----FDPSVVEIFLAlsSGASLLIvptsvKLLPSKLASVLFSHHRVT-VLQATP------TL 292
Cdd:PRK06087 221 ARLNLTWQDVFMMPAPLGhatgFLHGVTAPFLI--GARSVLL-----DIFTPDACLALLEQQRCTcMLGATPfiydllNL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 293 LRRFGSQLikstvlsatTSLRVLALGGEAFPSLTVLRSWRgegNKTQIFNVYGITEVSSWAtiYRIPEKTLNSTLKCElp 372
Cdd:PRK06087 294 LEKQPADL---------SALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTESSPHA--VVNLDDPLSRFMHTD-- 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 373 vqlGFPLLGTVVEVRDTNGFTI------QEGS--GQVFLGgrnrvcFLDDevtvPLGTMRA--------TGDFVTV-KDG 435
Cdd:PRK06087 358 ---GYAAAGVEIKVVDEARKTLppgcegEEASrgPNVFMG------YLDE----PELTARAldeegwyySGDLCRMdEAG 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 436 EIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDA----SVKEYIFKELQKYLPS 507
Cdd:PRK06087 425 YIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLgersCAYVVLKAPhhslTLEEVVAFFSRKRVAK 504
                        570       580
                 ....*....|....*....|....*...
gi 557786167 508 HAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK06087 505 YKYPEHIVVIDKLPRTASGKIQKFLLRK 532
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
194-528 1.79e-14

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: 77.23  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 194 YVLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL---TFDPSVveIFLALSSGA-SLLIVPTSVKL 268
Cdd:cd17634  236 FILYTSGTTGKPKgVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVgwvTGHSYL--LYGPLACGAtTLLYEGVPNWP 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLASVLfSHHRVTVLQATPTLLRRF---GSQLIKSTVLSattSLRVLALGGEAFPSLTVLRSWRG-EGNKTQIFNVY 344
Cdd:cd17634  314 TPARMWQVV-DKHGVNILYTAPTAIRALmaaGDDAIEGTDRS---SLRILGSVGEPINPEAYEWYWKKiGKEKCPVVDTW 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 345 GITEVsSWATIYRIPEKTlnsTLKCELPVQlgfPLLGTVVEVRDTNGFTIQEGS-GQVFLG----GRNRVCFLDDE---V 416
Cdd:cd17634  390 WQTET-GGFMITPLPGAI---ELKAGSATR---PVFGVQPAVVDNEGHPQPGGTeGNLVITdpwpGQTRTLFGDHErfeQ 462
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 417 TV--PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSK 489
Cdd:cd17634  463 TYfsTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAikgqAPYAYVVLN 542
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 557786167 490 D---------ASVKEYIFKELQKYlpshAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17634  543 HgvepspelyAELRNWVRKEIGPL----ATPDVVHWVDSLPKTRSGKI 586
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
196-528 3.46e-14

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


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 75.63  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 196 LHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDP-------SVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd05973   94 MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwayglyYAITGPLALGHPTILLEGGFSVES 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLasvlfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATT---SLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYG 345
Cdd:cd05973  170 TWRVI-----ERLGVTNLAGSPTAYR----LLMAAGAEVPARpkgRLRRVSSAGE--PLTPEVIRWFDAALGVPIHDHYG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 346 ITEVSswatiyripeKTLNSTLKCELPVQ---LGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-----FLDDEV 416
Cdd:cd05973  239 QTELG----------MVLANHHALEHPVHagsAGRAMPGWRVAVLDDDGDELGPGEpGRLAIDIANSPLmwfrgYQLPDT 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 417 TVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFMV---S 488
Cdd:cd05973  309 PAIDGGYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGvpdpERTEVVKAFVVlrgG 388
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 557786167 489 KDASvkEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05973  389 HEGT--PALADELQLHvkkrLSAHAYPRTIHFVDELPKTPSGKI 430
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
198-529 8.56e-14

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: 74.44  E-value: 8.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASP---LTFDPSVVEIFlALSSGASLLIVPTSVkllPSKLA 274
Cdd:cd05958  105 TSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPplaFTFGLGGVLLF-PFGVGASGVLLEEAT---PDLLL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 275 SVLfSHHRVTVLQATPTLLR------RFGSQLIkstvlsatTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITE 348
Cdd:cd05958  181 SAI-ARYKPTVLFTAPTAYRamlahpDAAGPDL--------SSLRKCVSAGEALPA-ALHRAWK-EATGIPIIDGIGSTE 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 vsswatIYRIpekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDE--VTVPLGTMRA 425
Cdd:cd05958  250 ------MFHI---FISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTiGRLAVRGPTGCRYLADKrqRTYVQGGWNI 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 426 TGD-FVTVKDGEIFFLGRKDSQIKRHGkrLNIELVqQVAEELQQ---VESCAVTWY-NQEKLIL---FMVSK-DASVKEY 496
Cdd:cd05958  321 TGDtYSRDPDGYFRHQGRSDDMIVSGG--YNIAPP-EVEDVLLQhpaVAECAVVGHpDESRGVVvkaFVVLRpGVIPGPV 397
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 557786167 497 IFKELQKYLPSHAV----PDELVLIDSLPFTSHGKID 529
Cdd:cd05958  398 LARELQDHAKAHIApykyPRAIEFVTELPRTATGKLQ 434
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
193-528 8.77e-14

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: 74.46  E-value: 8.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaspLTFDPSVVE-----IFLALSSGASLLIVPTsvK 267
Cdd:cd05969   92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW----CTADPGWVTgtvygIWAPWLNGVTNVVYEG--R 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 LLPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSLTVlrSWRGEGNKTQIFNVY 344
Cdd:cd05969  166 FDAESWYGII-ERVKVTVWYTAPTAIRmlmKEGDELARKYDLS---SLRFIHSVGEPLNPEAI--RWGMEVFGVPIHDTW 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 345 GITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL--------------GGRN 407
Cdd:cd05969  240 WQTETGSImiANYPCMPIK----------PGSMGKPLPGVKAAVVDENGNELPPGTkGILALkpgwpsmfrgiwndEERY 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 408 RVCFLDDEVTvplgtmraTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTwyNQEKLIL-- 484
Cdd:cd05969  310 KNSFIDGWYL--------TGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVI--GKPDPLRge 379
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786167 485 ----FMVSKDA-----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05969  380 iikaFISLKEGfepsdELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
192-529 1.38e-13

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 74.07  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiF---------LALSSGASLLIV 262
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM---------FhvhawglpyLALMAGAKQVIP 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 263 PtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFN 342
Cdd:PRK06187 240 R---RFDPENLLD-LIETERVTFFFAVPTIWQMLLKAPRAYFV--DFSSLRLVIYGGAALP-PALLREFK-EKFGIDLVQ 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 343 VYGITEVSSWATIYRIPEKTLNSTlkcELPVQLGFPLLGtvVEVR--DTNGFTI--QEGS-GQVFLGGRN--RVCFLDDE 415
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQW---TKRRSAGRPLPG--VEARivDDDGDELppDGGEvGEIIVRGPWlmQGYWNRPE 386
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 416 VTVPL---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ELvqqvaEEL----QQVESCAV------TWyn 478
Cdd:PRK06187 387 ATAETidgGWLH-TGDVGYIdEDGYLYITDRIKDVIISGGE--NIyprEL-----EDAlyghPAVAEVAVigvpdeKW-- 456
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557786167 479 QEKLILFMVSKD-ASVKEyifKELQKYLPSH----AVPDELVLIDSLPFTSHGKID 529
Cdd:PRK06187 457 GERPVAVVVLKPgATLDA---KELRAFLRGRlakfKLPKRIAFVDELPRTSVGKIL 509
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
170-537 2.09e-13

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: 73.68  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 170 ISSEHVNEEKAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEI 249
Cdd:cd05908   95 ITEEEVLCELADE---------LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAF 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 250 FLA-LSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLqATPTllrrFGSQLIKSTVLSAT------TSLRVLALGGEAF 322
Cdd:cd05908  166 HLApLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIV-SSPN----FGYKYFLKTLKPEKandwdlSSIRMILNGAEPI 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 323 PS------LTVLRSWRgeGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTL-------------------KCELPVQLGF 377
Cdd:cd05908  241 DYelchefLDHMSKYG--LKRNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsECLTFVEVGK 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 378 PLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNrvcflddeVTV-----PLGTMRA--------TGDFVTVKDGEIFFLGRK 443
Cdd:cd05908  319 PIDETDIRICDEDNKILPDGYiGHIQIRGKN--------VTPgyynnPEATAKVftddgwlkTGDLGFIRNGRLVITGRE 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 444 DSQIKRHGKRLNIELVQQVAEELQQVES-----CAV--TWYNQEKLILFMVSKDaSVKEYIfkELQKYLPSHAVP----- 511
Cdd:cd05908  391 KDIIFVNGQNVYPHDIERIAEELEGVELgrvvaCGVnnSNTRNEEIFCFIEHRK-SEDDFY--PLGKKIKKHLNKrggwq 467
                        410       420
                 ....*....|....*....|....*..
gi 557786167 512 -DELVLIDSLPFTSHGKIDVSELNKIY 537
Cdd:cd05908  468 iNEVLPIRRIPKTTSGKVKRYELAQRY 494
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
192-535 3.34e-13

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: 72.75  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDPSvvEIFLALSSGASLLIVPTSV----- 266
Cdd:cd05972   83 PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA----DPG--WAKGAWSSFFGPWLLGATVfvyeg 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 267 -KLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEafpSLT--VLRSWRGEGNKTqIFNV 343
Cdd:cd05972  157 pRFDAERILELL-ERYGVTSFCGPPTAYRMLIKQDLSSYKFS---HLRLVVSAGE---PLNpeVIEWWRAATGLP-IRDG 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 344 YGITEVSSwatiyripekTLNSTLKCEL-PVQLGFPLLGTVVEVRDTNG----------FTIQEGSGQVFLGgrnrvcFL 412
Cdd:cd05972  229 YGQTETGL----------TVGNFPDMPVkPGSMGRPTPGYDVAIIDDDGrelppgeegdIAIKLPPPGLFLG------YV 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DDEVtvplgTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQQVAeelqqVESCAVTWYN 478
Cdd:cd05972  293 GDPE-----KTEAsirgdyylTGDRAYRdEDGYFWFVGRADDIIKSSGYRIgpfEVEsaLLEHPA-----VAEAAVVGSP 362
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 479 QEkLILFMV------SKDASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05972  363 DP-VRGEVVkafvvlTSGYEPSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
192-533 4.65e-13

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: 72.08  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIV---PNIQHFRVLFDITqEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd05971   90 PALIIYTSGTTGPPKGALHAHRVLLghlPGVQFPFNLFPRD-GDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05971  169 DPKAALDLM-SRYGVTTAFLPPTALKMMRQQ--GEQLKHAQVKLRAIATGGE--SLGEELLGWAREQFGVEVNEFYGQTE 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 ----VSSWATIYRIPektlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----DDEVTV- 418
Cdd:cd05971  244 cnlvIGNCSALFPIK------------PGSMGKPIPGHRVAIVDDNGTPLPPGEvGEIAVELPDPVAFLgywnNPSATEk 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 419 -PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY----NQEKLILFMVSKDAS 492
Cdd:cd05971  312 kMAGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdpiRGEIVKAFVVLNPGE 391
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 557786167 493 VK-EYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05971  392 TPsDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
192-529 5.14e-13

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: 72.35  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LSSGASLLIVPtsvKLLP 270
Cdd:cd05926  151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLStLAAGGSVVLPP---RFSA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASvLFSHHRVTVLQATPT----LLRRFgsqliKSTVLSATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFNVYGI 346
Cdd:cd05926  228 STFWP-DVRDYNATWYTAVPTihqiLLNRP-----EPNPESPPPKLRFIRSCSASLP-PAVLEALE-ATFGAPVLEAYGM 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSSWATIYRIPEktlnstlKCELPVQLGFPllgTVVEVR--DTNGFTIQEG-SGQVFLGGRNrVC--FLDD-----EV 416
Cdd:cd05926  300 TEAAHQMTSNPLPP-------GPRKPGSVGKP---VGVEVRilDEDGEILPPGvVGEICLRGPN-VTrgYLNNpeanaEA 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 417 TVPLGTMRaTGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV-----TWYNQEKLILFMVSKD 490
Cdd:cd05926  369 AFKDGWFR-TGDLgYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgvpdEKYGEEVAAAVVLREG 447
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 557786167 491 ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05926  448 ASVtEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
PRK13382 PRK13382
bile acid CoA ligase;
195-533 1.64e-12

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 70.94  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHKcivPNIQHFRVLFDIT---QEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 271
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpwrAEEPTVIVAPMFHAWGFSQLVLAASLACTIV---TRRRFDPE 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 klASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNktQIFNVYGITEVS 350
Cdd:PRK13382 275 --ATLdLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD--VIYNNYNATEAG 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 351 sWATIyRIPEktlnstlkcEL---PVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLggRNRVCFldDEVTVplGT---- 422
Cdd:PRK13382 351 -MIAT-ATPA---------DLraaPDTAGRPAEGTEIRILDQDFREVPTGEvGTIFV--RNDTQF--DGYTS--GStkdf 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 423 ---MRATGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVK 494
Cdd:PRK13382 414 hdgFMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQygqrLAAFVVLKPGASA 493
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 557786167 495 --EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK13382 494 tpETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
192-529 2.94e-12

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: 68.51  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASlLIVPTSVKLLPS 271
Cdd:cd17630    2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAE-LVLLERNQALAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 KLAsvlfsHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPS-LT---VLRSWRgegnktqIFNVYGIT 347
Cdd:cd17630   81 DLA-----PPGVTHVSLVPTQLQRL---LDSGQGPAALKSLRAVLLGGAPIPPeLLeraADRGIP-------LYTTYGMT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 348 EVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGtvVEVRDTNGFTIQEGSGQVFLGGRNRVC---FLDDevtvplGTMR 424
Cdd:cd17630  146 ETASQVATKRPDGFGRGG---------VGVLLPG--RELRIVEDGEIWVGGASLAMGYLRGQLvpeFNED------GWFT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 425 aTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW-----YNQeKLILFMVSKDASVKEYIF 498
Cdd:cd17630  209 -TKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGvpdeeLGQ-RPVAVIVGRGPADPAELR 286
                        330       340       350
                 ....*....|....*....|....*....|.
gi 557786167 499 KELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17630  287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
192-528 3.08e-12

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 70.08  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiflALSSG-ASLLIVPTSVK--- 267
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM-----------AHQTGfMYGLMMPVMLGata 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 ----LLPSKLASVLFSHHRVT-VLQATPtllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSLTVLRSWRGEGnkTQI 340
Cdd:PRK13295 268 vlqdIWDPARAAELIRTEGVTfTMASTP-----FLTDLTRAVKESGRPvsSLRTFLCAGAPIPGALVERARAALG--AKI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 341 FNVYGITEVSSWATIY--RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI---QEGSGQV-----FLG--GRNR 408
Cdd:PRK13295 341 VSAWGMTENGAVTLTKldDPDERASTTD---------GCPLPGVEVRVVDADGAPLpagQIGRLQVrgcsnFGGylKRPQ 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 409 VCFLDDEvtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----I 483
Cdd:PRK13295 412 LNGTDAD-----GWFD-TGDLARIdADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLgeraC 485
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 557786167 484 LFMVSKDASvkEYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 528
Cdd:PRK13295 486 AFVVPRPGQ--SLDFEEMVEFLKAQKVakqyiPERLVVRDALPRTPSGKI 533
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
192-528 1.30e-11

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: 67.70  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLIVPtsvKLL 269
Cdd:cd05934   83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPL-FhiNAQAVSVLAALSVGATLVLLP---RFS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 PSKLASVLFSHHrVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITEV 349
Cdd:cd05934  159 ASRFWSDVRRYG-ATVTNYLGAML----SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMTET 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 350 SSwATIYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGTMRA--- 425
Cdd:cd05934  232 IV-GVIGPRDEPR--------RPGSIGRPAPGYEVRIVDDDGQELPAGEpGELVIRGLRGWGFFKGYYNMPEATAEAmrn 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 426 ----TGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV----TWYNQEKLILFMVSKDASV--K 494
Cdd:cd05934  303 gwfhTGDlGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvavpDEVGEDEVKAVVVLRPGETldP 382
                        330       340       350
                 ....*....|....*....|....*....|....
gi 557786167 495 EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05934  383 EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
PRK07788 PRK07788
acyl-CoA synthetase; Validated
195-533 1.36e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 68.03  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHkciVPNIQHFRVLFD---ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 271
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPE---PSPLAPLAGLLSrvpFRAGETTLLPAPMFHATGWAHLTLAMALGSTVV---LRRRFDPE 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 272 K-LASVlfSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITEVS 350
Cdd:PRK07788 286 AtLEDI--AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV--LYNLYGSTEVA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 351 sWATIYRIPEKTLNSTLkcelpvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLG----------GRNRVCflddevtvp 419
Cdd:PRK07788 362 -FATIATPEDLAEAPGT-------VGRPPKGVTVKILDENGNEVPRGvVGRIFVGngfpfegytdGRDKQI--------- 424
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 420 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV------TWYnqEKLILFMVSKDAS 492
Cdd:PRK07788 425 IDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeEFG--QRLRAFVVKAPGA 502
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 557786167 493 ------VKEYIFKELQKylpsHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK07788 503 aldedaIKDYVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKREL 545
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
195-536 1.41e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 67.96  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGAsLLIVPTsvKLLPSK 272
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGG-VIIVPR--KFEPTK 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 273 lASVLFSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSL---RVLALGGEAFPsLTVLRSWR------GEGnktqifnv 343
Cdd:PRK06839 230 -ALSMIEKHKVTVVMGVPTI-----HQALINCSKFETTNLqsvRWFYNGGAPCP-EELMREFIdrgflfGQG-------- 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 344 YGITEVSswATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGT 422
Cdd:PRK06839 295 FGMTETS--PTVFMLSEEDARRK-----VGSIGKPVLFCDYELIDENKNKVEVGEvGELLIRGPNVMKEYWNRPDATEET 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 423 MR----ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASV 493
Cdd:PRK06839 368 IQdgwlCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeipIAFIVKKSSSV 447
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 557786167 494 --KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 536
Cdd:PRK06839 448 liEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
195-538 2.85e-11

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: 67.13  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLI---VPTSVKllP 270
Cdd:cd05968  241 IIYTSGTTGKPKgTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPK--A 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLaSVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsltvLRSW------RGEGNKTqIFNVY 344
Cdd:cd05968  319 DRL-WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWN----PEPWnwlfetVGKGRNP-IINYS 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 345 GITEVSswATIYRipektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFL----GGRNRVCFLDDEVTVPL 420
Cdd:cd05968  393 GGTEIS--GGILG------NVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLlapwPGMTRGFWRDEDRYLET 464
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 421 GTMR-----ATGDFVTVKDGEIFF-LGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVSKD 490
Cdd:cd05968  465 YWSRfdnvwVHGDFAYYDEEGYFYiLGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkgEAIVCFVVLKP 544
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557786167 491 A-SVKEYIFKELQKYLPSHA----VPDELVLIDSLPFTSHGKIDVSELNKIYL 538
Cdd:cd05968  545 GvTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
198-535 3.29e-11

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: 66.50  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVpnIQHFRVL----FDITQEDVLFLASPLtFD------PsvveiFLALSSGASLliVPTSVK 267
Cdd:cd12119  171 TSGTTGNPKGVVYSHRSLV--LHAMAALltdgLGLSESDVVLPVVPM-FHvnawglP-----YAAAMVGAKL--VLPGPY 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 LLPSKLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 346
Cdd:cd12119  241 LDPASLAE-LIEREGVTFAAGVPTVWQGLLDHLeANGRDLS---SLRRVVIGGSAVPR-SLIEAFEERG--VRVIHAWGM 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQ---EGSGQVFLGGrNRVC---FLDDEVTV 418
Cdd:cd12119  314 TETSPLGTVARPPSEHSNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPwdgKAVGELQVRG-PWVTksyYKNDEESE 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 419 PL---GTMRaTGDFVTV-KDGEIFFLGR-KDSqIKRHGKRL-NIELvQQVAEELQQVESCAV------TWynQEKLILFM 486
Cdd:cd12119  393 ALtedGWLR-TGDVATIdEDGYLTITDRsKDV-IKSGGEWIsSVEL-ENAIMAHPAVAEAAVigvphpKW--GERPLAVV 467
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557786167 487 VSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd12119  468 VLKEgATVtAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
193-529 3.39e-11

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: 66.58  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-----PSVVEIFLAlssGASLLIVPTsvk 267
Cdd:cd05920  142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfplacPGVLGTLLA---GGRVVLAPD--- 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 llPSKLASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSlTVLRSWRGE-GNKTQifNVYG 345
Cdd:cd05920  216 --PSPDAAFpLIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSP-ALARRVPPVlGCTLQ--QVFG 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 346 ITEvsSWATIYRI--PEKTLNSTlkcelpvQlGFPLL-GTVVEVRDTNGFTIQEGS-GQVFLGG------------RNRV 409
Cdd:cd05920  289 MAE--GLLNYTRLddPDEVIIHT-------Q-GRPMSpDDEIRVVDEEGNPVPPGEeGELLTRGpytirgyyrapeHNAR 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 410 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 484
Cdd:cd05920  359 AFTPD------GFYR-TGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAmpdeLLGERSCA 431
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 557786167 485 FMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05920  432 FVVLRDPPPS---AAQLRRFLrerglAAYKLPDRIEFVDSLPLTAVGKID 478
PRK07638 PRK07638
acyl-CoA synthetase; Validated
170-536 3.70e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 66.34  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 170 ISSEHVNE----EKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdps 245
Cdd:PRK07638 119 IEIDEWKRmiekYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTL----- 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 246 VVEIFL-----ALSSGASLLIVPtsvKLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQlikstvlsattslrvlalggE 320
Cdd:PRK07638 194 VHSLFLygaisTLYVGQTVHLMR---KFIPNQVLDKL-ETENISVMYTVPTMLESLYKE--------------------N 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 321 AFP--SLTVLRS---WRGEGNK--------TQIFNVYGITEVSSWAtiYRIPEktlNSTLKcelPVQLGFPLLGTVVEVR 387
Cdd:PRK07638 250 RVIenKMKIISSgakWEAEAKEkiknifpyAKLYEFYGASELSFVT--ALVDE---ESERR---PNSVGRPFHNVQVRIC 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 388 DTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVPLGTMRATGdFVTvKDGEIFFLGRKDSQIKRHGkrLNI--E 457
Cdd:PRK07638 322 NEAGEEVQKGeigtvyvkSPQFFMGYIIGGVLARELNADGWMTVRDVG-YED-EEGFIYIVGREKNMILFGG--INIfpE 397
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 458 LVQQVAEELQQVESCAVT------WYNQEKLILfmvsKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVS 531
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVIgvpdsyWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473

                 ....*
gi 557786167 532 ELNKI 536
Cdd:PRK07638 474 EAKSW 478
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
193-546 5.14e-11

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 66.53  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdpsvveiflALSSGASLLIVpTSVK--L 268
Cdd:PRK06814  796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVfhSF---------GLTGGLVLPLL-SGVKvfL 865
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  269 LPSKLasvlfsHHRVT---VLQATPTLLrrFGSqlikSTVLS--ATT-------SLRVLALGGEAFPSLTvlRSWRGEGN 336
Cdd:PRK06814  866 YPSPL------HYRIIpelIYDTNATIL--FGT----DTFLNgyARYahpydfrSLRYVFAGAEKVKEET--RQTWMEKF 931
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  337 KTQIFNVYGITEVSswatiyriPEKTLNSTLKCELpvqlgfpllGTV------VEVR--DTNGftIQEGsGQVFLGGRNr 408
Cdd:PRK06814  932 GIRILEGYGVTETA--------PVIALNTPMHNKA---------GTVgrllpgIEYRlePVPG--IDEG-GRLFVRGPN- 990
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  409 vcflddevtVPLGTMRA---------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL-QQVES 471
Cdd:PRK06814  991 ---------VMLGYLRAenpgvleppadgwydTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALH 1061
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557786167  472 CAVTWYNQ---EKLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNYINLKSE 546
Cdd:PRK06814 1062 AAVSIPDArkgERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
192-474 1.95e-10

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: 64.15  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDV--LFLasPLTfdpSVVE----IFLALSSGASLLIVPtS 265
Cdd:cd05907   89 LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRhlSFL--PLA---HVFErragLYVPLLAGARIYFAS-S 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 266 VKLLPSKLASVlfshhRVTVLQATPTLLRRF--GSQLIKST-------VLSATTSLRVLALGGEAFPsLTVLRSWRGEGn 336
Cdd:cd05907  163 AETLLDDLSEV-----RPTVFLAVPRVWEKVyaAIKVKAVPglkrklfDLAVGGRLRFAASGGAPLP-AELLHFFRALG- 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 337 kTQIFNVYGITEVSSWATIyripektlnSTLKCELPVQLGFPLLGTVVEVRDTNgfTIQEGSGQVFLGGRNrvcflDDEV 416
Cdd:cd05907  236 -IPVYEGYGLTETSAVVTL---------NPPGDNRIGTVGKPLPGVEVRIADDG--EILVRGPNVMLGYYK-----NPEA 298
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557786167 417 TVPLGTMR---ATGDFVTVK-DGEIFFLGR-KDSQIKRHGKrlNIELvQQVAEELQQ---VESCAV 474
Cdd:cd05907  299 TAEALDADgwlHTGDLGEIDeDGFLHITGRkKDLIITSGGK--NISP-EPIENALKAsplISQAVV 361
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
193-533 2.17e-10

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: 63.52  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVrvphkcivpnIQHFRVLF----------DITQEDVLFLASPLtFDPSVVEIFL-ALSSGASLLI 261
Cdd:cd05912   80 ATIMYTSGTTGKPKGV----------QQTFGNHWwsaigsalnlGLTEDDNWLCALPL-FHISGLSILMrSVIYGMTVYL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 262 VPtsvKLLPSKLASVLFSHhRVTVLQATPTLLRRfgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGnkTQIF 341
Cdd:cd05912  149 VD---KFDAEQVLHLINSG-KVTIISVVPTMLQR----LLEILGEGYPNNLRCILLGGGPAP-KPLLEQCKEKG--IPVY 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 342 NVYGITEVSSWATiyripekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGftIQEGSGQVFLGGRNRV-CFL---DDEVT 417
Cdd:cd05912  218 QSYGMTETCSQIV-------TLSPEDALNKIGSAGKPLFPVELKIEDDGQ--PPYEVGEILLKGPNVTkGYLnrpDATEE 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 418 VPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 492
Cdd:cd05912  289 SFENGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvpVAFVVSERPI 368
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 557786167 493 VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05912  369 SEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
16-535 5.02e-10

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: 62.69  E-value: 5.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHCDFQGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd05941    1 DRIAIVDDGDS------ITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  96 lsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDgkekyekekiksissehv 175
Cdd:cd05941   75 ---------ELEYVI------------------------------------TDSEPSLVLDP------------------ 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 176 neekaeehmdlrlkhclAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LS 254
Cdd:cd05941   92 -----------------ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLF 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 255 SGAsllivptSVKLLP---SKLASVLFSHHRVTVLQATPTLLRR------FGSQLIKSTVLSATTSLRVLALGGEAFPsL 325
Cdd:cd05941  155 AGA-------SVEFLPkfdPKEVAISRLMPSITVFMGVPTIYTRllqyyeAHFTDPQFARAAAAERLRLMVSGSAALP-V 226
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 326 TVLRSWRGEGNKTqIFNVYGITEVSswatiyripeKTLNSTLKCE-LPVQLGFPLLGtvVEVR--DTNGFT--------- 393
Cdd:cd05941  227 PTLEEWEAITGHT-LLERYGMTEIG----------MALSNPLDGErRPGTVGMPLPG--VQARivDEETGEplprgevge 293
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 394 IQEGSGQVFLGGRNRVCFLDDEVTvPLGTMRaTGDFVTVK-DGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVES 471
Cdd:cd05941  294 IQVRGPSVFKEYWNKPEATKEEFT-DDGWFK-TGDLGVVDeDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSE 371
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167 472 CAV------TWynQEKLILFMVSKD--ASVKEYIFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05941  372 CAVigvpdpDW--GERVVAVVVLRAgaAALSLEELKEwAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
PRK07529 PRK07529
AMP-binding domain protein; Validated
192-535 5.19e-10

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 63.05  E-value: 5.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLiVPTSVKLL 269
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-FhvNALLVTGLAPLARGAHVV-LATPQGYR 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 -PSKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSA-TTSLRVlALGGEAFPSLTVLRSWRgEGNKTQIFNVYG 345
Cdd:PRK07529 293 gPGVIANFwkIVERYRINFLSGVPTVY----AALLQVPVDGHdISSLRY-ALCGAAPLPVEVFRRFE-AATGVRIVEGYG 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 346 ITEVSSWATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEV--RDTNGFTIQE------------GSGqVFLG----GR 406
Cdd:PRK07529 367 LTEATCVSSVnPPDGERRIGS---------VGLRLPYQRVRVviLDDAGRYLRDcavdevgvlciaGPN-VFSGyleaAH 436
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 407 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIElVQQVAEEL---QQVESCAVTW------ 476
Cdd:PRK07529 437 NKGLWLED------GWLN-TGDLGRIdADGYFWLTGRAKDLIIRGGH--NID-PAAIEEALlrhPAVALAAAVGrpdaha 506
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 477 ------YNQEKlilfmvsKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK07529 507 gelpvaYVQLK-------PGASATE---AELLAFARDHiaeraAVPKHVRILDALPKTAVGKIFKPALRR 566
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
192-529 7.87e-10

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 63.02  E-value: 7.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlfLASPLTFDPS---VVEIFLALSSGASLLIVPTsvkl 268
Cdd:PRK08633  784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDV--ILSSLPFFHSfglTVTLWLPLLEGIKVVYHPD---- 857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  269 lPSKLASV--LFSHHRVTVLQATPTLLRRFgsqlIKSTVLSAT--TSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVY 344
Cdd:PRK08633  858 -PTDALGIakLVAKHRATILLGTPTFLRLY----LRNKKLHPLmfASLRLVVAGAEKLK--PEVADAFEEKFGIRILEGY 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  345 GITEVSSWATIyRIP--EKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFT---------IQEGSGQVFLGgrnrvcFLD 413
Cdd:PRK08633  931 GATETSPVASV-NLPdvLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFEelppgedglILIGGPQVMKG------YLG 1003
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  414 D-----EVTVPLGTMR--ATGD--------FVTVKD---------GEIFFLGRkdsqikrhgkrlnielvqqVAEELQQV 469
Cdd:PRK08633 1004 DpektaEVIKDIDGIGwyVTGDkghldedgFLTITDrysrfakigGEMVPLGA-------------------VEEELAKA 1064
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786167  470 -----ESCAVTWYNQEK----LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:PRK08633 1065 lggeeVVFAVTAVPDEKkgekLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
198-608 1.33e-09

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: 62.00  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 276
Cdd:TIGR03443  423 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTADDIgTPGRLAEW 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   277 LfSHHRVTVLQATPTLlrrfgSQLikstvLSATTSlrvlalggEAFPSL-------TVL-----RSWRGEGNKTQIFNVY 344
Cdd:TIGR03443  502 M-AKYGATVTHLTPAM-----GQL-----LSAQAT--------TPIPSLhhaffvgDILtkrdcLRLQTLAENVCIVNMY 562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   345 GITEVSSWATIYRIPEKTLNST----LKCELP-------VQLgfpL------------LGTVVE--VRD----------- 388
Cdd:TIGR03443  563 GTTETQRAVSYFEIPSRSSDSTflknLKDVMPagkgmknVQL---LvvnrndrtqtcgVGEVGEiyVRAgglaegylglp 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   389 --------TNGFT-----------IQEGSGQVFLGGRNRvcflddevtvplgtMRATGDF-VTVKDGEIFFLGRKDSQIK 448
Cdd:TIGR03443  640 elnaekfvNNWFVdpshwidldkeNNKPEREFWLGPRDR--------------LYRTGDLgRYLPDGNVECCGRADDQVK 705
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   449 RHGKRL-----------------NIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKDASV-KEYIFKELQKY------ 504
Cdd:TIGR03443  706 IRGFRIelgeidthlsqhplvreNVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEEsSDPVVKGLIKYrklikd 785
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   505 --------LPSHAVPDELVLIDSLPFTSHGKID--------VSELNKIYLNYINLKSENKLSGKE----DLWEKLqylwk 564
Cdd:TIGR03443  786 ireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDkpalpfpdTAQLAAVAKNRSASAADEEFTETEreirDLWLEL----- 860
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 557786167   565 stlnLPEDLLRV-PDESlFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:TIGR03443  861 ----LPNRPATIsPDDS-FFDLGGHSILATRMIFELRKKLNVELP 900
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
192-554 1.91e-09

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: 60.84  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLaLSSGASllIVPTSVKLL 269
Cdd:cd17640   90 LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERS-AEYFI-FACGCS--QAYTSIRTL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 PSKLASVlfshhRVTVLQATPTLLRRFGSQLIKSTVLSATTS------------LRVLALGGEAFPSlTVLRSWRGEGnk 337
Cdd:cd17640  166 KDDLKRV-----KPHYIVSVPRLWESLYSGIQKQVSKSSPIKqflflfflsggiFKFGISGGGALPP-HVDTFFEAIG-- 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 338 TQIFNVYGITEVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGTVVEVRD--TNGFTIQEGSGQVFLGGrnrvcfldDE 415
Cdd:cd17640  238 IEVLNGYGLTETSPVVSARRLKCNVRGS---------VGRPLPGTEIKIVDpeGNVVLPPGEKGIVWVRG--------PQ 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 416 VTV-----PLGTMRA--------TGDFVT-VKDGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE 480
Cdd:cd17640  301 VMKgyyknPEATSKVldsdgwfnTGDLGWlTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK 380
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557786167 481 KLILFMVSKdasvkeyiFKELQKYLPSHAVpdelvlidSLPFTSHGKIDVSELNKIYLNYINLKSENKLSGKED 554
Cdd:cd17640  381 RLGALIVPN--------FEELEKWAKESGV--------KLANDRSQLLASKKVLKLYKNEIKDEISNRPGFKSF 438
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
192-474 2.07e-09

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: 60.69  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLF--DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvkll 269
Cdd:cd05911  148 TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP------ 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 psKLASVLF----SHHRVTVLQATPTLLrrfgSQLIKSTVLSATT--SLRVLALGGEAFpSLTVLRSWRGEGNKTQIFNV 343
Cdd:cd05911  222 --KFDSELFldliEKYKITFLYLVPPIA----AALAKSPLLDKYDlsSLRVILSGGAPL-SKELQELLAKRFPNATIKQG 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 344 YGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI----QEG-----SGQVFLG--GR---NRV 409
Cdd:cd05911  295 YGMTETGGILTVNPDGDDKPGSV---------GRLLPNVEAKIVDDDGKDSlgpnEPGeicvrGPQVMKGyyNNpeaTKE 365
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557786167 410 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlnielvqQV--AE------ELQQVESCAV 474
Cdd:cd05911  366 TFDED------GWLH-TGDIGYFdEDGYLYIVDRKKELIKYKGF--------QVapAEleavllEHPGVADAAV 424
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
194-528 3.23e-09

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: 60.36  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 194 YVLHTSGTTGIPKivrvphkCIVPN-----IQH---FRVLFDITQEDVLF------------LASpltfdpsvveiflAL 253
Cdd:cd05943  253 YILYSSGTTGLPK-------CIVHGaggtlLQHlkeHILHCDLRPGDRLFyyttcgwmmwnwLVS-------------GL 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 254 SSGASLLIVPTSvKLLPSKLASV-LFSHHRVTVLQATPTL---LRRFGSQLIKSTVLSattSLRVLALGGEAFPSLTVLR 329
Cdd:cd05943  313 AVGATIVLYDGS-PFYPDTNALWdLADEEGITVFGTSAKYldaLEKAGLKPAETHDLS---SLRTILSTGSPLKPESFDY 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 330 SWRGEGNKTQIFNVYGITEVSSwATIYRIPEktlnstlkceLPVQLG---FPLLGTVVEVRDTNGFTIQEGSGQVflggr 406
Cdd:cd05943  389 VYDHIKPDVLLASISGGTDIIS-CFVGGNPL----------LPVYRGeiqCRGLGMAVEAFDEEGKPVWGEKGEL----- 452
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 407 nrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDSQIKRHGKRL-NIELVQ 460
Cdd:cd05943  453 --VC------TKPFPSMpvgfwndpdgsryRAAyfakypgvwahGDWIEItPRGGVVILGRSDGTLNPGGVRIgTAEIYR 524
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 461 QVaEELQQV-ESCAVTWYNQ---EKLILFMVSK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05943  525 VV-EKIPEVeDSLVVGQEWKdgdERVILFVKLRegvelDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
PRK03584 PRK03584
acetoacetate--CoA ligase;
194-528 5.25e-09

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 59.81  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 194 YVLHTSGTTGIPKivrvphkCIVPN-----IQHFRVL---FDITQEDVLF------------LASpltfdpsvveiflAL 253
Cdd:PRK03584 267 WILYSSGTTGLPK-------CIVHGhggilLEHLKELglhCDLGPGDRFFwyttcgwmmwnwLVS-------------GL 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 254 SSGASLLIVPTSvkllPSKL-ASVLF---SHHRVTVLQATP---TLLRRFGSQLIKSTVLSAttsLRVLALGG-----EA 321
Cdd:PRK03584 327 LVGATLVLYDGS----PFYPdPNVLWdlaAEEGVTVFGTSAkylDACEKAGLVPGETHDLSA---LRTIGSTGsplppEG 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 322 FpsltvlrSW--RGEGNKTQIFNVYGITEVSSwatiyripektlnstlkC------ELPV---QLGFPLLGTVVEVRDTN 390
Cdd:PRK03584 400 F-------DWvyEHVKADVWLASISGGTDICS-----------------CfvggnpLLPVyrgEIQCRGLGMAVEAWDED 455
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 391 GFTIQEGSGQVflggrnrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDS 445
Cdd:PRK03584 456 GRPVVGEVGEL-------VC------TKPFPSMplgfwndpdgsryRDAyfdtfpgvwrhGDWIEItEHGGVVIYGRSDA 522
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 446 QIKRHGKRLNI-ELVQQVaEELQQV-ESCAV--TWYNQ-EKLILFMVSK-----DASVKEYIFKELQKYL-PSHaVPDEL 514
Cdd:PRK03584 523 TLNRGGVRIGTaEIYRQV-EALPEVlDSLVIgqEWPDGdVRMPLFVVLAegvtlDDALRARIRTTIRTNLsPRH-VPDKI 600
                        410
                 ....*....|....
gi 557786167 515 VLIDSLPFTSHGKI 528
Cdd:PRK03584 601 IAVPDIPRTLSGKK 614
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1-443 5.97e-09

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 59.53  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167   1 MTLQELVHKAASCYMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHcdfqGIReiglycqPG----IDLPS--- 73
Cdd:PRK07656   5 MTLPELLARAARRFGDKEAYVFGD------QRLTYAELNARVRRAAAALAAL----GIG-------KGdrvaIWAPNsph 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  74 WI---LGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFKSFHETLLNydtftVEHndlvlfrlhwkntE 150
Cdd:PRK07656  68 WViaaLGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPA-----LEH-------------V 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 151 VNLMLNDGKEKYEKEKIKS--ISSEHVNEEKAEEHMDLrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDI 228
Cdd:PRK07656 130 VICETEEDDPHTEKMKTFTdfLAAGDPAERAPEVDPDD-----VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 229 TQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPtsvKLLPSKLASvLFSHHRVTVLQATPTLLRrfgsQLIKSTVL 306
Cdd:PRK07656 205 TEGDRYLAANPFfhVFGYKAG-VNAPLMRGATILPLP---VFDPDEVFR-LIETERITVLPGPPTMYN----SLLQHPDR 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 307 SAT--TSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRI--PEKTLNSTlkcelpvqLGFPLLGT 382
Cdd:PRK07656 276 SAEdlSSLRLAVTGAASMP-VALLERFESELGVDIVLTGYGLSEASGVTTFNRLddDRKTVAGT--------IGTAIAGV 346
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167 383 VVEVRDTNGFTIQEG-SGQVFLGGRNrVC--FLDDevtvPLGTMRA--------TGDFVTV-KDGEIFFLGRK 443
Cdd:PRK07656 347 ENKIVNELGEEVPVGeVGELLVRGPN-VMkgYYDD----PEATAAAidadgwlhTGDLGRLdEEGYLYIVDRK 414
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
192-528 7.94e-09

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 59.30  E-value: 7.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD---ITQEDVLFLASPL--TFDPSVVEIFLALSSGASLLI----- 261
Cdd:PRK08974 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpllHPGKELVVTALPLyhIFALTVNCLLFIELGGQNLLItnprd 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 262 VPTSVKLLpsklasvlfSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRvLALGGEAFPSLTVLRSWRgEGNKTQ 339
Cdd:PRK08974 288 IPGFVKEL---------KKYPFTAITGVNTLF----NALLNNEEFQELdfSSLK-LSVGGGMAVQQAVAERWV-KLTGQY 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 340 IFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDTNGFTIQEGSG--------QVFLGGRNRvcf 411
Cdd:PRK08974 353 LLEGYGLTECSPLVSVNPYDLDYYSGSI--------GLPVPSTEIKLVDDDGNEVPPGEPgelwvkgpQVMLGYWQR--- 421
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 412 ldDEVTVPL---GTMrATGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ELVQQVAEELQQVESCAVTWYNQ---EK 481
Cdd:PRK08974 422 --PEATDEVikdGWL-ATGDIAVMdEEGFLRIVDRKKDMILVSG--FNVypnEIEDVVMLHPKVLEVAAVGVPSEvsgEA 496
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 557786167 482 LILFMVSKDASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:PRK08974 497 VKIFVVKKDPSLtEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
198-533 4.98e-08

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: 56.37  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 276
Cdd:cd17647  117 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTQDDIgTPGRLAEW 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 277 LfSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIY 356
Cdd:cd17647  196 M-AKYGATVTHLTPAM-----GQLLTAQATTPFPKLHHAFFVGDILTKRDCLR-LQTLAENVRIVNMYGTTETQRAVSYF 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 357 RIPEKTLNST----LKCELPVQLGF---PLLgtVVEVRDTNGFTIQEGSGQVFL--GGR----------NRVCFLDD--- 414
Cdd:cd17647  269 EVPSRSSDPTflknLKDVMPAGRGMlnvQLL--VVNRNDRTQICGIGEVGEIYVraGGLaegyrglpelNKEKFVNNwfv 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 415 ------EVTVPLGT------------MRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRL-----------------NIEL 458
Cdd:cd17647  347 epdhwnYLDKDNNEpwrqfwlgprdrLYRTGDLgRYLPNGDCECCGRADDQVKIRGFRIelgeidthisqhplvreNITL 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 459 VQQVAEElqqvESCAVTWY-----NQEKLILFMVSKDASVK-EYIFKELQKY--------------LPSHAVPDELVLID 518
Cdd:cd17647  427 VRRDKDE----EPTLVSYIvprfdKPDDESFAQEDVPKEVStDPIVKGLIGYrklikdireflkkrLASYAIPSLIVVLD 502
                        410
                 ....*....|....*
gi 557786167 519 SLPFTSHGKIDVSEL 533
Cdd:cd17647  503 KLPLNPNGKVDKPKL 517
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
195-533 8.78e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 55.77  E-value: 8.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIV-RVPHkcIVPNIQHFRVLFDITQEDV---LFLASPLTFDPSVVEIFLALSSGASLLivptSVKLLP 270
Cdd:PRK13383 179 VLLTSGTTGKPKGVpRAPQ--LRSAVGVWVTILDRTRLRTgsrISVAMPMFHGLGLGMLMLTIALGGTVL----THRHFD 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAF-PSLTvLRSWRGEGNKtqIFNVYGITEV 349
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLdPTLG-QRFMDTYGDI--LYNGYGSTEV 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 350 SswatiyrIPEKTLNSTLKcELPVQLGFPLLGTVVEVRDTNGFTI-QEGSGQVFLGGR-NRVCFLDDEVTVPLGTMRATG 427
Cdd:PRK13383 330 G-------IGALATPADLR-DAPETVGKPVAGCPVRILDRNNRPVgPRVTGRIFVGGElAGTRYTDGGGKAVVDGMTSTG 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 428 DFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSKD------ASVKEY 496
Cdd:PRK13383 402 DMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghRLAAFVVLHPgsgvdaAQLRDY 481
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 557786167 497 IFKELQKYlpshAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK13383 482 LKDRVSRF----EQPRDINIVSSIPRNPTGKVLRKEL 514
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
192-528 1.01e-07

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


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 55.18  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALSSGASLLIVPTSVKllp 270
Cdd:cd05935   86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVgSLNTAVYVGGTYVLMARWDR--- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 sKLASVLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSLTVLRSWRgegnKTQIFNV--YGIT 347
Cdd:cd05935  163 -ETALELIEKYKVTFWTNIPTMLVDLLATPeFKTRDLS---SLKVLTGGGAPMPPAVAEKLLK----LTGLRFVegYGLT 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 348 EVsswatiyrIPEKTLNSTLKCELPVqLGFPLLGTVVEVRD-TNGFTIQEG-SGQVFLGG------------RNRVCFLD 413
Cdd:cd05935  235 ET--------MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNeVGEIVVRGpqifkgywnrpeETEESFIE 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 414 DE-----VTVPLGTMRAtgdfvtvkDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 484
Cdd:cd05935  306 IKgrrffRTGDLGYMDE--------EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISvpdeRVGEEVKA 377
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 557786167 485 FMVSKDA----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05935  378 FIVLRPEyrgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
178-535 1.10e-07

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: 55.55  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 178 EKAEEHMDLRLKHCLAYVLH-TSGTTGIPKIVRVPHKCI-VPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALS 254
Cdd:cd05928  161 EASTEHHCVETGSQEPMAIYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 255 SGASLLivptsVKLLPSKLASVL---FSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAF-PSltVLRS 330
Cdd:cd05928  241 QGACVF-----VHHLPRFDPLVIlktLSSYPITTFCGAPTVYRMLVQQDLSSYKFP---SLQHCVTGGEPLnPE--VLEK 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 331 WRgegNKT--QIFNVYGITEVSSWATIYRipektlnsTLKCElPVQLGFPLLGTVVEVRDTNGFTI---QEGSGQVFLGG 405
Cdd:cd05928  311 WK---AQTglDIYEGYGQTETGLICANFK--------GMKIK-PGSMGKASPPYDVQIIDDNGNVLppgTEGDIGIRVKP 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 406 RNRVCFLDDEVTVPLGTMRAT-GDF-------VTVKDGEIFFLGRKDSQIKRHGKRLN-IELVQQVAEELQQVESCAVTW 476
Cdd:cd05928  379 IRPFGLFSGYVDNPEKTAATIrGDFyltgdrgIMDEDGYFWFMGRADDVINSSGYRIGpFEVESALIEHPAVVESAVVSS 458
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557786167 477 YNQ---EKLILFMV------SKDasvKEYIFKELQKYLPS----HAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05928  459 PDPirgEVVKAFVVlapqflSHD---PEQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRD 527
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
192-537 1.12e-07

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: 55.37  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFL-ALSSGASLLIVPTSVKLLP 270
Cdd:cd05906  169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLrAVYLGCQQVHVPTEEILAD 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVLFSHHRVTVLQAtP----TLLRRFGSQLIKSTV-LSattSLRVLALGGEAFPSLTV---LRSWRGEGNKTQIFN 342
Cdd:cd05906  249 PLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWdLS---SLRYLVNAGEAVVAKTIrrlLRLLEPYGLPPDAIR 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 343 -VYGITEVSSWATIYRIPEkTLNSTLKCELpVQLGFPLLGTVVEVRDTNGFTIQEG-------SGQVFLGG------RNR 408
Cdd:cd05906  325 pAFGMTETCSGVIYSRSFP-TYDHSQALEF-VSLGRPIPGVSMRIVDDEGQLLPEGevgrlqvRGPVVTKGyynnpeANA 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 409 VCFLDDevtvplGTMRaTGDFVTVKDGEIFFLGRKDSQIKRHG-KRLNIELvQQVAEELQQVES-----CAVTWYNQ--E 480
Cdd:cd05906  403 EAFTED------GWFR-TGDLGFLDNGNLTITGRTKDTIIVNGvNYYSHEI-EAAVEEVPGVEPsftaaFAVRDPGAetE 474
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 481 KLILFMVSkdASVKEYIFKELQKYLPSHAV------PDELVLI--DSLPFTSHGKIDVSELNKIY 537
Cdd:cd05906  475 ELAIFFVP--EYDLQDALSETLRAIRSVVSrevgvsPAYLIPLpkEEIPKTSLGKIQRSKLKAAF 537
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
197-540 1.17e-07

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 55.14  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 197 HTSGTTGIPKIVRVPHKcivPNIQHFRVlfdITQEDVLFLASPLTFDPsVVEIFLALSSGASLLIVPTSVKL-LP-SKL- 273
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHR---SNVLHALM---ANNGDALGTSAADTMLP-VVPLFHANSWGIAFSAPSMGTKLvMPgAKLd 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 274 -ASV--LFSHHRVTVLQATPT----LLrrfgsQLIKSTVLSATTsLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 346
Cdd:PRK06018 257 gASVyeLLDTEKVTFTAGVPTvwlmLL-----QYMEKEGLKLPH-LKMVVCGGSAMPR-SMIKAFEDMG--VEVRHAWGM 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 347 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQEgSGQVFlgGRNRVC-------------- 410
Cdd:PRK06018 328 TEMSPLGTLAALKPPFSKLPGDARLDVLQkqGYPPFGVEMKITDDAGKELPW-DGKTF--GRLKVRgpavaaayyrvdge 404
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 411 FLDDEvtvplgTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN-IELvQQVAEELQQVESCAVT------WYNQEKL 482
Cdd:PRK06018 405 ILDDD------GFFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISsIDL-ENLAVGHPKVAEAAVIgvyhpkWDERPLL 477
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557786167 483 ILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY 540
Cdd:PRK06018 478 IVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDY 535
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
198-474 1.35e-07

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 55.19  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVpnIQHFRVLFDI--TQEDVLFLASPLtfdpsvVEIFlALSSGASLLIVPTSVKLLP---SK 272
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALI--VQSLAKIAIVgyGEDDVYLHTAPL------CHIG-GLSSALAMLMVGACHVLLPkfdAK 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 273 LASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVSSW 352
Cdd:PLN02860 251 AALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSR-LLPDAKKLFPNAKLFSAYGMTEACSS 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 353 ATIYRIPEKTLNS----TLKCELPVQLGFPLLGTV--------VEVRDtnGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL 420
Cdd:PLN02860 330 LTFMTLHDPTLESpkqtLQTVNQTKSSSVHQPQGVcvgkpaphVELKI--GLDESSRVGRILTRGPHVMLGYWGQNSETA 407
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 421 GTMRA-----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 474
Cdd:PLN02860 408 SVLSNdgwldTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
198-366 4.36e-07

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 53.05  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSkLAS 275
Cdd:cd05917   10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPSFDPLAV-LEA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 276 VlfSHHRVTVLQATPTL-LRRFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSSWAT 354
Cdd:cd05917   88 I--EKEKCTALHGVPTMfIAELEHPDFDKFDLS---SLRTGIMAGAPCPP-ELMKRVIEVMNMKDVTIAYGMTETSPVST 161
                        170
                 ....*....|....*
gi 557786167 355 IYRI---PEKTLNST 366
Cdd:cd05917  162 QTRTddsIEKRVNTV 176
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
192-444 4.49e-07

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 53.43  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlFLAspltfdpsVVEIF----------LALSSGASLLI 261
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESV-VLA--------VLPLFhvtgmvhsmnAPIYAGATVVL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 262 VPTSVKllpsKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPS--------LTVLRSWR 332
Cdd:PRK08314 263 MPRWDR----EAAARLIERYRVTHWTNIPTMVVDFlASPGLAERDLS---SLRYIGGGGAAMPEavaerlkeLTGLDYVE 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 333 GegnktqifnvYGITEVSSwATIYRIPEKTlnsTLKCelpvqLGFPLLGTVVEVRDTNgfTIQE-GSG----------QV 401
Cdd:PRK08314 336 G----------YGLTETMA-QTHSNPPDRP---KLQC-----LGIPTFGVDARVIDPE--TLEElPPGevgeivvhgpQV 394
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 557786167 402 FLGGRNRvcflddevtvPLGTMRAtgdFVTVkDGEIFF----LGRKD 444
Cdd:PRK08314 395 FKGYWNR----------PEATAEA---FIEI-DGKRFFrtgdLGRMD 427
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
193-533 4.83e-07

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: 53.28  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPniqhfRVLFDITQEDVLFLAS-------PLTFDPSVVEIFLALSSGASLLIVPTS 265
Cdd:cd05923  153 AFVFYTSGTTGLPKGAVIPQRAAES-----RVLFMSTQAGLRHGRHnvvlglmPLYHVIGFFAVLVAALALDGTYVVVEE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 266 VKllpSKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVY 344
Cdd:cd05923  228 FD---PADALKLIEQERVTSLFATPTHLDALaAAAEFAGLKLS---SLRHVTFAGATMPD-AVLERVN-QHLPGEKVNIY 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 345 GITEVSSwATIYRIPekTLNSTLKCELPVQLGF-PLLGTVVE---VRDTNGFTIQEGSGQVFLGGRNRvcFLDDEVTVPL 420
Cdd:cd05923  300 GTTEAMN-SLYMRDA--RTGTEMRPGFFSEVRIvRIGGSPDEalaNGEEGELIVAAAADAAFTGYLNQ--PEATAKKLQD 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 421 GTMRaTGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKE 495
Cdd:cd05923  375 GWYR-TGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwgqsVTACVVPREGTLSA 453
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 557786167 496 yifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05923  454 ---DELDQFcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
193-473 9.16e-07

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 52.46  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLLP 270
Cdd:cd05910   88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLfaLFGPA-----LGLTS-----VIP---DMDP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASV----LFS---HHRVTVLQATPTLLR---RFGSQLIKStvlsaTTSLRVLALGGEAFPSLTVLRSWRGEGNKTQI 340
Cdd:cd05910  155 TRPARAdpqkLVGairQYGVSIVFGSPALLErvaRYCAQHGIT-----LPSLRRVLSAGAPVPIALAARLRKMLSDEAEI 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 341 FNVYGITE---VSSwatiyrIPEKTLNSTlKCELPVQ-----LGFPLLGTVVEVRDTNGFTIQE--GSGQVFLGGRNRVC 410
Cdd:cd05910  230 LTPYGATEalpVSS------IGSRELLAT-TTAATSGgagtcVGRPIPGVRVRIIEIDDEPIAEwdDTLELPRGEIGEIT 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 411 FLDDEVTV-----PLGTMRA------------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC 472
Cdd:cd05910  303 VTGPTVTPtyvnrPVATALAkiddnsegfwhrMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382

                 .
gi 557786167 473 A 473
Cdd:cd05910  383 A 383
PRK08316 PRK08316
acyl-CoA synthetase; Validated
191-537 1.02e-06

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 52.24  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 191 CLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGASLLIV--PTSV 266
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL-YHCAQLDVFLgpYLYVGATNVILdaPDPE 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 267 KLLPsklasvLFSHHRVTVLQATPT----LLRrfgSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFN 342
Cdd:PRK08316 251 LILR------TIEAERITSFFAPPTvwisLLR---HPDFDTRDLS---SLRKGYYGASIMP-VEVLKELRERLPGLRFYN 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 343 VYGITEVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGtvVEVR--DTNGFTIQEG--------SGQVFLGgrnrvcFL 412
Cdd:PRK08316 318 CYGQTEIAPLATVLG-PEEHL------RRPGSAGRPVLN--VETRvvDDDGNDVAPGevgeivhrSPQLMLG------YW 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 413 DD-EVTVP-----------LGTMRATGdFVTVKDgeifflgRKDSQIKRHGkrlniELV--QQVAEELQQ---VESCAVT 475
Cdd:PRK08316 383 DDpEKTAEafrggwfhsgdLGVMDEEG-YITVVD-------RKKDMIKTGG-----ENVasREVEEALYThpaVAEVAVI 449
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557786167 476 WYNQEKLI----LFMVSKD-ASVKEyifKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIY 537
Cdd:PRK08316 450 GLPDPKWIeavtAVVVPKAgATVTE---DELIAHcrarLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
294-535 1.18e-06

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 51.58  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 294 RRFGS----QLIKS-TVLSATTSLRVLA---LGGEAFPSlTVLRSWRGEGnkTQIFNVYGITEVSSwatiyripektlns 365
Cdd:PRK07824 127 RRYTSlvpmQLAKAlDDPAATAALAELDavlVGGGPAPA-PVLDAAAAAG--INVVRTYGMSETSG-------------- 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 366 tlKCelpVQLGFPLLGTVVEVRDtngftiqegsGQVFLGG-------RNRVcflDDEVTVPLGTMRaTGDFVTVKDGEIF 438
Cdd:PRK07824 190 --GC---VYDGVPLDGVRVRVED----------GRIALGGptlakgyRNPV---DPDPFAEPGWFR-TDDLGALDDGVLT 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 439 FLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL---ILFMVSKDASVKEYIfKELQKY----LPSHAVP 511
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLgqrVVAAVVGDGGPAPTL-EALRAHvartLDRTAAP 329
                        250       260
                 ....*....|....*....|....
gi 557786167 512 DELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK07824 330 RELHVVDELPRRGIGKVDRRALVR 353
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
310-536 3.69e-06

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 50.59  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 310 TSLRVLALGGEAFPSLTVLRsWRGEGNKTqIFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDT 389
Cdd:PRK12492 333 SALKLTNSGGTALVKATAER-WEQLTGCT-IVEGYGLTETSPVASTNPYGELARLGTV--------GIPVPGTALKVIDD 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 390 NGFtiqegsgQVFLGGRNRVCFLDDEV-----TVPLGTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN 455
Cdd:PRK12492 403 DGN-------ELPLGERGELCIKGPQVmkgywQQPEATAEAldaegwfkTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVY 475
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 456 IELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKeyiFKELQKY----LPSHAVPDELVLIDSLPFTSHGK 527
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAIGVPDERsgeaVKLFVVARDPGLS---VEELKAYckenFTGYKVPKHIVLRDSLPMTPVGK 552

                 ....*....
gi 557786167 528 IDVSELNKI 536
Cdd:PRK12492 553 ILRRELRDI 561
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
191-533 6.95e-06

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: 49.80  E-value: 6.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 191 CLAYVlhTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLASPLTFDPSVV--EIFLALSSGASLLIVPTSvKL 268
Cdd:cd05970  188 LLVYF--SSGTTGMPKMVEHDFTYPLGHIVTAKYWQNV-REGGLHLTVADTGWGKAVwgKIYGQWIAGAAVFVYDYD-KF 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 269 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAFpSLTVLRSWRgEGNKTQIFNVYGITE 348
Cdd:cd05970  264 DPKALLEKL-SKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEAL-NPEVFNTFK-EKTGIKLMEGFGQTE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 -VSSWATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVflggrnrVCFLDDEVtvPLGTMRA- 425
Cdd:cd05970  338 tTLTIATFPWMEPK----------PGSMGKPAPGYEIDLIDREGRSCEAGeEGEI-------VIRTSKGK--PVGLFGGy 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 426 -----------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LI 483
Cdd:cd05970  399 ykdaektaevwhdgyyhTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvVK 478
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 484 LFMV-SKDASVKEYIFKELQKYLPSHAVPDE----LVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05970  479 ATIVlAKGYEPSEELKKELQDHVKKVTAPYKypriVEFVDELPKTISGKIRRVEI 533
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
195-528 7.87e-06

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: 49.04  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGASllIVPTSVKLLPSK 272
Cdd:cd17638    5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYK-AGIVACLLTGAT--VVPVAVFDVDAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 273 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITE 348
Cdd:cd17638   82 LEAI--ERERITVLPGPPTL---FQSLLdhpgRKKFDLS---SLRAAVTGAATVPVELVRR-MRSELGFETVLTAYGLTE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 349 VSSwATIYRI--PEKTLNSTlkcelpvqLGFPLLGTVVEVRDtngftiqegSGQVFLGGRN-RVCFLDDevtvPLGTMRA 425
Cdd:cd17638  153 AGV-ATMCRPgdDAETVATT--------CGRACPGFEVRIAD---------DGEVLVRGYNvMQGYLDD----PEATAEA 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 426 --------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 492
Cdd:cd17638  211 idadgwlhTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgKAFVVARPGV 290
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 557786167 493 --VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17638  291 tlTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
72-290 1.17e-05

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 48.94  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  72 PSWI---LGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVE-KKQINKFKSFHETLLnydtfTVEHndLVLFrlhwk 147
Cdd:COG1022   76 PEWViadLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELP-----SLRH--IVVL----- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 148 ntevnlmlnDGKEKYEKEKIKSIS------SEHVNEEKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQH 221
Cdd:COG1022  144 ---------DPRGLRDDPRLLSLDellalgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557786167 222 FRVLFDITQEDV--LFLasPL--TFDpSVVEIFlALSSGASlLIVPTSVKLLPSKLASVlfshhRVTVLQATP 290
Cdd:COG1022  215 LLERLPLGPGDRtlSFL--PLahVFE-RTVSYY-ALAAGAT-VAFAESPDTLAEDLREV-----KPTFMLAVP 277
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
407-529 2.70e-05

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: 47.83  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 407 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNielvqqvAEELQ-------QVESCAVTWYN 478
Cdd:COG1021  401 NARAFTPD------GFYR-TGDLVRRtPDGYLVVEGRAKDQINRGGEKIA-------AEEVEnlllahpAVHDAAVVAMP 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 479 Q----EKLILFMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 529
Cdd:COG1021  467 DeylgERSCAFVVPRGEPLT---LAELRRFLrerglAAFKLPDRLEFVDALPLTAVGKID 523
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
192-447 7.12e-05

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: 46.28  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdPSVVEIFLALSSGAS--LLIVPTSVK 267
Cdd:cd05914   91 VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLhhIY-PLTFTLLLPLLNGAHvvFLDKIPSAK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 268 LLPSKLASV----------LFSHHRVTVLQ------------ATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsL 325
Cdd:cd05914  170 IIALAFAQVtptlgvpvplVIEKIFKMDIIpkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN-P 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 326 TVLRSWRGEGNKTQIfnVYGITEVSSWATiYRIPEKT-LNSTlkcelpvqlGFPLLGTVVEVRDTNGFTiqeGSGQVFLG 404
Cdd:cd05914  249 DVEEFLRTIGFPYTI--GYGMTETAPIIS-YSPPNRIrLGSA---------GKVIDGVEVRIDSPDPAT---GEGEIIVR 313
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 557786167 405 GRN--RVCFLDDEVTV----PLGTMRaTGDFVT-VKDGEIFFLGRKDSQI 447
Cdd:cd05914  314 GPNvmKGYYKNPEATAeafdKDGWFH-TGDLGKiDAEGYLYIRGRKKEMI 362
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
552-608 7.50e-05

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 41.76  E-value: 7.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557786167 552 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:COG0236    3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
193-355 9.56e-05

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 45.96  E-value: 9.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVL--FLASPLTFDPSVVEIFLALssgASLLIVPTSVKLLP 270
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMmsFLPPFHAYGFNSCTLFPLL---SGVPVVFAYNPLYP 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVLFSHHrVTVLQATPTllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSltvlrSWRGEGNKT----QIFNVY 344
Cdd:PRK06334 263 KKIVEMIDEAK-VTFLGSTPV----FFDYILKTAKKQESClpSLRFVVIGGDAFKD-----SLYQEALKTfphiQLRQGY 332
                        170
                 ....*....|.
gi 557786167 345 GITEVSSWATI 355
Cdd:PRK06334 333 GTTECSPVITI 343
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
193-536 1.66e-04

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 45.47  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGAsllivptSVKLLP 270
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLT-VGLFTPLLTGA-------EVFLYP 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLasvlfsHHRV----------TVLQATPTLL---RRFGSQLikstvlsATTSLRVLALGGEAFpSLTVLRSWRgEGNK 337
Cdd:PRK08043 440 SPL------HYRIvpelvydrncTVLFGTSTFLgnyARFANPY-------DFARLRYVVAGAEKL-QESTKQLWQ-DKFG 504
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 338 TQIFNVYGITEVSSWATIyRIPEKTLNSTLKCELPvqlgfpllgtVVEVRDTNGFTIQEGsGQVFLGGRN------RVcF 411
Cdd:PRK08043 505 LRILEGYGVTECAPVVSI-NVPMAAKPGTVGRILP----------GMDARLLSVPGIEQG-GRLQLKGPNimngylRV-E 571
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 412 LDDEVTVP-----LGTMRA----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ-- 479
Cdd:PRK08043 572 KPGVLEVPtaenaRGEMERgwydTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDas 651
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557786167 480 --EKLILFmvSKDASVKEyifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 536
Cdd:PRK08043 652 kgEALVLF--TTDSELTR---EKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
193-535 1.72e-04

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 45.16  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL--FDITQEDVLFLASPLTFDPSVVEIFLALSSGASLliVPTSVKLLP 270
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPL--VFPGPDLSA 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 271 SKLASVL-FSHHRVTvlQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSLtVLRSWRgEGNKTQIFNVYGITEV 349
Cdd:PRK05620 262 PTLAKIIaTAMPRVA--HGVPTLWIQLMVHYLKNP--PERMSLQEIYVGGSAVPPI-LIKAWE-ERYGVDVVHVWGMTET 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 350 SSWATIYRIPEKTLNSTL------KCELPVQLGFPLL--GTVVEVRDTNGFTIQ----------------EGSGQVFLGG 405
Cdd:PRK05620 336 SPVGTVARPPSGVSGEARwayrvsQGRFPASLEYRIVndGQVMESTDRNEGEIQvrgnwvtasyyhspteEGGGAASTFR 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 406 RNRVCFLDDEVTVPlGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK--- 481
Cdd:PRK05620 416 GEDVEDANDRFTAD-GWLR-TGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwge 493
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 482 --LILFMVSKD----ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK05620 494 rpLAVTVLAPGieptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
195-350 3.08e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 44.38  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSk 272
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFG-MVLANLGCMTVGACLVYPNEAFDPLAT- 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 273 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:PRK12583 284 LQAV--EEERCTALYGVPTM---FIAELdhpqRGNFDLS---SLRTGIMAGAPCP-IEVMRRVMDEMHMAEVQIAYGMTE 354

                 ..
gi 557786167 349 VS 350
Cdd:PRK12583 355 TS 356
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
557-608 3.92e-04

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: 39.08  E-value: 3.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557786167  557 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
192-355 5.81e-04

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: 43.36  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF----RVLFDITQEDVLFLASPLT--FDPSVVEIFLA------LSSGASL 259
Cdd:cd05927  116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAhiFERVVEALFLYhgakigFYSGDIR 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 260 LIVPTSVKLLPSKLASV--LFS--HHRV-TVLQATPTLLRR---FGSQL----IKSTVLSATTSLRVL-------ALGGE 320
Cdd:cd05927  196 LLLDDIKALKPTVFPGVprVLNriYDKIfNKVQAKGPLKRKlfnFALNYklaeLRSGVVRASPFWDKLvfnkikqALGGN 275
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 557786167 321 -------AFPS----LTVLRSWRGegnkTQIFNVYGITEVSSWATI 355
Cdd:cd05927  276 vrlmltgSAPLspevLEFLRVALG----CPVLEGYGQTECTAGATL 317
PRK09274 PRK09274
peptide synthase; Provisional
192-349 6.81e-04

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 43.35  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLL 269
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLfaLFGPA-----LGMTS-----VIP---DMD 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 270 PSKLASV----LFS---HHRVTVLQATPTLLRRFGsQLIKSTVLSATTSLRVLALGGEAFPSLTV-LRSWRGEGnkTQIF 341
Cdd:PRK09274 243 PTRPATVdpakLFAaieRYGVTNLFGSPALLERLG-RYGEANGIKLPSLRRVISAGAPVPIAVIErFRAMLPPD--AEIL 319

                 ....*...
gi 557786167 342 NVYGITEV 349
Cdd:PRK09274 320 TPYGATEA 327
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
193-350 8.21e-04

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 42.84  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPN-IQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVkLLPS 271
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA-FDPG 255
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786167 272 KLASVLfSHHRVTVLQATPTllrRFGSQLIKSTVLSATTSLRVLALGGeAFPSLTVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:PRK07786 256 QLLDVL-EAEKVTGIFLVPA---QWQAVCAEQQARPRDLALRVLSWGA-APASDTLLRQMAATFPEAQILAAFGQTEMS 329
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
191-296 1.12e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 42.30  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 191 CLAYVLHTSGTTGIPKIVR--VPHKCI----VPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIvpt 264
Cdd:PRK13390 149 CGAVMLYSSGTTGFPKGIQpdLPGRDVdapgDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVL--- 225
                         90       100       110
                 ....*....|....*....|....*....|..
gi 557786167 265 sVKLLPSKLASVLFSHHRVTVLQATPTLLRRF 296
Cdd:PRK13390 226 -AKRFDAQATLGHVERYRITVTQMVPTMFVRL 256
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
198-474 1.25e-03

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: 42.17  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCiVPnIQHFRVLFDITQE--DV-LFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPSKLA 274
Cdd:cd05974   93 TSGTTSKPKLVEHTHRS-YP-VGHLSTMYWIGLKpgDVhWNISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 275 SVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAF-PSL--TVLRSWrgegNKTqIFNVYGITEVSS 351
Cdd:cd05974  170 AAL-VRYGVTTLCAPPTVWR----MLIQQDLASFDVKLREVVGAGEPLnPEVieQVRRAW----GLT-IRDGYGQTETTA 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 352 WATiyripektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFL-----DDEVT--VPLGTMR 424
Cdd:cd05974  240 LVG---------NSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVGLMkgyagDPDKTahAMRGGYY 310
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 557786167 425 ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 474
Cdd:cd05974  311 RTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
PRK07787 PRK07787
acyl-CoA synthetase; Validated
193-533 1.34e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 42.28  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL----------------------TFDPSVVEIF 250
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLfhvhglvlgvlgplrignrfvhTGRPTPEAYA 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 251 LALSSGASLLI-VPTsvkllpsklasvlfSHHRVTvlqATPTLLRRFGSQ--LIK-STVLSATTSLRVLALGGEAfpslT 326
Cdd:PRK07787 211 QALSEGGTLYFgVPT--------------VWSRIA---ADPEAARALRGArlLVSgSAALPVPVFDRLAALTGHR----P 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 327 VLRswrgegnktqifnvYGITE----VSSWATIYRIPEktlnstlkcelpvQLGFPLLGTVVEVRDTNGFTIQE-----G 397
Cdd:PRK07787 270 VER--------------YGMTEtlitLSTRADGERRPG-------------WVGLPLAGVETRLVDEDGGPVPHdgetvG 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 398 SGQV-----FLGGRNR-----VCFLDDevtvplGTMRaTGDFVTVK-DGEIFFLGRKDSQ-IKRHGKRLNIELVQQVAEE 465
Cdd:PRK07787 323 ELQVrgptlFDGYLNRpdataAAFTAD------GWFR-TGDVAVVDpDGMHRIVGRESTDlIKSGGYRIGAGEIETALLG 395
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557786167 466 LQQVESCAVTWYNQEKL----ILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK07787 396 HPGVREAAVVGVPDDDLgqriVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
198-294 1.62e-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: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 198 TSGTTGIPKIVRVPHKCIVpNIQHFRVLFDITQEDVLFLASPLTFDP-SVVEIFLALSSGASLlivptsvkLLPSKLASV 276
Cdd:cd05938  152 TSGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSgFLLGIGGCIELGATC--------VLKPKFSAS 222
                         90       100
                 ....*....|....*....|..
gi 557786167 277 LF----SHHRVTVLQATPTLLR 294
Cdd:cd05938  223 QFwddcRKHNVTVIQYIGELLR 244
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
735-830 2.25e-03

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 41.34  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 735 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 811
Cdd:COG1520    9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86
                         90
                 ....*....|....*....
gi 557786167 812 DRIesSACVSKCGNFIVVG 830
Cdd:COG1520   87 EPL--SGGVGADGGLVVVG 103
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
196-264 3.18e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 41.17  E-value: 3.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557786167 196 LHTSGTTGIPKIVRVPhkcivpniqHFRVL---------FDITQEDVLFLASPLTFDPSVVEIF-LALSSGASLLIVPT 264
Cdd:PRK13388 156 IFTSGTTGAPKAVRCS---------HGRLAfagralterFGLTRDDVCYVSMPLFHSNAVMAGWaPAVASGAAVALPAK 225
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
198-252 3.28e-03

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 41.13  E-value: 3.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 198 TSGTTGIPKIVRVPHKCIVPNI--QHFRVLFDItQEDVL--------------FLASPLTFDPSVVEI----FLA 252
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAeaMFVAAEFDV-ETDVMvswlplfhdmgmvgFLTVPMYFGAELVKVtpmdFLR 233
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
750-830 3.95e-03

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 40.30  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167  750 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 829
Cdd:TIGR03300  35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110

                  .
gi 557786167  830 G 830
Cdd:TIGR03300 111 G 111
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
193-261 4.14e-03

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 4.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557786167 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL------TFDPSVVeiflaLSSGASLLI 261
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLyhntggTVAWSSV-----LAAGATLAL 271
PRK07514 PRK07514
malonyl-CoA synthase; Validated
192-295 6.15e-03

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 40.24  E-value: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557786167 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-----TFdpsvVEIFLALSSGASLLIVPtsv 266
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLF----VATNVALLAGASMIFLP--- 230
                         90       100
                 ....*....|....*....|....*....
gi 557786167 267 KLLPSKLASVLfshHRVTVLQATPTLLRR 295
Cdd:PRK07514 231 KFDPDAVLALM---PRATVMMGVPTFYTR 256
 
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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