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Conserved domains on  [gi|499188982|ref|WP_010886522|]
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MULTISPECIES: plipastatin non-ribosomal peptide synthetase PpsE [Bacillus]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 11436933)

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

EC:  6.2.1.-
Gene Ontology:  GO:0031177|GO:0019184|GO:0016874|GO:0044550
PubMed:  26604034|28526268|29444491|20153164|26429504

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 19-1043 0e+00

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


:

Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPhlsGPRQVVMTEREFHLN 98
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG---RPVQVIQPVVAAPLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:COG1020    96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLDPVRP-----YSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKE 253
Cdd:COG1020   176 GAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:COG1020   256 LARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAepFTCQ--PLFDIQANTALKQE-----LIDHIIVFENYPlqqkiadsADQTDSP-LQIDQVQVSEQSG-YNFNLVVA 404
Cdd:COG1020   334 LAA--YAHQdlPFERLVEELQPERDlsrnpLFQVMFVLQNAP--------ADELELPgLTLEPLELDSGTAkFDLTLTVV 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  405 P-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFR 483
Cdd:COG1020   404 EtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  484 EQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:COG1020   484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQKGLEQN-AAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVV 642
Cdd:COG1020   564 RLAYMLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  643 SLVRNSN-YTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLA 721
Cdd:COG1020   644 NLLAWMQrRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  722 QVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYA--GPIPIGKPISNSTAYILD 799
Cdd:COG1020   724 DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDAdgGSVPIGRPIANTRVYVLD 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:COG1020   804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRI 883

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD---FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:COG1020   884 ELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaalLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  956 DRSALPIPENKPAKRQNiILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFE 1035
Cdd:COG1020   964 DRLALPAPAAAAAAAAA-APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042


                  ....*...
gi 499188982 1036 HPTIAQLA 1043
Cdd:COG1020  1043 AAAAAAAA 1050
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 1070-1270 6.74e-24

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


The actual alignment was detected with superfamily member pfam00975:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 223  Bit Score: 101.31  E-value: 6.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1070 LFCFPPISGFGIYFKDLALLLNEKAAVY-----GFHFIEQ-----DTRIEQYVNCMTDIQPEGPYVLLGYSAGGNLAFEV 1139
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLavqypGRGRGEPplnsiEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1140 AQAMERKGLEVSDFIIVDAY---LKEQPLPIDTGNDESAAYL------PEAVREKvmkkkrnyQEYWAQLL-----NEGH 1205
Cdd:pfam00975   83 ARRLERQGEAVRSLFLSDASaphTVRYEASRAPDDDEVVAEFtdeggtPEELLED--------EELLSMLLpalraDYRA 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  1206 IKASIHFIEAG--IHPETSGHTGLTKWEGACGNYSEYTGFGAHKDMLEGT--YAEKNADIILDILEKIT 1270
Cdd:pfam00975  155 LESYSCPPLDAqsATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDhfYLIEHLEAVLEIIEAKL 223
 
Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 19-1043 0e+00

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


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPhlsGPRQVVMTEREFHLN 98
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG---RPVQVIQPVVAAPLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:COG1020    96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLDPVRP-----YSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKE 253
Cdd:COG1020   176 GAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:COG1020   256 LARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAepFTCQ--PLFDIQANTALKQE-----LIDHIIVFENYPlqqkiadsADQTDSP-LQIDQVQVSEQSG-YNFNLVVA 404
Cdd:COG1020   334 LAA--YAHQdlPFERLVEELQPERDlsrnpLFQVMFVLQNAP--------ADELELPgLTLEPLELDSGTAkFDLTLTVV 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  405 P-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFR 483
Cdd:COG1020   404 EtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  484 EQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:COG1020   484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQKGLEQN-AAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVV 642
Cdd:COG1020   564 RLAYMLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  643 SLVRNSN-YTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLA 721
Cdd:COG1020   644 NLLAWMQrRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  722 QVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYA--GPIPIGKPISNSTAYILD 799
Cdd:COG1020   724 DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDAdgGSVPIGRPIANTRVYVLD 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:COG1020   804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRI 883

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD---FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:COG1020   884 ELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaalLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  956 DRSALPIPENKPAKRQNiILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFE 1035
Cdd:COG1020   964 DRLALPAPAAAAAAAAA-APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042


                  ....*...
gi 499188982 1036 HPTIAQLA 1043
Cdd:COG1020  1043 AAAAAAAA 1050
PRK12467 PRK12467
peptide synthase; Provisional
 10-1174 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 827.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   10 TIKKIKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGsLSYDWFQRSIQAIIDRHDIFRTVFLpHVPHLSGPRQVV 89
Cdd:PRK12467 2639 AVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFL-WDGELEEPLQVV 2716

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   90 MTEREFHLNSEDISHLPtnDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEF 169
Cdd:PRK12467 2717 YKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEV 2794

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  170 MQIYqsihAGKPLSLDPVRpYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPR-VSDKETKESYHREDLIFSLNKPLT 248
Cdd:PRK12467 2795 LQRY----FGQPPPAREGR-YRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARaLYPAPAEAVAGHGAHYLHLDATQT 2869

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  249 DKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIR 328
Cdd:PRK12467 2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  329 CQKEMLEAEPFTCQPLFDIQANTAL-KQELIDHIIVFENYPLQQKIADSADQTdspLQIDQVQVSEQSGYNFNLVVAPGE 407
Cdd:PRK12467 2950 VQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGAPSG---LRFGAVSSREQTNYPLTLAVGLGD 3026

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  408 ELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFREQAE 487
Cdd:PRK12467 3027 TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVA 3106

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  488 KTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSF 567
Cdd:PRK12467 3107 RTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  568 MLEETQAKMLIVQKGLEQN--AAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLV 645
Cdd:PRK12467 3187 MIEDSGVKLLLTQAHLLEQlpAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHL 3266

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 RNS-NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDkSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQV- 723
Cdd:PRK12467 3267 CWIaEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDa 3345

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 -RADMFRgLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRD---YAGPIPIGKPISNSTAYILD 799
Cdd:PRK12467 3346 gGADCAS-LDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDavcEAPYAPIGRPVAGRSIYVLD 3424

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL-PGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:PRK12467 3425 GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTD--TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  957 RSALPIPENKpaKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEH 1036
Cdd:PRK12467 3585 RKALPDPDAK--GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSA 3662

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1037 PTIAQLAEKLyskQLTAANEQHVIKLN--QHGAQNLFCFPPISGFGIYFKDLALLLNEKAAVYGF---HFIE---QDTRI 1108
Cdd:PRK12467 3663 PTIAELAGYS---PLGDVPVNLLLDLNrlETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLtcrHLLDdgwQDTSL 3739

                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1109 E----QYVNCMTDIQPEGPYVLLGYSAGGNLAFEVAQAMERKGLEVSDFIIVDAYLkeqPLPIDTGNDES 1174
Cdd:PRK12467 3740 QamavQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTL---PLPDEFVPQAE 3806
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 480-960 0e+00

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: 759.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDaQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVID-EALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQ 719
Cdd:cd12117   160 GVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  720 LAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDY--AGPIPIGKPISNSTAYI 797
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDevAGSIPIGRPIANTRVYV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKR 877
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAAVTLREKD-GEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd12117   400 IELGEIEAALRAHPGVREAVVVVREDAgGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479


                  ....
gi 499188982  957 RSAL 960
Cdd:cd12117   480 RRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 503-898 2.21e-157

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: 477.53  E-value: 2.21e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   503 SYKELDKRSNALARELIQ-KGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQK 581
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   582 GLEQNAAFSGTCIISDAQGLMEEND-----IPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR-NSNYTSASG 655
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDdapapPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAwLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   656 DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLL-ENDITVLFLTTALFNQLAQVRADMFRGLHTL 734
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIaEHPVTVLNLTPSLLALLAAALPPALASLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   735 YVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAG---PIPIGKPISNSTAYILDTKGRLLPIGVPG 811
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPresPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   812 ELCVGGDGVAKGYLNRVDLTNAVFSPHPFLP--GERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLE 889
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 499188982   890 MEGVQEAAV 898
Cdd:TIGR01733  401 HPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 14-462 4.34e-132

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


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 412.88  E-value: 4.34e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982    14 IKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvpHLSGPRQVVMTER 93
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQ--ENGEPVQVILEER 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982    94 EFHLNSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIY 173
Cdd:pfam00668   79 PFELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   174 QSIHAGKPLSLDPVRPYSTYISWLTNR----DKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTD 249
Cdd:pfam00668  159 QQLLKGEPLPLPPKTPYKDYAEWLQQYlqseDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   250 KLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRC 329
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   330 QKEMLEAEPFTCQPLFDIQANTALKQE-----LIDHIIVFENYPLQQKIADSADQTDSPLQIdQVQVSEQSGYNFNLVVA 404
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYLGQDSQEEEFQLSELDLSV-SSVIEEEAKYDLSLTAS 395

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982   405 P-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIV 462
Cdd:pfam00668  396 ErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1070-1270 6.74e-24

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


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 101.31  E-value: 6.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1070 LFCFPPISGFGIYFKDLALLLNEKAAVY-----GFHFIEQ-----DTRIEQYVNCMTDIQPEGPYVLLGYSAGGNLAFEV 1139
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLavqypGRGRGEPplnsiEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1140 AQAMERKGLEVSDFIIVDAY---LKEQPLPIDTGNDESAAYL------PEAVREKvmkkkrnyQEYWAQLL-----NEGH 1205
Cdd:pfam00975   83 ARRLERQGEAVRSLFLSDASaphTVRYEASRAPDDDEVVAEFtdeggtPEELLED--------EELLSMLLpalraDYRA 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  1206 IKASIHFIEAG--IHPETSGHTGLTKWEGACGNYSEYTGFGAHKDMLEGT--YAEKNADIILDILEKIT 1270
Cdd:pfam00975  155 LESYSCPPLDAqsATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDhfYLIEHLEAVLEIIEAKL 223
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1069-1159 1.01e-07

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 54.47  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1069 NLFCFPPISGFGIYFKDLALLLNEKAAVY-------GFHFIEQ-DTRIEQYVN-CMTDIQP--EGPYVLLGYSAGGNLAF 1137
Cdd:COG3208     8 RLFCFPYAGGSASAYRPWAAALPPDIEVLavqlpgrGDRLGEPpLTSLEELADdLAEELAPllDRPFALFGHSMGALLAF 87

                          90       100
                  ....*....|....*....|..
gi 499188982 1138 EVAQAMERKGLEVSDFIIVDAY 1159
Cdd:COG3208    88 ELARRLERRGRPLPAHLFVSGR 109
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 977-1046 6.56e-07

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.40  E-value: 6.56e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499188982    977 RNLVEEELANIWKQVLGV---NTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKL 1046
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1122-1178 9.09e-06

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


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 47.99  E-value: 9.09e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982   1122 GPYVLLGYSAGGNLAFEVAQAMERKGLEVSDFIIVDAYLKEQPLPIDTGNDESAAYL 1178
Cdd:smart00824   64 RPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPPGDPAPEGWLPELLRGVF 120
 
Name Accession Description Interval E-value
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 19-1043 0e+00

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


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPhlsGPRQVVMTEREFHLN 98
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG---RPVQVIQPVVAAPLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:COG1020    96 VVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLDPVRP-----YSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKE 253
Cdd:COG1020   176 GAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:COG1020   256 LARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETL 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAepFTCQ--PLFDIQANTALKQE-----LIDHIIVFENYPlqqkiadsADQTDSP-LQIDQVQVSEQSG-YNFNLVVA 404
Cdd:COG1020   334 LAA--YAHQdlPFERLVEELQPERDlsrnpLFQVMFVLQNAP--------ADELELPgLTLEPLELDSGTAkFDLTLTVV 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  405 P-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFR 483
Cdd:COG1020   404 EtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  484 EQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:COG1020   484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQKGLEQN-AAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVV 642
Cdd:COG1020   564 RLAYMLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  643 SLVRNSN-YTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLA 721
Cdd:COG1020   644 NLLAWMQrRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  722 QVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYA--GPIPIGKPISNSTAYILD 799
Cdd:COG1020   724 DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDAdgGSVPIGRPIANTRVYVLD 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:COG1020   804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRI 883

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD---FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:COG1020   884 ELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaalLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  956 DRSALPIPENKPAKRQNiILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFE 1035
Cdd:COG1020   964 DRLALPAPAAAAAAAAA-APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042


                  ....*...
gi 499188982 1036 HPTIAQLA 1043
Cdd:COG1020  1043 AAAAAAAA 1050
PRK12467 PRK12467
peptide synthase; Provisional
 10-1174 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 827.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   10 TIKKIKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGsLSYDWFQRSIQAIIDRHDIFRTVFLpHVPHLSGPRQVV 89
Cdd:PRK12467 2639 AVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFL-WDGELEEPLQVV 2716

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   90 MTEREFHLNSEDISHLPtnDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEF 169
Cdd:PRK12467 2717 YKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEV 2794

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  170 MQIYqsihAGKPLSLDPVRpYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPR-VSDKETKESYHREDLIFSLNKPLT 248
Cdd:PRK12467 2795 LQRY----FGQPPPAREGR-YRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARaLYPAPAEAVAGHGAHYLHLDATQT 2869

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  249 DKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIR 328
Cdd:PRK12467 2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  329 CQKEMLEAEPFTCQPLFDIQANTAL-KQELIDHIIVFENYPLQQKIADSADQTdspLQIDQVQVSEQSGYNFNLVVAPGE 407
Cdd:PRK12467 2950 VQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGAPSG---LRFGAVSSREQTNYPLTLAVGLGD 3026

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  408 ELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFREQAE 487
Cdd:PRK12467 3027 TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVA 3106

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  488 KTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSF 567
Cdd:PRK12467 3107 RTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  568 MLEETQAKMLIVQKGLEQN--AAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLV 645
Cdd:PRK12467 3187 MIEDSGVKLLLTQAHLLEQlpAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHL 3266

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 RNS-NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDkSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQV- 723
Cdd:PRK12467 3267 CWIaEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDa 3345

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 -RADMFRgLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRD---YAGPIPIGKPISNSTAYILD 799
Cdd:PRK12467 3346 gGADCAS-LDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDavcEAPYAPIGRPVAGRSIYVLD 3424

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL-PGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:PRK12467 3425 GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTD--TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  957 RSALPIPENKpaKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEH 1036
Cdd:PRK12467 3585 RKALPDPDAK--GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSA 3662

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1037 PTIAQLAEKLyskQLTAANEQHVIKLN--QHGAQNLFCFPPISGFGIYFKDLALLLNEKAAVYGF---HFIE---QDTRI 1108
Cdd:PRK12467 3663 PTIAELAGYS---PLGDVPVNLLLDLNrlETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLtcrHLLDdgwQDTSL 3739

                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1109 E----QYVNCMTDIQPEGPYVLLGYSAGGNLAFEVAQAMERKGLEVSDFIIVDAYLkeqPLPIDTGNDES 1174
Cdd:PRK12467 3740 QamavQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTL---PLPDEFVPQAE 3806
PRK12316 PRK12316
peptide synthase; Provisional
 14-1064 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 791.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   14 IKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGsLSYDWFQRSIQAIIDRHDIFRTVFLpHVPHLSGPRQVVMTER 93
Cdd:PRK12316 4099 IEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFV-WQGELGRPLQVVHKQV 4176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   94 EFHLNSEDISHLPtnDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIY 173
Cdd:PRK12316 4177 SLPFAELDWRGRA--DLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  174 qsihAGKPLSlDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLP---RVSDKETKESYhrEDLIFSLNKPLTDK 250
Cdd:PRK12316 4255 ----SGRPPA-QPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAqaiARADLRSANGY--GEHVRELDATATAR 4327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  251 LKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQ 330
Cdd:PRK12316 4328 LREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQ 4407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  331 KEMLEAEPFTCQPLFDIQANTALKQE-LIDHIIVFENYPLQQKIADSADQTdspLQIDQVQVSEQSGYNFNLVVAPGEEL 409
Cdd:PRK12316 4408 RQNLALREHEHTPLYEIQRWAGQGGEaLFDSLLVFENYPVSEALQQGAPGG---LRFGEVTNHEQTNYPLTLAVGLGETL 4484

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  410 VIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFREQAEKT 489
Cdd:PRK12316 4485 SLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMT 4564

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:PRK12316 4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQKGLEQN--AAFSGTCIISDAQGLME---ENDIPINIssSPDDLAYIMYTSGSTGRPKGVMITNRnvvSL 644
Cdd:PRK12316 4645 EDSGAALLLTQSHLLQRlpIPDGLASLALDRDEDWEgfpAHDPAVRL--HPDNLAYVIYTSGSTGRPKGVAVSHG---SL 4719

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  645 VRNSNYTSA----SGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLtPDRFGAYLLENDITVLFLTTALFNQL 720
Cdd:PRK12316 4720 VNHLHATGEryelTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWD-PERLYAEIHEHRVTVLVFPPVYLQQL 4798

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  721 AQ---VRADMFRGLHTLYvGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFE-MKRDYAGP--IPIGKPISNST 794
Cdd:PRK12316 4799 AEhaeRDGEPPSLRVYCF-GGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKaRDGDACGAayMPIGTPLGNRS 4877

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  795 AYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKI 873
Cdd:PRK12316 4878 GYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKI 4957

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  874 RGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV------GDHKKTDTDFRAD----LARVLPDYMIPQHWVR 943
Cdd:PRK12316 4958 RGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVpqdpalADADEAQAELRDElkaaLRERLPEYMVPAHLVF 5037

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  944 VERMPLTGNGKIDRSALPIPEnKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQ 1023
Cdd:PRK12316 5038 LARMPLTPNGKLDRKALPQPD-ASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLE 5116

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|.
gi 499188982 1024 QNIDIPIDFLFEHPTIAqlaekLYSKQLTAANEQHVIKLNQ 1064
Cdd:PRK12316 5117 LGLELPLRELFQTPTLA-----AFVELAAAAGSGDDEKFDD 5152
PRK12316 PRK12316
peptide synthase; Provisional
 14-1064 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 775.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   14 IKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGsLSYDWFQRSIQAIIDRHDIFRTVFLpHVPHLSGPRQVVMTER 93
Cdd:PRK12316 1553 IADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFL-WQDGLEQPLQVIHKQV 1630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   94 EFHLNSEDISHLPtnDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIY 173
Cdd:PRK12316 1631 ELPFAELDWRGRE--DLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY 1708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  174 qsihAGKPLSlDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIfSLNKPLTDKLKE 253
Cdd:PRK12316 1709 ----AGQPVA-APGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQ-LLDPAQTRALAE 1782

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:PRK12316 1783 FARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALN 1862

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAEPFTCQPLFDIQANTALKQE-LIDHIIVFENYPLQQKIADSADQTdspLQIDQVQVSEQSGYNFNLVVAPGEELVIK 412
Cdd:PRK12316 1863 LALREHEHTPLYDIQRWAGQGGEaLFDSLLVFENYPVAEALKQGAPAG---LVFGRVSNHEQTNYPLTLAVTLGETLSLQ 1939

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  413 FSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFREQAEKTPDH 492
Cdd:PRK12316 1940 YSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEA 2019

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  493 TALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEET 572
Cdd:PRK12316 2020 IAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDS 2099

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  573 QAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPIN---ISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN 649
Cdd:PRK12316 2100 GAALLLTQRHLLERLPLPAGVARLPLDRDAEWADYPDTapaVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAG 2179

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  650 YTSASGD-DRFIMTGSISFDAVTFEMFGALLNGASLhIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQV--RAD 726
Cdd:PRK12316 2180 ERYELSPaDCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHaeRDG 2258

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  727 MFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAG---PIPIGKPISNSTAYILDTKGR 803
Cdd:PRK12316 2259 RPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgaaYVPIGRALGNRRAYILDADLN 2338

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  804 LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAE 882
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGE 2418

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  883 IEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTD--TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK12316 2419 IEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDllAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  961 PIPEnKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIA 1040
Cdd:PRK12316 2499 PKPD-VSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLA 2577

                        1050      1060
                  ....*....|....*....|....
gi 499188982 1041 QLAEKLYSKQLTAANEQHVIKLNQ 1064
Cdd:PRK12316 2578 AFAASLESGQTSRAPVLQKVTRVQ 2601
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 480-960 0e+00

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: 759.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDaQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVID-EALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQ 719
Cdd:cd12117   160 GVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  720 LAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDY--AGPIPIGKPISNSTAYI 797
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDevAGSIPIGRPIANTRVYV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKR 877
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAAVTLREKD-GEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd12117   400 IELGEIEAALRAHPGVREAVVVVREDAgGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479


                  ....
gi 499188982  957 RSAL 960
Cdd:cd12117   480 RRAL 483
PRK12467 PRK12467
peptide synthase; Provisional
 19-1056 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 693.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHLN 98
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRF---VQDEEGFRQVIDASLSLTIP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:PRK12467  128 LDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLdPVRP--YSTYI----SWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLK 252
Cdd:PRK12467  208 GREPSL-PALPiqYADYAiwqrSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  253 ETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKE 332
Cdd:PRK12467  287 ALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRT 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  333 MLEAE-----PF-----TCQPLFDIQANtALKQELIDHiivfenYPLQQKIADSADQTDSPLQIDQVQVSEQSGyNFNLV 402
Cdd:PRK12467  365 ALGAQahqdlPFeqlveALQPERSLSHS-PLFQVMFNH------QNTATGGRDREGAQLPGLTVEELSWARHTA-QFDLA 436

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  403 VAPGEE---LVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKnHTII 479
Cdd:PRK12467  437 LDTYESaqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP-DCVH 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:PRK12467  516 QLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQ----KGLEQNAAFSGTCIISDA---QGLMEENDiPINIssSPDDLAYIMYTSGSTGRPK 632
Cdd:PRK12467  596 YPQDRLAYMLDDSGVRLLLTQshllAQLPVPAGLRSLCLDEPAdllCGYSGHNP-EVAL--DPDNLAYVIYTSGSTGQPK 672

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  633 GVMITNRNVVSLVRN-SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLF 711
Cdd:PRK12467  673 GVAISHGALANYVCViAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLK 752

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 LTTALFNQLAQV-RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYA--GPIPIGK 788
Cdd:PRK12467  753 IVPSHLQALLQAsRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERdfGNVPIGQ 832

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  789 PISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLP-GERIYRTGDLARWLPDGNLEYISRI 867
Cdd:PRK12467  833 PLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRM 912

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  868 DRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV-------GDHKKTDTDFRADLARVLPDYMIPQH 940
Cdd:PRK12467  913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAH 992

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  941 WVRVERMPLTGNGKIDRSALPIPENKPaKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTL 1020
Cdd:PRK12467  993 LLLLDSLPLTPNGKLDRKALPKPDASA-VQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRV 1071

                        1050      1060      1070
                  ....*....|....*....|....*....|....*.
gi 499188982 1021 KHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANE 1056
Cdd:PRK12467 1072 RQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPA 1107
PRK12316 PRK12316
peptide synthase; Provisional
 19-1056 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 650.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphvPHLSGPR-QVVMTEREFHL 97
Cdd:PRK12316   51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF----PRGADDSlAQVPLDRPLEV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:PRK12316  127 EFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVrP--YSTYI----SWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKL 251
Cdd:PRK12316  207 TGAEPGLPAL-PiqYADYAlwqrSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEAL 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  252 KETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQK 331
Cdd:PRK12316  286 RGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  332 EMLEAE-----PFTcqplfdiQANTALKQEL-IDHIIVFE-NYPLQQKIAD-SADQTDSPLQIDQVQVSEQSGyNFNLVV 403
Cdd:PRK12316  364 TVLGAQahqdlPFE-------RLVEALKVERsLSHSPLFQvMYNHQPLVADiEALDTVAGLEFGQLEWKSRTT-QFDLTL 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  404 ---APGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIID 480
Cdd:PRK12316  436 dtyEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHR 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  481 LFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAEL 560
Cdd:PRK12316  516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  561 PPERVSFMLEETQAKMLIVQKGLEQNAAFSG--TCIISDAQGLMEEN--DIPINISSSPDDLAYIMYTSGSTGRPKGVMI 636
Cdd:PRK12316  596 PAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgvQVLDLDRPAAWLEGysEENPGTELNPENLAYVIYTSGSTGKPKGAGN 675

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  637 TNRNVVSLVR--NSNYTSASGDdRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTT 714
Cdd:PRK12316  676 RHRALSNRLCwmQQAYGLGVGD-TVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 754

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  715 ALFNQLAQ-VRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNS 793
Cdd:PRK12316  755 SMLQAFLQdEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANL 834

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  794 TAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKI 873
Cdd:PRK12316  835 ACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 914

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  874 RGKRIEPAEIEARLLEMEGVQEAAVTLreKDGEaQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTG 951
Cdd:PRK12316  915 RGLRIELGEIEARLLEHPWVREAAVLA--VDGK-QLVGYVVLESEGGDWreALKAHLAASLPEYMVPAQWLALERLPLTP 991

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  952 NGKIDRSALPIPENKPAKrQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKhQQNIDIPID 1031
Cdd:PRK12316  992 NGKLDRKALPAPEASVAQ-QGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRAR-QAGIQLSPR 1069

                        1050      1060
                  ....*....|....*....|....*
gi 499188982 1032 FLFEHPTIAQLAEKLYSKQLTAANE 1056
Cdd:PRK12316 1070 DLFQHQTIRSLALVAKAGQATAADQ 1094
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 17-443 0e+00

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


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 636.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPhvPHLSGPRQVVMTEREFH 96
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVW--EGLGEPLQVVLKDRKLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 LNSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:cd19543    79 WRELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 HAGKPLSLDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKETAK 256
Cdd:cd19543   159 GEGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELAR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  257 QHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEA 336
Cdd:cd19543   239 QHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLEL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  337 EPFTCQPLFDIQANTALKQELIDHIIVFENYPLQQKIADSADQtdSPLQIDQVQVSEQSGYNFNLVVAPGEELVIKFSYN 416
Cdd:cd19543   319 REHEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEEEQDE--DGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYD 396

                         410       420
                  ....*....|....*....|....*..
gi 499188982  417 AFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19543   397 AEVFDEATIERLLGHLRRVLEQVAANP 423
PRK12467 PRK12467
peptide synthase; Provisional
 19-1043 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 636.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHLN 98
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF---VQEDGRTRQVIHPVGSLTLE 1194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDIshLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:PRK12467 1195 EPLL--LAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQ 1272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLdPVRP--YSTYI----SWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLK 252
Cdd:PRK12467 1273 GQSLQL-PALPiqYADYAvwqrQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLR 1351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  253 ETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRP-SEIpgvEQMIGLFINTIPIRIKTHQDETFHELLIRCQK 331
Cdd:PRK12467 1352 ALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNrAET---EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQ 1428

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  332 EMLEAE-----PFTcqplfdiQANTALKQEL-IDHIIVFENYPLQQKIADSADQTDSPLQIDQVQVSEQSGyNFNLVVAP 405
Cdd:PRK12467 1429 AALEAQahqdlPFE-------QLVEALQPERsLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQTA-QFDLTLDT 1500

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  406 GEE---LVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLF 482
Cdd:PRK12467 1501 YESsegLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLI 1580

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  483 REQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPP 562
Cdd:PRK12467 1581 EDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR 1660

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  563 ERVSFMLEETQAKMLIVQKGL-EQNAAFSGT-CIISDAQGLMEENDIPIN--ISSSPDDLAYIMYTSGSTGRPKGVMITN 638
Cdd:PRK12467 1661 ERLAYMIEDSGIELLLTQSHLqARLPLPDGLrSLVLDQEDDWLEGYSDSNpaVNLAPQNLAYVIYTSGSTGRPKGAGNRH 1740

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  639 RNVVSLVR-NSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALF 717
Cdd:PRK12467 1741 GALVNRLCaTQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  718 NQLAQV--RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKR-DYAG--PIPIGKPISN 792
Cdd:PRK12467 1821 QQLLQMdeQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRkDLEGrdSVPIGQPIAN 1900

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  793 STAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQM 871
Cdd:PRK12467 1901 LSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  872 KIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV-GDHKKTDTD---------FRADLARVLPDYMIPQHW 941
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVpTDPGLVDDDeaqvalraiLKNHLKASLPEYMVPAHL 2060

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  942 VRVERMPLTGNGKIDRSALPIPeNKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLK 1021
Cdd:PRK12467 2061 VFLARMPLTPNGKLDRKALPAP-DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRAR 2139

                        1050      1060
                  ....*....|....*....|..
gi 499188982 1022 hQQNIDIPIDFLFEHPTIAQLA 1043
Cdd:PRK12467 2140 -QAGIRFTPKDLFQHQTVQSLA 2160
PRK05691 PRK05691
peptide synthase; Validated
 14-1063 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 615.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   14 IKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVF-------LPHVPHLSGPr 86
Cdd:PRK05691 3254 IEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFswnagetMLQVIHKPGR- 3332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   87 qvvmTEREFhlnsEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVM 166
Cdd:PRK05691 3333 ----TPIDY----LDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLM 3404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  167 QEFMQIYQSIHAGKPLSLDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSAPSPLPrvSDKETKESYHRE-------DL 239
Cdd:PRK05691 3405 NDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPIP--SDRPFLREHAGDsggmvvgDC 3482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  240 IFSLNKPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQD 319
Cdd:PRK05691 3483 YTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAA 3562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  320 E---TFHELLIRCQKEMLEAEPFTCQPLFDIQANTALK--QELIDHIIVFENYPLQQKIADSADQTDSplqidqvqvSEQ 394
Cdd:PRK05691 3563 GqrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPkgQPLFDSLFVFENAPVEVSVLDRAQSLNA---------SSD 3633

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  395 SG---YNFNL--VVAPGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTK 469
Cdd:PRK05691 3634 SGrthTNFPLtaVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSE 3713

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  470 TEYPKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK05691 3714 RDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKA 3793

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVQKG-LEQNAAFSGTCIISDAQGLMEENDIPIN--------ISSSPDDLAY 620
Cdd:PRK05691 3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcREQARALLDELGCANRPRLLVWEEVQAGevashnpgIYSGPDNLAY 3873

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  621 IMYTSGSTGRPKGVMITNR----NVVSLVrnsNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPD 696
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRgmlnNQLSKV---PYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQ 3950

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFF-- 774
Cdd:PRK05691 3951 GLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFrv 4030

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  775 EMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLA 853
Cdd:PRK05691 4031 DLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLA 4110

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  854 RWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVG-----DHKKTDTDFRADL 928
Cdd:PRK05691 4111 RRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPhqtvlAQGALLERIKQRL 4190

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  929 ARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPENKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGG 1008
Cdd:PRK05691 4191 RAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGG 4270

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499188982 1009 HSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANEQHVIKLN 1063
Cdd:PRK05691 4271 HSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGSAIDEQKVDRLS 4325
PRK12316 PRK12316
peptide synthase; Provisional
 19-1043 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 614.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPHLSGPRQVVMTEREFHLN 98
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLED 2683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDIShlptndqNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHA 178
Cdd:PRK12316 2684 CAGVA-------DAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARR 2756

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  179 GKPLSLDPVR-PYSTYI----SWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKE 253
Cdd:PRK12316 2757 GEQPTLPPLPlQYADYAawqrAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLA 2836

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRpsEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQA 2914

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAEPFTCQPLFD----IQANTALKQE-LIDHIIVFENYPLQQKIADSADQtdspLQIDQVQVSEQSGYNFNLVVAPgEE 408
Cdd:PRK12316 2915 LGAQAHQDLPFEQlveaLQPERSLSHSpLFQVMYNHQSGERAAAQLPGLHI----ESFAWDGAATQFDLALDTWESA-EG 2989

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  409 LVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTKTEYPKNHTIIDLFREQAEK 488
Cdd:PRK12316 2990 LGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVER 3069

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  489 TPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFM 568
Cdd:PRK12316 3070 TPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYM 3149

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  569 LEETQAKMLIVQKGLE--QNAAFSGTCIISDAQGLMEENdipINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR 646
Cdd:PRK12316 3150 LEDSGAQLLLSQSHLRlpLAQGVQVLDLDRGDENYAEAN---PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLC 3226

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  647 NSNYTSASG-DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVL-FLTTALFNQLAQVR 724
Cdd:PRK12316 3227 WMQQAYGLGvGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLhAYPSMLQAFLEEED 3306

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  725 ADMFRGLHTLYVGGEALSPALMNAVRhacPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRL 804
Cdd:PRK12316 3307 AHRCTSLKRIVCGGEALPADLQQQVF---AGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEP 3383

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  805 LPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIE 884
Cdd:PRK12316 3384 VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE 3463

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  885 ARLLEMEGVQEAAVTLREKDgeaQLYTHYVGDHKKTD--TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPI 962
Cdd:PRK12316 3464 ARLLEHPWVREAVVLAVDGR---QLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  963 PEnKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKhQQNIDIPIDFLFEHPTIAQL 1042
Cdd:PRK12316 3541 PD-AALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRAR-QAGIRFTPKDLFQHQTIQGL 3618


                  .
gi 499188982 1043 A 1043
Cdd:PRK12316 3619 A 3619
PRK05691 PRK05691
peptide synthase; Validated
 48-1058 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 601.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   48 IKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvphlSG-PRQVVMTEREFHLNSEDISHLPTNDQNEYIERFKEKDKQKGF 126
Cdd:PRK05691  706 LRGELDEAALRASFQRLVERHESLRTRFYER----DGvALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPF 781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  127 DLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHAGKPLSLDPVR-PYSTYISW----LTNRD 201
Cdd:PRK05691  782 DLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPlGYADYGAWqrqwLAQGE 861

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  202 KEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTD 281
Cdd:PRK05691  862 AARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQG 941

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  282 DVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEAEPFTCQPlFDiQANTALKQELIDHI 361
Cdd:PRK05691  942 DIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLP-FE-QLVEALPQAREQGL 1017

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  362 I-VFENYplQQKIADSADQTDSPLQIDQVQVSEQSGYNFNLvvaPGEE-----LVIKFSYNAFVYDAAWISCIKRQFTQA 435
Cdd:PRK05691 1018 FqVMFNH--QQRDLSALRRLPGLLAEELPWHSREAKFDLQL---HSEEdrngrLTLSFDYAAELFDAATIERLAEHFLAL 1092

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  436 LSTAAQHPHMPIADFSFLDATEKEQIvTQFNNTKTEyPKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALA 515
Cdd:PRK05691 1093 LEQVCEDPQRALGDVQLLDAAERAQL-AQWGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLA 1170

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  516 RELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQKG-LEQNAAFSGTCI 594
Cdd:PRK05691 1171 HYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHlLERLPQAEGVSA 1250

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  595 ISdaqglMEENDIPINISSSP------DDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSA-SGDDRFIMTGSISF 667
Cdd:PRK05691 1251 IA-----LDSLHLDSWPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYAlDDSDVLMQKAPISF 1325

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  668 DAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQ-VRADMFRGLHTLYVGGEALSPALM 746
Cdd:PRK05691 1326 DVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDePLAAACTSLRRLFSGGEALPAELR 1405

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  747 NAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLN 826
Cdd:PRK05691 1406 NRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLG 1485

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  827 RVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDG 905
Cdd:PRK05691 1486 RPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAA 1565

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  906 EAQLYTHYVGDHKKTDTDFR--ADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPEnkpAKRQNIILPRNLVEEE 983
Cdd:PRK05691 1566 GAQLVGYYTGEAGQEAEAERlkAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV---WQQREHVEPRTELQQQ 1642

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  984 LANIWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANEQH 1058
Cdd:PRK05691 1643 IAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQ 1717
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 490-960 0e+00

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


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 588.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN 649
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  650 YT-SASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRAD-M 727
Cdd:cd05930   127 EAyPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELaA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  728 FRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFE--MKRDYAGPIPIGKPISNSTAYILDTKGRLL 805
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRvpPDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  806 PIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEA 885
Cdd:cd05930   287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499188982  886 RLLEMEGVQEAAVTLREK-DGEAQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05930   367 ALLAHPGVREAAVVAREDgDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 481-964 0e+00

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


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 566.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  481 LFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAEL 560
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  561 PPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRN 640
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  641 VVSLVRN-SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQ 719
Cdd:cd17655   162 VVNLVEWaNKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  720 LAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPD-LALHNIYGPTENTTFSTFF--EMKRDYAGPIPIGKPISNSTAY 796
Cdd:cd17655   242 LDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYqyEPETDQQVSVPIGKPLGNTRIY 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  797 ILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGK 876
Cdd:cd17655   322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:cd17655   402 RIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481


                  ....*....
gi 499188982  956 DRSALPIPE 964
Cdd:cd17655   482 DRKALPEPD 490
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 482-961 1.96e-162

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: 494.17  E-value: 1.96e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  482 FREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELP 561
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  562 PERVSFMLEETQAKMLIVQKGLEQNAAF-SGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRN 640
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVeLVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  641 VVSLVRNSNYTSASG-DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQ 719
Cdd:cd17651   161 LANLVAWQARASSLGpGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  720 LAQVRADMFR---GLHTLYVGGEALSpaLMNAVRHAC---PDLALHNIYGPTEnTTFSTFFEMKRDYAG---PIPIGKPI 790
Cdd:cd17651   241 LAEHGRPLGVrlaALRYLLTGGEQLV--LTEDLREFCaglPGLRLHNHYGPTE-THVVTALSLPGDPAAwpaPPPIGRPI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  791 SNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQ 870
Cdd:cd17651   318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQ 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  871 MKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKD-GEAQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERM 947
Cdd:cd17651   398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRpGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPSAFVLLDAL 477

                         490
                  ....*....|....
gi 499188982  948 PLTGNGKIDRSALP 961
Cdd:cd17651   478 PLTPNGKLDRRALP 491
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
19-1184 1.29e-161

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 517.67  E-value: 1.29e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVmtEREFHLN 98
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRF---TEDNGEVWQWV--DPALTFP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   99 SEDISHLPTNDQNEYIER-FKEKDKQKGFDL-QKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:PRK10252   84 LPEIIDLRTQPDPHAAAQaLMQADLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 HAGKPLSLDPVRPYST----YISWLTNRDKEKAAAYWDTYLKNYS-----APSPLPRVSdkeTKESYHRedliFSLNKPL 247
Cdd:PRK10252  164 LRGEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLPppaslSPAPLPGRS---ASADILR----LKLEFTD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  248 TDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGR-PSEIPGVEQMIglfINTIPIRIKTHQDETFHELL 326
Cdd:PRK10252  237 GAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlGSAALTATGPV---LNVLPLRVHIAAQETLPELA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  327 IRCQKEM--------LEAEpftcQPLFD---IQANTALKQELIDhIIVFenyplqqkiadsadqtDSPLQIDQVQ-VSEQ 394
Cdd:PRK10252  314 TRLAAQLkkmrrhqrYDAE----QIVRDsgrAAGDEPLFGPVLN-IKVF----------------DYQLDFPGVQaQTHT 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  395 SGY----NFNLVVAPGEE--LVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIvTQFNNT 468
Cdd:PRK10252  373 LATgpvnDLELALFPDEHggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNAT 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  469 KTEYPKNhTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLK 548
Cdd:PRK10252  452 AVEIPET-TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AGGAYLPLDAELPPERVSFMLEETQAKMLIVQKglEQNAAFSGTCIISDAQ--GLMEENDIPINISSSPDDLAYIMYTSG 626
Cdd:PRK10252  531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA--DQLPRFADVPDLTSLCynAPLAPQGAAPLQLSQPHHTAYIIFTSG 608

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  627 STGRPKGVMITNRNVVS-LVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLhiidksTMLTPD--RFGAYLL 703
Cdd:PRK10252  609 STGRPKGVMVGQTAIVNrLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKL------VMAEPEahRDPLAMQ 682

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  704 ----ENDITVL-FLTT---ALFNQLAQVRA-DMFRGLHTLYVGGEALSPALMNAVrHACPDLALHNIYGPTEN----TTF 770
Cdd:PRK10252  683 qffaEYGVTTThFVPSmlaAFVASLTPEGArQSCASLRQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAavdvSWY 761

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  771 STFFEMKRDYAG-PIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRT 849
Cdd:PRK10252  762 PAFGEELAAVRGsSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRT 841

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  850 GDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLR------EKDGEAQLYTHYV----GDHKK 919
Cdd:PRK10252  842 GDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLvsqsGLPLD 921

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  920 TDtDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPE--NKPAKRqniiLPRNLVEEELANIWKQVLGVNTI 997
Cdd:PRK10252  922 TS-ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElkAQVPGR----APKTGTETIIAAAFSSLLGCDVV 996

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  998 SIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANE--QHVIKLNQHGAQNLFCFPP 1075
Cdd:PRK10252  997 DADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLgfGTILPLREGDGPTLFCFHP 1076

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1076 ISGFGIYFKDLALLLNEKAAVYGFhfieQDTR--------------IEQYVNCMTDIQPEGPYVLLGYSAGGNLAFEVAQ 1141
Cdd:PRK10252 1077 ASGFAWQFSVLSRYLDPQWSIYGI----QSPRpdgpmqtatsldevCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAA 1152

                        1210      1220      1230      1240
                  ....*....|....*....|....*....|....*....|....*.
gi 499188982 1142 AMERKGLEVSDFIIVDAYlkeqplPIDTGN---DESAAYLPEAVRE 1184
Cdd:PRK10252 1153 RLRARGEEVAFLGLLDTW------PPETQNwreKEANGLDPEVLAE 1192
PRK05691 PRK05691
peptide synthase; Validated
 19-1057 4.55e-159

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 530.13  E-value: 4.55e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphvPHLSG-PRQVVMTEREFHL 97
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTF----PSVDGvPVQQVAEDSGLRM 1805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:PRK05691 1806 DWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFL 1885

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVrP-----YSTYI-SWLTNRDKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESyHREDLI-FSLNKPLTDK 250
Cdd:PRK05691 1886 DDRESPLEPL-PvqyldYSVWQrQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQS-HRGELYrFDLSPELAAR 1963

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  251 LKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQ 330
Cdd:PRK05691 1964 VRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR--PESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVR 2041

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  331 KEMLEAE-----PF-------------TCQPLFDIQANTalkqelidhiivfENYPLQQKiadsadQTDSPLQIDQVqVS 392
Cdd:PRK05691 2042 QTVIEGQshqdlPFdhlvealqpprsaAYNPLFQVMCNV-------------QRWEFQQS------RQLAGMTVEYL-VN 2101

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  393 EQSGYNFNL---VVAPGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIVTQFNNTK 469
Cdd:PRK05691 2102 DARATKFDLnleVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEA 2181

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  470 TEYPKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK05691 2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVQKGL-----EQNAAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYT 624
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgELPAGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYT 2341

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  625 SGSTGRPKGVmitnrnVVSLVRNSNYTSASgDDRFIMTG--------SISFDAVTFEMFGALLNGASLhIIDKSTMLTPD 696
Cdd:PRK05691 2342 SGSTGKPKGV------VVSHGEIAMHCQAV-IERFGMRAddcelhfySINFDAASERLLVPLLCGARV-VLRAQGQWGAE 2413

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYV--GGEALSPALMNAVRHACPDLALHNIYGPTENTTF---S 771
Cdd:PRK05691 2414 EICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCitGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMplaC 2493

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  772 TFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLP-GERIYRTG 850
Cdd:PRK05691 2494 LAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTG 2573

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  851 DLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD------- 923
Cdd:PRK05691 2574 DLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEaqaalre 2653

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  924 -FRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPENKpAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDD 1002
Cdd:PRK05691 2654 aLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE-LNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDN 2732

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982 1003 FFAIGGHSLRALQVIHTLKhQQNIDI-PIDfLFEHPTIAQLAEKLYSKQLTAAnEQ 1057
Cdd:PRK05691 2733 FFELGGDSILSIQVVSRAR-QLGIHFsPRD-LFQHQTVQTLAAVATHSEAAQA-EQ 2785
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 503-898 2.21e-157

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: 477.53  E-value: 2.21e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   503 SYKELDKRSNALARELIQ-KGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQK 581
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   582 GLEQNAAFSGTCIISDAQGLMEEND-----IPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR-NSNYTSASG 655
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDdapapPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAwLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   656 DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLL-ENDITVLFLTTALFNQLAQVRADMFRGLHTL 734
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIaEHPVTVLNLTPSLLALLAAALPPALASLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   735 YVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAG---PIPIGKPISNSTAYILDTKGRLLPIGVPG 811
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPresPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   812 ELCVGGDGVAKGYLNRVDLTNAVFSPHPFLP--GERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLE 889
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400


                   ....*....
gi 499188982   890 MEGVQEAAV 898
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 490-960 2.94e-152

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: 466.77  E-value: 2.94e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQKGLEQNAAFSGTCIISDAQGLmEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN 649
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  650 YTSASG-DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMF 728
Cdd:cd12116   160 ERLGLGpGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RGLHTLyVGGEALSPALmnAVRHACPDLALHNIYGPTENTTFSTFFEMkRDYAGPIPIGKPISNSTAYILDTKGRLLPIG 808
Cdd:cd12116   240 AGLTAL-CGGEALPPDL--AARLLSRVGSLWNLYGPTETTIWSTAARV-TAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  809 VPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL-PGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARL 887
Cdd:cd12116   316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  888 LEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKT-DTD-FRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd12116   396 AAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAApDAAaLRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 490-961 2.26e-150

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: 460.18  E-value: 2.26e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNS- 648
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQi 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  649 NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALfnqLAQVRADMF 728
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAA---LAALPPDDL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RGLHTLYVGGEALSPALmnaVRHACPDLALHNIYGPTENTTFSTFFEMKRDyAGPIPIGKPISNSTAYILDTKGRLLPIG 808
Cdd:cd17652   204 PDLRTLVVAGEACPAEL---VDRWAPGRRMINAYGPTETTVCATMAGPLPG-GGVPPIGRPVPGTRVYVLDARLRPVPPG 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  809 VPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARL 887
Cdd:cd17652   280 VPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAAL 359

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  888 LEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALP 961
Cdd:cd17652   360 TEHPGVAEAVVVVRDdRPGDKRLVAYVVPAPGAAPTaaELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 490-960 1.73e-147

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: 453.30  E-value: 1.73e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN 649
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  650 YT-SASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMF 728
Cdd:cd17643   127 RWfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDG 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RGLHTL-YV--GGEALSPALM----NAVRHACPDLAlhNIYGPTENTTFSTFFEMKRDYAGPI---PIGKPISNSTAYIL 798
Cdd:cd17643   207 RDPLALrYVifGGEALEAAMLrpwaGRFGLDRPQLV--NMYGITETTVHVTFRPLDAADLPAAaasPIGRPLPGLRVYVL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  799 DTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKR 877
Cdd:cd17643   285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTGNGK 954
Cdd:cd17643   365 IELGEIEAALATHPSVRDAAVIVREdEPGDTRLVAYVVADDGAAADiaELRALLKELLPDYMVPARYVPLDALPLTVNGK 444


                  ....*.
gi 499188982  955 IDRSAL 960
Cdd:cd17643   445 LDRAAL 450
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 480-960 1.60e-146

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: 452.11  E-value: 1.60e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd17646     2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd17646    82 YPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVS-LVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLhiidksTMLTPDRFG--AYLL----ENDITVL-F 711
Cdd:cd17646   162 GIVNrLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARL------VVARPGGHRdpAYLAalirEHGVTTChF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 LTTALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVrHACPDLALHNIYGPTENTTFSTFFEMKRD-YAGPIPIGKPI 790
Cdd:cd17646   236 VPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARF-LALPGAELHNLYGPTEAAIDVTHWPVRGPaETPSVPIGRPV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  791 SNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQ 870
Cdd:cd17646   315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  871 MKIRGKRIEPAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDTD---FRADLARVLPDYMIPQHWVRVER 946
Cdd:cd17646   395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAaPAGAARLVGYVVPAAGAAGPDtaaLRAHLAERLPEYMVPAAFVVLDA 474

                         490
                  ....*....|....
gi 499188982  947 MPLTGNGKIDRSAL 960
Cdd:cd17646   475 LPLTANGKLDRAAL 488
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 480-960 9.89e-142

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


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 437.90  E-value: 9.89e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd12115     3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd12115    83 YPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAIEHR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVSLVRNSNyTSASGDDR--FIMTGSISFDAVTFEMFGALLNGASLHIIDKSTML--TPDRFGAYLLEndiTVLFLTTA 715
Cdd:cd12115   129 NAAAFLQWAA-AAFSAEELagVLASTSICFDLSVFELFGPLATGGKVVLADNVLALpdLPAAAEVTLIN---TVPSAAAE 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  716 LfnqlaqVRADMF-RGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNST 794
Cdd:cd12115   205 L------LRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQ 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  795 AYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIR 874
Cdd:cd12115   279 AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  875 GKRIEPAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKK--TDTDFRADLARVLPDYMIPQHWVRVERMPLTG 951
Cdd:cd12115   359 GFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVAEPGAagLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438


                  ....*....
gi 499188982  952 NGKIDRSAL 960
Cdd:cd12115   439 NGKIDRSAL 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 481-961 1.45e-140

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: 434.67  E-value: 1.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  481 LFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAEL 560
Cdd:cd17645     3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  561 PPERVSFMLEETQAKMLIvqkgleqnaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRN 640
Cdd:cd17645    83 PGERIAYMLADSSAKILL----------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHHN 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  641 VVSLVR-NSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQ 719
Cdd:cd17645   129 LVNLCEwHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQ 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  720 LAQVRADMFRglhTLYVGGEALSPALMNAVRhacpdlaLHNIYGPTENTTFSTFFEMKRDYAGpIPIGKPISNSTAYILD 799
Cdd:cd17645   209 FMQLDNQSLR---VLLTGGDKLKKIERKGYK-------LVNNYGPTENTVVATSFEIDKPYAN-IPIGKPIDNTRVYILD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIE 879
Cdd:cd17645   278 EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIE 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  880 PAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRS 958
Cdd:cd17645   358 PGEIEPFLMNHPLIELAAVLAKEdADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437


                  ...
gi 499188982  959 ALP 961
Cdd:cd17645   438 ALP 440
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 490-961 3.97e-139

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: 431.41  E-value: 3.97e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinissSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-S 648
Cdd:cd17649    81 EDSGAGLLLTH---------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAtA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  649 NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMF 728
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RG----LHTLYVGGEALSPALmnaVRHACP-DLALHNIYGPTENTTFSTFFEMKRD--YAGP-IPIGKPISNSTAYILDT 800
Cdd:cd17649   208 DGrppsLRLYIFGGEALSPEL---LRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGaaRAGAsMPIGRPLGGRSAYILDA 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  801 KGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL-PGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIE 879
Cdd:cd17649   285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  880 PAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD----FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:cd17649   365 LGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444


                  ....*.
gi 499188982  956 DRSALP 961
Cdd:cd17649   445 DRKALP 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 489-961 1.12e-137

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: 428.43  E-value: 1.12e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  489 TPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFM 568
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  569 LEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNS 648
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  649 -NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRA-- 725
Cdd:cd17656   161 rEKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREfi 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  726 -DMFRGLHTLYVGGEAL---SPALMNAVRHACpdlALHNIYGPTENTTFSTFfemKRDYAGPI----PIGKPISNSTAYI 797
Cdd:cd17656   241 nRFPTCVKHIITAGEQLvitNEFKEMLHEHNV---HLHNHYGPSETHVVTTY---TINPEAEIpelpPIGKPISNTWIYI 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKR 877
Cdd:cd17656   315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAAVTLREKD-GEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd17656   395 IELGEIEAQLLNHPGVSEAVVLDKADDkGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474


                  ....*
gi 499188982  957 RSALP 961
Cdd:cd17656   475 RKALP 479
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 14-462 4.34e-132

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


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 412.88  E-value: 4.34e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982    14 IKNIYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvpHLSGPRQVVMTER 93
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQ--ENGEPVQVILEER 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982    94 EFHLNSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIY 173
Cdd:pfam00668   79 PFELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   174 QSIHAGKPLSLDPVRPYSTYISWLTNR----DKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTD 249
Cdd:pfam00668  159 QQLLKGEPLPLPPKTPYKDYAEWLQQYlqseDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   250 KLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRC 329
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   330 QKEMLEAEPFTCQPLFDIQANTALKQE-----LIDHIIVFENYPLQQKIADSADQTDSPLQIdQVQVSEQSGYNFNLVVA 404
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYLGQDSQEEEFQLSELDLSV-SSVIEEEAKYDLSLTAS 395

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982   405 P-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPHMPIADFSFLDATEKEQIV 462
Cdd:pfam00668  396 ErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 477-961 2.90e-131

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: 411.06  E-value: 2.90e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMI 636
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  637 TNRNVVSLVRN-SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTA 715
Cdd:cd17644   127 EHQSLVNLSHGlIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  716 LFNQLA----QVRADMFRGLHTLYVGGEALSPALMNAVRHAC-PDLALHNIYGPTENTTFSTFFEMKRDYAGPI---PIG 787
Cdd:cd17644   207 YWHLLVlellLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATIAATVCRLTQLTERNItsvPIG 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  788 KPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL--PGERIYRTGDLARWLPDGNLEYIS 865
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLG 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  866 RIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKD-GEAQLYTHYVGDHKKTD--TDFRADLARVLPDYMIPQHWV 942
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQpGNKRLVAYIVPHYEESPstVELRQFLKAKLPDYMIPSAFV 446

                         490
                  ....*....|....*....
gi 499188982  943 RVERMPLTGNGKIDRSALP 961
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 490-960 1.35e-127

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: 400.69  E-value: 1.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQkgleqnaafsgtciisdaqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR--N 647
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHawR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  648 SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALfnqlaqVRADM 727
Cdd:cd17650   127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAL------IRPVM 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  728 ---------FRGLHTLYVGGEALSPA-LMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDY---AGPIPIGKPISNST 794
Cdd:cd17650   201 ayvyrngldLSAMRLLIVGSDGCKAQdFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPlgdSANVPIGRPLPNTA 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  795 AYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIR 874
Cdd:cd17650   281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  875 GKRIEPAEIEARLLEMEGVQEAAVTLRE-KDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNG 953
Cdd:cd17650   361 GFRIELGEIESQLARHPAIDEAVVAVREdKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNG 440


                  ....*..
gi 499188982  954 KIDRSAL 960
Cdd:cd17650   441 KVDRRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 480-960 3.36e-123

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


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 389.98  E-value: 3.36e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd05918     3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVqkgleqnaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd05918    83 HPLQRLQEILQDTGAKVVLT---------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEHR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVSLVRN-SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLtpDRFGAYLLENDITVLFLTTALFN 718
Cdd:cd05918   130 ALSTSALAhGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRL--NDLAGFINRLRVTWAFLTPSVAR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 QLaqvRADMFRGLHTLYVGGEALSPALmnaVRHACPDLALHNIYGPTENTTFSTFFEMKRDyAGPIPIGKPIsNSTAYIL 798
Cdd:cd05918   208 LL---DPEDVPSLRTLVLGGEALTQSD---VDTWADRVRLINAYGPAECTIAATVSPVVPS-TDPRNIGRPL-GATCWVV 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  799 D--TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHP-------FLPGERIYRTGDLARWLPDGNLEYISRIDR 869
Cdd:cd05918   280 DpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDT 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  870 QMKIRGKRIEPAEIEARLLE-MEGVQEAAVTL-REKDGEAQ------LYTHYVGDHKKTDTDF---------------RA 926
Cdd:cd05918   360 QVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVvKPKDGSSSpqlvafVVLDGSSSGSGDGDSLflepsdefralvaelRS 439

                         490       500       510
                  ....*....|....*....|....*....|....
gi 499188982  927 DLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05918   440 KLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 490-960 8.51e-122

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: 386.24  E-value: 8.51e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEEnDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN 649
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAP-APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  650 YTSA-SGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMF 728
Cdd:cd12114   160 RRFAvGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RGLHTL---YVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKR--DYAGPIPIGKPISNSTAYILDTKGR 803
Cdd:cd12114   240 ALLPSLrlvLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEvpPDWRSIPYGRPLANQRYRVLDPRGR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  804 LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPflPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEI 883
Cdd:cd12114   320 DCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEI 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  884 EARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKT---DTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd12114   398 EAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTpiaPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 480-960 1.12e-117

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: 373.57  E-value: 1.12e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVqkgleqnaafsgtciisdaqglmeendipiniSSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd17653    81 LPSARIQAILRTSGATLLLT--------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVSLVRNSNYTSASG-DDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPdrfgaylLENDITVLFLTTALfn 718
Cdd:cd17653   129 GVLNYVSQPPARLDVGpGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAH-------VARTVDALMSTPSI-- 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 qLAQVRADMFRGLHTLYVGGEALSPALmnaVRHACPDLALHNIYGPTENTTFSTFFEMkrdYAG-PIPIGKPISNSTAYI 797
Cdd:cd17653   200 -LSTLSPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTMTEL---LPGqPVTIGKPIPNSTCYI 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKR 877
Cdd:cd17653   273 LDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFR 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEAR-LLEMEGVQEAAVTLREKdgeaQLYTHYVGDHKKTDtDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd17653   353 INLEEIEEVvLQSQPEVTQAAAIVVNG----RLVAFVTPETVDVD-GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427


                  ....
gi 499188982  957 RSAL 960
Cdd:cd17653   428 RKAL 431
AMP-binding pfam00501
AMP-binding enzyme;
482-874 1.94e-116

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 369.72  E-value: 1.94e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   482 FREQAEKTPDHTAL-VYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAEL 560
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   561 PPERVSFMLEETQAKMLIVQ--------KGLEQNAAFSGTCIISDAQGLMEENDIPINISS-----------SPDDLAYI 621
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDdalkleelLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPadvppppppppDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   622 MYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGD-----DRFIMTGSISFDA-VTFEMFGALLNGASLHIIDKSTMLTP 695
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFglgpdDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   696 DRFGAYLLENDITVLFLTTALFNQLAQVRA---DMFRGLHTLYVGGEALSPALMNAVRHACPDlALHNIYGPTENTTFST 772
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGApkrALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   773 FFEMKRDYAGPIP-IGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPhpflpgERIYRTG 850
Cdd:pfam00501  320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393

                          410       420
                   ....*....|....*....|....
gi 499188982   851 DLARWLPDGNLEYISRIDRQMKIR 874
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 486-960 4.85e-114

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: 364.26  E-value: 4.85e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLIVqkgleqnaafsgtciisdaqglmeendipinissSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLV 645
Cdd:cd05945    81 REILDAAKPALLIA----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 R-NSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITV---------LFLTTA 715
Cdd:cd05945   127 NwMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVwvstpsfaaMCLLSP 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  716 LFNQ--LAQVRADMFrglhtlyvGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKR---DYAGPIPIGKPI 790
Cdd:cd05945   207 TFTPesLPSLRHFLF--------CGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPevlDGYDRLPIGYAK 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  791 SNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPflpGERIYRTGDLARWLPDGNLEYISRIDRQ 870
Cdd:cd05945   279 PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQ 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  871 MKIRGKRIEPAEIEARLLEMEGVQEAAVTLR-EKDGEAQLYTHYVGDHKKTD---TDFRADLARVLPDYMIPQHWVRVER 946
Cdd:cd05945   356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAEAgltKAIKAELAERLPPYMIPRRFVYLDE 435

                         490
                  ....*....|....
gi 499188982  947 MPLTGNGKIDRSAL 960
Cdd:cd05945   436 LPLNANGKIDRKAL 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 490-961 2.87e-111

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: 357.10  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKG-FRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFM 568
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  569 LEETQAKMLIvqkgleqnaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLvRNS 648
Cdd:cd17648    81 LEDTGARVVI----------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNL-RTS 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  649 ----NYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVR 724
Cdd:cd17648   126 lserYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  725 ADmfrGLHTLYVGGEALSPALMNAVRHACPDLALhNIYGPTENTTFSTffemKRDYAGPIP----IGKPISNSTAYILDT 800
Cdd:cd17648   206 LP---HLKRVDAAGEEFTAPVFEKLRSRFAGLII-NAYGPTETTVTNH----KRFFPGDQRfdksLGRPVRNTKCYVLND 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  801 KGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPF-LPGE-------RIYRTGDLARWLPDGNLEYISRIDRQMK 872
Cdd:cd17648   278 AMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVK 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  873 IRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQ------LYTHYVGDHKK-TDTDFRADLARVLPDYMIPQHWVRVE 945
Cdd:cd17648   358 IRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHvPESDLLSFLRAKLPRYMVPARLVRLE 437

                         490
                  ....*....|....*.
gi 499188982  946 RMPLTGNGKIDRSALP 961
Cdd:cd17648   438 GIPVTINGKLDVRALP 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 478-960 8.60e-111

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: 355.66  E-value: 8.60e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  478 IIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLD 557
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  558 AELPPERVSFMLEETQAKMLIVqkgleqnaafsgtciisdaqglmeendipinissspddlAYIMYTSGSTGRPKGVMIT 637
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  638 NRNVVSLVRNSN-YTSASGDDRFIMTGSISFD-AVTFEMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTA 715
Cdd:COG0318   122 HRNLLANAAAIAaALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  716 LFNQLAQV----RADmFRGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPIS 791
Cdd:COG0318   199 MLARLLRHpefaRYD-LSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLP 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  792 NSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQM 871
Cdd:COG0318   277 GVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  872 KIRGKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGEAQL-YTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMP 948
Cdd:COG0318   350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVpdEKWGERVVaFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELP 429

                         490
                  ....*....|..
gi 499188982  949 LTGNGKIDRSAL 960
Cdd:COG0318   430 RTASGKIDRRAL 441
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 17-443 1.49e-94

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


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 310.15  E-value: 1.49e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVF-LPHVPHlsgPRQVVMTEREF 95
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFiEDGLGQ---PVQVVHRQAQV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   96 HLNSEDISHLptNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCI-WSHHHILMDGWCLGIVMQEFMQIYQ 174
Cdd:cd19536    78 PVTELDLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  175 SIHAGKPLSLDPVRPYSTYISWL-TNRDKEKAAAYWDTYLKNYSAPsPLPRVSDKETKESYHREDLIFSLnkPLTDKLKE 253
Cdd:cd19536   156 QLLEYKPLSLPPAQPYRDFVAHErASIQQAASERYWREYLAGATLA-TLPALSEAVGGGPEQDSELLVSV--PLPVRSRS 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIkTHQDETFHELLIRCQKEM 333
Cdd:cd19536   233 LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRV-TLSEETVEDLLKRAQEQE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAEPFTCQPLFDIQANTAlKQELIDHIIVFENYPLQQKIADSADqtDSPLQIDQVQVSEQSGYNFNLVVAP-GEELVIK 412
Cdd:cd19536   312 LESLSHEQVPLADIQRCSE-GEPLFDSIVNFRHFDLDFGLPEWGS--DEGMRRGLLFSEFKSNYDVNLSVLPkQDRLELK 388

                         410       420       430
                  ....*....|....*....|....*....|.
gi 499188982  413 FSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19536   389 LAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 209-1043 5.10e-81

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: 292.35  E-value: 5.10e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   209 WDTYLKNYSApSPLPRVSDKETKESYHREDLIFSLNKpltdklKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGav 288
Cdd:TIGR03443    2 WSERLDNPTL-SVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLG-- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   289 VSGRPSEIPGVeqmiglfintipIRIKTHQDETFHELLIRCQKEMLEAEPftcqplfdiQANTALKqELIDHIIV---FE 365
Cdd:TIGR03443   73 TSSNKSGRPFV------------LRLNITPELSFLQLYAKVSEEEKEGAS---------DIGVPFD-ELSEHIQAakkLE 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   366 NYPLQQKIAdSADQTDSPlqidQVQVSEQSGYNFNLVVAPGE-ELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHPH 444
Cdd:TIGR03443  131 RTPPLFRLA-FQDAPDNQ----QTTYSTGSTTDLTVFLTPSSpELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   445 MPIADFSFLDATEKEQIVtqfNNTK----TEYpkNHTIIDLFREQAEKTPDHTALV---------YGNMSISYKELDKRS 511
Cdd:TIGR03443  206 EPIGKVSLITPSQKSLLP---DPTKdldwSGF--RGAIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEAS 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   512 NALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV------------ 579
Cdd:TIGR03443  281 NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekagtldqlvr 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   580 ---QKGLEQNAAFSGTCIISDAQ---GLME--ENDI----------PINISSSPDDLAYIMYTSGSTGRPKGVMitNRNV 641
Cdd:TIGR03443  361 dyiDKELELRTEIPALALQDDGSlvgGSLEggETDVlapyqalkdtPTGVVVGPDSNPTLSFTSGSEGIPKGVL--GRHF 438

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   642 vSLVRNSNYTSA----SGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALf 717
Cdd:TIGR03443  439 -SLAYYFPWMAKrfglSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM- 516

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   718 NQLAQVRAD-MFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGP---------IPIG 787
Cdd:TIGR03443  517 GQLLSAQATtPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRSSDStflknlkdvMPAG 596

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   788 KPISNSTAYILDTKGRLLPIGVP--GELCVGGDGVAKGYLNRVDLTNAVF----------------------SPHPFLPG 843
Cdd:TIGR03443  597 KGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFvnnwfvdpshwidldkennkpeREFWLGPR 676

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   844 ERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEaAVTL--REKDGEAQLYTHYVGDHKKTD 921
Cdd:TIGR03443  677 DRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLvrRDKDEEPTLVSYIVPQDKSDE 755

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   922 ----------------------------TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPENK------P 967
Cdd:TIGR03443  756 leefksevddeessdpvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAqlaavaK 835

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982   968 AKRQNIILPR-NLVEEELANIWKQVL--GVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLA 1043
Cdd:TIGR03443  836 NRSASAADEEfTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFA 914
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 18-443 4.45e-76

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


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 258.88  E-value: 4.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   18 YPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPHlsgPRQVVMTERE-FH 96
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGR---YEQVVLDKTVrFR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 LNSEDISHLptNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:cd19066    79 IEIIDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 HAGKPLSLDPVRPYSTYISWLTNR----DKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLK 252
Cdd:cd19066   157 ERQKPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  253 ETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKE 332
Cdd:cd19066   237 EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  333 MLEAEPFTCQP--LFDIQAN---TALKQELIDHIIVFENYPLQQKIADSAdQTDSPLqidqVQVSEQSGYNFNLVVAPGE 407
Cdd:cd19066   315 SREAIEHQRVPfiELVRHLGvvpEAPKHPLFEPVFTFKNNQQQLGKTGGF-IFTTPV----YTSSEGTVFDLDLEASEDP 389

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 499188982  408 --ELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19066   390 dgDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
478-960 2.37e-75

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 259.44  E-value: 2.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  478 IIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLD 557
Cdd:PRK04813    4 IIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  558 AELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQ-GLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMI 636
Cdd:PRK04813   84 VSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKdIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  637 TNRNVVSLVR--NSNYTSASGDdRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVlFLTT 714
Cdd:PRK04813  164 SHDNLVSFTNwmLEDFALPEGP-QFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINV-WVST 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  715 ALFNQLA----QVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFF----EMKRDYAgPIPI 786
Cdd:PRK04813  242 PSFADMClldpSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIeitdEMLDQYK-RLPI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  787 GKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpFLPGERIYRTGDLARwLPDGNLEYISR 866
Cdd:PRK04813  321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAGY-LEDGLLFYQGR 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  867 IDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV--GDHKKTDtDF------RADLARVLPDYMIP 938
Cdd:PRK04813  397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVvpKEEDFER-EFeltkaiKKELKERLMEYMIP 475

                         490       500
                  ....*....|....*....|..
gi 499188982  939 QHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK04813  476 RKFIYRDSLPLTPNGKIDRKAL 497
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 17-443 2.28e-74

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


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 253.00  E-value: 2.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLfHSFLRkEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPhVPHLSGPRQVVMteREFH 96
Cdd:cd19542     1 IYPCTPMQEGML-LSQLR-SPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVE-SSAEGTFLQVVL--KSLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 LNsedISHLPTNDQNEYIERFKEKDKQKGFdlqKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:cd19542    76 PP---IEEVETDEDSLDALTRDLLDDPTLF---GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 hagkplSLDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSaPSPLPRVSDKETKESYHredlifSLNKPLTDKLKETAK 256
Cdd:cd19542   150 ------LLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGAS-PCAFPSLSPKRPAERSL------SSTRRSLAKLEAFCA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  257 QHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEA 336
Cdd:cd19542   217 SLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRS 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  337 EPFTCQPLFDIQANTALK--QELIDHIIVFENYPlqqkiadSADQTDSPLQIDQVQVSEQSGYNFNL---VVAPGEELVI 411
Cdd:cd19542   297 LPHQHLSLREIQRALGLWpsGTLFNTLVSYQNFE-------ASPESELSGSSVFELSAAEDPTEYPVaveVEPSGDSLKV 369

                         410       420       430
                  ....*....|....*....|....*....|..
gi 499188982  412 KFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19542   370 SLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 478-966 8.61e-73

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


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 251.99  E-value: 8.61e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   478 IIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLD 557
Cdd:TIGR01734    2 LIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   558 AELPPERVSFMLEETQAKMLIVQKGLEQNaaFSGTCIIS-DAQGLMEENDIPINISS--SPDDLAYIMYTSGSTGRPKGV 634
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAELSID--AVGTQIITlSALEQAETSGGPVSFDHavKGDDNYYIIYTSGSTGNPKGV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   635 MITNRNVVSLVR-NSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVlFLT 713
Cdd:TIGR01734  160 QISHDNLVSFTNwMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNV-WVS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   714 TALFNQLAQV----RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKR---DYAGPIPI 786
Cdd:TIGR01734  239 TPSFVDMCLLdpnfNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQeilDQYPRLPI 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   787 G--KPISNstAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPflpGERIYRTGDLARwLPDGNLEYI 864
Cdd:TIGR01734  319 GfaKPDMN--LFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHE---GQPAYRTGDAGT-ITDGQLFYQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   865 SRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLR-EKDGE-AQLYTHYVGDHKKTDTDF------RADLARVLPDYM 936
Cdd:TIGR01734  393 GRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKyNKDHKvEYLIAAIVPETEDFEKEFqltkaiKKELKKSLPAYM 472

                          490       500       510
                   ....*....|....*....|....*....|
gi 499188982   937 IPQHWVRVERMPLTGNGKIDRSALPIPENK 966
Cdd:TIGR01734  473 IPRKFIYRDQLPLTANGKIDRKALAEEVNG 502
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 617-956 4.42e-71

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: 241.42  E-value: 4.42e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTmltP 695
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAlAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---P 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  696 DRFGAYLLENDITVLFLTTALFNQLaqVRADMFRG-----LHTLYVGGEALSPALMNAVrHACPDLALHNIYGPTENTTF 770
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARL--LKAPESAGydlssLRALVSGGAPLPPELLERF-EEAPGIKLVNGYGLTETGGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  771 STFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFsphpflpGERIYRTG 850
Cdd:cd04433   155 VATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  851 DLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV---GDHKKTDTDFRAD 927
Cdd:cd04433   228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVvlrPGADLDAEELRAH 307

                         330       340
                  ....*....|....*....|....*....
gi 499188982  928 LARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd04433   308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 482-957 1.65e-67

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: 234.81  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  482 FREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELP 561
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  562 PERVSFMLEETQAKMLIvqkgleqnaafsgtciisdaqglmeendipinissspDDLAYIMYTSGSTGRPKGVMITNRNV 641
Cdd:cd17631    81 PPEVAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  642 VSLVRNSNYT-SASGDDRFIMTGSIsFDAVTFEMFGA--LLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFN 718
Cdd:cd17631   124 LWNAVNALAAlDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQ 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 QLAQ-VRADMFR--GLHTLYVGGEALSPALMNAVRHAcpDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTA 795
Cdd:cd17631   200 ALLQhPRFATTDlsSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEV 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  796 YILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFsphpflpGERIYRTGDLARWLPDGNLeYIsrIDR--QMKI 873
Cdd:cd17631   278 RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYL-YI--VDRkkDMII 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  874 R-GKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGEAQlyTHYV---GDHKKTDTDFRADLARVLPDYMIPQHWVRVERM 947
Cdd:cd17631   348 SgGENVYPAEVEDVLYEHPAVAEVAVIGVpdEKWGEAV--VAVVvprPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425

                         490
                  ....*....|
gi 499188982  948 PLTGNGKIDR 957
Cdd:cd17631   426 PRNATGKILK 435
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 17-423 7.35e-67

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


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 232.59  E-value: 7.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvpHLSGPRQVVMTEREFH 96
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWR--DRAEPLQYVRDDLAPP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 LNSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:cd19547    79 WALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 HAGKPLSLDPVRPYSTYISWLTNR--DKEKAAAYWDTYLKNYSaPSPLPRV-SDKETKesYHreDLIFSLNKPLTDKLKE 253
Cdd:cd19547   159 AHGREPQLSPCRPYRDYVRWIRARtaQSEESERFWREYLRDLT-PSPFSTApADREGE--FD--TVVHEFPEQLTRLVNE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  254 TAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEM 333
Cdd:cd19547   234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  334 LEAEPFTCQPLFDIQANTALKQ----ELIDHIIVFENYPlqqkiADSADQTDSPLQIDQVQVSEQSGYNFNLVVAPGEEL 409
Cdd:cd19547   314 ATTAAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYP-----EDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKL 388

                         410
                  ....*....|....
gi 499188982  410 VIKFSYNAFVYDAA 423
Cdd:cd19547   389 AFHFNYDTTHFTRA 402
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 18-443 8.54e-63

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


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 220.69  E-value: 8.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   18 YPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHL 97
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTF---VEVDGEPVQVILPPLPLPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:cd19531    79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVRP-YSTYISW----LTNRDKEKAAAYWDTYLKNysAPSPL------PRVSDKETKESYHRedliFSLNKP 246
Cdd:cd19531   159 AGRPSPLPPLPIqYADYAVWqrewLQGEVLERQLAYWREQLAG--APPVLelptdrPRPAVQSFRGARVR----FTLPAE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  247 LTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHELL 326
Cdd:cd19531   233 LTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR--AELEGLIGFFVNTLVLRTDLSGDPTFRELL 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  327 IRCQKEMLEAepFTCQ--------------------PLFDIqantalkqelidhIIVFENYPLQQkiADSADQTDSPLQI 386
Cdd:cd19531   311 ARVRETALEA--YAHQdlpfeklvealqperdlsrsPLFQV-------------MFVLQNAPAAA--LELPGLTVEPLEV 373

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  387 DQ--------VQVSEQsgynfnlvvapGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19531   374 DSgtakfdltLSLTET-----------DGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 513-1271 3.19e-62

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


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 229.59  E-value: 3.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  513 ALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGT 592
Cdd:COG3319    41 LLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALALALLALLLA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  593 CIISDAQGLMEENDIPINISS-SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIMTGSISFDAVT 671
Cdd:COG3319   121 ALLLALAALAAAAAAAALAAAaAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALAL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  672 FEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVRH 751
Cdd:COG3319   201 ALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLAL 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  752 ACPDLALHNIYGPTENTTFSTFFEM-----KRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLN 826
Cdd:COG3319   281 LLLAAAAALAAGGTATTAAVTTTAAaaapgVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGR 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  827 RVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGE 906
Cdd:COG3319   361 GLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAA 440

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  907 AQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPENKPAKRQNIILPRNLVEEELAN 986
Cdd:COG3319   441 AAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALAL 520

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  987 IWKQVLGVNTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANEQHVIKLNQHG 1066
Cdd:COG3319   521 LLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGS 600

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1067 AQNLFCFPPISGFGIYFKDLALLLNEKAAVYGFHFI------EQDTRIEQ----YVNCMTDIQPEGPYVLLGYSAGGNLA 1136
Cdd:COG3319   601 GPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPgldggePPPASVEEmaarYVEAIRAVQPEGPYHLLGWSFGGLVA 680

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1137 FEVAQAMERKGLEVSDFIIVDAYLKEQPLPID-------------------TGNDESAAYLPEAVREKVMKK-------- 1189
Cdd:COG3319   681 YEMARQLEAQGEEVALLVLLDSYAPGALARLDeaellaallrdlargvdlpLDAEELRALDPEERLARLLERlreaglpa 760

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1190 -------KRNYQEYWA--QLLNE---GHIKASIHFIEAGIHPETSGHTGLTKWEG-ACGNYSEYTGFGAHKDMLEGTYAE 1256
Cdd:COG3319   761 gldaerlRRLLRVFRAnlRALRRyrpRPYDGPVLLFRAEEDPPGRADDPALGWRPlVAGGLEVHDVPGDHFSMLREPHVA 840

                         810
                  ....*....|....*
gi 499188982 1257 KNADIILDILEKITS 1271
Cdd:COG3319   841 ELAAALRAALAAAEA 855
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 480-960 1.30e-61

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


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 220.04  E-value: 1.30e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:TIGR03098    4 HLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   560 LPPERVSFMLEETQAKMLI--------VQKGLEQNAAFSGTCIISDAQGLMEENDIPINIS---------------SSPD 616
Cdd:TIGR03098   84 LKAEQVAHILADCNVRLLVtsserldlLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwpkllalgdadpphpVIDS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   617 DLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDkstMLTP 695
Cdd:TIGR03098  164 DMAAILYTSGSTGRPKGVVLSHRNLVAgAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD---YLLP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   696 DRFGAYLLENDITVLFLTTALFNQLAQV--RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEntTF-ST 772
Cdd:TIGR03098  241 RDVLKALEKHGITGLAAVPPLWAQLAQLdwPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE--AFrST 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   773 FFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHP------FLPGERI 846
Cdd:TIGR03098  319 YLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgelHLPELAV 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   847 YrTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV--TLREKDGEAQLYTHYVGDHKKTDTD- 923
Cdd:TIGR03098  399 W-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfgVPDPTLGQAIVLVVTPPGGEELDRAa 477

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 499188982   924 FRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:TIGR03098  478 LLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 499-960 2.68e-59

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


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 211.56  E-value: 2.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  499 NMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI 578
Cdd:cd17654    14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  579 VQKglEQNAAFSgtcIISDAQGLMEendipiniSSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYT-SASGDD 657
Cdd:cd17654    94 QNK--ELDNAPL---SFTPEHRHFN--------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLfNITSED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  658 RFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLE-NDITVLFLTTALFNQLAQVRADMF-----RGL 731
Cdd:cd17654   161 ILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTvlsatSSL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  732 HTLYVGGEAL-SPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAgPIPIGKPISNSTAYILDTKGRllpiGVP 810
Cdd:cd17654   241 RVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDS-PVQLGSPLLGTVIEVRDQNGS----EGT 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  811 GELCVGGdgvakgyLNRVDLTNAVFSphpfLPGERIYRTGDLARwLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEM 890
Cdd:cd17654   316 GQVFLGG-------LNRVCILDDEVT----VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  891 EGVQEAAVTLREKDgeaQLYTHYVGDHKKT---DTDFRADLAR-VLPDYMipqhwVRVERMPLTGNGKIDRSAL 960
Cdd:cd17654   384 LGVESCAVTLSDQQ---RLIAFIVGESSSSrihKELQLTLLSShAIPDTF-----VQIDKLPLTSHGKVDKSEL 449
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 501-955 2.98e-59

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: 212.46  E-value: 2.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQ 580
Cdd:cd05911    10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 -KGLE--QNAA-----------FSGT-------CIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd05911    90 pDGLEkvKEAAkelgpkdkiivLDDKpdgvlsiEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVVS---LVRNSNYTSASGDDRFImtGSISFDAVT--FEMFGALLNGASLHIIDK---STMLTpdrfgayLLEN-DITVL 710
Cdd:cd05911   170 NLIAnlsQVQTFLYGNDGSNDVIL--GFLPLYHIYglFTTLASLLNGATVIIMPKfdsELFLD-------LIEKyKITFL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  711 FLTTALFNQLA---QVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEntTFSTFFEMKRDYAGPIPIG 787
Cdd:cd05911   241 YLVPPIAAALAkspLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE--TGGILTVNPDGDDKPGSVG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  788 KPISNSTAYILDTKGR-LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISR 866
Cdd:cd05911   319 RLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL------HTGDIGYFDEDGYLYIVDR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  867 IDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV--TLREKDGEaqLYTHYVgDHKKTDTDFRADLARVLPDYMIPQHWVR- 943
Cdd:cd05911   393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVigIPDEVSGE--LPRAYV-VRKPGEKLTEKEVKDYVAKKVASYKQLRg 469

                         490
                  ....*....|....*.
gi 499188982  944 ----VERMPLTGNGKI 955
Cdd:cd05911   470 gvvfVDEIPKSASGKI 485
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 17-443 1.20e-58

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


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 207.54  E-value: 1.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLFHSFLRKeeGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPHlsGPRQVVMTErefh 96
Cdd:cd19545     1 IYPCTPLQEGLMALTARQP--GAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSG--GLLQVVVKE---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 lnsEDISHLPTNDQNEYIErfkeKDKQKGFDLQKDmLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSI 176
Cdd:cd19545    73 ---SPISWTESTSLDEYLE----EDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  177 HagkplsLDPVRPYSTYISWLTNRDKEKAAAYWDTYLKNYSAPS--PLPRVSD--KETKESYHREDLIFSLnkpltdklk 252
Cdd:cd19545   145 P------VPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVfpPLPSSRYqpRPDATLEHSISLPSSA--------- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  253 etakQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKE 332
Cdd:cd19545   210 ----SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKD 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  333 MLEAEPFTCQPLFDIQA--NTALKQELIDHIIVFENYPlqqkiaDSADQTDSPLQIDQV--QVSEQSGYNFNLVVAP-GE 407
Cdd:cd19545   286 LLDMIPFEHTGLQNIRRlgPDARAACNFQTLLVVQPAL------PSSTSESLELGIEEEseDLEDFSSYGLTLECQLsGS 359

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 499188982  408 ELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19545   360 GLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 478-960 1.99e-58

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: 209.34  E-value: 1.99e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  478 IIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLD 557
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  558 AELPPERVSFMLEETQAKMLIV----QKGLEQNAAFSGTCIIsdaqglmeendipinissSPDDLAYIMYTSGSTGRPKG 633
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVavsfTDLLAAGAPLGERVAL------------------TPEDVAVLQYTSGTTGVPKG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  634 VMITNRNVVSlvrNSNYTSA------SGDDRFIMTGSI--SFdAVTFEMFGALLNGASLHIIdksTMLTPDRFGAYLLEN 705
Cdd:cd05936   143 AMLTHRNLVA---NALQIKAwledllEGDDVVLAALPLfhVF-GLTVALLLPLALGATIVLI---PRFRPIGVLKEIRKH 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  706 DITVLFLTTALFNQLAQVRADMFRGLHTLYV---GGEALSPALMNAVRHA--CPdlaLHNIYGPTEN---TTFSTFFEmk 777
Cdd:cd05936   216 RVTIFPGVPTMYIALLNAPEFKKRDFSSLRLcisGGAPLPVEVAERFEELtgVP---IVEGYGLTETspvVAVNPLDG-- 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  778 RDYAGpiPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLP 857
Cdd:cd05936   291 PRKPG--SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-------DGWLRTGDIGYMDE 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  858 DGNLeYIsrIDRQ--MKIR-GKRIEPAEIEARLLEMEGVQEAAVT--LREKDGEAqlyTH-YV---GDHKKTDTDFRADL 928
Cdd:cd05936   362 DGYF-FI--VDRKkdMIIVgGFNVYPREVEEVLYEHPAVAEAAVVgvPDPYSGEA---VKaFVvlkEGASLTEEEIIAFC 435

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499188982  929 ARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05936   436 REQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 20-262 3.27e-57

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 197.95  E-value: 3.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   20 LSHMQEGMLFhsfLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHLNS 99
Cdd:COG4908     1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF---VEEDGEPVQRIDPDADLPLEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  100 EDISHLPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHAG 179
Cdd:COG4908    75 VDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  180 KPLSLDPV-RPYSTYISWLTNR----DKEKAAAYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKET 254
Cdd:COG4908   155 EPPPLPELpIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKAL 234


                  ....*...
gi 499188982  255 AKQHGVTL 262
Cdd:COG4908   235 AKAHGATV 242
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 501-963 7.35e-55

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


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 200.44  E-value: 7.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVq 580
Cdd:cd17647    20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 kgleqnaafsgtciISDAqglmeendipiNISSSPDDLAYIMYTSGSTGRPKGVMitNRNvVSLVRNSNYTSA----SGD 656
Cdd:cd17647    99 --------------IRAA-----------GVVVGPDSNPTLSFTSGSEGIPKGVL--GRH-FSLAYYFPWMAKrfnlSEN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  657 DRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYV 736
Cdd:cd17647   151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  737 GGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGP---------IPIGKPISNSTAYILD--TKGRLL 805
Cdd:cd17647   231 VGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDPtflknlkdvMPAGRGMLNVQLLVVNrnDRTQIC 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  806 PIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFL----------------------PGERIYRTGDLARWLPDGNLEY 863
Cdd:cd17647   311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYRTGDLGRYLPNGDCEC 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  864 ISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEaAVTL--REKDGEAQLYTHYVGDHKKTDT------------------- 922
Cdd:cd17647   391 CGRADDQVKIRGFRIELGEIDTHISQHPLVRE-NITLvrRDKDEEPTLVSYIVPRFDKPDDesfaqedvpkevstdpivk 469

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499188982  923 ----------DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIP 963
Cdd:cd17647   470 gligyrklikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 477-960 7.52e-55

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 200.41  E-value: 7.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:PRK06187    7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGLEQNAA-------FSGTCIISDAQGLMEEN--------------DIPINISSSP 615
Cdd:PRK06187   87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAailpqlpTVRTVIVEGDGPAAPLApevgeyeellaaasDTFDFPDIDE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  616 DDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNY-TSASGDDRFImtgsisfdaVTFEMFG---------ALLNGASLH 685
Cdd:PRK06187  167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAwLKLSRDDVYL---------VIVPMFHvhawglpylALMAGAKQV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  686 IIDKstmLTPDRFGAYLLENDITVLFLT----TALFNQLAQVRADmFRGLHTLYVGGEALSPALMNA--VRHACPdlaLH 759
Cdd:PRK06187  238 IPRR---FDPENLLDLIETERVTFFFAVptiwQMLLKAPRAYFVD-FSSLRLVIYGGAALPPALLREfkEKFGID---LV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  760 NIYGPTENTTFSTFFEMKRDYAGPIPI----GKPISNSTAYILDTKGRLLP--IGVPGELCVGGDGVAKGYLNRVDLTna 833
Cdd:PRK06187  311 QGYGMTETSPVVSVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEAT-- 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  834 vfsphpflpGERI----YRTGDLARWLPDGNLeYIS-RIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVtLREKD---G 905
Cdd:PRK06187  389 ---------AETIdggwLHTGDVGYIDEDGYL-YITdRIKDVIISGGENIYPRELEDALYGHPAVAEVAV-IGVPDekwG 457

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499188982  906 EAQLYthYV---GDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06187  458 ERPVA--VVvlkPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 510-960 1.60e-54

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: 197.66  E-value: 1.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  510 RSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGA----YLPLDAELPPERVSFMLEETQAKMLIVQKGLEQ 585
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  586 NAAFSGTC-----IISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN-YTSASGDDRF 659
Cdd:cd05922    82 RLRDALPAspdpgTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAeYLGITADDRA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  660 IMTGSISFDAVTFEMFGALLNGASLhIIDKSTMLtPDRFGAYLLENDITVLFLTTALFNQLAQV-RADMfrGLHTL-YV- 736
Cdd:cd05922   162 LTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRLgFDPA--KLPSLrYLt 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  737 -GGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCV 815
Cdd:cd05922   238 qAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVH 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  816 GGDGVAKGYLNRvdltnAVFSPHPFLPGERIYrTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQE 895
Cdd:cd05922   318 RGPNVMKGYWND-----PPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIE 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  896 AAVTLREKDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05922   392 AAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 477-960 4.79e-54

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 197.82  E-value: 4.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGL----------------------EQNAAFSGTC-----IISDAQGLMEENDIpi 609
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGLFlgvdysattrlpalehvvicetEEDDPHTEKMktftdFLAAGDPAERAPEV-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  610 nissSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFIMTGSIsfdavtFEMFG-------ALLNG 681
Cdd:PRK07656  164 ----DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADwAEYLGLTEGDRYLAANPF------FHVFGykagvnaPLMRG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  682 ASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYV---GGEALSPALMNAVRHACPDLAL 758
Cdd:PRK07656  234 ATILPLPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLavtGAASMPVALLERFESELGVDIV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  759 HNIYGPTENTTFSTFFEMKRDyAGPIP--IGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFS 836
Cdd:PRK07656  311 LTGYGLSEASGVTTFNRLDDD-RKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAID 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  837 PHPFLpgeriyRTGDLARWLPDGNLeYIsrIDRQ--MKIRGK-RIEPAEIEARLLEMEGVQEAAV--TLREKDGEA-QLY 910
Cdd:PRK07656  390 ADGWL------HTGDLGRLDEEGYL-YI--VDRKkdMFIVGGfNVYPAEVEEVLYEHPAVAEAAVigVPDERLGEVgKAY 460

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 499188982  911 THYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK07656  461 VVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
480-960 1.90e-48

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 182.62  E-value: 1.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNM-----SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYL 554
Cdd:COG0365    13 NCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  555 PLDAELPPERVSFMLEETQAKMLIVQKG-------------LEQNAAFSGT---CIISDAQG-------------LMEEN 605
Cdd:COG0365    93 PVFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkekVDEALEELPSlehVIVVGRTGadvpmegdldwdeLLAAA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  606 DIPINISS-SPDDLAYIMYTSGSTGRPKGVMITNRNVVSlvrnsnYTSASG--------DDRFIMTGSISFdaVTFE--- 673
Cdd:COG0365   173 SAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGYLV------HAATTAkyvldlkpGDVFWCTADIGW--ATGHsyi 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  674 MFGALLNGASLHIID-KSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRG-----LHTLYVGGEALSPALMN 747
Cdd:COG0365   245 VYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydlssLRLLGSAGEPLNPEVWE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  748 AVRHA--CPdlaLHNIYGPTENTTFstffemkrdYAGPIP--------IGKPISNSTAYILDTKGRLLPIGVPGELCVGG 817
Cdd:COG0365   325 WWYEAvgVP---IVDGWGQTETGGI---------FISNLPglpvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  818 D--GVAKGYLNRVDLT-NAVFSPHPflpgeRIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQ 894
Cdd:COG0365   393 PwpGMFRGYWNDPERYrETYFGRFP-----GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  895 EAAVTLREkdgeaqlytHYVGDHK-------KTDTDFRADLARVLpdymipQHWVR--------------VERMPLTGNG 953
Cdd:COG0365   468 EAAVVGVP---------DEIRGQVvkafvvlKPGVEPSDELAKEL------QAHVReelgpyaypreiefVDELPKTRSG 532


                  ....*..
gi 499188982  954 KIDRSAL 960
Cdd:COG0365   533 KIMRRLL 539
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
467-898 8.37e-48

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 181.45  E-value: 8.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  467 NTKTEYPKNHTIIDLFREQAEKTPDHTALVY----GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMIS 542
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  543 VLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV--QKGLEQNAAFSGTC-----IISDAQGLMEENDIPINISS-- 613
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLLEVRDELpslrhIVVLDPRGLRDDPRLLSLDEll 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 -------------------SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN-YTSASGDDRFimtgsISF--DAVT 671
Cdd:COG1022   162 algrevadpaelearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLeRLPLGPGDRT-----LSFlpLAHV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  672 FE---MFGALLNGASLHIIDKSTMLTPD----------------------------------------------RFGAYL 702
Cdd:COG1022   237 FErtvSYYALAAGATVAFAESPDTLAEDlrevkptfmlavprvwekvyagiqakaeeagglkrklfrwalavgrRYARAR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  703 LENDI--TVLFLTTALFNQL--AQVRADMFRGLHTLYVGGEALSPAL---MNAVrhacpDLALHNIYGPTENTTFSTFFE 775
Cdd:COG1022   317 LAGKSpsLLLRLKHALADKLvfSKLREALGGRLRFAVSGGAALGPELarfFRAL-----GIPVLEGYGLTETSPVITVNR 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  776 MKRdyagpipigkpisnstaYILDTKGRLLP-----IGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTG 850
Cdd:COG1022   392 PGD-----------------NRIGTVGPPLPgvevkIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWL------HTG 448

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 499188982  851 DLARWLPDGNLEYISRIDRQMKIR-GKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:COG1022   449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 490-960 2.33e-47

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: 177.50  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALV--YGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSF 567
Cdd:cd05926     1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  568 MLEETQAKMLIVQKGLE---QNAAFSGTCII-------------SDAQGLMEENDIPINISSS----PDDLAYIMYTSGS 627
Cdd:cd05926    81 YLADLGSKLVLTPKGELgpaSRAASKLGLAIlelaldvgvliraPSAESLSNLLADKKNAKSEgvplPDDLALILHTSGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  628 TGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFImtgsisfdaVTFEMF------GALLngASLhiIDKSTMLTPDRFGA 700
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNiTNTYKLTPDDRTL---------VVMPLFhvhglvASLL--STL--AAGGSVVLPPRFSA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  701 YLLENDI---------TVLFLTTALfnqLAQVRADMFRGLHTLYV---GGEALSPALMNAV--RHACPDLalhNIYGPTE 766
Cdd:cd05926   228 STFWPDVrdynatwytAVPTIHQIL---LNRPEPNPESPPPKLRFirsCSASLPPAVLEALeaTFGAPVL---EAYGMTE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  767 NT--TFSTFFEMKRDYAG--PIPIGKPISnstayILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLp 842
Cdd:cd05926   302 AAhqMTSNPLPPGPRKPGsvGKPVGVEVR-----ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWF- 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  843 geriyRTGDLARWLPDGNLEYISRIdRQMKIR-GKRIEPAEIEARLLEMEGVQEAAV--TLREKDGEA-QLYTHYVGDHK 918
Cdd:cd05926   376 -----RTGDLGYLDADGYLFLTGRI-KELINRgGEKISPLEVDGVLLSHPAVLEAVAfgVPDEKYGEEvAAAVVLREGAS 449

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 499188982  919 KTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05926   450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 17-318 6.92e-44

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


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 165.30  E-value: 6.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   17 IYPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvpHLSGPRQVVMteREFH 96
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWE--GLSEPVQVVW--RQAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   97 LNSEDISHLPTNDQNEYIERFKEKDKQKgFDLQKDMLMRislFKTAKDEH----VCIWSHHHILMDGWCLGIVMQEFmqi 172
Cdd:cd19544    77 LPVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLR---AHVAEDPAngrwLLLLLFHHLISDHTSLELLLEEI--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  173 yQSIHAGKPLSLDPVRPYSTYI--SWLTNRDKEkAAAYWDTYLKNYSAPSpLP------RVSDKETKESyHREdlifsLN 244
Cdd:cd19544   150 -QAILAGRAAALPPPVPYRNFVaqARLGASQAE-HEAFFREMLGDVDEPT-APfglldvQGDGSDITEA-RLA-----LD 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  245 KPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEIPGVEQMIGLFINTIPIRIKTHQ 318
Cdd:cd19544   221 AELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGG 294
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 18-443 1.91e-43

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


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 164.08  E-value: 1.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   18 YPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHL 97
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRF---TEEEGEPYQWIDPYTPVPI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHLPtnDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:cd19533    79 RHIDLSGDP--DPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVRPYSTYI----SWLTNRDKEKAAAYWdtyLKNYSAPSPLPRVSDKETKES--YHREDLIFSLNkpLTDKL 251
Cdd:cd19533   157 KGRPAPPAPFGSFLDLVeeeqAYRQSERFERDRAFW---TEQFEDLPEPVSLARRAPGRSlaFLRRTAELPPE--LTRTL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  252 KETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQK 331
Cdd:cd19533   232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGA--AARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  332 EMLEAEPFTCQPLFDIQ---ANTALKQELIDHIIVFENYPLQQKIADSADQTDS----PLQIDQVQVSEqsgynfnlvVA 404
Cdd:cd19533   310 ELRSLLRHQRYRYEDLRrdlGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNlssgPTNDLSIFVYD---------RD 380

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 499188982  405 PGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19533   381 DESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 480-960 3.78e-43

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: 165.62  E-value: 3.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd05959     8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFMLEETQAKMLIVQKGLEQNAAFSG--------TCIISDAQG-----LMEENDIP------INISSSPDDLAY 620
Cdd:cd05959    88 LTPDDYAYYLEDSRARVVVVSGELAPVLAAALtksehtlvVLIVSGGAGpeagaLLLAELVAaeaeqlKPAATHADDPAF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  621 IMYTSGSTGRPKGVMITNRNV----VSLVRNSNYTSAsgDDRFIMTGSISF-----DAVTFEM-FGAllngaslhiidkS 690
Cdd:cd05959   168 WLYSSGSTGRPKGVVHLHADIywtaELYARNVLGIRE--DDVCFSAAKLFFayglgNSLTFPLsVGA------------T 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  691 TML-----TPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYV---GGEALSPALMNAVRhacpDLALHNIY 762
Cdd:cd05959   234 TVLmperpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvsAGEALPAEVGERWK----ARFGLDIL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  763 ---GPTE--NTTFSTFFEMKRdyagPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSp 837
Cdd:cd05959   310 dgiGSTEmlHIFLSNRPGRVR----YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ- 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  838 hpflpGErIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT-LREKDGEAQLYTHYV-- 914
Cdd:cd05959   385 -----GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTKPKAFVVlr 458

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 499188982  915 ---GDHKKTDTDFRADLARVLPDYMIPqHWVR-VERMPLTGNGKIDRSAL 960
Cdd:cd05959   459 pgyEDSEALEEELKEFVKDRLAPYKYP-RWIVfVDELPKTATGKIQRFKL 507
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 502-961 6.50e-43

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: 162.85  E-value: 6.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVqk 581
Cdd:cd05934     4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqnaafsgtciisdaqglmeendipinissspdDLAYIMYTSGSTGRPKGVMITNRNVVSLVR-NSNYTSASGDDRFI 660
Cdd:cd05934    82 -----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYySARRFGLGEDDVYL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSISF-DAVTFEMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYVGGE 739
Cdd:cd05934   127 TVLPLFHiNAQAVSVLAALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYG 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  740 ALSPALMNAV---RHACPdlaLHNIYGPTEnTTFSTFFEmkRD-YAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCV 815
Cdd:cd05934   204 APNPPELHEEfeeRFGVR---LLEGYGMTE-TIVGVIGP--RDePRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  816 ---GGDGVAKGYLNRVDLTNAVFsPHPFlpgeriYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEG 892
Cdd:cd05934   278 rglRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPA 350

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499188982  893 VQEAAV-TLREKDGEAQLYTHYVGDHKKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALP 961
Cdd:cd05934   351 VREAAVvAVPDEVGEDEVKAVVVLRPGETLDpeELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 19-443 7.98e-43

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


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 162.55  E-value: 7.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLF-HSFlrkEEG--AYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPhlSGPRQVVMTEREF 95
Cdd:cd19539     3 PLSFAQERLWFiDQG---EDGgpAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDG--GVPRQEILPPGPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   96 HLNSEDISHlPTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQS 175
Cdd:cd19539    78 PLEVRDLSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  176 IHAGKPLSLDPVR-PYSTYISWLTNRDKEKAAA----YWDTYLKNYSA---PSPLPRVS--DKETKesyhreDLIFSLNK 245
Cdd:cd19539   157 RRKGPAAPLPELRqQYKEYAAWQREALAAPRAAelldFWRRRLRGAEPtalPTDRPRPAgfPYPGA------DLRFELDA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  246 PLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFHEL 325
Cdd:cd19539   231 ELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  326 LIRCQKEMLEAEPFTCQPLFDIQANTALKQELIDHiivfenyPLQQkIADSADQTDSPLQIDQVQVSEQSG--------Y 397
Cdd:cd19539   309 IARVRKALVDAQRHQELPFQQLVAELPVDRDAGRH-------PLVQ-IVFQVTNAPAGELELAGGLSYTEGsdipdgakF 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 499188982  398 NFNLVVAP-GEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd19539   381 DLNLTVTEeGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 503-960 2.58e-42

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: 161.45  E-value: 2.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAkmlivqkg 582
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA-------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 leqnaafsgTCIISDAqglmeendipinisssPDDLAYIMYTSGSTGRPKGVMITNRnvVSLVRNSNYTSASgdDRFIMT 662
Cdd:cd05971    80 ---------SALVTDG----------------SDDPALIIYTSGTTGPPKGALHAHR--VLLGHLPGVQFPF--NLFPRD 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  663 GSISFDAVTFEMFGALLNG--ASLH-----IIDKSTMLTPDRFGAYLLENDITVLFLT-TAL--FNQLAQVRADMFRGLH 732
Cdd:cd05971   131 GDLYWTPADWAWIGGLLDVllPSLYfgvpvLAHRMTKFDPKAALDLMSRYGVTTAFLPpTALkmMRQQGEQLKHAQVKLR 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  733 TLYVGGEALSPALMNAVRHACPDlALHNIYGPTEN----TTFSTFFEMKrdyagPIPIGKPISNSTAYILDTKGRLLPIG 808
Cdd:cd05971   211 AIATGGESLGEELLGWAREQFGV-EVNEFYGQTECnlviGNCSALFPIK-----PGSMGKPIPGHRVAIVDDNGTPLPPG 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  809 VPGELCVG-GDGVAK-GYLNRVDLTNAVFSphpflpGERIyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEAR 886
Cdd:cd05971   285 EVGEIAVElPDPVAFlGYWNNPSATEKKMA------GDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEC 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  887 LLEMEGVQEAAVTLR--EKDGE-AQLYTHYVGDHKKTDT---DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05971   358 LLKHPAVLMAAVVGIpdPIRGEiVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 503-960 6.80e-42

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


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 159.81  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKmlivqkg 582
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 leqnaafsgtCIISDAqglmeendipinissspDDLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGDDRFIM 661
Cdd:cd05972    75 ----------AIVTDA-----------------EDPALIYFTSGTTGLPKGVLHTHSYPLGhIPTAAYWLGLRPDDIHWN 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  662 TGSISF-DAVTFEMFGALLNGASLhIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFR--GLHTLYVGG 738
Cdd:cd05972   128 IADPGWaKGAWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKfsHLRLVVSAG 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  739 EALSPALMNAVRhACPDLALHNIYGPTENT-TFSTFFEMKrdyAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCV-- 815
Cdd:cd05972   207 EPLNPEVIEWWR-AATGLPIRDGYGQTETGlTVGNFPDMP---VKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIkl 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  816 GGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQE 895
Cdd:cd05972   283 PPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE 355

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499188982  896 AAVTLREKDGEAQLYTHYV------GDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05972   356 AAVVGSPDPVRGEVVKAFVvltsgyEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 490-960 8.07e-42

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 162.08  E-value: 8.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIV------QKGLEQNAAFSG------TCIISDAQGLMEENDI----PINISSSPDDLAYIMYTSGSTGRPKG 633
Cdd:PRK06188  106 EDAGISTLIVdpapfvERALALLARVPSlkhvltLGPVPDGVDLLAAAAKfgpaPLVAAALPPDIAGLAYTGGTTGKPKG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  634 VMITNRNVVSLVrNSNYTSAS--GDDRFIMTGSISFDAVTFeMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLF 711
Cdd:PRK06188  186 VMGTHRSIATMA-QIQLAEWEwpADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITATF 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 LTT----ALFNQLAQVRADMfRGLHTLYVGGEALSPA-LMNAVRHACPDLALHniYGPTENTTFSTFFEmKRDYAGPIP- 785
Cdd:PRK06188  261 LVPtmiyALLDHPDLRTRDL-SSLETVYYGASPMSPVrLAEAIERFGPIFAQY--YGQTEAPMVITYLR-KRDHDPDDPk 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  786 ----IGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSpHPFLpgeriyRTGDLARWLPDGnl 861
Cdd:PRK06188  337 rltsCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-DGWL------HTGDVAREDEDG-- 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  862 eYISRIDRQ--MKIRGK-RIEPAEIEARLLEMEGVQEAAV--TLREKDGEAqlYTHYV---GDHKKTDTDFRADLARVLP 933
Cdd:PRK06188  408 -FYYIVDRKkdMIVTGGfNVFPREVEDVLAEHPAVAQVAVigVPDEKWGEA--VTAVVvlrPGAAVDAAELQAHVKERKG 484

                         490       500
                  ....*....|....*....|....*..
gi 499188982  934 DYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06188  485 SVHAPKQVDFVDSLPLTALGKPDKKAL 511
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 493-960 5.56e-41

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: 157.24  E-value: 5.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  493 TALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEET 572
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  573 QAKMLIVqkgleqnaafsgtciisdaqglmeendipinissSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR--NSNY 650
Cdd:cd05919    82 EARLVVT----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADamAREA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  651 TSASGDDRFIMTGSISFdavTFEM----FGALLNGASLhIIDkSTMLTPDRFGAYLLENDITVLFLTTALFNQL---AQV 723
Cdd:cd05919   128 LGLTPGDRVFSSAKMFF---GYGLgnslWFPLAVGASA-VLN-PGWPTAERVLATLARFRPTVLYGVPTFYANLldsCAG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIyGPTENttFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGR 803
Cdd:cd05919   203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI-GATEV--GHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  804 LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEI 883
Cdd:cd05919   280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  884 EARLLEMEGVQEAAVT-LREKDGEAQLYTHYVGDHKKTDT-----DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd05919   353 ESLIIQHPAVAEAAVVaVPESTGLSRLTAFVVLKSPAAPQeslarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432


                  ...
gi 499188982  958 SAL 960
Cdd:cd05919   433 FKL 435
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
483-960 1.32e-40

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 157.43  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  483 REQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPP 562
Cdd:PRK03640    9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  563 ERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLmEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRN-- 640
Cdd:PRK03640   89 EELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNG-PKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhw 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  641 --VVSLVRNSNYTSasgDDR-------FIMTG-SIsfdavtfeMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVL 710
Cdd:PRK03640  168 wsAVGSALNLGLTE---DDCwlaavpiFHISGlSI--------LMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTII 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  711 FLTTALFNQLAQVRADM-----FRGLhtLYVGGEALSPALMNAVRHACPdlaLHNIYGPTEntTFSTFFEMKRDYA---- 781
Cdd:PRK03640  234 SVVSTMLQRLLERLGEGtypssFRCM--LLGGGPAPKPLLEQCKEKGIP---VYQSYGMTE--TASQIVTLSPEDAltkl 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  782 GpiPIGKPISNSTAYILDtKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGDLARWLPDGNL 861
Cdd:PRK03640  307 G--SAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFL 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  862 eYIsrIDRQ--MKIR-GKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQL-YTHYVGDHKKTDTDFRADLARVLPDYMI 937
Cdd:PRK03640  377 -YV--LDRRsdLIISgGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVpVAFVVKSGEVTEEELRHFCEEKLAKYKV 453

                         490       500
                  ....*....|....*....|...
gi 499188982  938 PQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK03640  454 PKRFYFVEELPRNASGKLLRHEL 476
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 491-960 6.65e-40

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: 154.37  E-value: 6.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  491 DHTALVYGNMSISYKELDKRSNALARELIQKGFRKNET-AGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFML 569
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDrVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIvqkgleqnaafsgtciisdaqglmeendipinissspdDLAYIMYTSGSTGRPKGVMITNRNVVS----LV 645
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAAnvraLV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 RNSNYTSasgDDRFI-------MTGsisfdaVTFEMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLF------- 711
Cdd:cd05941   123 DAWRWTE---DDVLLhvlplhhVHG------LVNALLCPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMgvptiyt 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 --LTT--ALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVRHacpdLALHNI---YGPTE-NTTFSTFFEMKRdyagp 783
Cdd:cd05941   191 rlLQYyeAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEA----ITGHTLlerYGMTEiGMALSNPLDGER----- 261

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  784 IP--IGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWLPDGN 860
Cdd:cd05941   262 RPgtVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGY 335

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  861 LEYISRI-DRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT-LREKD-GEAqlYTHYV----GDHKKTDTDFRADLARVLP 933
Cdd:cd05941   336 YWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgVPDPDwGER--VVAVVvlraGAAALSLEELKEWAKQRLA 413

                         490       500
                  ....*....|....*....|....*..
gi 499188982  934 DYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05941   414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 476-898 2.42e-39

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 154.32  E-value: 2.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLP 555
Cdd:PRK08316   11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  556 LDAELPPERVSFMLEETQAKMLIVQKGLEQNA--------------------AFSGTCIISDAQGLMEENDIPINISSSP 615
Cdd:PRK08316   91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAeaalallpvdtlilslvlggREAPGGWLDFADWAEAGSVAEPDVELAD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  616 DDLAYIMYTSGSTGRPKGVMITNRNVVslvrnSNYTSA------SGDDRFIMTGSISFDAVTFEMFG-ALLNGASLHIID 688
Cdd:PRK08316  171 DDLAQILYTSGTESLPKGAMLTHRALI-----AEYVSCivagdmSADDIPLHALPLYHCAQLDVFLGpYLYVGATNVILD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  689 KStmlTPDRFGAYLLENDITVLFLT----TALFNQLAQVRADMfRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGP 764
Cdd:PRK08316  246 AP---DPELILRTIEAERITSFFAPptvwISLLRHPDFDTRDL-SSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQ 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  765 TENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpge 844
Cdd:PRK08316  322 TEIAPLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF---- 397

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499188982  845 riyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK08316  398 ---HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 486-907 4.08e-39

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


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 153.54  E-value: 4.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYG--NMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:cd05904    15 ASAHPSRPALIDAatGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQ-KGLEQNAAFSGTCIISD-AQGLMEENDIPINISS---------SPDDLAYIMYTSGSTGRPK 632
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTaELAEKLASLALPVVLLDsAEFDSLSFSDLLFEADeaeppvvviKQDDVAALLYSSGTTGRSK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  633 GVMITNRNVVSLVRNSNYTSASGDDRfimtgsisfDAVT------FEMFG-------ALLNGASLHII---DKSTML-TP 695
Cdd:cd05904   175 GVMLTHRNLIAMVAQFVAGEGSNSDS---------EDVFlcvlpmFHIYGlssfalgLLRLGATVVVMprfDLEELLaAI 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  696 DRFGayllendITVLFLTTALFnqLAQVRADM-----FRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENT-- 768
Cdd:cd05904   246 ERYK-------VTHLPVVPPIV--LALVKSPIvdkydLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTgv 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  769 TFSTF-FEMKRDYAGPIpiGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeri 846
Cdd:cd05904   317 VAMCFaPEKDRAKYGSV--GRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWL----- 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499188982  847 yRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTlREKDGEA 907
Cdd:cd05904   390 -HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI-PYPDEEA 448
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 501-898 7.98e-39

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: 151.21  E-value: 7.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVq 580
Cdd:cd05907     5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 kgleqnaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRF 659
Cdd:cd05907    84 --------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALAlAERLPATEGDRH 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  660 ImtgsiSF--DAVTFEM----FGALLNGASLHIIDKSTMLTPD--RFGAyllendiTVLFLTTALFN--QLAQVRADMFR 729
Cdd:cd05907   132 L-----SFlpLAHVFERraglYVPLLAGARIYFASSAETLLDDlsEVRP-------TVFLAVPRVWEkvYAAIKVKAVPG 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  730 GLHTLY------------VGGEALSPALMNAVRHACpdLALHNIYGPTENTTFSTFFEMKRDYAGPIpiGKPISNSTAYI 797
Cdd:cd05907   200 LKRKLFdlavggrlrfaaSGGAPLPAELLHFFRALG--IPVYEGYGLTETSAVVTLNPPGDNRIGTV--GKPLPGVEVRI 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTkgrllpigvpGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRI-DRQMKIRGK 876
Cdd:cd05907   276 ADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWL------HTGDLGEIDEDGFLHITGRKkDLIITSGGK 339

                         410       420
                  ....*....|....*....|..
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAV 898
Cdd:cd05907   340 NISPEPIENALKASPLISQAVV 361
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 486-898 4.20e-38

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 150.42  E-value: 4.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEEN-------DIPINISSSPDDLAYIMYTSGSTGRPKGVMITN 638
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRrlaqgglEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  639 RNVVSlvRNSNYTSASG---DDRFIMTGSI----SFD----AV-----------TFEMFGAL-------LNGASLHIIDK 689
Cdd:PRK06145  172 GNLHW--KSIDHVIALGltaSERLLVVGPLyhvgAFDlpgiAVlwvggtlrihrEFDPEAVLaaierhrLTCAWMAPVML 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  690 STMLT---PDRFgayllenDITVLFLTTALFNQLAQVRadmFRGLHTLYVGGEALspalmnavrhacpdlalhNIYGPTE 766
Cdd:PRK06145  250 SRVLTvpdRDRF-------DLDSLAWCIGGGEKTPESR---IRDFTRVFTRARYI------------------DAYGLTE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  767 NTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeri 846
Cdd:PRK06145  302 TCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF------ 375

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499188982  847 yRTGDLArWLPDGNLEYISRIDRQMKIRG-KRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK06145  376 -RSGDVG-YLDEEGFLYLTDRKKDMIISGgENIASSEVERVIYELPEVAEAAV 426
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 19-336 5.83e-38

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


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 147.99  E-value: 5.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLF-HSFLrKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHvPHLSGPRQVVMTEREFHL 97
Cdd:cd19532     3 PMSFGQSRFWFlQQYL-EDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTD-PEDGEPMQGVLASSPLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDIShlptnDQNEYIERFKEKDKQKgFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQsih 177
Cdd:cd19532    81 EHVQIS-----DEAEVEEEFERLKNHV-YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 aGKPLsLDPVRPYSTYISW----LTNRDKEKAAAYWDTYLKnySAPSPLP-----RVSDKETKESYHREDLIFSLNKPLT 248
Cdd:cd19532   152 -GQPL-LPPPLQYLDFAARqrqdYESGALDEDLAYWKSEFS--TLPEPLPllpfaKVKSRPPLTRYDTHTAERRLDAALA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  249 DKLKETAKQHGVT-----LatliqAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFH 323
Cdd:cd19532   228 ARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFA 300

                         330
                  ....*....|...
gi 499188982  324 ELLIRCQKEMLEA 336
Cdd:cd19532   301 DVLKETRDKAYAA 313
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 501-955 7.44e-37

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


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 145.22  E-value: 7.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL-----DAELppervSFMLEETQAK 575
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPIlpffrEHEL-----AFILRRAKAK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  576 MLIVQKGLEQNaafsgtciisdaqglmeendipiNISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN--SNYTSA 653
Cdd:cd05903    76 VFVVPERFRQF-----------------------DPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQyaERLGLG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  654 SGdDRFIM-------TGSIsfdavtFEMFGALLNGASLHIIDkstMLTPDRFGAYLLENDITVLFLTTALFNQLAQV--- 723
Cdd:cd05903   133 PG-DVFLVaspmahqTGFV------YGFTLPLLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLTDLLNAvee 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 RADMFRGLHTLYVGGEALSPALmnaVRHA--CPDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTK 801
Cdd:cd05903   203 AGEPLSRLRTFVCGGATVPRSL---ARRAaeLLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDT 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  802 GRLLPIGVPGELCVGGDGVAKGYLNRVDLTnAVFSPHPFlpgeriYRTGDLARWLPDGnleYIsRIDRQMK---IR-GKR 877
Cdd:cd05903   280 GATLAPGVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGW------FRTGDLARLDEDG---YL-RITGRSKdiiIRgGEN 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAAVT--------------LREKDGeaqlythyvgdHKKTDTDFRADLARV-LPDYMIPQHWV 942
Cdd:cd05903   349 IPVLEVEDLLLGHPGVIEAAVValpderlgeracavVVTKSG-----------ALLTFDELVAYLDRQgVAKQYWPERLV 417

                         490
                  ....*....|...
gi 499188982  943 RVERMPLTGNGKI 955
Cdd:cd05903   418 HVDDLPRTPSGKV 430
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 19-326 1.03e-36

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


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 144.71  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLF-HSFLRkEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPHVPHlsgPRQVVMTEREFHL 97
Cdd:cd20483     3 PMSTFQRRLWFlHNFLE-DKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDF---GEQQVLDDPSFHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHlpTNDQNEYIERFKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:cd20483    79 IVIDLSE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLS-LDPVR-PYSTYISW----LTNRDKEKAAAYWDTYLKNYSAPSPL--------PRVSDketkesYHREDLIFSL 243
Cdd:cd20483   157 AGRDLAtVPPPPvQYIDFTLWhnalLQSPLVQPLLDFWKEKLEGIPDASKLlpfakaerPPVKD------YERSTVEATL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  244 NKPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSeiPGVEQMIGLFINTIPIRIKTHQDETFH 323
Cdd:cd20483   231 DKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFD 308


                  ...
gi 499188982  324 ELL 326
Cdd:cd20483   309 DLL 311
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 477-960 1.99e-36

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: 146.06  E-value: 1.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGayLPL 556
Cdd:COG1021    26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAeLPPER---VSFMLEETQAKMLIVQKGL----------EQNAAFSG--TCIISDAQG-------LMEENDIPINISSS 614
Cdd:COG1021   104 FA-LPAHRraeISHFAEQSEAVAYIIPDRHrgfdyralarELQAEVPSlrHVLVVGDAGeftsldaLLAAPADLSEPRPD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN-YTSASGDDRFIMTGSISFDavtFEM-----FGALLNGASLHIid 688
Cdd:COG1021   183 PDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAeICGLDADTVYLAALPAAHN---FPLsspgvLGVLYAGGTVVL-- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  689 kSTMLTPDRFGAYLLENDITVlfltTAL--------FNQLAQVRADMfRGLHTLYVGGEALSPALMNAVRHA--CpdlAL 758
Cdd:COG1021   258 -APDPSPDTAFPLIERERVTV----TALvpplallwLDAAERSRYDL-SSLRVLQVGGAKLSPELARRVRPAlgC---TL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  759 HNIYGPTE---NTT---------FSTffemkrdyagpipIGKPISnstAY----ILDTKGRLLPIGVPGELCVGGDGVAK 822
Cdd:COG1021   329 QQVFGMAEglvNYTrlddpeeviLTT-------------QGRPIS---PDdevrIVDEDGNPVPPGEVGELLTRGPYTIR 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  823 GYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWLPDGNLEYISRIDRQMkIR-GKRIEPAEIEARLLEMEGVQEAAV--- 898
Cdd:COG1021   393 GYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVvam 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  899 ---TLREK-------DGE----AQLYTHyvgdhkktdtdFRadlARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:COG1021   466 pdeYLGERscafvvpRGEpltlAELRRF-----------LR---ERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 501-960 3.08e-35

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: 140.31  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVq 580
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 kgleqnaafsgtciisdaqglmeendipiniSSSPDDLAYIMYTSGSTGRPKGVMITNR----NVVSLVRNSNYTSASgd 656
Cdd:cd05935    80 -------------------------------GSELDDLALIPYTSGTTGLPKGCMHTHFsaaaNALQSAVWTGLTPSD-- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  657 drfIMTGSISFDAVTfEMFGALLngasLHIIDKSTMLTPDRFGAYLLENDIT---VLF---LTTALFNQLAQV--RADMF 728
Cdd:cd05935   127 ---VILACLPLFHVT-GFVGSLN----TAVYVGGTYVLMARWDRETALELIEkykVTFwtnIPTMLVDLLATPefKTRDL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  729 RGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGPTENTTFSTFFEMKRdyagpiP----IGKPISNSTAYILDTK-GR 803
Cdd:cd05935   199 SSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTHTNPPLR------PklqcLGIP*FGVDARVIDIEtGR 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  804 LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEI 883
Cdd:cd05935   272 ELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  884 EARLLEMEGVQEAAV--TLREKDGEAQ-----LYTHYVGdhKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd05935   349 EAKLYKHPAI*EVCVisVPDERVGEEVkafivLRPEYRG--KVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426


                  ....
gi 499188982  957 RSAL 960
Cdd:cd05935   427 WRLL 430
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 471-960 4.36e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 142.49  E-value: 4.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  471 EYPKNH-TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK06178   27 EYPHGErPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLD-----AELppervSFMLEETQAKMLIVQKGL--------EQNA-------AFSGTC---------------- 593
Cdd:PRK06178  107 GAVHVPVSplfreHEL-----SYELNDAGAEVLLALDQLapvveqvrAETSlrhvivtSLADVLpaeptlplpdslrapr 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  594 -IISDAQGLME-ENDIPINI---SSSPDDLAYIMYTSGSTGRPKGVMITNRNVVslvrnsnYTSAS-------GDDRFIM 661
Cdd:PRK06178  182 lAAAGAIDLLPaLRACTAPVplpPPALDALAALNYTGGTTGMPKGCEHTQRDMV-------YTAAAayavavvGGEDSVF 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  662 TGSISFDAVTFEMFGALL---NGASLHIIDK----STMLTPDRFGAyllenDITVLFLTTAL------------FNQLAQ 722
Cdd:PRK06178  255 LSFLPEFWIAGENFGLLFplfSGATLVLLARwdavAFMAAVERYRV-----TRTVMLVDNAVelmdhprfaeydLSSLRQ 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  723 VRADMFRglhtlyvggEALSPALmnavRHACPDLALHNI----YGPTENTTFSTF--------FEMKRDyagPIPIGKPI 790
Cdd:PRK06178  330 VRVVSFV---------KKLNPDY----RQRWRALTGSVLaeaaWGMTETHTCDTFtagfqdddFDLLSQ---PVFVGLPV 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  791 SNSTAYILD-TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDR 869
Cdd:PRK06178  394 PGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKE 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  870 QMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV---GDHKKTDTDFRADLARVLPDYMIPQhwVR-VE 945
Cdd:PRK06178  467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVqlkPGADLTAAALQAWCRENMAVYKVPE--IRiVD 544

                         570
                  ....*....|....*
gi 499188982  946 RMPLTGNGKIDRSAL 960
Cdd:PRK06178  545 ALPMTATGKVRKQDL 559
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 472-960 5.42e-35

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: 140.54  E-value: 5.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  472 YPKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGG 551
Cdd:cd05920    11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  552 ayLPLDAeLPPER---VSFMLEETQAKMLIVQkglEQNAAFsgtciisDAQGLMEEndipinISSSPDDLAYIMYTSGST 628
Cdd:cd05920    91 --VPVLA-LPSHRrseLSAFCAHAEAVAYIVP---DRHAGF-------DHRALARE------LAESIPEVALFLLSGGTT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  629 GRPKGVMITNRNVVSLVRnsnyTSA-----SGDDRFI--MTGSISFDAVTFEMFGALLNGASLHIidkSTMLTPDRFGAY 701
Cdd:cd05920   152 GTPKLIPRTHNDYAYNVR----ASAevcglDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVL---APDPSPDAAFPL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  702 LLENDITVLFLTTALFNQLAQVRADMFRG---LHTLYVGGEALSPALMNAVrHACPDLALHNIYGPTENTTFSTFFemkr 778
Cdd:cd05920   225 IEREGVTVTALVPALVSLWLDAAASRRADlssLRLLQVGGARLSPALARRV-PPVLGCTLQQVFGMAEGLLNYTRL---- 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  779 DYAGPIPI---GKPIS-NSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLAR 854
Cdd:cd05920   300 DDPDEVIIhtqGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVR 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  855 WLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKD--GEAQLYTHYVGDHKKTDTDFRADL-ARV 931
Cdd:cd05920   374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEllGERSCAFVVLRDPPPSAAQLRRFLrERG 453

                         490       500
                  ....*....|....*....|....*....
gi 499188982  932 LPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05920   454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 501-960 7.45e-35

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


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 138.63  E-value: 7.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMlivq 580
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 kgleqnaafsgtciisdaqglmeendipinissspDDLAYIMYTSGSTGRPKGVMITNRNvvslvrnsNYTSASG----- 655
Cdd:cd05912    77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFGN--------HWWSAIGsalnl 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  656 ----DDR-------FIMTG-SIsfdavtfeMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFNQLAQV 723
Cdd:cd05912   114 glteDDNwlcalplFHISGlSI--------LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEI 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 RADMF-RGLHTLYVGGEALSPALMNAVRHAcpDLALHNIYGPTEntTFSTFFEMKRDYAgPIPI---GKPISNSTAYILD 799
Cdd:cd05912   183 LGEGYpNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTE--TCSQIVTLSPEDA-LNKIgsaGKPLFPVELKIED 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKGRLlpiGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGDLARWLPDGNLeYIsrIDRQMKI---RGK 876
Cdd:cd05912   258 DGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFL-YV--LDRRSDLiisGGE 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTD-FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:cd05912   325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEeLIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404


                  ....*
gi 499188982  956 DRSAL 960
Cdd:cd05912   405 LRHEL 409
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 19-336 2.37e-34

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


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 137.78  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphvPHLSG-PRQVVMTEREFHL 97
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF----PEEDGvPYQLILEEDEATP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 nseDISHLPTnDQNEYIERFKEKDKQKgFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:cd19538    79 ---KLEIKEV-DEEELESEINEAVRYP-FDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVrP--YSTYISW---LTNRDKEKAA------AYWDTYLKNYSAPSPLPRVSDKETKESYHREDLIFSLNKP 246
Cdd:cd19538   154 KGEAPELAPL-PvqYADYALWqqeLLGDESDPDSliarqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  247 LTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELL 326
Cdd:cd19538   233 LHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELL 310

                         330
                  ....*....|
gi 499188982  327 IRCQKEMLEA 336
Cdd:cd19538   311 ERVKETNLEA 320
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 18-443 2.79e-34

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


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 137.45  E-value: 2.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   18 YPLSHMQEGMLFHSFLRKEEGAYVEQSLFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFlphVPHLSGPRQVVMTEREFHL 97
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVI---EEEDGVPFQKIEPSKPLSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   98 NSEDISHLptnDQNEYIERFKEKDKQKgFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIH 177
Cdd:cd20484    79 QEEDISSL---KESEIIAYLREKAKEP-FVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  178 AGKPLSLDPVRP-YSTYISW----LTNRDKEKAAAYWDTYLK----NYSAPSPLPRVSDKETKESYHREdlifSLNKPLT 248
Cdd:cd20484   155 QGKQPTLASSPAsYYDFVAWeqdmLAGAEGEEHRAYWKQQLSgtlpILELPADRPRSSAPSFEGQTYTR----RLPSELS 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  249 DKLKETAKQHGVTLATLIQAVWGVMLQQYNRTDDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELLIR 328
Cdd:cd20484   231 NQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRK 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  329 CQKEMLE-----AEPFTCQ------PLFdiQANTALKQELIDHIIVFENYPLQQKIADSADQtdspLQIDQVQVSEQSG- 396
Cdd:cd20484   309 LQLTVLDgldhaAYPFPAMvrdlniPRS--QANSPVFQVAFFYQNFLQSTSLQQFLAEYQDV----LSIEFVEGIHQEGe 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 499188982  397 YNFNL-VVAPGEELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQHP 443
Cdd:cd20484   383 YELVLeVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 617-960 6.18e-34

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: 133.61  E-value: 6.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVVSLVR--NSNYTSASGDDRFIMT--GSISFDAVtfeMFGALLNGASLHIIDKStm 692
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAglHSRLGFGGGDSWLLSLplYHVGGLAI---LVRSLLAGAELVLLERN-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 ltpDRFGAYLLENDITVLFLT-TALFNQLA--QVRADmFRGLHTLYVGGEALSPALmnAVRHACPDLALHNIYGPTEntt 769
Cdd:cd17630    76 ---QALAEDLAPPGVTHVSLVpTQLQRLLDsgQGPAA-LKSLRAVLLGGAPIPPEL--LERAADRGIPLYTTYGMTE--- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  770 fstffemkrdYAGPIPIGKPisnsTAYILDTKGRLLP-----IGVPGELCVGGDGVAKGYLNRVdltnavfsPHPFLPGE 844
Cdd:cd17630   147 ----------TASQVATKRP----DGFGRGGVGVLLPgrelrIVEDGEIWVGGASLAMGYLRGQ--------LVPEFNED 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  845 RIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVtLREKDGE--AQLYTHYVGDHKKTDT 922
Cdd:cd17630   205 GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFV-VGVPDEElgQRPVAVIVGRGPADPA 283

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 499188982  923 DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd17630   284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
485-960 4.82e-33

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 134.99  E-value: 4.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  485 QAEKTPDHTALVYGNMSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:PRK06839   11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQKGLeQNAAFSGTCIISDA-----QGLMEENDI-PINISSSPDDLAYIM-YTSGSTGRPKGVMI 636
Cdd:PRK06839   91 ELIFQLKDSGTTVLFVEKTF-QNMALSMQKVSYVQrvisiTSLKEIEDRkIDNFVEKNESASFIIcYTSGTTGKPKGAVL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  637 TNRNVV-SLVRNSNYTSASGDDRFIM------TGSISFDAvtfemFGALLNGASLHIIDKstmLTPDRFGAYLLENDITV 709
Cdd:PRK06839  170 TQENMFwNALNNTFAIDLTMHDRSIVllplfhIGGIGLFA-----FPTLFAGGVIIVPRK---FEPTKALSMIEKHKVTV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  710 LF----LTTALFNQLAQVRADmFRGLHTLYVGGealSPALMNAVRHACP-DLALHNIYGPTEnTTFSTFFEMKRDYA-GP 783
Cdd:PRK06839  242 VMgvptIHQALINCSKFETTN-LQSVRWFYNGG---APCPEELMREFIDrGFLFGQGFGMTE-TSPTVFMLSEEDARrKV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  784 IPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGDLARWLPDGnLEY 863
Cdd:PRK06839  317 GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDG-FVY 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  864 ISRIDRQMKIR-GKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGE-AQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQ 939
Cdd:PRK06839  389 IVGRKKEMIISgGENIYPLEVEQVINKLSDVYEVAVVGRqhVKWGEiPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468

                         490       500
                  ....*....|....*....|.
gi 499188982  940 HWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06839  469 EIVFLKELPKNATGKIQKAQL 489
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 485-960 5.18e-33

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 134.93  E-value: 5.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  485 QAEKTPDHTALV--YGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPP 562
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  563 ERVSFMLEETQAKMLI----VQKGLEQNAAFSGTCIISDAQGLMEENDIPinisssPDDLAYIMYTSGSTGRPKGVMITN 638
Cdd:PRK09088   84 SELDALLQDAEPRLLLgddaVAAGRTDVEDLAAFIASADALEPADTPSIP------PERVSLILFTSGTSGQPKGVMLSE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  639 RNVVSLVRNSNYTSasgddRFIMTGSISFDAVTFEMFG-------ALLNGASLHIidkSTMLTPDRFGAYLLENDITVlf 711
Cdd:PRK09088  158 RNLQQTAHNFGVLG-----RVDAHSSFLCDAPMFHIIGlitsvrpVLAVGGSILV---SNGFEPKRTLGRLGDPALGI-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 ltTALFN--QLAQV-------RADMFRGLHTLYVGGeALSPA------LMNAVRHACPdlalhniYGPTENttfSTFFEM 776
Cdd:PRK09088  228 --THYFCvpQMAQAfraqpgfDAAALRHLTALFTGG-APHAAedilgwLDDGIPMVDG-------FGMSEA---GTVFGM 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  777 KRDyAGPI-----PIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpGERIYRTGD 851
Cdd:PRK09088  295 SVD-CDVIrakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGD 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  852 LARWLPDGnleYISRIDRQ--MKIR-GKRIEPAEIEARLLEMEGVQEAAVT--LREKDGEAQLYTHYVGDHKKTD-TDFR 925
Cdd:PRK09088  368 IARRDADG---FFWVVDRKkdMFISgGENVYPAEIEAVLADHPGIRECAVVgmADAQWGEVGYLAIVPADGAPLDlERIR 444

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 499188982  926 ADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK09088  445 SHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 477-960 3.44e-32

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: 132.25  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVY--GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYL 554
Cdd:cd05923     2 TVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  555 PLDAELPPERVSFMLE--ETQAKMLIVQKGLEQNAAFSGTCII--SDAQGLME-ENDIPI--NISSSPDDLAYIMYTSGS 627
Cdd:cd05923    82 LINPRLKAAELAELIErgEMTAAVIAVDAQVMDAIFQSGVRVLalSDLVGLGEpESAGPLieDPPREPEQPAFVFYTSGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  628 TGRPKGVMITNR----NVVSLVRNSNYTSASGDdRFI----MTGSISFDAVtfeMFGALLNGASLHIIdksTMLTPDRFG 699
Cdd:cd05923   162 TGLPKGAVIPQRaaesRVLFMSTQAGLRHGRHN-VVLglmpLYHVIGFFAV---LVAALALDGTYVVV---EEFDPADAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  700 AYLLENDITVLFLTTALFNQLaqVRADMFRG-----LHTLYVGGEALSPALMNAVRHACPDLALhNIYGPTENTTfSTFF 774
Cdd:cd05923   235 KLIEQERVTSLFATPTHLDAL--AAAAEFAGlklssLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTEAMN-SLYM 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  775 EMKRDYAGpipiGKPISNSTAYILDTKGR---LLPIGVPGELCV--GGDGVAKGYLNRVDLTNAVFSphpflpgERIYRT 849
Cdd:cd05923   311 RDARTGTE----MRPGFFSEVRIVRIGGSpdeALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ-------DGWYRT 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  850 GDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTDFRAD-- 927
Cdd:cd05923   380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDqf 459

                         490       500       510
                  ....*....|....*....|....*....|....
gi 499188982  928 -LARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05923   460 cRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 503-960 4.75e-32

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: 131.09  E-value: 4.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQKG 582
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 LEQNaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYT-SASGDDRFIM 661
Cdd:cd05969    82 LYER--------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVlDLHPDDIYWC 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  662 TGSISFDAVTFE-MFGALLNGASLHIIDKStmLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFR-----GLHTLY 735
Cdd:cd05969   136 TADPGWVTGTVYgIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARkydlsSLRFIH 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  736 VGGEALSPalmNAVR--HACPDLALHNIYGPTENTTFstffeMKRDYAG----PIPIGKPISNSTAYILDTKGRLLPIGV 809
Cdd:cd05969   214 SVGEPLNP---EAIRwgMEVFGVPIHDTWWQTETGSI-----MIANYPCmpikPGSMGKPLPGVKAAVVDENGNELPPGT 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  810 PGELCVGGD--GVAKGYLN---RVDLTnavfsphpFLPGerIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIE 884
Cdd:cd05969   286 KGILALKPGwpSMFRGIWNdeeRYKNS--------FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  885 ARLLEMEGVQEAAVTLREKDGEAQLYTHYVG---DHKKTDtDFRADL---ARV-LPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd05969   356 SALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkeGFEPSD-ELKEEIinfVRQkLGAHVAPREIEFVDNLPKTRSGKIMR 434


                  ...
gi 499188982  958 SAL 960
Cdd:cd05969   435 RVL 437
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 486-959 6.02e-32

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


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 132.36  E-value: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVY------GNMSISYKELDKRSNALARELIQKGfRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAE 559
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPP---ERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEEND-IPINISSS-------PDDLAYIMYTSGST 628
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDlLPDTSAADwpppspdPDDIAYLQYTSGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  629 GRPKGVMITNRNVVSLVRnsNYTSASGDDRFIMTGS----------ISFdavtfeMFGALLNGASLHIIDKSTMLT-PDR 697
Cdd:cd05931   162 GTPKGVVVTHRNLLANVR--QIRRAYGLDPGDVVVSwlplyhdmglIGG------LLTPLYSGGPSVLMSPAAFLRrPLR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  698 FGAYLLENDITVlfltTALFN---QLAQVR---ADMfRGL-----HTLYVGGEALSPALMNA-----VRHACPDLALHNI 761
Cdd:cd05931   234 WLRLISRYRATI----SAAPNfayDLCVRRvrdEDL-EGLdlsswRVALNGAEPVRPATLRRfaeafAPFGFRPEAFRPS 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  762 YGPTENTTFSTF-----------FEMKRDYAGPIPI-------------GKPISNSTAYILDTKG-RLLPIGVPGELCVG 816
Cdd:cd05931   309 YGLAEATLFVSGgppgtgpvvlrVDRDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDPETgRELPDGEVGEIWVR 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  817 GDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARwLPDGNLeYIS-RIDRQMKIRGKRIEPAEIEARLLEMEGVQE 895
Cdd:cd05931   389 GPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGEL-YITgRLKDLIIVRGRNHYPQDIEATAEEAHPALR 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  896 ----AAVTLREKDGE-----AQLYTHYVG-DHKKTDTDFRADLARvlpdymipQHWVRVER--------MPLTGNGKIDR 957
Cdd:cd05931   467 pgcvAAFSVPDDGEErlvvvAEVERGADPaDLAAIAAAIRAAVAR--------EHGVAPADvvlvrpgsIPRTSSGKIQR 538


                  ..
gi 499188982  958 SA 959
Cdd:cd05931   539 RA 540
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 502-899 8.53e-32

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: 131.95  E-value: 8.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETA--GILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV 579
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPAPASfvGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  580 QKGLEqnaAFSgtciISDAQGLMEENDIPiNISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRF 659
Cdd:cd05927    86 DAGVK---VYS----LEEFEKLGKKNKVP-PPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKIN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  660 IMTGSIS-------FDAVTFEMFgaLLNGASL--------HIIDKSTMLTP----------DRFGAYLLENDITVLFLTT 714
Cdd:cd05927   158 PTDVYISylplahiFERVVEALF--LYHGAKIgfysgdirLLLDDIKALKPtvfpgvprvlNRIYDKIFNKVQAKGPLKR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  715 ALFN-----QLAQVRA------------------DMFRG-LHTLYVGGEALSPALMNAVRhACPDLALHNIYGPTEnTTF 770
Cdd:cd05927   236 KLFNfalnyKLAELRSgvvraspfwdklvfnkikQALGGnVRLMLTGSAPLSPEVLEFLR-VALGCPVLEGYGQTE-CTA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  771 STFFEMKRDYA-----GPIP------IGKPISNSTAyiLDTKGRllpigvpGELCVGGDGVAKGYLNRVDLTNAVFSPHP 839
Cdd:cd05927   314 GATLTLPGDTSvghvgGPLPcaevklVDVPEMNYDA--KDPNPR-------GEVCIRGPNVFSGYYKDPEKTAEALDEDG 384

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  840 FLpgeriyRTGDLARWLPDGNLeyiSRIDRQMKI----RGKRIEPAEIEARLLEMEGVQEAAVT 899
Cdd:cd05927   385 WL------HTGDIGEWLPNGTL---KIIDRKKNIfklsQGEYVAPEKIENIYARSPFVAQIFVY 439
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 473-960 7.40e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 129.09  E-value: 7.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGA 552
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  553 YLPLDAELPPERVSFMLEETQAKMLIVQ---KGLEQNAAFSG--------------TCIISDA--------------QGL 601
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVWpgfKGIDFAAILAAvppdalpplraiavVDDAADAtpapapgarvqlfaLPD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  602 MEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFI-----MTGSISFDAVtfemFG 676
Cdd:PRK06164  167 PAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLlaalpFCGVFGFSTL----LG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  677 ALLNGASLHIIDkstMLTPDRFGAYLLENDITVLFLTTALFNQLAQ---VRADMfrgLHTLYVGGEALSPALMNAVRHAC 753
Cdd:PRK06164  243 ALAGGAPLVCEP---VFDAARTARALRRHRVTHTFGNDEMLRRILDtagERADF---PSARLFGFASFAPALGELAALAR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  754 P-DLALHNIYGPTENTTFSTFFEMKRDYAGPI-PIGKPIS-NSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVD 829
Cdd:PRK06164  317 ArGVPLTGLYGSSEVQALVALQPATDPVSVRIeGGGRPASpEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPD 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  830 LTNAVFSPHPFlpgeriYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQL 909
Cdd:PRK06164  397 ATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVP 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  910 YTHYV-GDHKKTD-TDFRADLARVLPDYMIPQHWVRVERMPLT--GNG-KIDRSAL 960
Cdd:PRK06164  471 VAFVIpTDGASPDeAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 486-960 1.67e-30

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 127.97  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:PRK07786   27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLIVQKGLEQNAA-------FSGTCIISDAQG---------LMEENDIPINISSSPDDL-AYIMYTSGST 628
Cdd:PRK07786  107 AFLVSDCGAHVVVTEAALAPVATavrdivpLLSTVVVAGGSSddsvlgyedLLAEAGPAHAPVDIPNDSpALIMYTSGTT 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  629 GRPKGVMITNRNVVSLVRNSNYTSasgddRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPdrFGAY------- 701
Cdd:PRK07786  187 GRPKGAVLTHANLTGQAMTCLRTN-----GADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYP--LGAFdpgqlld 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  702 -LLENDITVLFLTTA-----LFNQLAQVRAdmfRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFSTFFE 775
Cdd:PRK07786  260 vLEAEKVTGIFLVPAqwqavCAEQQARPRD---LALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  776 MKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGDLARW 855
Cdd:PRK07786  337 GEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDLVRQ 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  856 LPDGnleYISRIDRQ--MKIR-GKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGEAQLYTHYV--GDHKKTDTDFRADL 928
Cdd:PRK07786  410 DEEG---YVWVVDRKkdMIISgGENIYCAEVENVLASHPDIVEVAVIGRadEKWGEVPVAVAAVrnDDAALTLEDLAEFL 486

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499188982  929 ARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK07786  487 TDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 493-960 4.61e-30

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: 124.90  E-value: 4.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  493 TALVYGNMSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGG---AYLPLdaeLPPERVSFM 568
Cdd:cd05958     2 TCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAiavATMPL---LRPKELAYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  569 LEETQ-AKMLIVQKgleqnaafsgtciisdaqglmeendipiniSSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVR- 646
Cdd:cd05958    79 LDKARiTVALCAHA------------------------------LTASDDICILAFTSGTTGAPKATMHFHRDPLASADr 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  647 -NSNYTSASGDDRFIMTGSISFdavTFEMFGALL----NGASLHIIDKStmlTPDRFGAYLLENDITVLF-LTTALFNQL 720
Cdd:cd05958   129 yAVNVLRLREDDRFVGSPPLAF---TFGLGGVLLfpfgVGASGVLLEEA---TPDLLLSAIARYKPTVLFtAPTAYRAML 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  721 AQVRAD--MFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIyGPTENttFSTFFEMKRDYAGPIPIGKPISNSTAYIL 798
Cdd:cd05958   203 AHPDAAgpDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGI-GSTEM--FHIFISARPGDARPGATGKPVPGYEAKVV 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  799 DTKGRLLPIGVPGELCVGGDGVAKGylnrvdltNAVFSPHPFLPGERIYrTGDLARWLPDGNLEYISRIDRQMKIRGKRI 878
Cdd:cd05958   280 DDEGNPVPDGTIGRLAVRGPTGCRY--------LADKRQRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNI 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  879 EPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVgdHKKTDTDFRADLARVLPD--------YMIPQHWVRVERMPLT 950
Cdd:cd05958   351 APPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFV--VLRPGVIPGPVLARELQDhakahiapYKYPRAIEFVTELPRT 428

                         490
                  ....*....|
gi 499188982  951 GNGKIDRSAL 960
Cdd:cd05958   429 ATGKLQRFAL 438
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 495-957 8.11e-30

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: 124.86  E-value: 8.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  495 LVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQA 574
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  575 KMLIVqkgleqnaafsgtciisdaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSA 653
Cdd:cd05914    81 KAIFV---------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGvKEVVLL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  654 SGDDRFIMTGSISFD-AVTFEMFGALLNGASLHIIDKstmLTPDRFGAyLLENDITVLFLT-----------TALFNQLA 721
Cdd:cd05914   128 GKGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDK---IPSAKIIA-LAFAQVTPTLGVpvplviekifkMDIIPKLT 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  722 ---------------QVRADMFRGLHTLY--------VGGEALSPALMNAVRHACPDLALHniYGPTENT---TFSTFFE 775
Cdd:cd05914   204 lkkfkfklakkinnrKIRKLAFKKVHEAFggnikefvIGGAKINPDVEEFLRTIGFPYTIG--YGMTETApiiSYSPPNR 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  776 MKRDYAGpipigKPISNSTAYILDTKgrllPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARW 855
Cdd:cd05914   282 IRLGSAG-----KVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWF------HTGDLGKI 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  856 LPDGNLeYISRIDRQMKI--RGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGD---HKKTDTDF------ 924
Cdd:cd05914   347 DAEGYL-YIRGRKKEMIVlsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLdvkALKQRNIIdaikwe 425

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 499188982  925 -RADLARVLPDY-MIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd05914   426 vRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 466-960 1.43e-29

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


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 125.30  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  466 NNTKTEYPKN----HTIIDLFreqAEKTPDHTALV----YGNMSI-SYKELDKRSNALARELIQKGFRKNETAGILAAHS 536
Cdd:cd05970     6 NNFSINVPENfnfaYDVVDAM---AKEYPDKLALVwcddAGEERIfTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  537 PEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI------VQKGLEQNAAFSGT------CIISDAQGLME- 603
Cdd:cd05970    83 YEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVaiaednIPEEIEKAAPECPSkpklvwVGDPVPEGWIDf 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  604 ----ENDIPI------NISSSPDDLAYIMYTSGSTGRPKgvMITNRNVVSL---VRNSNYTSASGDDRFIMTGSISF-DA 669
Cdd:cd05970   163 rkliKNASPDferptaNSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLghiVTAKYWQNVREGGLHLTVADTGWgKA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  670 VTFEMFGALLNGASLHIIDKStMLTPDRFGAYLLENDITVLFLTTALFNQLaqVRADM----FRGLHTLYVGGEALSPAL 745
Cdd:cd05970   241 VWGKIYGQWIAGAAVFVYDYD-KFDPKALLEKLSKYGVTTFCAPPTIYRFL--IREDLsrydLSSLRYCTTAGEALNPEV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  746 MNAVRHACpDLALHNIYGPTENT-TFSTFFEMKrdyAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGD-----G 819
Cdd:cd05970   318 FNTFKEKT-GIKLMEGFGQTETTlTIATFPWME---PKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  820 VAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT 899
Cdd:cd05970   394 LFGGYYKDAEKTAEVWH-------DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  900 -----LR----------EKDGEA-QLYTHYVGDHKKtdtdfradlaRVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05970   467 gvpdpIRgqvvkativlAKGYEPsEELKKELQDHVK----------KVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 486-955 3.91e-29

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 123.92  E-value: 3.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPER 564
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  565 VSFMLEETQAKMLIV-QKGLEQNAAFSGT----CII----SDA-------------------QGLMEENDIPIN------ 610
Cdd:PRK08314  100 LAHYVTDSGARVAIVgSELAPKVAPAVGNlrlrHVIvaqySDYlpaepeiavpawlraepplQALAPGGVVAWKealaag 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  611 -----ISSSPDDLAYIMYTSGSTGRPKGVMITNR----NVVSLVRNSNYTSASgddrfIMTGSISFDAVT---FEMFGAL 678
Cdd:PRK08314  180 lapppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWSNSTPES-----VVLAVLPLFHVTgmvHSMNAPI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  679 LNGASLHIidkstMLTPDRFGAYLLENDITVLFLT---TALFNQLAQVRADMFrGLHTL-YV--GGEALSPALMNAVRHA 752
Cdd:PRK08314  255 YAGATVVL-----MPRWDREAAARLIERYRVTHWTnipTMVVDFLASPGLAER-DLSSLrYIggGGAAMPEAVAERLKEL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 CpDLALHNIYGPTENTTFSTFFEMKRdyagpiP----IGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNR 827
Cdd:PRK08314  329 T-GLDYVEGYGLTETMAQTHSNPPDR------PklqcLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNR 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  828 VDLTNAVFSPhpfLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV--TLREKDG 905
Cdd:PRK08314  402 PEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACViaTPDPRRG 478

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  906 EAQ-----LYTHYVGdhkKTDTDFRADLAR-VLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:PRK08314  479 ETVkavvvLRPEARG---KTTEEEIIAWAReHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 476-956 5.39e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 123.46  E-value: 5.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGA--- 552
Cdd:PRK07798    3 WNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVpvn 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  553 -----------YLPLDAELPP--------ERVSFMLEET-QAKMLIVQKGLEQNAAFSGTciISDAQGLMEENDIPINIS 612
Cdd:PRK07798   83 vnyryvedelrYLLDDSDAVAlvyerefaPRVAEVLPRLpKLRTLVVVEDGSGNDLLPGA--VDYEDALAAGSPERDFGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  613 SSPDDLaYIMYTSGSTGRPKGVM----------------ITNRNVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFG 676
Cdd:PRK07798  161 RSPDDL-YLLYTGGTTGMPKGVMwrqedifrvllggrdfATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  677 ALLNGASLHIIDKSTmLTPDRFGAYLLENDITVLFLT-TALFNQLAQVRADMFRG-LHTLYV---GGEALSPALMNAVRH 751
Cdd:PRK07798  240 ALFSGQTVVLLPDVR-FDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYdLSSLFAiasGGALFSPSVKEALLE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  752 ACPDLALHNIYGPTEntTFSTFFEMKRDyaGPIPIGKP---ISNSTAYILDTKGRLLP-IGVPGELCVGGDgVAKGYLNR 827
Cdd:PRK07798  319 LLPNVVLTDSIGSSE--TGFGGSGTVAK--GAVHTGGPrftIGPRTVVLDEDGNPVEPgSGEIGWIARRGH-IPLGYYKD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  828 VDLTNAVFsphPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLR--EKDG 905
Cdd:PRK07798  394 PEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVpdERWG 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  906 EA-----QLYthyvGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK07798  471 QEvvavvQLR----EGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 502-1008 1.02e-28

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: 121.31  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVqk 581
Cdd:cd17640     6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqnaafsgtciisdaqglmeENDipinisssPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFI 660
Cdd:cd17640    84 ----------------------END--------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSlSDIVPPQPGDRFL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 mtgSI-----SFDAVtFEMFgALLNGASLHIIDKSTMLTpD--RFGAYLLendITVLFLTTALFNQL-AQVRADMF---R 729
Cdd:cd17640   134 ---SIlpiwhSYERS-AEYF-IFACGCSQAYTSIRTLKD-DlkRVKPHYI---VSVPRLWESLYSGIqKQVSKSSPikqF 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  730 GLHTLYVGGE---------ALSPAL---MNAVrhacpDLALHNIYGPTENTTFSTFFEMKRDYAGpiPIGKPISNSTAYI 797
Cdd:cd17640   205 LFLFFLSGGIfkfgisgggALPPHVdtfFEAI-----GIEVLNGYGLTETSPVVSARRLKCNVRG--SVGRPLPGTEIKI 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGR-LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIR-G 875
Cdd:cd17640   278 VDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRAKDTIVLSnG 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  876 KRIEPAEIEARLLEMEGVQEAAVtlrekdgeaqlythyVGDHKKTdtdfradL-ARVLPDYMIPQHWVRvermplTGNGK 954
Cdd:cd17640   352 ENVEPQPIEEALMRSPFIEQIMV---------------VGQDQKR-------LgALIVPNFEELEKWAK------ESGVK 403

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  955 IDRSALPIPENKP--AKRQNIIlprnLVEEELANIWKQVLGVNTISIDDDFFAIGG 1008
Cdd:cd17640   404 LANDRSQLLASKKvlKLYKNEI----KDEISNRPGFKSFEQIAPFALLEEPFIENG 455
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 615-957 1.40e-28

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: 118.53  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSlvrNSNYTS----ASGDDRFIMTGSIsfdavtFEMFG-------ALLNGAs 683
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVN---NGYFIGerlgLTEQDRLCIPVPL------FHCFGsvlgvlaCLTHGA- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  684 lhiidksTMLTPDR-FGAYLLENDI-----TVLFLTTALF-NQLAQVRADMFrGLHTLYVG---GEALSPALMNAVRHAC 753
Cdd:cd05917    71 -------TMVFPSPsFDPLAVLEAIekekcTALHGVPTMFiAELEHPDFDKF-DLSSLRTGimaGAPCPPELMKRVIEVM 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  754 PDLALHNIYGPTENTTFSTffeMKRDYAGPI----PIGKPISNSTAYILDTKGR-LLPIGVPGELCVGGDGVAKGYLNRV 828
Cdd:cd05917   143 NMKDVTIAYGMTETSPVST---QTRTDDSIEkrvnTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  829 DLTNAVFSphpflpGERIYRTGDLARWLPDGNLEYISRIdRQMKIRG-KRIEPAEIEARLLEMEGVQEAAV--TLREKDG 905
Cdd:cd05917   220 EKTAEAID------GDGWLHTGDLAVMDEDGYCRIVGRI-KDMIIRGgENIYPREIEEFLHTHPKVSDVQVvgVPDERYG 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  906 EA-----QLYTHyvgdHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd05917   293 EEvcawiRLKEG----AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 488-960 2.33e-28

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


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 121.48  E-value: 2.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  488 KTPDHTALV--YGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL-----DAEL 560
Cdd:cd17642    29 SVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTndiynEREL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  561 ------PPERVSFMLEETQAKMLIVQKGLEqnaaFSGTCII----SDAQGLMEEN-----DIPINISSSP---------D 616
Cdd:cd17642   109 dhslniSKPTIVFCSKKGLQKVLNVQKKLK----IIKTIIIldskEDYKGYQCLYtfitqNLPPGFNEYDfkppsfdrdE 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVV---SLVRNSNYTSASGDDRFIMTGSISFDAvtFEMF---GALLNGASLHIIDKs 690
Cdd:cd17642   185 QVALIMNSSGSTGLPKGVQLTHKNIVarfSHARDPIFGNQIIPDTAILTVIPFHHG--FGMFttlGYLICGFRVVLMYK- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  691 tmLTPDRFGAYLLENDITVLFLTTALFNQLAQ---VRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEN 767
Cdd:cd17642   262 --FEEELFLRSLQDYKVQSALLVPTLFAFFAKstlVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTET 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 TtfSTFFEMKRDYAGPIPIGKPISNSTAYILD-TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeri 846
Cdd:cd17642   340 T--SAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWL----- 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  847 yRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHY-VGDHKKTDTDfr 925
Cdd:cd17642   413 -HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVvVLEAGKTMTE-- 489

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 499188982  926 ADLARVLPDYMIPQHWVR-----VERMPLTGNGKIDRSAL 960
Cdd:cd17642   490 KEVMDYVASQVSTAKRLRggvkfVDEVPKGLTGKIDRRKI 529
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 473-960 5.77e-28

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 120.25  E-value: 5.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGA 552
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  553 YLPLDAELPPERVSFMLEETQAKMLIVQKGL--------EQNAAFSGTCIISDAQGL----------MEENDIPINISS- 613
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVVEAALlaaleaadPGDLPLPAVWLLDAPASVsvpagwstapLPPLDAPAPAAAv 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMF-GALLNGASLHIIDKstm 692
Cdd:PRK06155  178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFfQALLAGATYVLEPR--- 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTPDRFGAYLLENDITVLFLTTALFNQL-AQVRADMFRGlHTLYVG-GEALSPALMNAVRHACpDLALHNIYGPTEnTTF 770
Cdd:PRK06155  255 FSASGFWPAVRRHGATVTYLLGAMVSILlSQPARESDRA-HRVRVAlGPGVPAALHAAFRERF-GVDLLDGYGSTE-TNF 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  771 StfFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGD---GVAKGYLNRVDLTNAVFSPHPFLPGERIY 847
Cdd:PRK06155  332 V--IAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVV 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  848 RTgdlarwlPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV-----TLREKDGEAQlythyVGDHKKTDT 922
Cdd:PRK06155  410 RD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfpvpsELGEDEVMAA-----VVLRDGTAL 477

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 499188982  923 DFrADLARV----LPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06155  478 EP-VALVRHceprLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 617-957 6.11e-28

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


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 115.97  E-value: 6.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRN-VVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIidkSTMLTP 695
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  696 DRFGAYLLENDITVLFLTTALFNQLAQVRADMFRgLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEnTTFSTFfE 775
Cdd:cd17633    78 KSWIRKINQYNATVIYLVPTMLQALARTLEPESK-IKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSE-LSFITY-N 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  776 MKRDYAGPIPIGKPISNSTAYILDTKGrllpiGVPGELCVGGDGVAKGYLnrvdlTNAVFSPHPFlpgeriYRTGDLARW 855
Cdd:cd17633   155 FNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV-----RGGFSNPDGW------MSVGDIGYV 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  856 LPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT--LREKDGEAQLYThYVGDhKKTDTDFRADLARVLP 933
Cdd:cd17633   219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgiPDARFGEIAVAL-YSGD-KLTYKQLKRFLKQKLS 296

                         330       340
                  ....*....|....*....|....
gi 499188982  934 DYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd17633   297 RYEIPKKIIFVDSLPYTSSGKIAR 320
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 475-960 1.77e-27

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 119.00  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  475 NHTIIDLFREQAEKTPDHTALV-YGNMS-----ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLK 548
Cdd:PRK13295   23 DRTINDDLDACVASCPDKTAVTaVRLGTgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AGGAYLPLdaelPP---ER-VSFMLEETQAKMLIVQK-------------------GLEQNAAFSGTCIISDAQGLME-- 603
Cdd:PRK13295  103 IGAVLNPL----MPifrEReLSFMLKHAESKVLVVPKtfrgfdhaamarrlrpelpALRHVVVVGGDGADSFEALLITpa 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  604 ---ENDIPINISSS---PDDLAYIMYTSGSTGRPKGVMITNRNVVSlvRNSNYTSASGddrfIMTGSISFDAVTFEMFGA 677
Cdd:PRK13295  179 weqEPDAPAILARLrpgPDDVTQLIYTSGTTGEPKGVMHTANTLMA--NIVPYAERLG----LGADDVILMASPMAHQTG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  678 LLNGASLHIIDKSTML-----TPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYV---GGEALSPALmnaV 749
Cdd:PRK13295  253 FMYGLMMPVMLGATAVlqdiwDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTflcAGAPIPGAL---V 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  750 RHACPDLALH--NIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNR 827
Cdd:PRK13295  330 ERARAALGAKivSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  828 VDLTNAVFsphpflpgERIYRTGDLARWLPDGnleYIsRIDRQMK---IRG-KRIEPAEIEARLLEMEGVQEAAVTL--R 901
Cdd:PRK13295  410 PQLNGTDA--------DGWFDTGDLARIDADG---YI-RISGRSKdviIRGgENIPVVEIEALLYRHPAIAQVAIVAypD 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  902 EKDGEAQlyTHYVGDHKKTDTDFRA-----DLARVLPDYmIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK13295  478 ERLGERA--CAFVVPRPGQSLDFEEmveflKAQKVAKQY-IPERLVVRDALPRTPSGKIQKFRL 538
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
472-960 1.12e-26

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 116.39  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  472 YPKNHTIIDLFREQAEKTPDHTALV--YGNmSISYKELDKRSNALARELIQKGFrknETAGILAAHSP---EFMISVLAV 546
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVVdnHGA-SYTYSALDHAASRLANWLLAKGI---EPGDRVAFQLPgwcEFTIIYLAC 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  547 LKAGGAYLPLDAELPPERVSFMLEETQAKMLI-----------------------------VQKGLEQNAAFSGTCIISD 597
Cdd:PRK06087   95 LKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlfkqtrpvdlilplqnqlpqlqqivgVDKLAPATSSLSLSQIIAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  598 AQGLMEendiPINISSspDDLAYIMYTSGSTGRPKGVMITNRNVV----SLVRNSNYTSasgDDRFIMTGSIS-----FD 668
Cdd:PRK06087  175 YEPLTT----AITTHG--DELAAVLFTSGTEGLPKGVMLTHNNILaserAYCARLNLTW---QDVFMMPAPLGhatgfLH 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  669 AVTFEMfgalLNGASLHIIDKstmLTPDRFGAYLLENDIT-VLFLTTALFNQLAQVRADMFRgLHTL--YVGGEALSPAl 745
Cdd:PRK06087  246 GVTAPF----LIGARSVLLDI---FTPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPAD-LSALrfFLCGGTTIPK- 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  746 mNAVRHACP-DLALHNIYGPTENTTFSTffemkrdyagpIPIGKPIS-----NSTAY------ILDTKGRLLPIGVPGEL 813
Cdd:PRK06087  317 -KVARECQQrGIKLLSVYGSTESSPHAV-----------VNLDDPLSrfmhtDGYAAagveikVVDEARKTLPPGCEGEE 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  814 CVGGDGVAKGYLNRVDLTNAVfsphpfLPGERIYRTGDLARWLPDGNLEYISRiDRQMKIR-GKRIEPAEIEARLLEMEG 892
Cdd:PRK06087  385 ASRGPNVFMGYLDEPELTARA------LDEEGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPK 457

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  893 VQEAAVTLR--EKDGE-----AQLYTHYvgdHKKTDTDFRADLARV-LPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06087  458 IHDACVVAMpdERLGErscayVVLKAPH---HSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 614-960 1.41e-26

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


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 115.51  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFImtGSISFdavtFEMFG-------ALLNGasLH 685
Cdd:cd05909   145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQiTAIFDPNPEDVVF--GALPF----FHSFGltgclwlPLLSG--IK 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  686 IIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQ-VRADMFRGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGP 764
Cdd:cd05909   217 VVFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARaAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGT 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  765 TE-------NTTFSTFFEMKrdyagpipIGKPISNSTAYILDTKGRL-LPIGVPGELCVGGDGVAKGYLNRVDLTNavfs 836
Cdd:cd05909   296 TEcspvisvNTPQSPNKEGT--------VGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTS---- 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  837 phpFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQ-EAAVTLR--EKDGEAQ--LYT 911
Cdd:cd05909   364 ---FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVpdGRKGEKIvlLTT 440

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499188982  912 HYVGDhkktdtdfRADLARVL-----PDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05909   441 TTDTD--------PSSLNDILknagiSNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 491-898 3.41e-26

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 114.99  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  491 DHTALVY----GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVS 566
Cdd:PRK04319   59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  567 FMLEETQAKMLIVQKGLEQ------------------NAAFSGTCIisDAQGLMEENDIPINIS-SSPDDLAYIMYTSGS 627
Cdd:PRK04319  139 DRLEDSEAKVLITTPALLErkpaddlpslkhvllvgeDVEEGPGTL--DFNALMEQASDEFDIEwTDREDGAILHYTSGS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  628 TGRPKGVM----------ITNRNVVSLvrnsnytsaSGDDRFIMTGsisfDA--VT---FEMFGALLNGASLhIIDKSTM 692
Cdd:PRK04319  217 TGKPKGVLhvhnamlqhyQTGKYVLDL---------HEDDVYWCTA----DPgwVTgtsYGIFAPWLNGATN-VIDGGRF 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 lTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGL------HTLYVGgEALSPalmNAVR--HACPDLALHNIYGP 764
Cdd:PRK04319  283 -SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYdlsslrHILSVG-EPLNP---EVVRwgMKVFGLPIHDNWWM 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  765 TEnttfsTFFEMKRDYAG----PIPIGKPISNSTAYILDTKGRLLPIGVPGELCV--GGDGVAKGYLNrvdltNAVFSPH 838
Cdd:PRK04319  358 TE-----TGGIMIANYPAmdikPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWN-----NPEKYES 427

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  839 PFLPGerIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK04319  428 YFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 477-960 1.92e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 111.79  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGfRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQ--GLMEEN-DIPINISSSPDDLAYIMYTSGSTGRPKG 633
Cdd:PRK07638   81 DIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkRMIEKYlPTYAPIENVQNAPFYMGFTSGSTGKPKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  634 VMITNRN-VVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFL 712
Cdd:PRK07638  161 FLRAQQSwLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  713 TTALFNQLaqVRADMFR-GLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEnTTFSTFFEMKRDYAGPIPIGKPIS 791
Cdd:PRK07638  238 VPTMLESL--YKENRVIeNKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE-LSFVTALVDEESERRPNSVGRPFH 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  792 NSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTnavfsphPFLPGERIYRTGDLARWLPDGNLeYISRIDRQM 871
Cdd:PRK07638  315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLA-------RELNADGWMTVRDVGYEDEEGFI-YIVGREKNM 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  872 KIRGK-RIEPAEIEARLLEMEGVQEAAVTLREKD--GE-AQLYTHYVGDHKKtdtdFRADLARVLPDYMIPQHWVRVERM 947
Cdd:PRK07638  387 ILFGGiNIFPEEIESVLHEHPAVDEIVVIGVPDSywGEkPVAIIKGSATKQQ----LKSFCLQRLSSFKIPKEWHFVDEI 462

                         490
                  ....*....|...
gi 499188982  948 PLTGNGKIDRSAL 960
Cdd:PRK07638  463 PYTNSGKIARMEA 475
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 490-955 2.01e-25

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: 113.06  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVY-GNM-----SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:cd17634    67 GDRTAIIYeGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLI-----------------VQKGLEQNAAFSGTCIISDAQG---------------LM-----EEND 606
Cdd:cd17634   147 AVAGRIIDSSSRLLItadggvragrsvplkknVDDALNPNVTSVEHVIVLKRTGsdidwqegrdlwwrdLIakaspEHQP 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  607 IPINisssPDDLAYIMYTSGSTGRPKGVMITN-----------RNVVSLVRNSNYTSASgDDRFIMTGSisfdavtFEMF 675
Cdd:cd17634   227 EAMN----AEDPLFILYTSGTTGKPKGVLHTTggylvyaattmKYVFDYGPGDIYWCTA-DVGWVTGHS-------YLLY 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  676 GALLNGASLHIID-KSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRG-----LHTLYVGGEALSP-ALMNA 748
Cdd:cd17634   295 GPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrssLRILGSVGEPINPeAYEWY 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  749 VRH----ACPdlaLHNIYGPTENttfSTFFEMKRDYAGPIPIG---KPISNSTAYILDTKGRLLPIGVPGELCVGGD--G 819
Cdd:cd17634   375 WKKigkeKCP---VVDTWWQTET---GGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpG 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  820 VAKGYLNRVDLTNAVFsphpFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT 899
Cdd:cd17634   449 QTRTLFGDHERFEQTY----FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVV 524

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499188982  900 -LREKDGEAQLYTHYVGDHKKTDTD-----FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:cd17634   525 gIPHAIKGQAPYAYVVLNHGVEPSPelyaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 481-955 2.06e-25

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 112.06  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  481 LFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAEL 560
Cdd:PRK07470   12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  561 PPERVSFMLEETQAKMLIVQKGLEQNAA--------FSGTCIISDAQG------LMEEN--DIPINISSSPDDLAYIMYT 624
Cdd:PRK07470   92 TPDEVAYLAEASGARAMICHADFPEHAAavraaspdLTHVVAIGGARAgldyeaLVARHlgARVANAAVDHDDPCWFFFT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  625 SGSTGRPKGVMITNRNVVSLVRNSNytsasGDdrfIMTGSISFDA--VTfemfGALLNGASLHII------DKSTMLTPD 696
Cdd:PRK07470  172 SGTTGRPKAAVLTHGQMAFVITNHL-----AD---LMPGTTEQDAslVV----APLSHGAGIHQLcqvargAATVLLPSE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGA---------YLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYVGgealSPALMNAVRHACPDLA--LHNIYGPT 765
Cdd:PRK07470  240 RFDPaevwalverHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG----APMYRADQKRALAKLGkvLVQYFGLG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  766 ENTTFSTFFEMKRDYAGPIP------IGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHP 839
Cdd:PRK07470  316 EVTGNITVLPPALHDAEDGPdarigtCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGW 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  840 FlpgeriyRTGDLARWLPDGNLeYISRIDRQMKIR-GKRIEPAEIEARLLEMEGVQEAAVtLREKD---GEaqlythyVG 915
Cdd:PRK07470  396 F-------RTGDLGHLDARGFL-YITGRASDMYISgGSNVYPREIEEKLLTHPAVSEVAV-LGVPDpvwGE-------VG 459

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 499188982  916 --------DHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:PRK07470  460 vavcvardGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 474-957 4.71e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 111.40  E-value: 4.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  474 KNHTIIDLFREQAEKTPDHTALVYGNMSI--SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGG 551
Cdd:PRK12583   16 LTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  552 AYLPLDAELPPERVSFMLEETQAKMLI----------------VQKGLEQNAAFSGTC---------------------- 593
Cdd:PRK12583   96 ILVNINPAYRASELEYALGQSGVRWVIcadafktsdyhamlqeLLPGLAEGQPGALACerlpelrgvvslapapppgfla 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  594 ---IISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVslvrNSNYTSA-----SGDDRFIMTGSI 665
Cdd:PRK12583  176 wheLQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIL----NNGYFVAeslglTEHDRLCVPVPL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  666 sfdavtFEMFGALLngASLHIIDK-STMLTP-DRFGAYLL-----ENDITVLF-LTTALFNQLAQVRADMFrGLHTLYVG 737
Cdd:PRK12583  252 ------YHCFGMVL--ANLGCMTVgACLVYPnEAFDPLATlqaveEERCTALYgVPTMFIAELDHPQRGNF-DLSSLRTG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  738 GEALSPALMNAVRHACPDLALHNI---YGPTENTTFSTffemKRDYAGPIP-----IGKPISNSTAYILDTKGRLLPIGV 809
Cdd:PRK12583  323 IMAGAPCPIEVMRRVMDEMHMAEVqiaYGMTETSPVSL----QTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  810 PGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIdRQMKIR-GKRIEPAEIEARLL 888
Cdd:PRK12583  399 IGELCTRGYSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRS-KDMIIRgGENIYPREIEEFLF 471

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  889 EMEGVQEAAV--TLREKDGE---AQLYTHyvGDHKKTDTDFRaDLARV-LPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:PRK12583  472 THPAVADVQVfgVPDEKYGEeivAWVRLH--PGHAASEEELR-EFCKArIAHFKVPRYFRFVDEFPMTVTGKVQK 543
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 476-960 7.12e-25

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: 110.83  E-value: 7.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVYGNMS----ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGG 551
Cdd:cd05906    10 RTLLELLLRAAERGPTKGITYIDADGseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  552 AYLPL----------DAELPPERVSFMLEE----TQAKM---LIVQKGLEQNAAFSGTcIISDAQGLMEENDIPInisSS 614
Cdd:cd05906    90 VPAPLtvpptydepnARLRKLRHIWQLLGSpvvlTDAELvaeFAGLETLSGLPGIRVL-SIEELLDTAADHDLPQ---SR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDrfimtgSISFDAVTFEMFGALLNgasLHIID------ 688
Cdd:cd05906   166 PDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ------DVFLNWVPLDHVGGLVE---LHLRAvylgcq 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  689 -----KSTMLT-PDRFGAYLLENDITVLF---LTTALFNQLAQVRADM---FRGLHTLYVGGEALSPALMNAV-----RH 751
Cdd:cd05906   237 qvhvpTEEILAdPLRWLDLIDRYRVTITWapnFAFALLNDLLEEIEDGtwdLSSLRYLVNAGEAVVAKTIRRLlrllePY 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  752 ACPDLALHNIYGPTEntTFSTFFEMKRDYAGPIP-------IGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGY 824
Cdd:cd05906   317 GLPPDAIRPAFGMTE--TCSGVIYSRSFPTYDHSqalefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  825 LNRVDLTNAVFSPHPFlpgeriYRTGDLArWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQE---AAVTLR 901
Cdd:cd05906   395 YNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVR 467

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  902 EKDGEA-QLYTHYV------GDHKKTDTDFRADLAR---VLPDYMIPqhwVRVERMPLTGNGKIDRSAL 960
Cdd:cd05906   468 DPGAETeELAIFFVpeydlqDALSETLRAIRSVVSRevgVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 65-336 7.29e-25

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


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 109.05  E-value: 7.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   65 IDRHDIFRTVFlPHVPHlsGPRQVVMTEREFHLnseDISHLPTN--DQNEYIERFKEKdkqkGFDLQKDMLMRISLFKTA 142
Cdd:cd19540    49 VARHESLRTVF-PEDDG--GPYQVVLPAAEARP---DLTVVDVTedELAARLAEAARR----GFDLTAELPLRARLFRLG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  143 KDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHAGK-----PLsldPVRpYSTYISWL-----TNRDKEKAAA----Y 208
Cdd:cd19540   119 PDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRapdwaPL---PVQ-YADYALWQrellgDEDDPDSLAArqlaY 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  209 WDTYLKnySAPSPL--------PRVSdketkeSYHREDLIFSLNKPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRT 280
Cdd:cd19540   195 WRETLA--GLPEELelptdrprPAVA------SYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAG 266

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  281 DDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEA 336
Cdd:cd19540   267 DDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 783-1046 1.49e-24

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 105.60  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  783 PIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLE 862
Cdd:COG3433    19 VIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  863 YISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWV 942
Cdd:COG3433    99 LERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  943 RVERMPLTGNGKIDRSALPIPENKPAKRQN----IILPRNLVEEELANIWKQVLGV--NTISIDDDFFAIGGHSLRALQV 1016
Cdd:COG3433   179 VALDALLLLALKVVARAAPALAAAEALLAAaspaPALETALTEEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQL 258

                         250       260       270
                  ....*....|....*....|....*....|
gi 499188982 1017 IHTLKhQQNIDIPIDFLFEHPTIAQLAEKL 1046
Cdd:COG3433   259 VERWR-KAGLDVSFADLAEHPTLAAWWALL 287
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 503-960 2.09e-24

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


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 108.87  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQKG 582
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 LEQ-NAAFSGTC------IISDAQGLMEENDIPINIS-------SSPD---------DLAYIMYTSGSTGRPKGVMITNR 639
Cdd:cd12119   107 FLPlLEAIAPRLptvehvVVMTDDAAMPEPAGVGVLAyeellaaESPEydwpdfdenTAAAICYTSGTTGNPKGVVYSHR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  640 NVV--SLVRNSNYTSASGDDRFIMTGSISFDAVTFEM-FGALLNGASLhiidkstmLTPDRF--GAYLLE--NDITVLF- 711
Cdd:cd12119   187 SLVlhAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLpYAAAMVGAKL--------VLPGPYldPASLAEliEREGVTFa 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 -----LTTALFNQLAQVRADMFrGLHTLYVGGEALSPALMNA-------VRHAcpdlalhniYGPTENTTFSTF------ 773
Cdd:cd12119   259 agvptVWQGLLDHLEANGRDLS-SLRRVVIGGSAVPRSLIEAfeergvrVIHA---------WGMTETSPLGTVarppse 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  774 -----FEMKRDYAgpIPIGKPISNSTAYILDTKGRLLPI-GVP-GELCVGGDGVAKGYLNRvDLTNAVFSPHPFLpgeri 846
Cdd:cd12119   329 hsnlsEDEQLALR--AKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKN-DEESEALTEDGWL----- 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  847 yRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGE-----AQLYthyvGDHKK 919
Cdd:cd12119   401 -RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVphPKWGErplavVVLK----EGATV 475

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 499188982  920 TDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd12119   476 TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 502-898 5.89e-24

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 107.27  E-value: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV-- 579
Cdd:PRK07514   29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCdp 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  580 --QKGLEQNAAFSGTCII----SDAQG-LME----ENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVS----L 644
Cdd:PRK07514  109 anFAWLSKIAAAAGAPHVetldADGTGsLLEaaaaAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSnaltL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  645 VRNSNYTSasgDDRFIMTGSIsFDavTFEMF----GALLNGASlhiidkstMLTPDRFGAyllenditvlfltTALFNQL 720
Cdd:PRK07514  189 VDYWRFTP---DDVLIHALPI-FH--THGLFvatnVALLAGAS--------MIFLPKFDP-------------DAVLALM 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  721 AqvRADMFRGLHTLYV---GGEALSPAlmnAVRH-------ACPDLAL----------HNI---YGPTE---NTtfSTFF 774
Cdd:PRK07514  242 P--RATVMMGVPTFYTrllQEPRLTRE---AAAHmrlfisgSAPLLAEthrefqertgHAIlerYGMTEtnmNT--SNPY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  775 EMKRdyagpIP--IGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGD 851
Cdd:PRK07514  315 DGER-----RAgtVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGD 383

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 499188982  852 LARWLPDGnleYISRIDRQ--MKIRGK-RIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK07514  384 LGKIDERG---YVHIVGRGkdLIISGGyNVYPKEVEGEIDELPGVVESAV 430
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1070-1270 6.74e-24

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


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 101.31  E-value: 6.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1070 LFCFPPISGFGIYFKDLALLLNEKAAVY-----GFHFIEQ-----DTRIEQYVNCMTDIQPEGPYVLLGYSAGGNLAFEV 1139
Cdd:pfam00975    3 LFCFPPAGGSASSFRSLARRLPPPAEVLavqypGRGRGEPplnsiEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  1140 AQAMERKGLEVSDFIIVDAY---LKEQPLPIDTGNDESAAYL------PEAVREKvmkkkrnyQEYWAQLL-----NEGH 1205
Cdd:pfam00975   83 ARRLERQGEAVRSLFLSDASaphTVRYEASRAPDDDEVVAEFtdeggtPEELLED--------EELLSMLLpalraDYRA 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  1206 IKASIHFIEAG--IHPETSGHTGLTKWEGACGNYSEYTGFGAHKDMLEGT--YAEKNADIILDILEKIT 1270
Cdd:pfam00975  155 LESYSCPPLDAqsATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDhfYLIEHLEAVLEIIEAKL 223
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 483-960 8.44e-24

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 106.85  E-value: 8.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   483 REQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPP 562
Cdd:TIGR02262   12 RNVVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   563 ERVSFMLEETQAKMLIVQKGL----EQNAAFSGT----CIISDAQG--------LMEENDIPINISSSPDDLAYIMYTSG 626
Cdd:TIGR02262   92 DDYAYMLEDSRARVVFVSGALlpviKAALGKSPHlehrVVVGRPEAgevqlaelLATESEQFKPAATQADDPAFWLYSSG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   627 STGRPKGVMITNRNVVSLVRNSnytsaSGDDRFIMTGSISFDAVTFEMFGALLNGASLHI-IDKSTMLTPDRFGAyllen 705
Cdd:TIGR02262  172 STGMPKGVVHTHSNPYWTAELY-----ARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMsVGATTVLMGERPTP----- 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   706 ditvlfltTALFNQLAQVRADMFRGLHTLYVG---------------------GEALsPALMNAVRHACPDLALHNIYGP 764
Cdd:TIGR02262  242 --------DAVFDRLRRHQPTIFYGVPTLYAAmladpnlpsedqvrlrlctsaGEAL-PAEVGQRWQARFGVDIVDGIGS 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   765 TEntTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpGE 844
Cdd:TIGR02262  313 TE--MLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ------GE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   845 RIyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT-LREKDG--EAQLYTHYVGDHKKTD 921
Cdd:TIGR02262  385 WT-RSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVgVADEDGliKPKAFVVLRPGQTALE 463

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 499188982   922 TDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:TIGR02262  464 TELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKL 502
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
476-960 1.60e-23

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 106.50  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYL 554
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  555 PLDAELPPERVSFMLEETQAKMLIVQ-------------------------------------------KGLEQNAAFSG 591
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVLVVIdnfgttvqqviadtpvkqvittglgdmlgfpkaalvnfvvkyvKKLVPEYRING 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  592 TCIISDAQGLMEENDIPiNISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGD----DRFIMTG--- 663
Cdd:PRK08751  185 AIRFREALALGRKHSMP-TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAnMQQAHQWLAGTGKleegCEVVITAlpl 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  664 ----SISFDAVTFEMFGallnGASLHIIDKSTM------LTPDRFGAYLLENDITVLFLTTALFNQLAqvradmFRGLHT 733
Cdd:PRK08751  264 yhifALTANGLVFMKIG----GCNHLISNPRDMpgfvkeLKKTRFTAFTGVNTLFNGLLNTPGFDQID------FSSLKM 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  734 LYVGGEALSPALMNAVRHACpDLALHNIYGPTENTTFSTFFEMK-RDYAGPIpiGKPISNSTAYILDTKGRLLPIGVPGE 812
Cdd:PRK08751  334 TLGGGMAVQRSVAERWKQVT-GLTLVEAYGLTETSPAACINPLTlKEYNGSI--GLPIPSTDACIKDDAGTVLAIGEIGE 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  813 LCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEG 892
Cdd:PRK08751  411 LCIKGPQVMKGYWKRPEETAKVMDADGWL------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPG 484

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  893 VQE-AAVTL-REKDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK08751  485 VLEvAAVGVpDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 488-899 2.32e-23

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 106.08  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  488 KTPDHTALV--YGNMSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYL---PLDAELP 561
Cdd:PLN02574   51 NHNGDTALIdsSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnPSSSLGE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  562 -PERVS-------FMLEETQAKML---IVQKGLEQNAAF-SGTCIISDAQGLM-EENDIPINISSSPDDLAYIMYTSGST 628
Cdd:PLN02574  131 iKKRVVdcsvglaFTSPENVEKLSplgVPVIGVPENYDFdSKRIEFPKFYELIkEDFDFVPKPVIKQDDVAAIMYSSGTT 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  629 GRPKGVMITNRNVVSLV------RNSNYtSASGDDRFIMTGSISFDAVTFEMF--GALLNGASLHII---DKSTMLTP-D 696
Cdd:PLN02574  211 GASKGVVLTHRNLIAMVelfvrfEASQY-EYPGSDNVYLAALPMFHIYGLSLFvvGLLSLGSTIVVMrrfDASDMVKViD 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGayllendIT----VLFLTTALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTENTTFST 772
Cdd:PLN02574  290 RFK-------VThfpvVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGT 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  773 F-FEMK--RDYAGpipIGKPISNSTAYILD-TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyR 848
Cdd:PLN02574  363 RgFNTEklSKYSS---VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------R 433

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499188982  849 TGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT 899
Cdd:PLN02574  434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT 484
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 502-867 3.68e-23

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


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 104.99  E-value: 3.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG----GAYlpldAELPPERVSFMLEETQAkml 577
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNipivTVY----ATLGEDALIHSLNETEC--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  578 ivqkgleqnaafsgTCIISDaqglmeendipinisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLV-----RNSNYTS 652
Cdd:cd17639    79 --------------SAIFTD---------------GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIaglgdRVPELLG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  653 AsgDDRFimtgsISF--------DAVTFEMF--GALLNGAS-LHIIDKS--------TMLTPDRF--------------- 698
Cdd:cd17639   130 P--DDRY-----LAYlplahifeLAAENVCLyrGGTIGYGSpRTLTDKSkrgckgdlTEFKPTLMvgvpaiwdtirkgvl 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  699 ---------------GAY-----LLENDITVLFLTTALFNqlaQVRADMFRGLHTLYVGGEALSPA---LMNAVrhACPD 755
Cdd:cd17639   203 aklnpmgglkrtlfwTAYqsklkALKEGPGTPLLDELVFK---KVRAALGGRLRYMLSGGAPLSADtqeFLNIV--LCPV 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  756 LalhNIYGPTE---NTTFSTFFEMKRDYAGPipigkPISNSTAYILDTK-GRLLPIGVP--GELCVGGDGVAKGYLNRVD 829
Cdd:cd17639   278 I---QGYGLTEtcaGGTVQDPGDLETGRVGP-----PLPCCEIKLVDWEeGGYSTDKPPprGEILIRGPNVFKGYYKNPE 349

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 499188982  830 LTNAVFSphpflpGERIYRTGDLARWLPDGNLEYISRI 867
Cdd:cd17639   350 KTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRK 381
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 486-961 4.37e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 105.39  E-value: 4.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLI--------VQKGLEQNAAFSGTCIISDAQGLMEENDIPInissspDDLA----------------YI 621
Cdd:PRK07788  139 AEVAAREGVKALVyddeftdlLSALPPDLGRLRAWGGNPDDDEPSGSTDETL------DDLIagsstaplpkppkpggIV 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  622 MYTSGSTGRPKGVMitnRNVVSLvrnsnytsasgddrFIMTGSIsFDAVTFEMFGALLNGASL-H----------IIDKS 690
Cdd:PRK07788  213 ILTSGTTGTPKGAP---RPEPSP--------------LAPLAGL-LSRVPFRAGETTLLPAPMfHatgwahltlaMALGS 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  691 TMLTPDRFGA---------YLLENDITVLFLTTALFNQLAQVRADM-FRGLHTLYVGGEALSPALMNAVRHACPDLaLHN 760
Cdd:PRK07788  275 TVVLRRRFDPeatlediakHKATALVVVPVMLSRILDLGPEVLAKYdTSSLKIIFVSGSALSPELATRALEAFGPV-LYN 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  761 IYGPTENT--TFSTFFEMKRD--YAGPIPIGkpisnSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNrvdltnavfS 836
Cdd:PRK07788  354 LYGSTEVAfaTIATPEDLAEApgTVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD---------G 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  837 PHPflpgERI---YRTGDLARWLPDGNLeYISRIDRQMKIR-GKRIEPAEIEARLLEMEGVQEAAVT----------LR- 901
Cdd:PRK07788  420 RDK----QIIdglLSSGDVGYFDEDGLL-FVDGRDDDMIVSgGENVFPAEVEDLLAGHPDVVEAAVIgvddeefgqrLRa 494

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  902 ---EKDGEA---QLYTHYVGDHkktdtdfradLARvlpdYMIPQHWVRVERMPLTGNGKIDRSALP 961
Cdd:PRK07788  495 fvvKAPGAAldeDAIKDYVRDN----------LAR----YKVPRDVVFLDELPRNPTGKVLKRELR 546
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 477-955 4.81e-23

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


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 104.30  E-value: 4.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:cd12118     5 TPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNAL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEEND-IPINissspddlayimYTSGSTGRPKGVM 635
Cdd:cd12118    85 NTRLDAEEIAFILRHSEAKVLFVDREFEYEDLLAEGDPDFEWIPPADEWDpIALN------------YTSGTTGRPKGVV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  636 ITNRnvvslvrnSNYTSASGDdrfIMTGSISFDAV---TFEMFGAllNG----------ASLHI-IDKstmLTPDRFGAY 701
Cdd:cd12118   153 YHHR--------GAYLNALAN---ILEWEMKQHPVylwTLPMFHC--NGwcfpwtvaavGGTNVcLRK---VDAKAIYDL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  702 LLENDIT-------VLfltTALFNQLAQVRADMFRGLHTLyVGGEALSPALMNAVRhacpDLALH--NIYGPTENTTFST 772
Cdd:cd12118   217 IEKHKVThfcgaptVL---NMLANAPPSDARPLPHRVHVM-TAGAPPPAAVLAKME----ELGFDvtHVYGLTETYGPAT 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  773 FFEMKRDYAG---------------PIPIGKPISnstayILDTKGRllpIGVP------GELCVGGDGVAKGYLNRVDLT 831
Cdd:cd12118   289 VCAWKPEWDElpteerarlkarqgvRYVGLEEVD-----VLDPETM---KPVPrdgktiGEIVFRGNIVMKGYLKNPEAT 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  832 NAVFSphpflpgERIYRTGDLARWLPDGnleYISRIDRQMKI---RGKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGE 906
Cdd:cd12118   361 AEAFR-------GGWFHSGDLAVIHPDG---YIEIKDRSKDIiisGGENISSVEVEGVLYKHPAVLEAAVVARpdEKWGE 430

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499188982  907 AQlyTHYV---GDHKKTDTDFRADLARVLPDYMIPQHWVRVErMPLTGNGKI 955
Cdd:cd12118   431 VP--CAFVelkEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 471-957 5.93e-23

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 105.08  E-value: 5.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  471 EYPKNhTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG 550
Cdd:PRK05605   28 DYGDT-TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  551 GAYL---PL--DAELPP-------------ERVSFMLEE---------------TQAKMLIVQKGL--------EQNAAF 589
Cdd:PRK05605  107 AVVVehnPLytAHELEHpfedhgarvaivwDKVAPTVERlrrttpletivsvnmIAAMPLLQRLALrlpipalrKARAAL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  590 SGTC--------IISDAQGLmeENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGDDRFI 660
Cdd:PRK05605  187 TGPApgtvpwetLVDAAIGG--DGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKAWVPGLGDGPER 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSISFdavtFEMFGALLNGASLHIIDKSTMLTPdRFGAYLLENDI-----TVLFLTTALFNQLAQVRADMFRGLHTL- 734
Cdd:PRK05605  265 VLAALPM----FHAYGLTLCLTLAVSIGGELVLLP-APDIDLILDAMkkhppTWLPGVPPLYEKIAEAAEERGVDLSGVr 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  735 --YVGGEALSPALMNAVRHACPDLaLHNIYGPTENTtfstffemkrdyagPIPIGKPISNS--TAYI------------- 797
Cdd:PRK05605  340 naFSGAMALPVSTVELWEKLTGGL-LVEGYGLTETS--------------PIIVGNPMSDDrrPGYVgvpfpdtevrivd 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  798 LDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVfsphpFLPGerIYRTGDLARWLPDGNLEYISRIdRQMKIRGK- 876
Cdd:PRK05605  405 PEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKS-----FLDG--WFRTGDVVVMEEDGFIRIVDRI-KELIITGGf 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAVT-LREKDGEAQLYTHYV-GDHKKTDTD-FRADLARVLPDYMIPQHWVRVERMPLTGNG 953
Cdd:PRK05605  477 NVYPAEVEEVLREHPGVEDAAVVgLPREDGSEEVVAAVVlEPGAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556


                  ....
gi 499188982  954 KIDR 957
Cdd:PRK05605  557 KVRR 560
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 473-898 7.49e-23

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 104.29  E-value: 7.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNHTIIDLFREQAEKTPDHTALVYG--NMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG 550
Cdd:PLN02330   25 PDKLTLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  551 GAYLPLDAELPPERVSFMLEETQAKMLIVQ-------KGLEQNAAFSGTCIISDAQGLME-------ENDIPINISSSPD 616
Cdd:PLN02330  105 GVFSGANPTALESEIKKQAEAAGAKLIVTNdtnygkvKGLGLPVIVLGEEKIEGAVNWKElleaadrAGDTSDNEEILQT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIMT-GSISFdavtFEMFGAL-LNGASLHiiDKSTMLT 694
Cdd:PLN02330  185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTlGLIPF----FHIYGITgICCATLR--NKGKVVV 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 PDRFGAYLLENDITVLFLTTA------LFNQLAQVRADMFR----GLHTLYVGGEALSPALMNAVRHACPDLALHNIYGP 764
Cdd:PLN02330  259 MSRFELRTFLNALITQEVSFApivppiILNLVKNPIVEEFDlsklKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  765 TENTTFS-TFFEMKRDYAgpipIGKpiSNSTAYIL----------DTkGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNA 833
Cdd:PLN02330  339 TEHSCITlTHGDPEKGHG----IAK--KNSVGFILpnlevkfidpDT-GRSLPKNTPGELCVRSQCVMQGYYNNKEETDR 411

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  834 VFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PLN02330  412 TIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
PLN02246 PLN02246
4-coumarate--CoA ligase
 484-907 8.82e-23

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 104.29  E-value: 8.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  484 EQAEKTPDHTALVYGNM--SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELP 561
Cdd:PLN02246   31 ERLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  562 PERVSFMLEETQAKMLIVQ-------KGLEQNAAFSGTCIISDAQGLM--------EENDIPiNISSSPDDLAYIMYTSG 626
Cdd:PLN02246  111 PAEIAKQAKASGAKLIITQscyvdklKGLAEDDGVTVVTIDDPPEGCLhfseltqaDENELP-EVEISPDDVVALPYSSG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  627 STGRPKGVMITNRNVVSLVR--------NSNYTSasgDDRFI----MTGSISFDAVtfeMFGALLNGASLHIIDKSTMLT 694
Cdd:PLN02246  190 TTGLPKGVMLTHKGLVTSVAqqvdgenpNLYFHS---DDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPKFEIGA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 pdrfgayLLE----NDITVLFLTTALFNQLAQ---VRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEN 767
Cdd:PLN02246  264 -------LLEliqrHKVTIAPFVPPIVLAIAKspvVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEA 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 ttfSTFFEMKRDYAG-PIPI-----GKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNavfsphpf 840
Cdd:PLN02246  337 ---GPVLAMCLAFAKePFPVksgscGTVVRNAELKIVDPEtGASLPRNQPGEICIRGPQIMKGYLNDPEATA-------- 405

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  841 lpgeriyRTGDLARWLPDGNLEYISR------IDRQ---MKIRGKRIEPAEIEARLLEMEGVQEAAVTLReKDGEA 907
Cdd:PLN02246  406 -------NTIDKDGWLHTGDIGYIDDddelfiVDRLkelIKYKGFQVAPAELEALLISHPSIADAAVVPM-KDEVA 473
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 473-944 1.15e-22

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 104.19  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGA 552
Cdd:PRK08279   34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  553 YLPLDAELPPERVSFMLEETQAKMLIVqkGLEQNAAFSGT----------CIISDAQGLMEENDIPINISSS-------- 614
Cdd:PRK08279  114 VALLNTQQRGAVLAHSLNLVDAKHLIV--GEELVEAFEEAradlarpprlWVAGGDTLDDPEGYEDLAAAAAgapttnpa 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 ------PDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFIMT--------GSISFDAVtfemfgaLL 679
Cdd:PRK08279  192 srsgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGfGGLLRLTPDDVLYCClplyhntgGTVAWSSV-------LA 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  680 NGASLHIIDK-STmltpDRFGAYLLENDITvLF-----LTTALFNQLAQvraDMFRGlHTL-YVGGEALSPALMNAV--R 750
Cdd:PRK08279  265 AGATLALRRKfSA----SRFWDDVRRYRAT-AFqyigeLCRYLLNQPPK---PTDRD-HRLrLMIGNGLRPDIWDEFqqR 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  751 HACPDLAlhNIYGPTE-NTTFSTFFEmKRDYAG--PIPIGKPIS------NSTAYILDTKGRLLPIGvPGE--LCVG--G 817
Cdd:PRK08279  336 FGIPRIL--EFYAASEgNVGFINVFN-FDGTVGrvPLWLAHPYAivkydvDTGEPVRDADGRCIKVK-PGEvgLLIGriT 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  818 DGVA-KGYL-----NRVDLTNAvfsphpFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEME 891
Cdd:PRK08279  412 DRGPfDGYTdpeasEKKILRDV------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  892 GVQEAA---VTLREKDGEAQLYTHYVGDHKKTD-TDFRADLARVLPDYMIPQhWVRV 944
Cdd:PRK08279  486 GVEEAVvygVEVPGTDGRAGMAAIVLADGAEFDlAALAAHLYERLPAYAVPL-FVRL 541
PRK08315 PRK08315
AMP-binding domain protein; Validated
 477-955 1.38e-22

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 103.74  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVY--GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG---- 550
Cdd:PRK08315   17 TIGQLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGailv 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  551 -------------------------------GAYLPLDAELPPE------------------RVSFMLEETQAKMLivqk 581
Cdd:PRK08315   97 tinpayrlseleyalnqsgckaliaadgfkdSDYVAMLYELAPElatcepgqlqsarlpelrRVIFLGDEKHPGML---- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqnaAFSGtcIISDAQGLMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNVV---SLV-RNSNYTSasgDD 657
Cdd:PRK08315  173 ------NFDE--LLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngYFIgEAMKLTE---ED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  658 R------FimtgsisfdavtFEMFGALLngASLHIIDK-STMLTP-DRFgaylleNDITVLFLT-----TALFN------ 718
Cdd:PRK08315  242 RlcipvpL------------YHCFGMVL--GNLACVTHgATMVYPgEGF------DPLATLAAVeeercTALYGvptmfi 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 -QLAQVRADMFrGLHTLYVGGEALSPalmnavrhaCP---------DLALHNI---YGPTENTTFSTF------FEmKRD 779
Cdd:PRK08315  302 aELDHPDFARF-DLSSLRTGIMAGSP---------CPievmkrvidKMHMSEVtiaYGMTETSPVSTQtrtddpLE-KRV 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  780 YAgpipIGKPISNSTAYILD-TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPD 858
Cdd:PRK08315  371 TT----VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWM------HTGDLAVMDEE 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  859 GNLEYISRIdRQMKIR-GKRIEPAEIEARLLEMEGVQEAAV--TLREKDGEAqlythyVG-------DHKKTDTDFRA-- 926
Cdd:PRK08315  441 GYVNIVGRI-KDMIIRgGENIYPREIEEFLYTHPKIQDVQVvgVPDEKYGEE------VCawiilrpGATLTEEDVRDfc 513

                         570       580       590
                  ....*....|....*....|....*....|.
gi 499188982  927 --DLARvlpdYMIPQHWVRVERMPLTGNGKI 955
Cdd:PRK08315  514 rgKIAH----YKIPRYIRFVDEFPMTVTGKI 540
PRK05691 PRK05691
peptide synthase; Validated
 476-1069 1.39e-22

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 106.02  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVY------GNMSISYKELDKRSNALARELiQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK05691    9 LTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPldaELPPE--------RVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISSS------- 614
Cdd:PRK05691   88 GVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAwqepalq 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVS---LVRNSnYTSASGDDRFImtgsISFDAVTFEM--FGALLNGASLHIidK 689
Cdd:PRK05691  165 PDDIAFLQYTSGSTALPKGVQVSHGNLVAneqLIRHG-FGIDLNPDDVI----VSWLPLYHDMglIGGLLQPIFSGV--P 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  690 STMLTPdrfgAYLLENDITVL---------------F---LTTALFNQLAQVRADMFRgLHTLYVGGEALSPALMNAVRH 751
Cdd:PRK05691  238 CVLMSP----AYFLERPLRWLeaiseyggtisggpdFayrLCSERVSESALERLDLSR-WRVAYSGSEPIRQDSLERFAE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  752 ---AC---PDlALHNIYGPTENTTFSTFFE--------------MKRDYAGP------IPIGKPISNSTAYILD-TKGRL 804
Cdd:PRK05691  313 kfaACgfdPD-SFFASYGLAEATLFVSGGRrgqgipaleldaeaLARNRAEPgtgsvlMSCGRSQPGHAVLIVDpQSLEV 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  805 LPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPflpGERIYRTGDLArWLPDGNLEYISRIDRQMKIRGKRIEPAEIE 884
Cdd:PRK05691  392 LGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  885 aRLLEMEgVQEAavtlreKDGEAQLYThyVGDHKKTDTDFRADLARVLPDYMIPQHWVRVER------------------ 946
Cdd:PRK05691  468 -KTVERE-VEVV------RKGRVAAFA--VNHQGEEGIGIAAEISRSVQKILPPQALIKSIRqavaeacqeapsvvllln 537

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  947 ---MPLTGNGKIDRSALPI-------------PENKPAKRQNIILPRNLVEEELANIWKQVLGVNTISIDDDFFAIGGHS 1010
Cdd:PRK05691  538 pgaLPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNS 617

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982 1011 LRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQLTAANEQHVI-------KLNQHGAQN 1069
Cdd:PRK05691  618 IAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIarlprgqALPQSLAQN 683
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
478-960 1.91e-22

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 103.04  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  478 IIDLFREQAEKTPDHTALVYGN--MSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLP 555
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTAdrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  556 LDAELPperVSFMLEETQAK----MLIVQKGLEQNAAFSGTCI--------ISDAQGLMEENDI-----PINISSSPDDL 618
Cdd:PRK05852   98 LDPALP---IAEQRVRSQAAgarvVLIDADGPHDRAEPTTRWWpltvnvggDSGPSGGTLSVHLdaatePTPATSTPEGL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  619 ----AYIMYTSGSTGRPKGVMITNRNVVSLVRN--SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGAslhiidksTM 692
Cdd:PRK05852  175 rpddAMIMFTGGTTGLPKMVPWTHANIASSVRAiiTGYRLSPRDATVAVMPLYHGHGLIAALLATLASGG--------AV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTP--DRFGAYLLENDITVLFLT--TAL--FNQLAQVRAD---MFRGLHTLYV---GGEALSPALMNAVRH--ACPDLAl 758
Cdd:PRK05852  247 LLParGRFSAHTFWDDIKAVGATwyTAVptIHQILLERAAtepSGRKPAALRFirsCSAPLTAETAQALQTefAAPVVC- 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  759 hnIYGPTENT--TFSTFFEMKRDYAGPIPIGKPISNSTA---YILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNA 833
Cdd:PRK05852  326 --AFGMTEAThqVTTTQIEGIGQTENPVVSTGLVGRSTGaqiRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  834 VFSpHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKdgeaQLYTHY 913
Cdd:PRK05852  404 NFT-DGWL------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPD----QLYGEA 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499188982  914 VG-------DHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK05852  473 VAavivpreSAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 476-959 4.51e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 102.33  E-value: 4.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVYGNM---------SISYKELDKRSNALARELIQKGfRKNETAGILAAHSPEFMISVLAV 546
Cdd:PRK05850    1 SSVPSLLRERASLQPDDAAFTFIDYeqdpagvaeTLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  547 LKAGGAYLPLDAELP---PERVSFMLEETQAKMLI--------VQKGLEQNAAFSGTCIIS-DAQGLmeenDIPINISSS 614
Cdd:PRK05850   80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLttsavvddVTEYVAPQPGQSAPPVIEvDLLDL----DSPRGSDAR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDL---AYIMYTSGSTGRPKGVMITNRNVVSLVRN--SNYTSASGDDRFIMTGSISFDAVTFEM------FGALLNGas 683
Cdd:PRK05850  156 PRDLpstAYLQYTSGSTRTPAGVMVSHRNVIANFEQlmSDYFGDTGGVPPPDTTVVSWLPFYHDMglvlgvCAPILGG-- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  684 lhiidKSTMLT--------PDRFGAYLLENDITVlfltTALFN---QLAqVR----ADM----FRGLHTLYVGGEALSPA 744
Cdd:PRK05850  234 -----CPAVLTspvaflqrPARWMQLLASNPHAF----SAAPNfafELA-VRktsdDDMagldLGGVLGIISGSERVHPA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  745 LMN--AVRHA---CPDLALHNIYGPTENTTF-----------STFFEMKRDYAGP------------IPIGKPISnSTAY 796
Cdd:PRK05850  304 TLKrfADRFApfnLRETAIRPSYGLAEATVYvatrepgqppeSVRFDYEKLSAGHakrcetgggtplVSYGSPRS-PTVR 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  797 ILDTKGRL-LPIGVPGELCVGGDGVAKGYLNRVDLTNAVF-----SPHPFLPGERIYRTGDLArWLPDGNLEYISRIDRQ 870
Cdd:PRK05850  383 IVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWLRTGDLG-FISEGELFIVGRIKDL 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  871 MKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEaQLYThyVGDHKK---TDTDFRADLARVLPDYM--IPQ-HWVRV 944
Cdd:PRK05850  462 LIVDGRNHYPDDIEATIQEITGGRVAAISVPDDGTE-KLVA--IIELKKrgdSDEEAMDRLRTVKREVTsaISKsHGLSV 538

                         570       580
                  ....*....|....*....|...
gi 499188982  945 E--------RMPLTGNGKIDRSA 959
Cdd:PRK05850  539 AdlvlvapgSIPITTSGKIRRAA 561
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 610-969 6.38e-22

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 101.76  E-value: 6.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  610 NISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSAS--GDDRFIMTGSISFD---AVTFEMFGALLNGASL 684
Cdd:PRK05677  201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSnlNEGCEILIAPLPLYhiyAFTFHCMAMMLIGNHN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  685 HII----DKSTM---LTPDRFGAYLLENditvlflttALFNQLAQ---VRADMFRGLHTLYVGGEALSPALMNAVRH--A 752
Cdd:PRK05677  281 ILIsnprDLPAMvkeLGKWKFSGFVGLN---------TLFVALCNneaFRKLDFSALKLTLSGGMALQLATAERWKEvtG 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 CPDLalhNIYGPTENTTFSTFFEMKRDYAGPIpiGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTN 832
Cdd:PRK05677  352 CAIC---EGYGMTETSPVVSVNPSQAIQVGTI--GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATD 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  833 AVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGV-QEAAVTL-REKDGEA-QL 909
Cdd:PRK05677  427 EILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVlQCAAIGVpDEKSGEAiKV 500

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  910 YTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPENKPAK 969
Cdd:PRK05677  501 FVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 614-956 7.91e-22

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 102.69  E-value: 7.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRfiMTGSISFdavtFEMFG-------ALLNGASL- 684
Cdd:PRK08633  780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQiSDVFNLRNDDV--ILSSLPF----FHSFGltvtlwlPLLEGIKVv 853

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  685 -HiidkstmltPD-----RFGAYLLENDITVLFLTTALFN---QLAQVRADMFRGLHTLYVGGEALSPALMNAVRHAcpd 755
Cdd:PRK08633  854 yH---------PDptdalGIAKLVAKHRATILLGTPTFLRlylRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK--- 921

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  756 lalHNI-----YGPTENTTFST----------FFEMKRDYAGPIpiGKPISNSTAYILD-TKGRLLPIGVPGELCVGGDG 819
Cdd:PRK08633  922 ---FGIrilegYGATETSPVASvnlpdvlaadFKRQTGSKEGSV--GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQ 996

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  820 VAKGYLNRVDLTNAVFSPhpfLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIE---ARLLEMEGVQEA 896
Cdd:PRK08633  997 VMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAKALGGEEVVFA 1073

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499188982  897 AVTL-REKDGE--AQLYTHyvgDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK08633 1074 VTAVpDEKKGEklVVLHTC---GAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 617-957 1.21e-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: 97.72  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVVSLVRN--SNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIIDKSTMLT 694
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 pdRFGAYLLENDITVLFLTTALFNQLAQVRADMFR---GLHTLYVGGEALSPAlMNAVRHACPDLALHNIYGPTEnTTFS 771
Cdd:cd17635    82 --SLFKILTTNAVTTTCLVPTLLSKLVSELKSANAtvpSLRLIGYGGSRAIAA-DVRFIEATGLTNTAQVYGLSE-TGTA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  772 TFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGD 851
Cdd:cd17635   158 LCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVNTGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  852 LARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVG----DHKKTDTDFRAD 927
Cdd:cd17635   231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeLDENAIRALKHT 310

                         330       340       350
                  ....*....|....*....|....*....|
gi 499188982  928 LARVLPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd17635   311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
474-960 2.22e-21

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 100.49  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  474 KNHTIIDLFREQAEKT--PDHTALvYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGG 551
Cdd:PRK06060    2 RNGNLAGLLAEQASEAgwYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  552 AYLPLDAELPPERVSFMLEETQAKMLIVQKGLEQNaaFSGTCIISDAQGLMEENDI-PINISS-SPDDLAYIMYTSGSTG 629
Cdd:PRK06060   81 MAFLANPELHRDDHALAARNTEPALVVTSDALRDR--FQPSRVAEAAELMSEAARVaPGGYEPmGGDALAYATYTSGTTG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  630 RPKGVMITNRNVVSLVRN--SNYTSASGDDRFIMTGSISF-----DAVTFEMF---GALLNgaSLHIIDKSTMLTPDRFg 699
Cdd:PRK06060  159 PPKAAIHRHADPLTFVDAmcRKALRLTPEDTGLCSARMYFayglgNSVWFPLAtggSAVIN--SAPVTPEAAAILSARF- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  700 ayllenDITVLFLTTALFNQLAQV-RADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEntTFSTFFEMKR 778
Cdd:PRK06060  236 ------GPSVLYGVPNFFARVIDScSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE--VGQTFVSNRV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  779 DYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRvdltnavfsPHPFLPGERIYRTGDLARWLPD 858
Cdd:PRK06060  308 DEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWLDTRDRVCIDSD 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  859 GNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT-LREKDGEAQLYTHYV-----GDHKKTDTDFRADLARVL 932
Cdd:PRK06060  379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVaVRESTGASTLQAFLVatsgaTIDGSVMRDLHRGLLNRL 458

                         490       500
                  ....*....|....*....|....*...
gi 499188982  933 PDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK06060  459 SAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 470-960 2.54e-21

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 99.71  E-value: 2.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  470 TEYPknhTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK07059   20 SQYP---SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVqkgLEQNAA------------------------FSGTC---IISDAQGLM 602
Cdd:PRK07059   97 GYVVVNVNPLYTPRELEHQLKDSGAEAIVV---LENFATtvqqvlaktavkhvvvasmgdllgFKGHIvnfVVRRVKKMV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  603 EENDIPINIS-----------------SSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSN------YTSASGDDRF 659
Cdd:PRK07059  174 PAWSLPGHVRfndalaegarqtfkpvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpaFEKKPRPDQL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  660 IMTGSISFdavtFEMFGALLNGaslhiidkstMLTPdRFGAY--LLEN--DITvlflttALFNQLAQVRADMFRGLHTLY 735
Cdd:PRK07059  254 NFVCALPL----YHIFALTVCG----------LLGM-RTGGRniLIPNprDIP------GFIKELKKYQVHIFPAVNTLY 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  736 vggealsPALMN--------------------AVRHA----------CPdlaLHNIYGPTENTTFSTFFEMKRD-YAGPI 784
Cdd:PRK07059  313 -------NALLNnpdfdkldfsklivangggmAVQRPvaerwlemtgCP---ITEGYGLSETSPVATCNPVDATeFSGTI 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  785 piGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWLPDGnleYI 864
Cdd:PRK07059  383 --GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERG---YT 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  865 SRIDRQ---MKIRGKRIEPAEIEARLLEMEGVQEAAV--TLREKDGEA-QLYThYVGDHKKTDTDFRADLARVLPDYMIP 938
Cdd:PRK07059  452 KIVDRKkdmILVSGFNVYPNEIEEVVASHPGVLEVAAvgVPDEHSGEAvKLFV-VKKDPALTEEDVKAFCKERLTNYKRP 530

                         570       580
                  ....*....|....*....|..
gi 499188982  939 QHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK07059  531 KFVEFRTELPKTNVGKILRREL 552
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 19-442 7.71e-21

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


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 96.94  E-value: 7.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   19 PLSHMQEgMLFHSFLrkEEGAYVEQS-LFTIKGSLSYDWFQRSIQAIIDRHDIFRTVFLPH----VPHLSGPrqvvmTER 93
Cdd:cd19534     3 PLTPIQR-WFFEQNL--AGRHHFNQSvLLRVPQGLDPDALRQALRALVEHHDALRMRFRREdggwQQRIRGD-----VEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   94 EFHLNSEDISHLptnDQNEYIERfKEKDKQKGFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDG--WclGIVMQEFMQ 171
Cdd:cd19534    75 LFRLEVVDLSSL---AQAAAIEA-LAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLEA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  172 IYQSIHAGKPLSLDPVRPYSTYISWLTNRDKEKA----AAYWDTYLKnySAPSPLPrvSDKETKESyHREDLIFSLNKPL 247
Cdd:cd19534   149 AYEQALAGEPIPLPSKTSFQTWAELLAEYAQSPAlleeLAYWRELPA--ADYWGLP--KDPEQTYG-DARTVSFTLDEEE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  248 TDKLKETAKQ------HGVTLATLIQAvwgvmLQQYNRTDDVvfgaVVS----GRPSEIPGVEQM--IGLFINTIPIRIK 315
Cdd:cd19534   224 TEALLQEANAayrteiNDLLLAALALA-----FQDWTGRAPP----AIFleghGREEIDPGLDLSrtVGWFTSMYPVVLD 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  316 THQDETFHELLIRCqKEMLEAEP------FTCQPLfdiqaNTALKQELIDHI---IVFeNYplqqkiadsADQTDSPLQI 386
Cdd:cd19534   295 LEASEDLGDTLKRV-KEQLRRIPnkgigyGILRYL-----TPEGTKRLAFHPqpeISF-NY---------LGQFDQGERD 358

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  387 DQVQVSEQSG--------------YNFNLVVAPGeELVIKFSYNAFVYDAAWISCIKRQFTQALSTAAQH 442
Cdd:cd19534   359 DALFVSAVGGggsdigpdtprfalLDINAVVEGG-QLVITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
PRK13382 PRK13382
bile acid CoA ligase;
475-963 1.31e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 97.52  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  475 NHTIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYL 554
Cdd:PRK13382   42 GMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  555 PLDAELPPERVSFMLEETQAKMLIVQKGLEQ--NAAFSGTC----II----SDAQGLMEE-NDIPIN--ISSSPDDLAYI 621
Cdd:PRK13382  122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSAtvDRALADCPqatrIVawtdEDHDLTVEVlIAAHAGqrPEPTGRKGRVI 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  622 MYTSGSTGRPKGVmitnrnvvslvRNSNYTSAsGDDRFIMTGS-------ISFDAVTFEM--FGALLNGASLhiidKSTM 692
Cdd:PRK13382  202 LLTSGTTGTPKGA-----------RRSGPGGI-GTLKAILDRTpwraeepTVIVAPMFHAwgFSQLVLAASL----ACTI 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTPDRFG-----AYLLENDITVLFLTTALFNQLAQVRADMF-----RGLHTLYVGGEALSPALMNAVRHACPDlALHNIY 762
Cdd:PRK13382  266 VTRRRFDpeatlDLIDRHRATGLAVVPVMFDRIMDLPAEVRnrysgRSLRFAAASGSRMRPDVVIAFMDQFGD-VIYNNY 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  763 GPTENTTFSTffEMKRDY-AGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYlnrvdlTNAvfSPHPFL 841
Cdd:PRK13382  345 NATEAGMIAT--ATPADLrAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSG--STKDFH 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  842 PGerIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYV---GDHK 918
Cdd:PRK13382  415 DG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVvlkPGAS 492

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 499188982  919 KTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIP 963
Cdd:PRK13382  493 ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 493-960 1.70e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 96.21  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  493 TALVYGNMSISYKELDKRSNALARELiqkgfRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEET 572
Cdd:PRK07787   17 DAVRIGGRVLSRSDLAGAATAVAERV-----AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  573 QAKMLIVQKGleqnaafsgtciiSDAQGLMEendIPINISS---------SPDDLAYIMYTSGSTGRPKGVMITNRNVVS 643
Cdd:PRK07787   92 GAQAWLGPAP-------------DDPAGLPH---VPVRLHArswhrypepDPDAPALIVYTSGTTGPPKGVVLSRRAIAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  644 ----LVRNSNYTsasGDDR-------FIMTGSIsfdavtFEMFGALLNGASLHIIDKstmLTPDRFgAYLLENDITVLFL 712
Cdd:PRK07787  156 dldaLAEAWQWT---ADDVlvhglplFHVHGLV------LGVLGPLRIGNRFVHTGR---PTPEAY-AQALSEGGTLYFG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  713 TTALFNQLAQVR--ADMFRGLHtLYVGGEALSPAlmnAVRHACPDLALHNI---YGPTEN-TTFSTFFEMKRDyagPIPI 786
Cdd:PRK07787  223 VPTVWSRIAADPeaARALRGAR-LLVSGSAALPV---PVFDRLAALTGHRPverYGMTETlITLSTRADGERR---PGWV 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  787 GKPISNSTAYILDTKGRLLPIGVP--GELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWLPDGNLEYI 864
Cdd:PRK07787  296 GLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIV 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  865 SR--IDrQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTDFRADL-ARVLPDYMIPQHW 941
Cdd:PRK07787  370 GResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFvAQQLSVHKRPREV 448

                         490
                  ....*....|....*....
gi 499188982  942 VRVERMPLTGNGKIDRSAL 960
Cdd:PRK07787  449 RFVDALPRNAMGKVLKKQL 467
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 502-960 3.38e-20

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


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 95.28  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVqk 581
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqNAAfsgtciisdaqglmeendipiNISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYT-SASGDDRFI 660
Cdd:cd05973    79 ----DAA---------------------NRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAvDLRPEDSFW 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSIS-----FDAVTfemfGALLNGASLHIID-----KSTMLTPDRFGAYLLENDITVLFLttaLFNQLAQVRADMFRG 730
Cdd:cd05973   134 NAADPGwayglYYAIT----GPLALGHPTILLEggfsvESTWRVIERLGVTNLAGSPTAYRL---LMAAGAEVPARPKGR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  731 LHTLYVGGEALSPALMNAVRhACPDLALHNIYGPTEnttFSTFFEMKRDYAGPI---PIGKPISNSTAYILDTKGRLLPI 807
Cdd:cd05973   207 LRRVSSAGEPLTPEVIRWFD-AALGVPIHDHYGQTE---LGMVLANHHALEHPVhagSAGRAMPGWRVAVLDDDGDELGP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  808 GVPGELCVGGDGVA----KGYLNRVDLTnavfsphpflPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEI 883
Cdd:cd05973   283 GEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  884 EARLLEMEGVQEAAVTLREKDGEAQLYTHYV---GDHKKTdTDFRADLARVLPDYMIPQHWVR----VERMPLTGNGKID 956
Cdd:cd05973   353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVvlrGGHEGT-PALADELQLHVKKRLSAHAYPRtihfVDELPKTPSGKIQ 431


                  ....
gi 499188982  957 RSAL 960
Cdd:cd05973   432 RFLL 435
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 471-858 1.28e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 94.73  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  471 EYPKNhtIIDLFREQAEKTPDHTALVYGN------MSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVL 544
Cdd:PRK12582   46 PYPRS--IPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  545 AVLKAGGAYLPLDaelPP--------ERVSFMLEETQAKMLIVQKGleqnAAFSGTCIISDAQG---LMEENDIPINISS 613
Cdd:PRK12582  124 AAMQAGVPAAPVS---PAyslmshdhAKLKHLFDLVKPRVVFAQSG----APFARALAALDLLDvtvVHVTGPGEGIASI 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 S---------------------PDDLAYIMYTSGSTGRPKGV------MITNRNVVSLVRNSNYTSASGDD------RFI 660
Cdd:PRK12582  197 AfadlaatpptaavaaaiaaitPDTVAKYLFTSGSTGMPKAVintqrmMCANIAMQEQLRPREPDPPPPVSldwmpwNHT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSISFDavtfemfGALLNGASLHIIDKSTMltPDRFG---AYLLENDITVLFLTTALFNQLAQ-------VRADMFRG 730
Cdd:PRK12582  277 MGGNANFN-------GLLWGGGTLYIDDGKPL--PGMFEetiRNLREISPTVYGNVPAGYAMLAEamekddaLRRSFFKN 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  731 LHTLYVGGEALSPALMN-----AVRHACPDLALHNIYGPTEN--TTFSTFFEMKRdyagPIPIGKPISNstayildTKGR 803
Cdd:PRK12582  348 LRLMAYGGATLSDDLYErmqalAVRTTGHRIPFYTGYGATETapTTTGTHWDTER----VGLIGLPLPG-------VELK 416

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  804 LLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWL-PD 858
Cdd:PRK12582  417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdPD 466
PRK07529 PRK07529
AMP-binding domain protein; Validated
 476-960 1.35e-19

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 94.64  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVY--------GNMSISYKELDKR----SNALAREliqkGFRKNETAGILAAHSPEFMISV 543
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADvtrtANLLHSL----GVGPGDVVAFLLPNLPETHFAL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  544 LAVLKAGGAYlPLDAELPPERVSFMLEETQAKMLI-----------------------VQKGLEQNAAFSGTCIISDAQG 600
Cdd:PRK07529  101 WGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqkvaevlaalpeLRTVVEVDLARYLPGPKRLAVP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  601 LMEEnDIPINI-------------------SSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIM 661
Cdd:PRK07529  180 LIRR-KAHARIldfdaelarqpgdrlfsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVF 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  662 TGSISF--DAVTFEMFGALLNGASLhiidksTMLTP---------DRFGAYLLENDITVLFLTTALFNQLAQV---RADM 727
Cdd:PRK07529  259 CGLPLFhvNALLVTGLAPLARGAHV------VLATPqgyrgpgviANFWKIVERYRINFLSGVPTVYAALLQVpvdGHDI 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  728 fRGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGPTENTTFSTffemkRDYA-GPIPIGK-----PISNSTAYILDTK 801
Cdd:PRK07529  333 -SSLRYALCGAAPLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSS-----VNPPdGERRIGSvglrlPYQRVRVVILDDA 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  802 GRLL---PIGVPGELCVGGDGVAKGYLNrvDLTNavfspHPFLPGERIYRTGDLARWLPDGNLeYISRIDRQMKIR-GKR 877
Cdd:PRK07529  406 GRYLrdcAVDEVGVLCIAGPNVFSGYLE--AAHN-----KGLWLEDGWLNTGDLGRIDADGYF-WLTGRAKDLIIRgGHN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  878 IEPAEIEARLLEMEGVQEAA----------------VTLreKDGeAQLYTHYVGDHKKTDTDFRAdlarvlpdyMIPQHW 941
Cdd:PRK07529  478 IDPAAIEEALLRHPAVALAAavgrpdahagelpvayVQL--KPG-ASATEAELLAFARDHIAERA---------AVPKHV 545

                         570
                  ....*....|....*....
gi 499188982  942 VRVERMPLTGNGKIDRSAL 960
Cdd:PRK07529  546 RILDALPKTAVGKIFKPAL 564
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 39-336 1.42e-19

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


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 92.94  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   39 AYVEqslFTIKGsLSYDWFQRSIQAIIDRHDIFRTVFLPhvphlSGpRQVVMTE-REFHLNSEDISHLPTNDQNEYIERF 117
Cdd:cd19535    28 AYLE---FDGED-LDPDRLERAWNKLIARHPMLRAVFLD-----DG-TQQILPEvPWYGITVHDLRGLSEEEAEAALEEL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  118 KEK--------DKQKGFDLQkdmlmrISLFKTAKDE-HVCIWShhhILMDGWCLGIVMQEFMQIYQsiHAGKPLSLDPV- 187
Cdd:cd19535    98 RERlshrvldvERGPLFDIR------LSLLPEGRTRlHLSIDL---LVADALSLQILLRELAALYE--DPGEPLPPLELs 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  188 -RPYSTYISWLTNRDKEKAAAYWDTYLKN-YSAPSpLPRVSDKETKESY---HREdliFSLNKPLTDKLKETAKQHGVTL 262
Cdd:cd19535   167 fRDYLLAEQALRETAYERARAYWQERLPTlPPAPQ-LPLAKDPEEIKEPrftRRE---HRLSAEQWQRLKERARQHGVTP 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  263 ATLIQAVWGVMLQQYNRTDDV-----VFGavvsgRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEA 336
Cdd:cd19535   243 SMVLLTAYAEVLARWSGQPRFllnltLFN-----RLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWED 316
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 490-898 1.83e-19

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 94.10  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  490 PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAelppeRVSFml 569
Cdd:PLN02860   21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNY-----RWSF-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  570 EETQAKMLIVQKGLeqnAAFSGTCiiSDAQGLMEENDIP-------------------------------------INIS 612
Cdd:PLN02860   94 EEAKSAMLLVRPVM---LVTDETC--SSWYEELQNDRLPslmwqvflespsssvfiflnsflttemlkqralgtteLDYA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  613 SSPDDLAYIMYTSGSTGRPKGVMITNRNVV--SLVRNS--NYTSasgDDRFIMT------GSISfDAVTFEMFGAllnga 682
Cdd:PLN02860  169 WAPDDAVLICFTSGTTGRPKGVTISHSALIvqSLAKIAivGYGE---DDVYLHTaplchiGGLS-SALAMLMVGA----- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  683 sLHII----DKSTMLTPdrfgayLLENDITVLFLTTALFNQLAQVRA-----DMFRGLHTLYVGGEALSPALMNAVRHAC 753
Cdd:PLN02860  240 -CHVLlpkfDAKAALQA------IKQHNVTSMITVPAMMADLISLTRksmtwKVFPSVRKILNGGGSLSSRLLPDAKKLF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  754 PDLALHNIYGPTENTTFSTFfemkrdyagpIPIGKPISNSTAYILDTKGR--LLPIGVPGELCVG--------------- 816
Cdd:PLN02860  313 PNAKLFSAYGMTEACSSLTF----------MTLHDPTLESPKQTLQTVNQtkSSSVHQPQGVCVGkpaphvelkigldes 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  817 ---------GDGVAKGYLNRVDLTNAVFSPHPFLPgeriyrTGDLArWLPD-GNLEYISRIDRQMKIRGKRIEPAEIEAR 886
Cdd:PLN02860  383 srvgriltrGPHVMLGYWGQNSETASVLSNDGWLD------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAV 455

                         490
                  ....*....|..
gi 499188982  887 LLEMEGVQEAAV 898
Cdd:PLN02860  456 LSQHPGVASVVV 467
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 45-326 2.02e-19

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


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 92.25  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   45 LFTIKGSLSYDWFQRSIQAIIDRHDIFRT--VFLPHVPH--LSGPRQVVMTEREFHLNSEdiSHLPtndqneyierfkek 120
Cdd:cd19537    29 ACRLSGDVDRDRLASAWNTVLARHRILRSryVPRDGGLRrsYSSSPPRVQRVDTLDVWKE--INRP-------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  121 dkqkgFDLQKDMLMRISLfktAKDEHVCIWSHhhILMDGWCLGIVMQEFMQIYQsihaGKPLsLDPVRPYSTYISWlTNR 200
Cdd:cd19537    93 -----FDLEREDPIRVFI---SPDTLLVVMSH--IICDLTTLQLLLREVSAAYN----GKLL-PPVRREYLDSTAW-SRP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  201 DKEKAAAYWDTYLKNYSaPSPLPRVSdkeTKESYHREDLIFSLNKPLTDKLKETAKQHGVTLATLIQAVWGVMLQQYNRT 280
Cdd:cd19537   157 ASPEDLDFWSEYLSGLP-LLNLPRRT---SSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDR 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 499188982  281 DDVVFGAVVSGRPSEipGVEQMIGLFINTIPIRIKT--HQDETFHELL 326
Cdd:cd19537   233 TDIVLGAPYLNRTSE--EDMETVGLFLEPLPIRIRFpsSSDASAADFL 278
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 502-954 2.62e-19

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


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 92.42  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVqk 581
Cdd:cd05940     4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqnaafsgtciisdaqglmeendipinissspdDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNY-TSASGDDRFI 660
Cdd:cd05940    82 -----------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGsGGALPSDVLY 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSISFD-AVTFEMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTL-YVGG 738
Cdd:cd05940   127 TCLPLYHStALIVGWSACLASGATLVIRKK---FSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVrMIFG 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  739 EALSPALMNAV--RHACPDLAlhNIYGPTENTTFSTFFEMKRDYAGPIP----IGKPIS------NSTAYILDTKGRLLP 806
Cdd:cd05940   204 NGLRPDIWEEFkeRFGVPRIA--EFYAATEGNSGFINFFGKPGAIGRNPsllrKVAPLAlvkydlESGEPIRDAEGRCIK 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  807 IGV--PGELC--VGGDGVAKGYLNRVDlTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAE 882
Cdd:cd05940   282 VPRgePGLLIsrINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTE 360

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  883 IEARLLEMEGVQEA---AVTLREKDGEAQLYTHYVGDHKKTD-TDFRADLARVLPDYMIPqHWVRVER-MPLTGNGK 954
Cdd:cd05940   361 VAAVLGAFPGVEEAnvyGVQVPGTDGRAGMAAIVLQPNEEFDlSALAAHLEKNLPGYARP-LFLRLQPeMEITGTFK 436
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 475-898 4.21e-18

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 89.36  E-value: 4.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  475 NHTIIDLFREQAEKTPDHTALVYGNM-----SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVQ-------KGLEQNAAFSGTCIISDAQGLMEENDIpINISS--------- 613
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyRQIQQEDATPLRHICLTRVALPADDGV-SSFTQlkaqqpatl 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 ------SPDDLAYIMYTSGSTGRPKGVMITNRNvvslVRNSNYTSA-----SGDDRFI-MTGSISFDAVTFEMFGALLNG 681
Cdd:PRK08008  165 cyapplSTDDTAEILFTSGTTSRPKGVVITHYN----LRFAGYYSAwqcalRDDDVYLtVMPAFHIDCQCTAAMAAFSAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  682 ASLHIIDKstmLTPDRFGAYLLENDITV----------LFLTTALFNQLAQVRADMFRGLHtlyvggeaLSPALMNA--- 748
Cdd:PRK08008  241 ATFVLLEK---YSARAFWGQVCKYRATItecipmmirtLMVQPPSANDRQHCLREVMFYLN--------LSDQEKDAfee 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  749 ---VRhacpdlaLHNIYGPTEnttfsTFFEMKRDYAG-----PiPIGKPISNSTAYILDTKGRLLPIGVPGELC---VGG 817
Cdd:PRK08008  310 rfgVR-------LLTSYGMTE-----TIVGIIGDRPGdkrrwP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPG 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  818 DGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAA 897
Cdd:PRK08008  377 KTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450


                  .
gi 499188982  898 V 898
Cdd:PRK08008  451 V 451
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 501-885 7.60e-18

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


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 89.05  E-value: 7.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  501 SISYKELDKRSNALAREL-IQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV 579
Cdd:cd17632    67 TITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  580 ---------------------------------QKGLE---QNAAFSGTCIISDAQGLMEENDIP----INISSSPDDLA 619
Cdd:cd17632   147 saehldlaveavleggtpprlvvfdhrpevdahRAALEsarERLAAVGIPVTTLTLIAVRGRDLPpaplFRPEPDDDPLA 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  620 YIMYTSGSTGRPKGVMITNRNVVSLVRnsnyTSASGDDRFIMTGS------ISFDAVTFEMFGALLNGASLHIIDKSTM- 692
Cdd:cd17632   227 LLIYTSGSTGTPKGAMYTERLVATFWL----KVSSIQDIRPPASItlnfmpMSHIAGRISLYGTLARGGTAYFAAASDMs 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 ---------------LTP-------DRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVR 750
Cdd:cd17632   303 tlfddlalvrptelfLVPrvcdmlfQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFM 382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  751 HACPDLALHNIYGPTEnttfstffemkrdyAGPIPIGKPISNSTayILDTKgrllPIGVP-------------GELCVGG 817
Cdd:cd17632   383 ESLLDLDLHDGYGSTE--------------AGAVILDGVIVRPP--VLDYK----LVDVPelgyfrtdrphprGELLVKT 442

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  818 DGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGD-LARWLPDgNLEYISRIDRQMKI-RGKRIEPAEIEA 885
Cdd:cd17632   443 DTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEA 505
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 486-961 8.19e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 88.51  E-value: 8.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLIVQKGLEQNAAFSG--TCIISDAQGLMEENDIPINISSSPddlAYIMYTSGSTGRPKGVmitnrnvvs 643
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADdaVAVIDPATAGAEESGGRPAVAAPG---RIVLLTSGTTGKPKGV--------- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  644 lVRNSNYTSASG------DDRFIMTGSISfdAVTFEMFGAL-LNGASLHIIDKSTMLTPDRFGA-------YLLEND-IT 708
Cdd:PRK13383  193 -PRAPQLRSAVGvwvtilDRTRLRTGSRI--SVAMPMFHGLgLGMLMLTIALGGTVLTHRHFDAeaalaqaSLHRADaFT 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  709 VLFLTTALFNQLA-QVRA-DMFRGLHTLYVGGEALSPALMNAVRHACPDLaLHNIYGPTENT--TFSTFFEMkRDYagPI 784
Cdd:PRK13383  270 AVPVVLARILELPpRVRArNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGigALATPADL-RDA--PE 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  785 PIGKPISNSTAYILDTKGRllPIG--VPGELCVGGDGVAKGYLNrvDLTNAVFsphpflpgERIYRTGDLARWLPDGNLE 862
Cdd:PRK13383  346 TVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTD--GGGKAVV--------DGMTSTGDMGYLDNAGRLF 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  863 YISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTDfradlARVLPDYMI----- 937
Cdd:PRK13383  414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD-----AAQLRDYLKdrvsr 488

                         490       500
                  ....*....|....*....|....*..
gi 499188982  938 ---PQHWVRVERMPLTGNGKIDRSALP 961
Cdd:PRK13383  489 feqPRDINIVSSIPRNPTGKVLRKELP 515
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
480-960 1.24e-17

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 88.12  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEktPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAylPLDAE 559
Cdd:PRK10946   29 DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  560 LPPERVSFM--LEETQAKMLIV--QKGLEQNAAF--------SGTCII---------SDAQGLMEENDIPINISSSPDDL 618
Cdd:PRK10946  105 FSHQRSELNayASQIEPALLIAdrQHALFSDDDFlntlvaehSSLRVVlllnddgehSLDDAINHPAEDFTATPSPADEV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  619 AYIMYTSGSTGRPKGVMITNRNVVSLVRNSN----YTSasgDDRFIMTGSIsfdAVTFEM-----FGALLNGASLhiidk 689
Cdd:PRK10946  185 AFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVeicgFTP---QTRYLCALPA---AHNYPMsspgaLGVFLAGGTV----- 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  690 stMLTPDR-----FgAYLLENDITVlfltTALF----------NQLAQVRADMfRGLHTLYVGGEALSPALMNAVrhacP 754
Cdd:PRK10946  254 --VLAPDPsatlcF-PLIEKHQVNV----TALVppavslwlqaIAEGGSRAQL-ASLKLLQVGGARLSETLARRI----P 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  755 DL---ALHNIYGPTE---NTT---------FSTffemkrdyagpipIGKPIS-NSTAYILDTKGRLLPIGVPGELCVGGD 818
Cdd:PRK10946  322 AElgcQLQQVFGMAEglvNYTrlddsderiFTT-------------QGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGP 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  819 GVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK10946  389 YTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAL 462

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  899 TLREKD--GEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK10946  463 VSMEDElmGEKSCAFLVVKEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 489-897 1.31e-17

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: 88.32  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  489 TPDHTALVYGN-----MSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPE 563
Cdd:cd05968    74 TRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  564 RVSFMLEETQAKMLIVQKG---------LEQNA------AFSGTCIISDAQGLMEENDIPINISSS-------------- 614
Cdd:cd05968   154 AAATRLQDAEAKALITADGftrrgrevnLKEEAdkacaqCPTVEKVVVVRHLGNDFTPAKGRDLSYdeeketagdgaert 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 -PDDLAYIMYTSGSTGRPKGVMITNRNV---VSLVRNSNYTSASGDDRFIMTgSISFDAVTFEMFGALLNGASLHIIDKS 690
Cdd:cd05968   234 eSEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQFDLKPGDLLTWFT-DLGWMMGPWLIFGGLILGATMVLYDGA 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  691 T-MLTPDRFGAYLLENDITVLFLTTALfnqlaqVRADMFRGlhTLYVGGEALSpalmnAVRhacpdlALHNIYGPTENTT 769
Cdd:cd05968   313 PdHPKADRLWRMVEDHEITHLGLSPTL------IRALKPRG--DAPVNAHDLS-----SLR------VLGSTGEPWNPEP 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  770 FSTFFEMKRDYAGPI--------------------PIgKPISNST------AYILDTKGRLLPIGVpGELCVGGD--GVA 821
Cdd:cd05968   374 WNWLFETVGKGRNPIinysggteisggilgnvlikPI-KPSSFNGpvpgmkADVLDESGKPARPEV-GELVLLAPwpGMT 451

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  822 KGYLNRVD-LTNAVFSPhpfLPGERIYrtGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAA 897
Cdd:cd05968   452 RGFWRDEDrYLETYWSR---FDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 472-966 1.47e-17

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 87.78  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  472 YPKN--HTI------IDLFREQ-AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMIS 542
Cdd:PRK06710   11 YPEEipSTIsydiqpLHKYVEQmASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  543 VLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI-----------VQKGLE----------------QNAAF------ 589
Cdd:PRK06710   91 YYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKiehvivtriadflpfpKNLLYpfvqkk 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  590 --------SGTCIISDAQGLMEENDIPINISSSPD-DLAYIMYTSGSTGRPKGVMITNRNVVS---LVRNSNYTSASGDD 657
Cdd:PRK06710  171 qsnlvvkvSESETIHLWNSVEKEVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSntlMGVQWLYNCKEGEE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  658 rfIMTGSISFdavtFEMFG--ALLNgasLHIIDKSTMLTPDRFGAYLLenditvlflttalFNQLAQVRADMFRGLHTLY 735
Cdd:PRK06710  251 --VVLGVLPF----FHVYGmtAVMN---LSIMQGYKMVLIPKFDMKMV-------------FEAIKKHKVTLFPGAPTIY 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  736 VG--------------------GEALSPALMNAVRHACPDLALHNIYGPTENT--TFSTFFEMKRDyagPIPIGKPISNS 793
Cdd:PRK06710  309 IAllnspllkeydissiracisGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpvTHSNFLWEKRV---PGSIGVPWPDT 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  794 TAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQMK 872
Cdd:PRK06710  386 EAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-------DGWLHTGDVGYMDEDGFFYVKDRKKDMIV 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  873 IRGKRIEPAEIEARLLEMEGVQEaAVTLREKD---GEA-QLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMP 948
Cdd:PRK06710  459 ASGFNVYPREVEEVLYEHEKVQE-VVTIGVPDpyrGETvKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELP 537

                         570
                  ....*....|....*...
gi 499188982  949 LTGNGKIDRSALPIPENK 966
Cdd:PRK06710  538 KTTVGKILRRVLIEEEKR 555
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 621-898 2.90e-17

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


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 84.66  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  621 IMYTSGSTGRPKGVMITNRNVvsLVRNSNY---TSASGDDRFIMTGSIsFDAVTfeMFGALlngASLHIIDKSTMLTpdR 697
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQAL--LAQALVLavlQAIDEGTVFLNSGPL-FHIGT--LMFTL---ATFHAGGTNVFVR--R 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  698 FGAY----LLEND-ITVLFLTTALFNQLAQVRADMFRGLHTLYVGG-----EALSPALMNAVRHACPDlalhniYGPTEN 767
Cdd:cd17636    75 VDAEevleLIEAErCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPaapewNDMATVDTSPWGRKPGG------YGQTEV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 TTFSTFFEMKRDYAGPIpiGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLtNAvfsphpflpgERI- 846
Cdd:cd17636   149 MGLATFAALGGGAIGGA--GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEV-NA----------RRTr 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  847 ---YRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:cd17636   216 ggwHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
616-960 3.24e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 84.71  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  616 DDLAYIMYTSGSTGRPKGVMITNRNVVslvrnsnytsASGD---DRFIMTGSISFDAVTFEMFG------ALLNGASLHI 686
Cdd:PRK07824   35 DDVALVVATSGTTGTPKGAMLTAAALT----------ASADathDRLGGPGQWLLALPAHHIAGlqvlvrSVIAGSEPVE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  687 IDKSTMLTPDRFGAYL--LENDITVLFLTTAlfnQLAQVRADM-----FRGLHTLYVGGEALSPALMNAVRHAcpDLALH 759
Cdd:PRK07824  105 LDVSAGFDPTALPRAVaeLGGGRRYTSLVPM---QLAKALDDPaataaLAELDAVLVGGGPAPAPVLDAAAAA--GINVV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  760 NIYGPTENTtfstffemkrdyAGPIPIGKPISNSTAYILDtkGRLLpigvpgelcVGGDGVAKGYLNRVDltnavfsPHP 839
Cdd:PRK07824  180 RTYGMSETS------------GGCVYDGVPLDGVRVRVED--GRIA---------LGGPTLAKGYRNPVD-------PDP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  840 FL-PGerIYRTGDLARwLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQ-LYTHYVGDH 917
Cdd:PRK07824  230 FAePG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQrVVAAVVGDG 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 499188982  918 KKTDT--DFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK07824  307 GPAPTleALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 503-932 3.34e-17

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


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 86.37  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQKg 582
Cdd:cd05932     8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 LEQNAAFsgtciisdAQGLMEEndiPINISSSP----------------------------DDLAYIMYTSGSTGRPKGV 634
Cdd:cd05932    87 LDDWKAM--------APGVPEG---LISISLPPpsaancqyqwddliaqhppleerptrfpEQLATLIYTSGTTGQPKGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  635 MITNRNVV-SLVRNSNYTSASGDDRfiMTGSISFDAVTFEMF---GALLNGASLHIIDkstmlTPDRFGAYLLENDITVL 710
Cdd:cd05932   156 MLTFGSFAwAAQAGIEHIGTEENDR--MLSYLPLAHVTERVFvegGSLYGGVLVAFAE-----SLDTFVEDVQRARPTLF 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  711 FLTTALFNQLAQ-----------------------VRADMFRGL---HTLYVGGEA--LSPALMNAVRHAcpDLALHNIY 762
Cdd:cd05932   229 FSVPRLWTKFQQgvqdkipqqklnlllkipvvnslVKRKVLKGLgldQCRLAGCGSapVPPALLEWYRSL--GLNILEAY 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  763 GPTENTTFSTffemkrdyagpipIGKPISNSTAYIldtkGRLLP-----IGVPGELCVGGDGVAKGYLNRVDLTNAVFSP 837
Cdd:cd05932   307 GMTENFAYSH-------------LNYPGRDKIGTV----GNAGPgvevrISEDGEILVRSPALMMGYYKDPEATAEAFTA 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  838 HPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKI-RGKRIEPAEIEARLLEMEGVQEAAVT---LREKDGEAQLYThy 913
Cdd:cd05932   370 DGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIgsgLPAPLALVVLSE-- 441

                         490
                  ....*....|....*....
gi 499188982  914 vGDHKKTDTDFRADLARVL 932
Cdd:cd05932   442 -EARLRADAFARAELEASL 459
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 48-339 3.52e-17

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


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 85.99  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   48 IKGSLSYDWFQRSIQAIIDRHDIFRTVFlphvphlSGPRQVVmteREFHLNSEDIS-HLP--TNDQNEYIERFKEKDKQK 124
Cdd:cd19546    35 LRGRLDRDALEAALGDVAARHEILRTTF-------PGDGGDV---HQRILDADAARpELPvvPATEEELPALLADRAAHL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  125 gFDLQKDMLMRISLFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHAGK-----PLSLDpvrpYSTYISW--- 196
Cdd:cd19546   105 -FDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRaperaPLPLQ----FADYALWere 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  197 LTN--RDKEKAA----AYWDTYLKNYSAPSPLPRVSDKETKESyHREDLI-FSLNKPLTDKLKETAKQHGVTLATLIQAV 269
Cdd:cd19546   180 LLAgeDDRDSLIgdqiAYWRDALAGAPDELELPTDRPRPVLPS-RRAGAVpLRLDAEVHARLMEAAESAGATMFTVVQAA 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  270 WGVMLQQYNRTDDVVFGAVVSgRPSEIPGVEQMIGLFINTIPIRIKTHQDETFHELLIRCQKEMLEAE-----PF 339
Cdd:cd19546   259 LAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARrhqdvPF 332
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 472-960 4.09e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 86.22  E-value: 4.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  472 YPKNHtiidlfreqAEKTPDHTALVYGNM--SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PRK13390    2 YPGTH---------AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCI---ISDAQGLMEENDIPINISSSPDDL------AY 620
Cdd:PRK13390   73 GLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLplrLSFGGEIDGFGSFEAALAGAGPRLteqpcgAV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  621 IMYTSGSTGRPKGVM--ITNRNVvslvrnsnytSASGDDRFIMTGSIsFDAVTFEMF---GALLNGASL------HIIDK 689
Cdd:PRK13390  153 MLYSSGTTGFPKGIQpdLPGRDV----------DAPGDPIVAIARAF-YDISESDIYyssAPIYHAAPLrwcsmvHALGG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  690 STMLTpDRFGA-----YLLENDITVLFLTTALFNQLAQVRADMFR--GLHTLYVGGEALSPALMNaVRHACPDL---ALH 759
Cdd:PRK13390  222 TVVLA-KRFDAqatlgHVERYRITVTQMVPTMFVRLLKLDADVRTryDVSSLRAVIHAAAPCPVD-VKHAMIDWlgpIVY 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  760 NIYGPTENTTFsTFFEMKRDYAGPIPIGKPISnSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSP-H 838
Cdd:PRK13390  300 EYYSSTEAHGM-TFIDSPDWLAHPGSVGRSVL-GDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaH 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  839 PFLPgeriyRTGDLARWLPDGnleYISRIDRQ--MKIRGK-RIEPAEIEARLLEMEGVQEAAVT---LREKDGEAQLYTH 912
Cdd:PRK13390  378 PFWT-----TVGDLGSVDEDG---YLYLADRKsfMIISGGvNIYPQETENALTMHPAVHDVAVIgvpDPEMGEQVKAVIQ 449

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  913 YVGDHKKTDtdfraDLARVLPDYM--------IPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK13390  450 LVEGIRGSD-----ELARELIDYTrsriahykAPRSVEFVDELPRTPTGKLVKGLL 500
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 621-957 4.62e-17

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


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 83.86  E-value: 4.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  621 IMYTSGSTGRPKGVMITNRNVVSLVRNSNYT-SASGDDR-------FIMTGSIsfdaVTFEMFGAllnGASLHIIDKstm 692
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAmGLTEADVylnmlplFHIAGLN----LALATFHA---GGANVVMEK--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFRGLHTL-YVGG-EAlsPALMNAVrHACPDLALHNIYGPTEN--- 767
Cdd:cd17637    75 FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrHVLGlDA--PETIQRF-EETTGATFWSLYGQTETsgl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 TTFSTFFEMkrdyagPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSP--Hpflpger 845
Cdd:cd17637   152 VTLSPYRER------PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNgwH------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  846 iyRTGDLARWLPDGNLEYISRIDRQMKIR--GKRIEPAEIEARLLEMEGVQEAAV----------------TLREKDG-E 906
Cdd:cd17637   219 --HTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVigvpdpkwgegikavcVLKPGATlT 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499188982  907 AQLYTHYVGDHkktdtdfradLARvlpdYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd17637   297 ADELIEFVGSR----------IAR----YKKPRYVVFVEALPKTADGSIDR 333
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 471-898 5.25e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 85.90  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  471 EYPKNHtiidlfreqAEKTPDHTALVYGNM--SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLK 548
Cdd:PRK13391    1 MYPGIH---------AQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AGGAYLPLDAELPPERVSFMLEETQAKMLI-------VQKGLEQNAAFSGTCIISDAQGLME-----------ENDIPIN 610
Cdd:PRK13391   72 SGLYYTCVNSHLTPAEAAYIVDDSGARALItsaakldVARALLKQCPGVRHRLVLDGDGELEgfvgyaeavagLPATPIA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  611 ISSSPDDLayiMYTSGSTGRPKGVM-------------ITN--RNVVSLVRNSNYTSA-----SGDDRFIMTG-SISFDA 669
Cdd:PRK13391  152 DESLGTDM---LYSSGTTGRPKGIKrplpeqppdtplpLTAflQRLWGFRSDMVYLSPaplyhSAPQRAVMLViRLGGTV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  670 VTFEMFGAllnGASLHIIDK----STMLTPDRFGAYL-LENDItvlflttalfnqlaQVRADmfrgLHTLYVGGEALSPa 744
Cdd:PRK13391  229 IVMEHFDA---EQYLALIEEygvtHTQLVPTMFSRMLkLPEEV--------------RDKYD----LSSLEVAIHAAAP- 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  745 lmnavrhaCPDLA-----------LHNIYGPTENTTFsTFFEMKRDYAGPIPIGKPISnSTAYILDTKGRLLPIGVPGEL 813
Cdd:PRK13391  287 --------CPPQVkeqmidwwgpiIHEYYAATEGLGF-TACDSEEWLAHPGTVGRAMF-GDLHILDDDGAELPPGEPGTI 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  814 CVGGdGVAKGYLNRVDLTNAVFSPHPFLPgeriyRTGDLARWLPDGnleYISRIDRQ--MKIRGK-RIEPAEIEARLLEM 890
Cdd:PRK13391  357 WFEG-GRPFEYLNDPAKTAEARHPDGTWS-----TVGDIGYVDEDG---YLYLTDRAafMIISGGvNIYPQEAENLLITH 427


                  ....*...
gi 499188982  891 EGVQEAAV 898
Cdd:PRK13391  428 PKVADAAV 435
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 502-898 5.99e-17

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: 84.93  E-value: 5.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQK 581
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  582 gleqnaafsgtciisdaqglmeendipiniSSSPDDLAYIMYTSGSTGRPKGVMITNRNV-VSLVRNSNYTSASGDDRFI 660
Cdd:cd05974    81 ------------------------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIGLKPGDVHW 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  661 MTGSISFDAVTFEMFGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFR-GLHTLYVGGE 739
Cdd:cd05974   131 NISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLREVVGAGE 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  740 ALSPALMNAVRHACpDLALHNIYGPTENTTFSTFFEMKRDYAGPIpiGKPISNSTAYILDTKGRllpIGVPGELCVG-GD 818
Cdd:cd05974   211 PLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQPVKAGSM--GRPLPGYRVALLDPDGA---PATEGEVALDlGD 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  819 ----GVAKGYLNRVDLTNAVFsphpflpGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQ 894
Cdd:cd05974   285 trpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVA 357


                  ....
gi 499188982  895 EAAV 898
Cdd:cd05974   358 EAAV 361
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 477-960 6.21e-17

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 86.03  E-value: 6.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALAREL-----IQKGFRknetagiLAAHSP---EFMISVLAVLK 548
Cdd:PRK12492   25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLqqhtdLVPGDR-------IAVQMPnvlQYPIAVFGALR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AG----------------------GA----YLPLDAE-----LPPERVSFMLEETQAKMLIVQKGLEQNA---------- 587
Cdd:PRK12492   98 AGlivvntnplytaremrhqfkdsGAralvYLNMFGKlvqevLPDTGIEYLIEAKMGDLLPAAKGWLVNTvvdkvkkmvp 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  588 AFSGTCIISDAQGLMEENDIPIN-ISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGDD-------- 657
Cdd:PRK12492  178 AYHLPQAVPFKQALRQGRGLSLKpVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnMLQVRACLSQLGPDgqplmkeg 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  658 RFIMTGSISFdavtFEMFGALLNGASLHIIDKSTMLTPD--------------RFGAYLLENDITVLFLTTALFNQLAqv 723
Cdd:PRK12492  258 QEVMIAPLPL----YHIYAFTANCMCMMVSGNHNVLITNprdipgfikelgkwRFSALLGLNTLFVALMDHPGFKDLD-- 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  724 radmFRGLHTLYVGGEALSPAlmNAVRHA----CpdlALHNIYGPTENTTFST---FFEMKRdyAGPIpiGKPISNSTAY 796
Cdd:PRK12492  332 ----FSALKLTNSGGTALVKA--TAERWEqltgC---TIVEGYGLTETSPVAStnpYGELAR--LGTV--GIPVPGTALK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  797 ILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVfsphpfLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGK 876
Cdd:PRK12492  399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAV--TLREKDGEAQLYTHYVGDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGK 954
Cdd:PRK12492  473 NVYPNEIEDVVMAHPKVANCAAigVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552


                  ....*.
gi 499188982  955 IDRSAL 960
Cdd:PRK12492  553 ILRREL 558
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 614-956 7.20e-17

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 83.97  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 SPDDLaYIMYTSGSTGRPKGVM-------ITNRNVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHI 686
Cdd:cd05924     2 SADDL-YILYTGGTTGMPKGVMwrqedifRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  687 IDKSTMLTPD-RFGAYLL-----ENDITVLFLT-----TALFNQLAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPD 755
Cdd:cd05924    81 LGGQTVVLPDdRFDPEEVwrtieKHKVTSMTIVgdamaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  756 LALHNIYGPTEnttfsTFFEMKRDYAGPIPIGKP--ISNSTAYILDTKGRLLPIGVPGELCVGGDG-VAKGYLNRVDLTN 832
Cdd:cd05924   161 ITLVDAFGSSE-----TGFTGSGHSAGSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  833 AVFsphPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGE---- 906
Cdd:cd05924   236 ETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpdERWGQevva 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499188982  907 -AQLYThyvgDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:cd05924   313 vVQLRE----GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
476-960 1.45e-16

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 84.72  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFREQAEKTPDHTALVygNMS--ISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGA 552
Cdd:PRK08974   23 QSLVDMFEQAVARYADQPAFI--NMGevMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  553 -------YLP--LDAELPP----------------ERVSFmleETQAKMLIVQKGLEQNAAFSGTC---IISDAQGLMEE 604
Cdd:PRK08974  101 vvnvnplYTPreLEHQLNDsgakaivivsnfahtlEKVVF---KTPVKHVILTRMGDQLSTAKGTLvnfVVKYIKRLVPK 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  605 NDIPINIS-----------------SSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASgddrFIMTGSISf 667
Cdd:PRK08974  178 YHLPDAISfrsalhkgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGP----LLHPGKEL- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  668 dAVT----FEMFGALLNGA-SLHIIDKSTMLTPDR----FGAYLLENDITVLFLTTALFNQLaqVRADMFRGLH----TL 734
Cdd:PRK08974  253 -VVTalplYHIFALTVNCLlFIELGGQNLLITNPRdipgFVKELKKYPFTAITGVNTLFNAL--LNNEEFQELDfsslKL 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  735 YVGGEAlspALMNAVRHACPDLALHNI---YGPTENTTFSTF--FEMKrDYAGPIpiGKPISNSTAYILDTKGRLLPIGV 809
Cdd:PRK08974  330 SVGGGM---AVQQAVAERWVKLTGQYLlegYGLTECSPLVSVnpYDLD-YYSGSI--GLPVPSTEIKLVDDDGNEVPPGE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  810 PGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLE 889
Cdd:PRK08974  404 PGELWVKGPQVMLGYWQRPEATDEVIK-------DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499188982  890 MEGVQEAAVTLREKDGEAQLYTHYV--GDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK08974  477 HPKVLEVAAVGVPSEVSGEAVKIFVvkKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 615-960 1.49e-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: 82.91  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIMTGSISF--DAVTFEMFGALLNGASLHIIDKSTM 692
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGPAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTPDRFGAY--LLEN-DITVLFLTTALFNQLAQV--RADMfRGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGPTEN 767
Cdd:cd05944    81 RNPGLFDNFwkLVERyRITSLSTVPTVYAALLQVpvNADI-SSLRFAMSGAAPLPVELRARFEDAT-GLPVVEGYGLTEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 TTFSTffemkRDY-AGPIPIGK-----PISNSTAYILDTKGRLL-PIGVP--GELCVGGDGVAKGYLNRVDLTNAvfsph 838
Cdd:cd05944   159 TCLVA-----VNPpDGPKRPGSvglrlPYARVRIKVLDGVGRLLrDCAPDevGEICVAGPGVFGGYLYTEGNKNA----- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  839 pfLPGERIYRTGDLARWLPDGNLeYISRIDRQMKIR-GKRIEPAEIEARLLEMEGVQEAAVTLR--EKDGEAQL-YTHYV 914
Cdd:cd05944   229 --FVADGWLNTGDLGRLDADGYL-FITGRAKDLIIRgGHNIDPALIEEALLRHPAVAFAGAVGQpdAHAGELPVaYVQLK 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 499188982  915 GDHKKTDTDFRADLARVLPDY-MIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05944   306 PGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 617-955 1.68e-16

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: 82.16  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFIMTGSIsfdavtFEMFG-------ALLNGASL---H 685
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAwADCADLTEDDRYLIINPF------FHTFGykagivaCLLTGATVvpvA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  686 IIDKSTMLtpdrfgaYLLEND-ITVLFLTTALFNQLAQVRADMFRGLHTLYV---GGEALSPALMNAVRHACPDLALHNI 761
Cdd:cd17638    75 VFDVDAIL-------EAIERErITVLPGPPTLFQSLLDHPGRKKFDLSSLRAavtGAATVPVELVRRMRSELGFETVLTA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  762 YGPTEnttfstffemkrdyAGPIPIGKPiSNSTAYILDTKGRLLP-----IGVPGELCVGGDGVAKGYLNRVDLTNAVFS 836
Cdd:cd17638   148 YGLTE--------------AGVATMCRP-GDDAETVATTCGRACPgfevrIADDGEVLVRGYNVMQGYLDDPEATAEAID 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  837 PHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGD 916
Cdd:cd17638   213 ADGWL------HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 499188982  917 HKK---TDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:cd17638   287 RPGvtlTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 502-887 2.35e-16

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 84.40  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIV-Q 580
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 KGLEQNAAFSGT--------CI---------------------ISDAQGLMEENDIPINISSsPDDLAYIMYTSGSTGRP 631
Cdd:PLN02387  187 KQLKKLIDISSQletvkrviYMddegvdsdsslsgssnwtvssFSEVEKLGKENPVDPDLPS-PNDIAVIMYTSGSTGLP 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  632 KGVMITNRNVVSLVrnSNYTSA----SGDDRFIM------TGSISFDAVTFEMFGALLNGASLHIIDKS----------- 690
Cdd:PLN02387  266 KGVMMTHGNIVATV--AGVMTVvpklGKNDVYLAylplahILELAAESVMAAVGAAIGYGSPLTLTDTSnkikkgtkgda 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  691 TMLTP----------DR-----------------------------------FGAYLLENditvLFLTTALFNQLAQVRA 725
Cdd:PLN02387  344 SALKPtlmtavpailDRvrdgvrkkvdakgglakklfdiaykrrlaaiegswFGAWGLEK----LLWDALVFKKIRAVLG 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  726 DMFRGlhtLYVGGEALSP---ALMNavrhACPDLALHNIYGPTENTTFSTFFEMKRDYAGpiPIGKPISNSTAYILD-TK 801
Cdd:PLN02387  420 GRIRF---MLSGGAPLSGdtqRFIN----ICLGAPIGQGYGLTETCAGATFSEWDDTSVG--RVGPPLPCCYVKLVSwEE 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  802 GRLLPIGVP---GELCVGGDGVAKGYLNRVDLTNAVFSPHPflPGERIYRTGDLARWLPDGNLEYISRIDRQMKIR-GKR 877
Cdd:PLN02387  491 GGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEY 568

                         490
                  ....*....|
gi 499188982  878 IEPAEIEARL 887
Cdd:PLN02387  569 VSLGKVEAAL 578
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 502-854 9.52e-16

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 82.09  E-value: 9.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLP-------LDAELppERVSFMLEETQA 574
Cdd:cd05921    26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPvspayslMSQDL--AKLKHLFELLKP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  575 KMLIVQKGleqnAAFS---------GTCIISDAQGLMEENDI--------PINISS-------SPDDLAYIMYTSGSTGR 630
Cdd:cd05921   104 GLVFAQDA----APFAralaaifplGTPLVVSRNAVAGRGAIsfaelaatPPTAAVdaafaavGPDTVAKFLFTSGSTGL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  631 PKGVMITNRNVVS--LVRNSNYTSASGDDRFI---------MTGSISFDAVtfemfgaLLNGASLHIIDKSTMltPDRFG 699
Cdd:cd05921   180 PKAVINTQRMLCAnqAMLEQTYPFFGEEPPVLvdwlpwnhtFGGNHNFNLV-------LYNGGTLYIDDGKPM--PGGFE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  700 ---AYLLENDITVLFLTTALFNQLAQ-------VRADMFRGLHTLYVGGEALSPALMN-----AVRHACPDLALHNIYGP 764
Cdd:cd05921   251 etlRNLREISPTVYFNVPAGWEMLVAalekdeaLRRRFFKRLKLMFYAGAGLSQDVWDrlqalAVATVGERIPMMAGLGA 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  765 TENTTFSTFFEMKRDYAGpiPIGKPISNSTAyildtkgRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpge 844
Cdd:cd05921   331 TETAPTATFTHWPTERSG--LIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF---- 397

                         410
                  ....*....|
gi 499188982  845 riYRTGDLAR 854
Cdd:cd05921   398 --YCLGDAAK 405
PRK09274 PRK09274
peptide synthase; Provisional
 482-861 3.07e-15

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 80.33  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  482 FREQAEKTPDHTALV----------YGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGG 551
Cdd:PRK09274   12 LPRAAQERPDQLAVAvpggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  552 AYLPLD------------AELPPE-----------RVSFMLEETQAKMLIVqkgLEQNAAFSGTCIISDAQGLMEENDIP 608
Cdd:PRK09274   92 VPVLVDpgmgiknlkqclAEAQPDafigipkahlaRRLFGWGKPSVRRLVT---VGGRLLWGGTTLATLLRDGAAAPFPM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  609 INisSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVrnsnytSASGDDRFIMTGSIsfDAVTF---EMFGALLNGASlh 685
Cdd:PRK09274  169 AD--LAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQI------EALREDYGIEPGEI--DLPTFplfALFGPALGMTS-- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  686 II---DKSTMLT--PDRFGAYLLENDITVLFLTTALFNQLAQ---VRADMFRGLHTLYVGGEALSPALMNAVRHACPDLA 757
Cdd:PRK09274  237 VIpdmDPTRPATvdPAKLFAAIERYGVTNLFGSPALLERLGRygeANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  758 -LHNIYGPTE---------NTTFSTFFEMKRDYAGpIPIGKPISNSTAYILD---------TKGRLLPIGVPGELCVGGD 818
Cdd:PRK09274  317 eILTPYGATEalpissiesREILFATRAATDNGAG-ICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGP 395

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 499188982  819 GVAKGYLNRVDLT--NAVFSPHpflpGERIYRTGDLARWLPDGNL 861
Cdd:PRK09274  396 MVTRSYYNRPEATrlAKIPDGQ----GDVWHRMGDLGYLDAQGRL 436
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 503-866 7.25e-15

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 78.66  E-value: 7.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGgaylpldaelppervsfmleetqAKMLIVQKG 582
Cdd:cd05910     4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAG-----------------------AVPVLIDPG 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  583 LEQNAAfsGTCIIsDAqglmeENDIPINISSSpDDLAYIMYTSGSTGRPKGVMITNRNVVSLVrnsnytSASGDDRFIMT 662
Cdd:cd05910    61 MGRKNL--KQCLQ-EA-----EPDAFIGIPKA-DEPAAILFTSGSTGTPKGVVYRHGTFAAQI------DALRQLYGIRP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  663 GSISFDAVT-FEMFGALLNGASlhIIDKSTMLTPDR------FGAyLLENDITVLFLTTALFNQLAQVRADMFRGLHTL- 734
Cdd:cd05910   126 GEVDLATFPlFALFGPALGLTS--VIPDMDPTRPARadpqklVGA-IRQYGVSIVFGSPALLERVARYCAQHGITLPSLr 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  735 --YVGGEALSPALMNAVRHACPDLA-LHNIYGPTE---------NTTFSTFFEMKRDYAGpIPIGKPISNSTAYILD--- 799
Cdd:cd05910   203 rvLSAGAPVPIALAARLRKMLSDEAeILTPYGATEalpvssigsRELLATTTAATSGGAG-TCVGRPIPGVRVRIIEidd 281

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  800 ------TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHpflPGERI-YRTGDLARWLPDGNLEYISR 866
Cdd:cd05910   282 epiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDEGRLWFCGR 352
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 473-960 7.37e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 79.22  E-value: 7.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNH---TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEfMISV-LAVLK 548
Cdd:PRK08162   12 AANYvplTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAhFGVPM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AGGAYLPLDAELPPERVSFMLEETQAKMLIVqkgleqNAAFSGtcIISDAQGLMEENDIP-INISSSPD----------- 616
Cdd:PRK08162   91 AGAVLNTLNTRLDAASIAFMLRHGEAKVLIV------DTEFAE--VAREALALLPGPKPLvIDVDDPEYpggrfigaldy 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 ---------DLAYIM-----------YTSGSTGRPKGVMITNRNVvslvrnsnYTSASGDdrfIMTGSISFDAV---TFE 673
Cdd:PRK08162  163 eaflasgdpDFAWTLpadewdaialnYTSGTTGNPKGVVYHHRGA--------YLNALSN---ILAWGMPKHPVylwTLP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  674 MFGAllNG----------ASLHI----IDKSTMLTPDRfgayllENDIT-------VLfltTALFNQLAQVRADMFRGLH 732
Cdd:PRK08162  232 MFHC--NGwcfpwtvaarAGTNVclrkVDPKLIFDLIR------EHGVThycgapiVL---SALINAPAEWRAGIDHPVH 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  733 TLyVGGEALSPALMNAVRHACPDLaLHnIYGPTENTTFSTFFEMKRDYAGpIPIGK------------PISNSTAyILDT 800
Cdd:PRK08162  301 AM-VAGAAPPAAVIAKMEEIGFDL-TH-VYGLTETYGPATVCAWQPEWDA-LPLDEraqlkarqgvryPLQEGVT-VLDP 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  801 KgRLLPigVP------GELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGDLARWLPDGnleYISRIDRQMKI- 873
Cdd:PRK08162  376 D-TMQP--VPadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDG---YIKIKDRSKDIi 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  874 --RGKRIEPAEIEARLLEMEGVQEAAVTLRE--------------KDG----EAQLYTHyvgdhkktdtdFRADLARvlp 933
Cdd:PRK08162  443 isGGENISSIEVEDVLYRHPAVLVAAVVAKPdpkwgevpcafvelKDGasatEEEIIAH-----------CREHLAG--- 508

                         570       580
                  ....*....|....*....|....*..
gi 499188982  934 dYMIPQHwVRVERMPLTGNGKIDRSAL 960
Cdd:PRK08162  509 -FKVPKA-VVFGELPKTSTGKIQKFVL 533
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 495-898 8.46e-15

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 78.79  E-value: 8.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  495 LVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQA 574
Cdd:PRK08276    5 MAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  575 KMLIV---------------QKGLEQNAAFSGTC--IISDAQGLMEENDIPINISSSPDDLAyimYTSGSTGRPKGV--- 634
Cdd:PRK08276   85 KVLIVsaaladtaaelaaelPAGVPLLLVVAGPVpgFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGIkrp 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  635 --------------------MITNRNVVSLVRNSNYTSASGddRFIMTgsisfdavtfemfgALLNGASLHIIDKstmLT 694
Cdd:PRK08276  162 lpgldpdeapgmmlallgfgMYGGPDSVYLSPAPLYHTAPL--RFGMS--------------ALALGGTVVVMEK---FD 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 PDRFGAYLLENDITVLFLTTALFNQL----AQVRA--DmfrglhtlyvggeaLSPalMNAVRHA---CPD---------- 755
Cdd:PRK08276  223 AEEALALIERYRVTHSQLVPTMFVRMlklpEEVRAryD--------------VSS--LRVAIHAaapCPVevkramidww 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  756 -LALHNIYGPTE--NTTFSTffemKRDYAG-PIPIGKPISnSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLT 831
Cdd:PRK08276  287 gPIIHEYYASSEggGVTVIT----SEDWLAhPGSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKT 361

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499188982  832 NAVFSPHPFlpgeriYRTGDLArWL-PDGNLeYISriDRQ--MKIRGK-RIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK08276  362 AAARNPHGW------VTVGDVG-YLdEDGYL-YLT--DRKsdMIISGGvNIYPQEIENLLVTHPKVADVAV 422
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 502-904 1.02e-14

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


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 79.00  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI--- 578
Cdd:cd17641    12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIaed 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  579 ---VQKGLEQNAAFSGT--CIISDAQGlMEENDIPINIS-------------------------SSPDDLAYIMYTSGST 628
Cdd:cd17641    92 eeqVDKLLEIADRIPSVryVIYCDPRG-MRKYDDPRLISfedvvalgraldrrdpglyerevaaGKGEDVAVLCTTSGTT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  629 GRPKGVMITNRNVVSlvRNSNYTSAS----GDDRFIMtgsISFDAVTFEMFG---ALLNGASLHIIDKSTMLTPDrfgay 701
Cdd:cd17641   171 GKPKLAMLSHGNFLG--HCAAYLAADplgpGDEYVSV---LPLPWIGEQMYSvgqALVCGFIVNFPEEPETMMED----- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  702 LLENDITVLFLTTALF-NQLAQVRADM----------------------------------------------------- 727
Cdd:cd17641   241 LREIGPTFVLLPPRVWeGIAADVRARMmdatpfkrfmfelgmklglraldrgkrgrpvslwlrlaswladallfrplrdr 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  728 --FRGLHTLYVGGEALSPALMNAVRHAcpDLALHNIYGPTENTTFSTffeMKRDyaGPIP---IGKPISNSTAYILDTkg 802
Cdd:cd17641   321 lgFSRLRSAATGGAALGPDTFRFFHAI--GVPLKQLYGQTELAGAYT---VHRD--GDVDpdtVGVPFPGTEVRIDEV-- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  803 rllpigvpGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKI-RGKRIEPA 881
Cdd:cd17641   392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQ 457

                         490       500
                  ....*....|....*....|...
gi 499188982  882 EIEARLLEMEGVQEAAVTLREKD 904
Cdd:cd17641   458 FIENKLKFSPYIAEAVVLGAGRP 480
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 477-960 1.13e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 78.91  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:PLN03102   15 TPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGLEQNAAFSGTCIISDAQGL------MEENDIPINISS--------------SPD 616
Cdd:PLN03102   95 NTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLnlpvifIHEIDFPKRPSSeeldyecliqrgepTPS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  617 DLAYIM------------YTSGSTGRPKGVMITNRNVvslvrnsnYTSASGDDRFIMTGSISFDAVTFEMF--------- 675
Cdd:PLN03102  175 LVARMFriqdehdpislnYTSGTTADPKGVVISHRGA--------YLSTLSAIIGWEMGTCPVYLWTLPMFhcngwtftw 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  676 GALLNGASLHIIDKSTmlTPDRFGAYLLENdITVLFLTTALFNQLAQ-VRADMFRGLHTLYV--GGEALSPALMNAVRHa 752
Cdd:PLN03102  247 GTAARGGTSVCMRHVT--APEIYKNIEMHN-VTHMCCVPTVFNILLKgNSLDLSPRSGPVHVltGGSPPPAALVKKVQR- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 cpdLALH--NIYGPTENTTFSTFFEMKRDYaGPIPIGKP--------ISNSTAYILDTKGRLLPIGVP------GELCVG 816
Cdd:PLN03102  323 ---LGFQvmHAYGLTEATGPVLFCEWQDEW-NRLPENQQmelkarqgVSILGLADVDVKNKETQESVPrdgktmGEIVIK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  817 GDGVAKGYLNRVDLTNAVFSpHPFLpgeriyRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEA 896
Cdd:PLN03102  399 GSSIMKGYLKNPKATSEAFK-HGWL------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  897 AVTLRE--------------KDGEaqlyTHYVGDHKKTDTDFRaDLARV----LPDYMIPQHWVRVERMPLTGNGKIDRS 958
Cdd:PLN03102  472 AVVAMPhptwgetpcafvvlEKGE----TTKEDRVDKLVTRER-DLIEYcrenLPHFMCPRKVVFLQELPKNGNGKILKP 546


                  ..
gi 499188982  959 AL 960
Cdd:PLN03102  547 KL 548
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 480-898 1.54e-14

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 78.52  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALvyGNMSIS-----------YKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLK 548
Cdd:PLN02614   49 DVFRMSVEKYPNNPML--GRREIVdgkpgkyvwqtYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  549 AGGAYLPLDAELPPERVSFMLEETQAKMLIVQ---------------KGLEQNAAFSGtciISDAQ-------GLM---- 602
Cdd:PLN02614  127 HGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEekkiselfktcpnstEYMKTVVSFGG---VSREQkeeaetfGLViyaw 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  603 ---------EENDIPINissSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLV-------RNSNyTSASGDDRFIMTGSIS 666
Cdd:PLN02614  204 deflklgegKQYDLPIK---KKSDICTIMYTSGTTGDPKGVMISNESIVTLIagvirllKSAN-AALTVKDVYLSYLPLA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  667 --FDAVTFEMFgaLLNGASLH--------IIDKSTMLTPDRF--------------------GAYLLENDITVLF----- 711
Cdd:PLN02614  280 hiFDRVIEECF--IQHGAAIGfwrgdvklLIEDLGELKPTIFcavprvldrvysglqkklsdGGFLKKFVFDSAFsykfg 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  712 ---------LTTALFNQL--AQVRADMFRGLHTLYVGGEALSPALMNAVR-HACPDLAlhNIYGPTENT--TFSTFFEmK 777
Cdd:PLN02614  358 nmkkgqshvEASPLCDKLvfNKVKQGLGGNVRIILSGAAPLASHVESFLRvVACCHVL--QGYGLTESCagTFVSLPD-E 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  778 RDYAGpiPIGKPISN---STAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLAR 854
Cdd:PLN02614  435 LDMLG--TVGPPVPNvdiRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGE 505

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 499188982  855 WLPDGNLEYISRIDRQMKI-RGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PLN02614  506 WQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWV 550
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 471-855 1.64e-14

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 78.38  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  471 EYPknHTIIDLFREQAEKTPDHTALVY-----GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLA 545
Cdd:PRK08180   36 DYP--RRLTDRLVHWAQEAPDRVFLAErgadgGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  546 VLKAGGAYLPLDaelPP--------ERVSFMLEETQAKMLIVQKGleqnAAFS---------GTCIISDA---------- 598
Cdd:PRK08180  114 AMYAGVPYAPVS---PAyslvsqdfGKLRHVLELLTPGLVFADDG----AAFAralaavvpaDVEVVAVRgavpgraatp 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  599 -QGLMEENDIP----INISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSlvrNSNYTSASGDDrFIMTGSISFDAV--- 670
Cdd:PRK08180  187 fAALLATPPTAavdaAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCA---NQQMLAQTFPF-LAEEPPVLVDWLpwn 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  671 -TF---EMFG-ALLNGASLHIID-KSTmltPDRFGAyLLEN--DI--TVLFLTTALFNQL-------AQVRADMFRGLHT 733
Cdd:PRK08180  263 hTFggnHNLGiVLYNGGTLYIDDgKPT---PGGFDE-TLRNlrEIspTVYFNVPKGWEMLvpalerdAALRRRFFSRLKL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  734 LYVGGEALSPALMN-----AVRHACPDLALHNIYGPTENTTFSTFFEMKRDYAGPIpiGKPISNSTAYILDTKGRLlpig 808
Cdd:PRK08180  339 LFYAGAALSQDVWDrldrvAEATCGERIRMMTGLGMTETAPSATFTTGPLSRAGNI--GLPAPGCEVKLVPVGGKL---- 412

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 499188982  809 vpgELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLARW 855
Cdd:PRK08180  413 ---EVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 483-960 5.52e-14

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: 76.35  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  483 REQAEKTPDHTALVYGN-----MSISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPL 556
Cdd:cd05928    18 KEKAGKRPPNPALWWVNgkgdeVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  557 DAELPPERVSFMLEETQAKMLIVQKGLEQNA-AFSGTC-------IISDA--------QGLMEE-NDIPINISSSPDDLA 619
Cdd:cd05928    98 TIQLTAKDILYRLQASKAKCIVTSDELAPEVdSVASECpslktklLVSEKsrdgwlnfKELLNEaSTEHHCVETGSQEPM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  620 YIMYTSGSTGRPKGVMITNRNV-VSLVRNSNYTSA--SGDDRFIMTGSISFDAVTFEMFGALLNGASL--HIIDKstmLT 694
Cdd:cd05928   178 AIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDltASDIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHHLPR---FD 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 PDRFGAYLLENDITVLFLTTALFNQLAQ--VRADMFRGLHTLYVGGEALSPALMNAVRHACpDLALHNIYGPTENT-TFS 771
Cdd:cd05928   255 PLVILKTLSSYPITTFCGAPTVYRMLVQqdLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQT-GLDIYEGYGQTETGlICA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  772 TFFEMKrdyAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELC--VGGD---GVAKGYLNRVDLTNAVFSphpflpGErI 846
Cdd:cd05928   334 NFKGMK---IKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGirVKPIrpfGLFSGYVDNPEKTAATIR------GD-F 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  847 YRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT-----LRekdGE---------AQLYTH 912
Cdd:cd05928   404 YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVsspdpIR---GEvvkafvvlaPQFLSH 480

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 499188982  913 yvgDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05928   481 ---DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 982-1041 9.39e-14

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: 66.82  E-value: 9.39e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499188982   982 EELANIWKQVLGVNT--ISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQ 1041
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 494-955 9.94e-14

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 75.51  E-value: 9.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  494 ALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQ 573
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  574 AKMLIVQKGL---------------------EQNAAFSgtciISDAQGLMEENDI----------PINISSSPDDLAYIm 622
Cdd:PRK12406   84 ARVLIAHADLlhglasalpagvtvlsvptppEIAAAYR----ISPALLTPPAGAIdwegwlaqqePYDGPPVPQPQSMI- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  623 YTSGSTGRPKGVMITNRN-----VVSLVRNSNYTSASGDdRFIMTGSISFDAV-TFEMFGALLnGASLHIIDKstmLTPD 696
Cdd:PRK12406  159 YTSGTTGHPKGVRRAAPTpeqaaAAEQMRALIYGLKPGI-RALLTGPLYHSAPnAYGLRAGRL-GGVLVLQPR---FDPE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGAYLLENDITVLFLTTALFNQL----AQVRA--DMFRGLHTlyVGGEALSPAlmnAVRHACPDL---ALHNIYGPTEn 767
Cdd:PRK12406  234 ELLQLIERHRITHMHMVPTMFIRLlklpEEVRAkyDVSSLRHV--IHAAAPCPA---DVKRAMIEWwgpVIYEYYGSTE- 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  768 TTFSTFFEMKRDYAGPIPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAK-GYLNRVDLTNAVfsphpflpgER- 845
Cdd:PRK12406  308 SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI---------DRg 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  846 -IYRTGDLARWLPDGNLeYISRIDRQMKIRGK-RIEPAEIEARLLEMEGVQEAAV--TLREKDGEAQLYthYVGDHKKTD 921
Cdd:PRK12406  379 gFITSGDVGYLDADGYL-FLCDRKRDMVISGGvNIYPAEIEAVLHAVPGVHDCAVfgIPDAEFGEALMA--VVEPQPGAT 455

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 499188982  922 TD---FRADLARVLPDYMIPQHWVRVERMPLTGNGKI 955
Cdd:PRK12406  456 LDeadIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 976-1050 1.18e-13

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: 67.19  E-value: 1.18e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499188982  976 PRNLVEEELANIWKQVLGVN--TISIDDDFFA-IGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKLYSKQ 1050
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PRK12316 PRK12316
peptide synthase; Provisional
 58-255 1.23e-13

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 76.53  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   58 QRSIQAIIDRHDIFRTVFLPHVPHLSGpRQVVMTEREFHLNSEDIshlptnDQNEYIERFKEkDKQKGFDLQKDMLMRIS 137
Cdd:PRK12316 3677 EAALQALVEHHDALRLRFVEDAGGWTA-EHLPVELGGALLWRAEL------DDAEELERLGE-EAQRSLDLADGPLLRAL 3748

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  138 LFKTAKDEHVCIWSHHHILMDGWCLGIVMQEFMQIYQSIHAGKPLSLdPVRP--YSTYISWLTN--RDKEKAA--AYWDT 211
Cdd:PRK12316 3749 LATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRL-PAKTssFKAWAERLQEhaRGEALKAelAYWQE 3827

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 499188982  212 YLKNysAPSPLPRVSDKETKESYHREDLIFSLNKPLTDKLKETA 255
Cdd:PRK12316 3828 QLQG--VSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQA 3869
PRK09192 PRK09192
fatty acyl-AMP ligase;
504-959 1.50e-13

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 75.04  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  504 YKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLdaELPP---------ERVSFMLEETQA 574
Cdd:PRK09192   52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMgfggresyiAQLRGMLASAQP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  575 KMLIVQKGLE---------QNAAFSGTciiSDAQGLMEENDIPINiSSSPDDLAYIMYTSGSTGRPKGVMITNRnvvSLV 645
Cdd:PRK09192  130 AAIITPDELLpwvneathgNPLLHVLS---HAWFKALPEADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHR---ALM 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 RNSNYTSASG-----DDRFI------------------MTGSISFDAVTFEMFgALLNGASLHIIDKS--TMLTPDRFGa 700
Cdd:PRK09192  203 ANLRAISHDGlkvrpGDRCVswlpfyhdmglvgflltpVATQLSVDYLPTRDF-ARRPLQWLDLISRNrgTISYSPPFG- 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  701 YLL------ENDITVLFLTTAlfnQLAQVRADMFRgLHTLYVGGEALSPALMNavrhacpDLALHNIYGPTENT---TFS 771
Cdd:PRK09192  281 YELcarrvnSKDLAELDLSCW---RVAGIGADMIR-PDVLHQFAEAFAPAGFD-------DKAFMPSYGLAEATlavSFS 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  772 --------------TFFEMKRDYAGPIP---------IGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVAKGYLNRv 828
Cdd:PRK09192  350 plgsgivveevdrdRLEYQGKAVAPGAEtrrvrtfvnCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD- 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  829 DLTNAVFSPHPFLpgeriyRTGDLArWLPDGNLEYISRIDRQMKIRGKRIEPAEIEaRLLEMEGV---QEAAVTLREKDG 905
Cdd:PRK09192  429 EESQDVLAADGWL------DTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIE-WIAEQEPElrsGDAAAFSIAQEN 500

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499188982  906 EAQLYThyVGDHKKTDTDFRADLARVLPDYMIPQHWVRV-------ERMPLTGNGKIDRSA 959
Cdd:PRK09192  501 GEKIVL--LVQCRISDEERRGQLIHALAALVRSEFGVEAavelvppHSLPRTSSGKLSRAK 559
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 615-898 1.85e-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: 74.45  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRN-SNYTSASGDDRFI--MT-----GSISFDAV-------TFEMFGAL- 678
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAiLNSTEWKTKDRILswMPlthdmGLIAFHLApliagmnQYLMPTRLf 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  679 -------LNGASLHiidKSTMLTPDRFGAYLLendITVLFLTTALFNQLAQVRAdmfrglhtLYVGGEALSPALMNAVRH 751
Cdd:cd05908   185 irrpilwLKKASEH---KATIVSSPNFGYKYF---LKTLKPEKANDWDLSSIRM--------ILNGAEPIDYELCHEFLD 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  752 ACPDL-----ALHNIYGPTENTTFSTFFEMKRDYAGPI--------------------------PIGKPISNSTAYILDT 800
Cdd:cd05908   251 HMSKYglkrnAILPVYGLAEASVGASLPKAQSPFKTITlgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRICDE 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  801 KGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLArWLPDGNLEYISRIDRQMKIRGKRIEP 880
Cdd:cd05908   331 DNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYP 403

                         330
                  ....*....|....*...
gi 499188982  881 AEIEARLLEMEGVQEAAV 898
Cdd:cd05908   404 HDIERIAEELEGVELGRV 421
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 843-964 5.75e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 72.38  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  843 GERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEaAVTLREKD---GE---AQlythYVGD 916
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE-AVVYRGKDpvaGErvkAK----VISH 363

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499188982  917 HKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSALPIPE 964
Cdd:PRK08308  364 EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 485-957 5.79e-13

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


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 73.44  E-value: 5.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   485 QAEKTPDHTALVY-----GNM-SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDA 558
Cdd:TIGR02188   66 HLEARPDKVAIIWegdepGEVrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   559 ELPPERVSFMLEETQAKMLI-----------------VQKGLEQNAAFSGTCII-----SDAQGLMEENDIPIN--ISSS 614
Cdd:TIGR02188  146 GFSAEALADRINDAGAKLVItadeglrggkviplkaiVDEALEKCPVSVEHVLVvrrtgNPVVPWVEGRDVWWHdlMAKA 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   615 PD----------DLAYIMYTSGSTGRPKGVM-----------ITNRNVVSLvrnsnytsaSGDDRFIMTGSISFdaVT-- 671
Cdd:TIGR02188  226 SAycepepmdseDPLFILYTSGSTGKPKGVLhttggyllyaaMTMKYVFDI---------KDGDIFWCTADVGW--ITgh 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   672 -FEMFGALLNGASlHIIDKSTMLTPD--RFGAYLLENDITVLFLT-TAlfnqlaqVRADM--------------FRGLHT 733
Cdd:TIGR02188  295 sYIVYGPLANGAT-TVMFEGVPTYPDpgRFWEIIEKHKVTIFYTApTA-------IRALMrlgdewvkkhdlssLRLLGS 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   734 LyvgGEALSP-ALMnavrhacpdlALHNIYGPTENTTFSTFFE------MKRDYAGPIPIgKPISNST------AYILDT 800
Cdd:TIGR02188  367 V---GEPINPeAWM----------WYYKVVGKERCPIVDTWWQtetggiMITPLPGATPT-KPGSATLpffgiePAVVDE 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   801 KGRLLPI-GVPGELCVGGD--GVAKG-YLNRVDLTNAVFSPHPflpgeRIYRTGDLARWLPDGNLEYISRIDRQMKIRGK 876
Cdd:TIGR02188  433 EGNPVEGpGEGGYLVIKQPwpGMLRTiYGDHERFVDTYFSPFP-----GYYFTGDGARRDKDGYIWITGRVDDVINVSGH 507

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982   877 RIEPAEIEARLLEMEGVQEAAVTLREKD--GEAqLYThYV--GDHKKTDTDFRADL----ARVLPDYMIPQHWVRVERMP 948
Cdd:TIGR02188  508 RLGTAEIESALVSHPAVAEAAVVGIPDDikGQA-IYA-FVtlKDGYEPDDELRKELrkhvRKEIGPIAKPDKIRFVPGLP 585


                   ....*....
gi 499188982   949 LTGNGKIDR 957
Cdd:TIGR02188  586 KTRSGKIMR 594
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 467-901 7.29e-13

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 72.84  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  467 NTKTEYPKNHTIIDLFREQAEKTPDHTALVYGNMS---------ISYKELDKRSNALARELIQKGFRKNETAgILAAHSP 537
Cdd:PRK07769   12 NGKIRFPPNTNLVRHVERWAKVRGDKLAYRFLDFSterdgvardLTWSQFGARNRAVGARLQQVTKPGDRVA-ILAPQNL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  538 EFMISVLAVLKAGGAYLPL-DAELP--PERVSFMLEETQAKMLI--------VQKGLEQNAAFSGTCIIS-DAqglmeen 605
Cdd:PRK07769   91 DYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILtttdsaegVRKFFRARPAKERPRVIAvDA------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  606 dIPINISSS-------PDDLAYIMYTSGSTGRPKGVMITNRNVVS-LVRNSNYTSASGDDRfimtgsisfdAVTF-EMFg 676
Cdd:PRK07769  164 -VPDEVGATwvppeanEDTIAYLQYTSGSTRIPAGVQITHLNLPTnVLQVIDALEGQEGDR----------GVSWlPFF- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  677 allngaslHIIDKSTMLTPDRFGAYllendITvlFLTTALF--------NQLAQVRADMF----------------RGL- 731
Cdd:PRK07769  232 --------HDMGLITVLLPALLGHY-----IT--FMSPAAFvrrpgrwiRELARKPGGTGgtfsaapnfafehaaaRGLp 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  732 ------------HTLYVGGEALSPALMNAVRHA-----CPDLALHNIYGPTENTTF-ST--------------------- 772
Cdd:PRK07769  297 kdgeppldlsnvKGLLNGSEPVSPASMRKFNEAfapygLPPTAIKPSYGMAEATLFvSTtpmdeeptviyvdrdelnagr 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  773 FFEMKRDYAGPIP---IGKPISNSTAYILDTK-GRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVFspHPFL------- 841
Cdd:PRK07769  377 FVEVPADAPNAVAqvsAGKVGVSEWAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATF--QNILksrlses 454

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982  842 ------PGERIYRTGDLARWLpDGNLeYIS-RIDRQMKIRGKRIEPAEIEArllemeGVQEAAVTLR 901
Cdd:PRK07769  455 haegapDDALWVRTGDYGVYF-DGEL-YITgRVKDLVIIDGRNHYPQDLEY------TAQEATKALR 513
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 502-885 2.26e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 71.31  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELiQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDA-ELP--PERVSFMLEETQ-AKML 577
Cdd:PRK12476   69 LTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApELPghAERLDTALRDAEpTVVL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  578 IVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISSS-------PDDLAYIMYTSGSTGRPKGVMITNR----NVVSLVr 646
Cdd:PRK12476  148 TTTAAAEAVEGFLRNLPRLRRPRVIAIDAIPDSAGESfvpveldTDDVSHLQYTSGSTRPPVGVEITHRavgtNLVQMI- 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  647 nsnytsASGDDRFIMTGSISFDAVTFEM------FGALLNGASLHIIDKSTMLTPDRFGAYLLENDITVLFLTTA---LF 717
Cdd:PRK12476  227 ------LSIDLLDRNTHGVSWLPLYHDMglsmigFPAVYGGHSTLMSPTAFVRRPQRWIKALSEGSRTGRVVTAApnfAY 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  718 NQLAQvradmfRGLHT-----------LYVGGEALSPALMNAVRHA-----CPDLALHNIYGPTENTTF----------- 770
Cdd:PRK12476  301 EWAAQ------RGLPAegddidlsnvvLIIGSEPVSIDAVTTFNKAfapygLPRTAFKPSYGIAEATLFvatiapdaeps 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  771 STFF---EMKRDYAGPIP-----------IGKPISNSTAYILD-TKGRLLPIGVPGELCVGGDGVAKGYLNRVDLTNAVF 835
Cdd:PRK12476  375 VVYLdreQLGAGRAVRVAadapnavahvsCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499188982  836 -----SPHP-------FLPGERIYRTGDLARWLpDGNLEYISRIDRQMKIRGKRIEPAEIEA 885
Cdd:PRK12476  455 gaklqSRLAegshadgAADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEA 515
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 497-960 3.02e-12

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


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 70.54  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  497 YGNMSISYKELDKRSNALARELI-QKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAK 575
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  576 MLIVqkgleqnaafsgtciisdaqglmeendipinissSPDDLAYIMYTSGSTGRPKGVMITN-RNVVSLVRNSNYTSAS 654
Cdd:cd05937    81 FVIV----------------------------------DPDDPAILIYTSGTTGLPKAAAISWrRTLVTSNLLSHDLNLK 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  655 GDDRF-----IMTGSISFDAvtfeMFGALLNGASLHIIDKstmLTPDRFGAYLLENDITVLFLTTALFNQLAQVRADMFR 729
Cdd:cd05937   127 NGDRTytcmpLYHGTAAFLG----ACNCLMSGGTLALSRK---FSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYD 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  730 GLHTLYVG-GEALSPALMNAVRH--ACPDLalHNIYGPTENTtfstfFEMKRDYAGPIPIGK-----PIS---------- 791
Cdd:cd05937   200 RDHKVRVAwGNGLRPDIWERFRErfNVPEI--GEFYAATEGV-----FALTNHNVGDFGAGAighhgLIRrwkfenqvvl 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  792 -----NSTAYILDTKGRL---LPIGVPGELCV----GGDGVAKGYLNRVDLTNAVFSPHPFLPGERIYRTGDLARWLPDG 859
Cdd:cd05937   273 vkmdpETDDPIRDPKTGFcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADG 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  860 NLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEA---AVTLREKDGEAQLYTHYVGDHKKTDTDFR----ADLARV- 931
Cdd:cd05937   353 RWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVPGHDGRAGCAAITLEESSAVPTEFTksllASLARKn 432

                         490       500       510
                  ....*....|....*....|....*....|
gi 499188982  932 LPDYMIPQhWVRV-ERMPLTGNGKIDRSAL 960
Cdd:cd05937   433 LPSYAVPL-FLRLtEEVATTDNHKQQKGVL 461
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
614-956 3.61e-12

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 71.15  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 SPDDLAYIMYTSGSTGRPKGVMITNRNVVSlvrNSNYTSASGDdrfIMTGSISFDAV-TFEMFG-------ALLNG---- 681
Cdd:PRK06814  791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLA---NRAQVAARID---FSPEDKVFNALpVFHSFGltgglvlPLLSGvkvf 864

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  682 ---ASLH--IIDKSTMLTpdrfGAyllendiTVLFLTTALFNQLAQVRA--DmFRGLHTLYVGGEALSPALMN--AVRHA 752
Cdd:PRK06814  865 lypSPLHyrIIPELIYDT----NA-------TILFGTDTFLNGYARYAHpyD-FRSLRYVFAGAEKVKEETRQtwMEKFG 932

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 cpdLALHNIYGPTEnttfstffemkrdyAGP-IPIGKPISNStayiLDTKGRLLPI---------GVP--GELCVGGDGV 820
Cdd:PRK06814  933 ---IRILEGYGVTE--------------TAPvIALNTPMHNK----AGTVGRLLPGieyrlepvpGIDegGRLFVRGPNV 991

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  821 AKGYLnRVDlTNAVFSPhpflPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEM-EGVQEAAVT 899
Cdd:PRK06814  992 MLGYL-RAE-NPGVLEP----PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVS 1065

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  900 LR-EKDGEA-QLYThyvgdhkkTDTDF-RADL-----ARVLPDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK06814 1066 IPdARKGERiILLT--------TASDAtRAAFlahakAAGASELMVPAEIITIDEIPLLGTGKID 1122
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 487-960 1.72e-11

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


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 68.50  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  487 EKTPDHTALVY-----GNM-SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG-------GAY 553
Cdd:cd05967    62 AGRGDQIALIYdspvtGTErTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  554 LPL-------DAE----------LPPER-------VSFMLEETQ---AKMLIVQKGL-EQNAAFSGTCIISDAQGLMEEN 605
Cdd:cd05967   142 AAKelasridDAKpklivtascgIEPGKvvpykplLDKALELSGhkpHHVLVLNRPQvPADLTKPGRDLDWSELLAKAEP 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  606 DIPINISSspDDLAYIMYTSGSTGRPKGVMITNR-NVVSLVRN-SN-YTSASGDDRFimTGSISFDAV--TFEMFGALLN 680
Cdd:cd05967   222 VDCVPVAA--TDPLYILYTSGTTGKPKGVVRDNGgHAVALNWSmRNiYGIKPGDVWW--AASDVGWVVghSYIVYGPLLH 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  681 GASLHIIDKSTMLTPDRfGAY--LLENditvlFLTTALFNQLAQVRA--------------DMFRgLHTLYVGGEALSPA 744
Cdd:cd05967   298 GATTVLYEGKPVGTPDP-GAFwrVIEK-----YQVNALFTAPTAIRAirkedpdgkyikkyDLSS-LRTLFLAGERLDPP 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  745 LMNAVRHACPDLALHNiYGPTEN----TTFSTFFEMKrdyagPIPIGKPISNSTAY---ILDTKGRLLPIGVPGELCVGG 817
Cdd:cd05967   371 TLEWAENTLGVPVIDH-WWQTETgwpiTANPVGLEPL-----PIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIKL 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  818 D---GVAKG-YLNRVDLTNAVFSPHPFLpgeriYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGV 893
Cdd:cd05967   445 PlppGCLLTlWKNDERFKKLYLSKFPGY-----YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAV 519

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  894 QEAAVTLREKDGEAQLYTHYV---GDHKKTDTDFRADLARVLPDYMIP----QHWVRVERMPLTGNGKIDRSAL 960
Cdd:cd05967   520 AECAVVGVRDELKGQVPLGLVvlkEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSGKILRRTL 593
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 485-957 2.56e-11

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


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 67.97  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  485 QAEKTPDHTALVY-GNM-----SISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDA 558
Cdd:cd05966    62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  559 ELPPERVSFMLEETQAKMLI-----------------VQKGLEQnaAFS-GTCIISDAQG----LMEENDIPIN--ISSS 614
Cdd:cd05966   142 GFSAESLADRINDAQCKLVItadggyrggkviplkeiVDEALEK--CPSvEKVLVVKRTGgevpMTEGRDLWWHdlMAKQ 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PD----------DLAYIMYTSGSTGRPKGVM-----------ITNRNVVslvrnsNYTSasgDDRFIMTGSISFdaVT-- 671
Cdd:cd05966   220 SPecepewmdseDPLFILYTSGSTGKPKGVVhttggyllyaaTTFKYVF------DYHP---DDIYWCTADIGW--ITgh 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  672 -FEMFGALLNGASlHIIDKSTMLTPD--RFGAYLLENDITVLFLT-TAL-----FNQLAQVRADM--FRGLHTLyvgGEA 740
Cdd:cd05966   289 sYIVYGPLANGAT-TVMFEGTPTYPDpgRYWDIVEKHKVTIFYTApTAIralmkFGDEWVKKHDLssLRVLGSV---GEP 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  741 LSP-ALMNAVRHA----CPdlaLHNIYGPTENTTFstffeMKRDYAGPIPIgKPISNST------AYILDTKGRLLPIGV 809
Cdd:cd05966   365 INPeAWMWYYEVIgkerCP---IVDTWWQTETGGI-----MITPLPGATPL-KPGSATRpffgiePAILDEEGNEVEGEV 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  810 PGELCVGGD--GVAKG-YLNRVDLTNAVFSPHPFLpgeriYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEAR 886
Cdd:cd05966   436 EGYLVIKRPwpGMARTiYGDHERYEDTYFSKFPGY-----YFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499188982  887 LLEMEGVQEAAVTLREKD--GEAqLYThYV--GDHKKTDTDFRADL----ARVLPDYMIPQHWVRVERMPLTGNGKIDR 957
Cdd:cd05966   511 LVAHPAVAEAAVVGRPHDikGEA-IYA-FVtlKDGEEPSDELRKELrkhvRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 610-896 4.00e-11

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 67.15  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  610 NISS-SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRFIMTGSISFDAVTFEMFGALLNGASLHIID 688
Cdd:PRK06334  176 GVSDkDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  689 KSTMLTPDRFGAYLLENDITVLFLTTALFNQL---AQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPT 765
Cdd:PRK06334  256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYIlktAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  766 ENT---TFSTFFEMKRDYAgpipIGKPISNSTAYILDTKGRL-LPIGVPGELCVGGDGVAKGYLNRvDLTNAVFSphpfL 841
Cdd:PRK06334  336 ECSpviTINTVNSPKHESC----VGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGE-DFGQGFVE----L 406

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499188982  842 PGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEA 896
Cdd:PRK06334  407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 719-961 7.44e-11

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 66.17  E-value: 7.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 QLAQVRADMFRGLHTLYVGGEALSPALMNAVRHACPDLALhnIYGPTEntTFSTFFEMKRD--YAGPIPIGKPISNSTAY 796
Cdd:PRK07445  220 RLLQLRPQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAP--TYGMTE--TASQIATLKPDdfLAGNNSSGQVLPHAQIT 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  797 ILDTKgrllpigvPGELCVGGDGVAKGYLnrvdltnavfsPHpFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGK 876
Cdd:PRK07445  296 IPANQ--------TGNITIQAQSLALGYY-----------PQ-ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEARLLEMEGVQEAAVT-LREKD-GEaQLYTHYVGDHKKTDTD-FRADLARVLPDYMIPQHWVRVERMPLTGNG 953
Cdd:PRK07445  356 NVYPAEVEAAILATGLVQDVCVLgLPDPHwGE-VVTAIYVPKDPSISLEeLKTAIKDQLSPFKQPKHWIPVPQLPRNPQG 434


                  ....*...
gi 499188982  954 KIDRSALP 961
Cdd:PRK07445  435 KINRQQLQ 442
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 502-884 8.79e-11

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 66.28  E-value: 8.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLE--ETQA----- 574
Cdd:PLN02736   79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNhaEVAAifcvp 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  575 ----------------KMLIVQKGLEQN----AAFSGTCIIS----DAQGLMEENDIpinISSSPDDLAYIMYTSGSTGR 630
Cdd:PLN02736  159 qtlntllsclseipsvRLIVVVGGADEPlpslPSGTGVEIVTysklLAQGRSSPQPF---RPPKPEDVATICYTSGTTGT 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  631 PKGVMITNRNVVSLVRNSNYTSASG-DDRFIMTGSIS--FDAVTFEM---FGALL---NGASLHIIDKSTMLTPDRFGAY 701
Cdd:PLN02736  236 PKGVVLTHGNLIANVAGSSLSTKFYpSDVHISYLPLAhiYERVNQIVmlhYGVAVgfyQGDNLKLMDDLAALRPTIFCSV 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  702 -LLENDI---------TVLFLTTALFNQ-----------------------LAQVRADMFRGLHTLYVGGEALSPALMNA 748
Cdd:PLN02736  316 pRLYNRIydgitnavkESGGLKERLFNAaynakkqalengknpspmwdrlvFNKIKAKLGGRVRFMSSGASPLSPDVMEF 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  749 VRhACPDLALHNIYGPTENT-TFSTFFEMKRDYAGpipIGKPISNSTAYILD-------TKGRLLPigvPGELCVGGDGV 820
Cdd:PLN02736  396 LR-ICFGGRVLEGYGMTETScVISGMDEGDNLSGH---VGSPNPACEVKLVDvpemnytSEDQPYP---RGEICVRGPII 468

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499188982  821 AKGYLNRVDLTNAVFSPHPFLpgeriyRTGDLARWLPDGNLEYisrIDRQMKI----RGKRIEPAEIE 884
Cdd:PLN02736  469 FKGYYKDEVQTREVIDEDGWL------HTGDIGLWLPGGRLKI---IDRKKNIfklaQGEYIAPEKIE 527
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 486-898 2.94e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 64.12  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERV 565
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  566 SFMLEETQAKMLIVqkgLEQNAAFSGTCIISdaqglMEENDIPINISSSPDDLAYIMYTSGSTGRPKGVMITNRNvvslv 645
Cdd:PRK09029   93 EELLPSLTLDFALV---LEGENTFSALTSLH-----LQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA----- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  646 rnsNYTSASGddrfimtgsisfdaVTFEM-FGA----------------------LLNGASLHIIDKSTM---------- 692
Cdd:PRK09029  160 ---HLASAEG--------------VLSLMpFTAqdswllslplfhvsgqgivwrwLYAGATLVVRDKQPLeqalagctha 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 -LTPD---RfgayLLENDITVLFLT----------TALFNQLAQvradmfRGLHTlYVGgealspalmnavrhacpdlal 758
Cdd:PRK09029  223 sLVPTqlwR----LLDNRSEPLSLKavllggaaipVELTEQAEQ------QGIRC-WCG--------------------- 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  759 hniYGPTEntTFSTFFEMKRD-YAGpipIGKPIsnstayildtKGRLLPIgVPGELCVGGDGVAKGYL---NRVDLTNAv 834
Cdd:PRK09029  271 ---YGLTE--MASTVCAKRADgLAG---VGSPL----------PGREVKL-VDGEIWLRGASLALGYWrqgQLVPLVND- 330

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499188982  835 fsphpflpgERIYRTGDLARWLpDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV 898
Cdd:PRK09029  331 ---------EGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 503-960 3.06e-10

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


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 63.98  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  503 SYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI---V 579
Cdd:cd05939     5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIfnlL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  580 QKGLEQNAAFSGTCIISDAQglmeendipinissspDDLAYImYTSGSTGRPKGVMITNRNVVSLVRNSNYT-SASGDDR 658
Cdd:cd05939    85 DPLLTQSSTEPPSQDDVNFR----------------DKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAfGMRPEDV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  659 FIMTGSISFDAVTFEMFG-ALLNGASLHIIDKstmLTPDRFGAYLLENDITVL-FLTTALFNQLAQVRADMFRGLHTLYV 736
Cdd:cd05939   148 VYDCLPLYHSAGGIMGVGqALLHGSTVVIRKK---FSASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKHNVRLA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  737 GGEALSPALMNAV--RHACPDLAlhNIYGPTENTTFSTFFEMKRDYAG----------PIPIGKPISNSTAYILDTKGRL 804
Cdd:cd05939   225 VGNGLRPQIWEQFvrRFGIPQIG--EFYGATEGNSSLVNIDNHVGACGfnsrilpsvyPIRLIKVDEDTGELIRDSDGLC 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  805 LPI--GVPGELcVG----GDGVAK--GYLNRVDlTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGK 876
Cdd:cd05939   303 IPCqpGEPGLL-VGkiiqNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGE 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  877 RIEPAEIEA---RLLEMEGVQEAAVTLREKDGEAQLYTHYVGDhKKTDTD-FRADLARVLPDYMIPQHWVRVERMPLTGN 952
Cdd:cd05939   381 NVSTTEVEGilsNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPE-RKVDLDrFSAVLAKSLPPYARPQFIRLLPEVDKTGT 459


                  ....*...
gi 499188982  953 GKIDRSAL 960
Cdd:cd05939   460 FKLQKTDL 467
PRK05857 PRK05857
fatty acid--CoA ligase;
477-965 3.32e-10

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 64.26  E-value: 3.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTALVY--GNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYL 554
Cdd:PRK05857   15 TVLDRVFEQARQQPEAIALRRcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  555 PLDAELPPERVSFMLEETQAKMLIVQKG-------LEQNAAFSGTCIISDAQGLME-----ENDIP-INISSSPDDLAYI 621
Cdd:PRK05857   95 MADGNLPIAAIERFCQITDPAAALVAPGskmassaVPEALHSIPVIAVDIAAVTREsehslDAASLaGNADQGSEDPLAM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  622 MYTSGSTGRPKGVMITNRN---VVSLVRNSNYtsasgddRFI--MTGSISFDAVTFEMFGAL---LNGaslhIIDKSTML 693
Cdd:PRK05857  175 IFTSGTTGEPKAVLLANRTffaVPDILQKEGL-------NWVtwVVGETTYSPLPATHIGGLwwiLTC----LMHGGLCV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  694 TPDRFGAYLLE----NDITVLFLTTALFNQLA---QVRADMFRGLHTLYVGGEALSPALMN-----AVRHA--------- 752
Cdd:PRK05857  244 TGGENTTSLLEilttNAVATTCLVPTLLSKLVselKSANATVPSLRLVGYGGSRAIAADVRfieatGVRTAqvyglsetg 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 CPDLALhniygPTENTTFStffemkRDYAGpiPIGKPISNSTAYILDTKGR--LLPIGVP----GELCVGGDGVAKGYLN 826
Cdd:PRK05857  324 CTALCL-----PTDDGSIV------KIEAG--AVGRPYPGVDVYLAATDGIgpTAPGAGPsasfGTLWIKSPANMLGYWN 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  827 RVDLTNAVFSphpflpgERIYRTGDLARWLPDGNLeYISRIDRQMKIRGK-RIEPAEIEARLLEMEGVQEAA-------- 897
Cdd:PRK05857  391 NPERTAEVLI-------DGWVNTGDLLERREDGFF-YIKGRSSEMIICGGvNIAPDEVDRIAEGVSGVREAAcyeipdee 462

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499188982  898 ---------VTLREKDGEAQL-YTHYVGDHKKTDTDfraDLARvlpdymiPQHWVRVERMPLTGNGKIDRSALPIPEN 965
Cdd:PRK05857  463 fgalvglavVASAELDESAARaLKHTIAARFRRESE---PMAR-------PSTIVIVTDIPRTQSGKVMRASLAAAAT 530
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 502-643 4.01e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 64.23  E-value: 4.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAV----LKAGGAYlpldAELPPERVSFMLEETQAKML 577
Cdd:PTZ00216  122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVY----ANLGEDALAYALRETECKAI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  578 I-----VQK--GLEQNAAFSGTCII-------------------SD--AQGLMEENDIPINISSSPDDLAYIMYTSGSTG 629
Cdd:PTZ00216  198 VcngknVPNllRLMKSGGMPNTTIIyldslpasvdtegcrlvawTDvvAKGHSAGSHHPLNIPENNDDLALIMYTSGTTG 277

                         170
                  ....*....|....
gi 499188982  630 RPKGVMITNRNVVS 643
Cdd:PTZ00216  278 DPKGVMHTHGSLTA 291
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
502-960 4.05e-10

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 64.03  E-value: 4.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQK-GFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLIVQ 580
Cdd:PRK05620   39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  581 KGLEQNAA-------------FSGTCIISDAQGLMEEN----------DIPINISSSPD----DLAYIMYTSGSTGRPKG 633
Cdd:PRK05620  119 PRLAEQLGeilkecpcvravvFIGPSDADSAAAHMPEGikvysyeallDGRSTVYDWPEldetTAAAICYSTGTTGAPKG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  634 VMITNRnvvSLVRNSnyTSASGDDRFIMTGSISF-------DAVTFEM-FGALLNGASLHIIDKStmLTPDRFgAYLLEN 705
Cdd:PRK05620  199 VVYSHR---SLYLQS--LSLRTTDSLAVTHGESFlccvpiyHVLSWGVpLAAFMSGTPLVFPGPD--LSAPTL-AKIIAT 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  706 DIT-----VLFLTTALFNQLAQVRADMFrGLHTLYVGGEALSPALMNAVRHACPDLALHnIYGPTENTTFSTFfemkrdy 780
Cdd:PRK05620  271 AMPrvahgVPTLWIQLMVHYLKNPPERM-SLQEIYVGGSAVPPILIKAWEERYGVDVVH-VWGMTETSPVGTV------- 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  781 AGPiPIGKPISNSTAYILdTKGRLlPIGV-----------------PGELCVGGDGVAKGYLN----RVDLTNAVFSPHP 839
Cdd:PRK05620  342 ARP-PSGVSGEARWAYRV-SQGRF-PASLeyrivndgqvmestdrnEGEIQVRGNWVTASYYHspteEGGGAASTFRGED 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  840 FLPGERIY------RTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVT--LREKDGEAQLYT 911
Cdd:PRK05620  419 VEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIgyPDDKWGERPLAV 498

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499188982  912 HYVGD----HKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGKIDRSAL 960
Cdd:PRK05620  499 TVLAPgiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 480-866 4.83e-09

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 60.63  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  480 DLFREQAEKTPDHTALVYGNMS---------ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAG 550
Cdd:PLN02861   47 QFFSDAVKKYPNNQMLGRRQVTdskvgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  551 GAYLPLDAELPPERVSFMLEETQAKMLIVQKG--------LEQNAAFSGTCI----ISDAQGlMEENDIPINISS----- 613
Cdd:PLN02861  127 ITYVPLYDTLGANAVEFIINHAEVSIAFVQESkissilscLPKCSSNLKTIVsfgdVSSEQK-EEAEELGVSCFSweefs 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  614 ------------SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNY------TSASGDDRFIMTGSIS--FDAVTFE 673
Cdd:PLN02861  206 lmgsldcelppkQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHllkvtdRVATEEDSYFSYLPLAhvYDQVIET 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  674 MFgaLLNGASL--------HIIDKSTMLTPDRF---------------------GA-----------YLLEN-------D 706
Cdd:PLN02861  286 YC--ISKGASIgfwqgdirYLMEDVQALKPTIFcgvprvydriytgimqkissgGMlrkklfdfaynYKLGNlrkglkqE 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  707 ITVLFLTTALFNQLAQVradmFRGLHTLYVGGEALSPALMNAVRHACPDLALHNIYGPTEN-----TTFSTFFEMKRDYA 781
Cdd:PLN02861  364 EASPRLDRLVFDKIKEG----LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScggcfTSIANVFSMVGTVG 439

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  782 GPIPIgkpisnstayildTKGRLLPI---------GVP-GELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriyRTGD 851
Cdd:PLN02861  440 VPMTT-------------IEARLESVpemgydalsDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGD 499

                         490
                  ....*....|....*
gi 499188982  852 LARWLPDGNLEYISR 866
Cdd:PLN02861  500 IGEWQPNGAMKIIDR 514
PLN02654 PLN02654
acetate-CoA ligase
 499-971 4.84e-09

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 60.68  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  499 NMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYLPLDAELPPERVSFMLEETQAKMLI 578
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  579 ----VQKGL----------------EQNAAFSGTCIISDAQGLMEENDIPIN----------ISSSP----------DDL 618
Cdd:PLN02654  198 tcnaVKRGPktinlkdivdaaldesAKNGVSVGICLTYENQLAMKREDTKWQegrdvwwqdvVPNYPtkcevewvdaEDP 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  619 AYIMYTSGSTGRPKGVMITNRNVVSLV----------RNSNYTSASGDDRFImTGSisfdavTFEMFGALLNGASLhIID 688
Cdd:PLN02654  278 LFLLYTSGSTGKPKGVLHTTGGYMVYTattfkyafdyKPTDVYWCTADCGWI-TGH------SYVTYGPMLNGATV-LVF 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  689 KSTMLTPDRFGAYllenDITVLFLTTALFNQLAQVRADMFRG-----------LHTLYVGGEALSPA----LMNAVRHA- 752
Cdd:PLN02654  350 EGAPNYPDSGRCW----DIVDKYKVTIFYTAPTLVRSLMRDGdeyvtrhsrksLRVLGSVGEPINPSawrwFFNVVGDSr 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  753 CPdlaLHNIYGPTENTTFstffeMKRDYAGPIPIgKPISNSTAY------ILDTKGRLLPIGVPGELCVGGDGvaKGYLN 826
Cdd:PLN02654  426 CP---ISDTWWQTETGGF-----MITPLPGAWPQ-KPGSATFPFfgvqpvIVDEKGKEIEGECSGYLCVKKSW--PGAFR 494

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  827 RVDLTNAVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAVTLREKDGE 906
Cdd:PLN02654  495 TLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  907 AQLYTHYVG--DHKKTDTDFRADL---------ARVLPDYMipqHWvrVERMPLTGNGKIDRSALpipeNKPAKRQ 971
Cdd:PLN02654  575 GQGIYAFVTlvEGVPYSEELRKSLiltvrnqigAFAAPDKI---HW--APGLPKTRSGKIMRRIL----RKIASRQ 641
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 502-901 1.27e-08

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 59.24  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  502 ISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKAGGAY-----------LPLDAElPPERVSFMLE 570
Cdd:PRK07768   30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLtmlhqptprtdLAVWAE-DTLRVIGMIG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  571 etqAKMLIVQKGLEQNA-AFSGTCIISDAQG-LMEENDIPInISSSPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNs 648
Cdd:PRK07768  109 ---AKAVVVGEPFLAAApVLEEKGIRVLTVAdLLAADPIDP-VETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEA- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  649 nytsasgddrfiMTGSISFDAVT---------FE---MFGAL----LNGASL----------------HIIDK--STMLT 694
Cdd:PRK07768  184 ------------MFVAAEFDVETdvmvswlplFHdmgMVGFLtvpmYFGAELvkvtpmdflrdpllwaELISKyrGTMTA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  695 PDRFgAYllenditvlflttALFNQLAQVRADMFR-GLHTLYV---GGEALSPALMN-----AVRHACPDLALHNIYGPT 765
Cdd:PRK07768  252 APNF-AY-------------ALLARRLRRQAKPGAfDLSSLRFalnGAEPIDPADVEdlldaGARFGLRPEAILPAYGMA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  766 ENT---TFSTFFE-MKRDY-----------AGP---------IPIGKPISNSTAYILDTKGRLLPIGVPGELCVGGDGVA 821
Cdd:PRK07768  318 EATlavSFSPCGAgLVVDEvdadllaalrrAVPatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  822 KGYLNrvdltnaVFSPHPFLPGERIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEA-AVTL 900
Cdd:PRK07768  398 PGYLT-------MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGnAVAV 470


                  .
gi 499188982  901 R 901
Cdd:PRK07768  471 R 471
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 602-879 2.77e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 58.19  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  602 MEENDIP-INISSS-PDDLAYIMYTSGSTGRPKGVMITNRN----VVSLVRNSNYTSASGDDRFimtgsiSFDAVT--FE 673
Cdd:PTZ00342  288 MTKNKTTnYKIQNEdPDFITSIVYTSGTSGKPKGVMLSNKNlyntVVPLCKHSIFKKYNPKTHL------SYLPIShiYE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  674 ---MFGALLNGASLHIIDKSTMLtpdrFGAYLLENDITVLFLTTALFNQ-----------------------LAQVRADM 727
Cdd:PTZ00342  362 rviAYLSFMLGGTINIWSKDINY----FSKDIYNSKGNILAGVPKVFNRiytnimteinnlpplkrflvkkiLSLRKSNN 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  728 FRG----------------------LHTLYVGGEALSPALMNAVRhacpdlALHNI-----YGPTEnTTFSTFFEMKRDY 780
Cdd:PTZ00342  438 NGGfskflegithisskikdkvnpnLEVILNGGGKLSPKIAEELS------VLLNVnyyqgYGLTE-TTGPIFVQHADDN 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  781 aGPIPIGKPISNSTAY------ILDTKGRLlpigvP-GELCVGGDGVAKGYLNRVDLTNAVFSPHPFlpgeriYRTGDLA 853
Cdd:PTZ00342  511 -NTESIGGPISPNTKYkvrtweTYKATDTL-----PkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIV 578

                         330       340
                  ....*....|....*....|....*..
gi 499188982  854 RWLPDGNLEYISRIDRQMKI-RGKRIE 879
Cdd:PTZ00342  579 QINKNGSLTFLDRSKGLVKLsQGEYIE 605
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
615-956 2.92e-08

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 58.18  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRnvvSLVRNSNYTSASGD----DRFiMTGSISFDA--VTFEMFGALLNGAS----- 683
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHK---SLLANVEQIKTIADftpnDRF-MSALPLFHSfgLTVGLFTPLLTGAEvflyp 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  684 --LH--IIDKstmLTPDRfgayllenDITVLFLTTALFNQLAQVRA--DMFRgLHTLYVGGEALSPalmnAVRHACPD-- 755
Cdd:PRK08043  440 spLHyrIVPE---LVYDR--------NCTVLFGTSTFLGNYARFANpyDFAR-LRYVVAGAEKLQE----STKQLWQDkf 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  756 -LALHNIYGPTEnttfstffemkrdYAGPIPIGKPIsnstAYILDTKGRLLP------IGVPG-----ELCVGGDGVAKG 823
Cdd:PRK08043  504 gLRILEGYGVTE-------------CAPVVSINVPM----AAKPGTVGRILPgmdarlLSVPGieqggRLQLKGPNIMNG 566

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  824 YLnRVDLTNAVFSPHPFLP-GER---IYRTGDLARWLPDGNLEYISRIDRQMKIRGKRI--EPAEIEARLLEMEGVQEAA 897
Cdd:PRK08043  567 YL-RVEKPGVLEVPTAENArGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVslEMVEQLALGVSPDKQHATA 645

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  898 VTLREKDGEAQ-LYThyvgdhkkTDTDFRAD----LARVL--PDYMIPQHWVRVERMPLTGNGKID 956
Cdd:PRK08043  646 IKSDASKGEALvLFT--------TDSELTREklqqYAREHgvPELAVPRDIRYLKQLPLLGSGKPD 703
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1069-1159 1.01e-07

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 54.47  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982 1069 NLFCFPPISGFGIYFKDLALLLNEKAAVY-------GFHFIEQ-DTRIEQYVN-CMTDIQP--EGPYVLLGYSAGGNLAF 1137
Cdd:COG3208     8 RLFCFPYAGGSASAYRPWAAALPPDIEVLavqlpgrGDRLGEPpLTSLEELADdLAEELAPllDRPFALFGHSMGALLAF 87

                          90       100
                  ....*....|....*....|..
gi 499188982 1138 EVAQAMERKGLEVSDFIIVDAY 1159
Cdd:COG3208    88 ELARRLERRGRPLPAHLFVSGR 109
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 612-984 1.59e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 55.90  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  612 SSSPddlAYIMYTSGSTGRPKGVMITN-RNVVSLVRNSNYTSASGDD-RFIMTGSISFdaVTFEMF--GALLNGASLHII 687
Cdd:PTZ00237  253 SSHP---LYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPtVVFSHSSIGW--VSFHGFlyGSLSLGNTFVMF 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  688 DKSTMLTP---DRFGAYLLENDITVLFLTTALFNQLAQVRADMFR--------GLHTLYVGGEALSPALMNAVRHACPDL 756
Cdd:PTZ00237  328 EGGIIKNKhieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIirskydlsNLKEIWCGGEVIEESIPEYIENKLKIK 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  757 ALhNIYGPTEN--TTFSTFFEMKRDYAG---PIPIGKPIsnstayILDTKGRLLPIGVPGELCVG---GDGVAKGYLNRV 828
Cdd:PTZ00237  408 SS-RGYGQTEIgiTYLYCYGHINIPYNAtgvPSIFIKPS------ILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKND 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  829 DLTNAVFSPHPflpgeRIYRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQE------------- 895
Cdd:PTZ00237  481 EKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLEccsigiydpdcyn 555

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  896 ---AAVTLREKDGEAQL----YTHYVGDHKKTDTDFRADLARVLpdyMIPQhwvrverMPLTGNGKIDRSALPIPENKPa 968
Cdd:PTZ00237  556 vpiGLLVLKQDQSNQSIdlnkLKNEINNIITQDIESLAVLRKII---IVNQ-------LPKTKTGKIPRQIISKFLNDS- 624

                         410
                  ....*....|....*.
gi 499188982  969 krqNIILPRNLVEEEL 984
Cdd:PTZ00237  625 ---NYQLPDNVNDSEI 637
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 477-866 2.65e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 55.21  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKTPDHTAL---------VYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISvlavL 547
Cdd:PLN02430   43 TAWDIFSKSVEKYPDNKMLgwrrivdgkVGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA----M 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  548 KAGGAY----LPLDAELPPERVSFMLEETQAKMLIVQ----KGL---EQNAAFSGTCIISDAQGLMEEND----IPINIS 612
Cdd:PLN02430  119 EACAAHslicVPLYDTLGPGAVDYIVDHAEIDFVFVQdkkiKELlepDCKSAKRLKAIVSFTSVTEEESDkasqIGVKTY 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  613 S------------------SPDDLAYIMYTSGSTGRPKGVMITNRNVVSLVRNSNYTSASGDDRfiMTGS---ISF---- 667
Cdd:PLN02430  199 SwidflhmgkenpsetnppKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDK--MTHDdvyLSFlpla 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  668 ---DAVTFEMFgaLLNGAS-------LHIIDKSTM-LTPDRFGAY--------------LLENDITVLFLTTALFN---- 718
Cdd:PLN02430  277 hilDRMIEEYF--FRKGASvgyyhgdLNALRDDLMeLKPTLLAGVprvferihegiqkaLQELNPRRRLIFNALYKykla 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  719 --------QLAQVRADM--FRG--------LHTLYVGGEALSPALMNAVRHACPDLALHNiYGPTENttfstffemkrdy 780
Cdd:PLN02430  355 wmnrgyshKKASPMADFlaFRKvkaklggrLRLLISGGAPLSTEIEEFLRVTSCAFVVQG-YGLTET------------- 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  781 AGPIPIGKPISNStayILDTKG--------RLL--------PIGVP--GELCVGGDGVAKGYLNRVDLTNAVFSPHPFlp 842
Cdd:PLN02430  421 LGPTTLGFPDEMC---MLGTVGapavynelRLEevpemgydPLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWF-- 495

                         490       500
                  ....*....|....*....|....
gi 499188982  843 geriyRTGDLARWLPDGNLEYISR 866
Cdd:PLN02430  496 -----HTGDIGEILPNGVLKIIDR 514
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 497-662 3.98e-07

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: 54.22  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  497 YGNMSISYKELDKRSNALARELI-QKGFRKNETAGILAAHSPEFMISVLAVLKAGGAYlpldAELPP--ERVSFM--LEE 571
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPV----AFLNTniRSKSLLhcFRC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  572 TQAKMLIV----QKGLEQNA-----------AFSGTCIISDAQGLMEEND------IPINISS--SPDDLAYIMYTSGST 628
Cdd:cd05938    77 CGAKVLVVapelQEAVEEVLpalradgvsvwYLSHTSNTEGVISLLDKVDaasdepVPASLRAhvTIKSPALYIYTSGTT 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 499188982  629 GRPKGVMITNRNVVSLvrnSNYTSASG---DDRFIMT 662
Cdd:cd05938   157 GLPKAARISHLRVLQC---SGFLSLCGvtaDDVIYIT 190
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 882-954 6.04e-07

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


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 48.31  E-value: 6.04e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982   882 EIEARLLEMEGVQEAAVTLR--EKDGEAqLYTHYV--GDHKKTDTDFRADLARVLPDYMIPQHWVRVERMPLTGNGK 954
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVpdELKGEA-PVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 977-1046 6.56e-07

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 48.40  E-value: 6.56e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499188982    977 RNLVEEELANIWKQVLGV---NTISIDDDFFAIGGHSLRALQVIHTLKHQQNIDIPIDFLFEHPTIAQLAEKL 1046
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 477-898 6.96e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 53.53  E-value: 6.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  477 TIIDLFREQAEKtpDHTALVYGNMSISYKELDKRSNALA---RELIQKGFRKNetAGILAAHSPEFMISVLAVLKAG--- 550
Cdd:PRK07867    6 TVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAaalRARLDPTRPPH--VGVLLDNTPEFSLLLGAAALSGivp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  551 --------GAYLPLDAELPPERVSFmleeTQAKMLIVQKGLEQNAAFSGTCIISDAQGLMEENDIPINISS-SPDDLAYI 621
Cdd:PRK07867   82 vglnptrrGAALARDIAHADCQLVL----TESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRVaDPDDLFML 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  622 MYTSGSTGRPKGVMITNRNVVSlvrnsnyTSASGDDRFimtgSISFDAVTF---EMF--GALLNGASLHIIDKSTMLTPD 696
Cdd:PRK07867  158 IFTSGTSGDPKAVRCTHRKVAS-------AGVMLAQRF----GLGPDDVCYvsmPLFhsNAVMAGWAVALAAGASIALRR 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  697 RFGAYllenditvlflttalfNQLAQVRAdmFRGLHTLYVGgEALSPALMNAVRhacPDLA---LHNIYG----PTENTT 769
Cdd:PRK07867  227 KFSAS----------------GFLPDVRR--YGATYANYVG-KPLSYVLATPER---PDDAdnpLRIVYGnegaPGDIAR 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  770 FSTFFEMK---------------RDYAGPiP--IGKPISNSTAY-----------ILDTKGRLLPIGVPGELC-VGGDGV 820
Cdd:PRK07867  285 FARRFGCVvvdgfgsteggvaitRTPDTP-PgaLGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGG 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  821 AKGYLNrvdltnavfspHPFLPGERI----YRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEA 896
Cdd:PRK07867  364 FEGYYN-----------DPEADAERMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432


                  ..
gi 499188982  897 AV 898
Cdd:PRK07867  433 AV 434
PLN02479 PLN02479
acetate-CoA ligase
 473-966 9.55e-07

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 53.31  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  473 PKNHTIID--LFREQAEKT-PDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAVLKA 549
Cdd:PLN02479   14 AANYTALTplWFLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  550 GGAYLPLDAELPPERVSFMLEETQAKMLIVQKGLeqnaaFSgtcIISDAQGLMEENDI-----PINI-----SSSPDDLA 619
Cdd:PLN02479   94 GAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEF-----FT---LAEEALKILAEKKKssfkpPLLIvigdpTCDPKSLQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  620 YIM---------------------------------YTSGSTGRPKGVMITNRNVvslvrnsnYTSASGDdrfIMTGSIS 666
Cdd:PLN02479  166 YALgkgaieyekfletgdpefawkppadewqsialgYTSGTTASPKGVVLHHRGA--------YLMALSN---ALIWGMN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  667 FDAV---TFEMFG----------ALLNGASLHIidksTMLTPDRFGAYLLENDITVLFLTTALFNQLAQV-RADMFRGL- 731
Cdd:PLN02479  235 EGAVylwTLPMFHcngwcftwtlAALCGTNICL----RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLp 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  732 HTLYV--GGEALSPALMNAVRHAcpDLALHNIYGPTENTTFSTFFEMKRDYAGPIPIGKPISNS---TAYI-------LD 799
Cdd:PLN02479  311 RVVHVmtAGAAPPPSVLFAMSEK--GFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNArqgVRYIglegldvVD 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  800 TKgRLLPigVP------GELCVGGDGVAKGYLNRVDLTNAVFSphpflpgERIYRTGDLARWLPDGnleYISRIDRQMKI 873
Cdd:PLN02479  389 TK-TMKP--VPadgktmGEIVMRGNMVMKGYLKNPKANEEAFA-------NGWFHSGDLGVKHPDG---YIEIKDRSKDI 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  874 ---RGKRIEPAEIEARLLEMEGVQEAAVTLREKDGEAQLYTHYVGDHKKTDTDFRADLAR--------VLPDYMIPQHwV 942
Cdd:PLN02479  456 iisGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEdimkfcreRLPAYWVPKS-V 534

                         570       580       590
                  ....*....|....*....|....*....|..
gi 499188982  943 RVERMPLTGNGKIDRSAL--------PIPENK 966
Cdd:PLN02479  535 VFGPLPKTATGKIQKHVLrakakemgPVKKSR 566
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1122-1178 9.09e-06

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


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 47.99  E-value: 9.09e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 499188982   1122 GPYVLLGYSAGGNLAFEVAQAMERKGLEVSDFIIVDAYLKEQPLPIDTGNDESAAYL 1178
Cdd:smart00824   64 RPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPPGDPAPEGWLPELLRGVF 120
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 476-560 2.99e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 45.48  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  476 HTIIDLFR---EQAEKTPDHTALVYGNMSISYKELDKRSNALARELIQKGFRKNETAGILAAHSPEFMISVLAV--LKAG 550
Cdd:PRK07868  444 HTRISLGRiiaEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALsrLGAV 523

                          90
                  ....*....|
gi 499188982  551 GAYLPLDAEL 560
Cdd:PRK07868  524 AVLMPPDTDL 533
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 615-960 3.12e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 45.02  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  615 PDDLAYIMYTSGSTGRPKGVMITNRNVVSLvrnsnytSASGDDRFIMTGSiSFDAVTFEMF--GALLNGASLHIIDKSTM 692
Cdd:PRK13388  149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAFA-------GRALTERFGLTRD-DVCYVSMPLFhsNAVMAGWAPAVASGAAV 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  693 LTPDRFGAYLLENDIT---VLFLT---TALFNQLAQV-RADmfRGLHTLYV--GGEAlSPALMNAV--RHACpdlALHNI 761
Cdd:PRK13388  221 ALPAKFSASGFLDDVRrygATYFNyvgKPLAYILATPeRPD--DADNPLRVafGNEA-SPRDIAEFsrRFGC---QVEDG 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  762 YGPTENTTFSTffemKRDYAGPIPIGKPISNSTAY-----------ILDTKGRLL-PIGVPGELC-VGGDGVAKGYLNRV 828
Cdd:PRK13388  295 YGSSEGAVIVV----REPGTPPGSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYYNNP 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  829 DLTnavfsphpflpGERI----YRTGDLARWLPDGNLEYISRIDRQMKIRGKRIEPAEIEARLLEMEGVQEAAV--TLRE 902
Cdd:PRK13388  371 EAT-----------AERMrhgmYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyaVPDE 439

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499188982  903 KDGEAQLYTHYVGDHKKTDTD-FRADLA--RVLPDYMIPQHwVRV-ERMPLTGNGKIDRSAL 960
Cdd:PRK13388  440 RVGDQVMAALVLRDGATFDPDaFAAFLAaqPDLGTKAWPRY-VRIaADLPSTATNKVLKREL 500
prpE PRK10524
propionyl-CoA synthetase; Provisional
 486-634 1.48e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 43.01  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  486 AEKTPDHTALVY------GNMSISYKELDKRSNALA---REL-IQKGFRK-------NETA-----------------GI 531
Cdd:PRK10524   63 LAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAamlRSLgVQRGDRVliympmiAEAAfamlacarigaihsvvfGG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499188982  532 LAAHS---------PEFMISVLAVLKAGG--AYLPL------DAELPPERVsfmleetqakmLIVQKGLEQNAAFSGTCI 594
Cdd:PRK10524  143 FASHSlaariddakPVLIVSADAGSRGGKvvPYKPLldeaiaLAQHKPRHV-----------LLVDRGLAPMARVAGRDV 211

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 499188982  595 isDAQGLME---ENDIPINI--SSSPddlAYIMYTSGSTGRPKGV 634
Cdd:PRK10524  212 --DYATLRAqhlGARVPVEWleSNEP---SYILYTSGTTGKPKGV 251
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 847-893 1.50e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 42.44  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499188982  847 YRTGDLARWLPDGN--------LEYIS-RIDRQMKIRGKRIEPAEIEARLLEMEGV 893
Cdd:COG1541   297 YRTGDLTRLLPEPCpcgrthprIGRILgRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 620-635 5.76e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 40.89  E-value: 5.76e-03
                          10
                  ....*....|....*.
gi 499188982  620 YIMYTSGSTGRPKGVM 635
Cdd:PRK00174  249 FILYTSGSTGKPKGVL 264
 
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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