|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1-631 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 1308.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 1 MAYHNPFIVNGKIKFPDNTNLVKHVEKWARVRGDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRI 80
Cdd:PRK07769 3 MAFHNPFDVNGKIRFPPNTNLVRHVERWAKVRGDKLAYRFLDFSTERDGVARDLTWSQFGARNRAVGARLQQVTKPGDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 81 AVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVD 160
Cdd:PRK07769 83 AILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERPRVIAVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 161 AVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLS 240
Cdd:PRK07769 163 AVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 241 PVLGHNFTFMTPAAFVRRPGRWIREMARKPEDAPdsEVFTVAPNFAFEHAAVRGVPKEGEPPLDLSNVKAILNGSEPVSP 320
Cdd:PRK07769 243 ALLGHYITFMSPAAFVRRPGRWIRELARKPGGTG--GTFSAAPNFAFEHAAARGLPKDGEPPLDLSNVKGLLNGSEPVSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 321 ASMRKFYEAFSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVEVPADSPKAVPQVSAGTIGVDE 400
Cdd:PRK07769 321 ASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 401 WAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILKSRISQSHAEGAPDDGMWVKTGDYGTYYKGHLY 480
Cdd:PRK07769 401 WAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRLSESHAEGAPDDALWVRTGDYGVYFDGELY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 481 IAGRIKDLVIIDGRNHYPQDLEYSAQEASKALRTGYVAAFSVPANQLPKEVFDNPHTGLKYDPDDSSEQLVIVAERAAGS 560
Cdd:PRK07769 481 ITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVVFDDSHAGLKFDPEDTSEQLVIVAERAPGA 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497642598 561 HKLDYQPIADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLRSGVGSPTAFANST 631
Cdd:PRK07769 561 HKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQPAFPDASD 631
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
3-630 |
0e+00 |
|
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.
Pssm-ID: 468483 [Multi-domain] Cd Length: 625 Bit Score: 1241.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 3 YHNPFIV-NGKIKFPDNTNLVKHVEKWARVRGDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIA 81
Cdd:NF038339 1 EFEPFLDeNGNIRFPDGATLVDHVERNARERADTLAYRFIDYSRERDGEARDLTWAQFGARLRAVAARLQQVTKPGDRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 82 VLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDA 161
Cdd:NF038339 81 ILAPQGLDYVVSFFAAIYAGNIAVPLFDPDEPGHTDRLHAVLGDCKPSAILTATSSAEGVRKFFRSLPAKERPRVIAVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 162 VPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSP 241
Cdd:NF038339 161 VPDSVGSTWVRPDADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPLFHDMGLLTVILPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 242 VLGHNFTFMTPAAFVRRPGRWIREMARKPEDAPdseVFTVAPNFAFEHAAVRGVPKEGEpPLDLSNVKAILNGSEPVSPA 321
Cdd:NF038339 241 LGGKYITIMSPAAFVRRPGRWIRELAAVSDGAG---TFAAAPNFAFEHAAARGLPKEGE-PLDLSNVIGLINGSEPVTTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 322 SMRKFYEAFSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVEVPADSPKAVPQVSAGTIGVDEW 401
Cdd:NF038339 317 SMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAKVIYVDREELNAGRIVEVDPDAPNAVAQVSCGYVARSQW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 402 AVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILKSRISQ-SHAEGAPDDGMWVKTGDYGTYYKGHLY 480
Cdd:NF038339 397 AVIVDPETGTELPDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLKSRLEEgSHAEGAPEDANWMRTGDYGVYYDGELY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 481 IAGRIKDLVIIDGRNHYPQDLEYSAQEASKALRTGYVAAFSVPANQLPKEVFDNPHTGLKYDPDDSSEQLVIVAERAAGS 560
Cdd:NF038339 477 ITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVPANQLPAEVFENSHSGLKYDADDSSEQLVIVAERAPGA 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 561 HKLDYQPIADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLRSGVgSPTAFANS 630
Cdd:NF038339 557 GKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACKAAYIDGTLRGGY-QQTAFPDA 625
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
11-619 |
0e+00 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 777.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 11 GKIKFPDNTNLVKHVEKWARVRGDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDY 90
Cdd:PRK12476 26 GNIALPPGTTLISLIERNIANVGDTVAYRYLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 91 LIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTW 170
Cdd:PRK12476 106 VAGFFAAIKAGTIAVPLFAPELPGHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRPRVIAIDAIPDSAGESF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 171 EPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQ-VLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTF 249
Cdd:PRK12476 186 VPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQmILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 250 MTPAAFVRRPGRWIREMArkpEDAPDSEVFTVAPNFAFEHAAVRGVPKEGEpPLDLSNVkAILNGSEPVSPASMRKFYEA 329
Cdd:PRK12476 266 MSPTAFVRRPQRWIKALS---EGSRTGRVVTAAPNFAYEWAAQRGLPAEGD-DIDLSNV-VLIIGSEPVSIDAVTTFNKA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 330 FSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVEVPADSPKAVPQVSAGTIGVDEWAVIVDPET 409
Cdd:PRK12476 341 FAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 410 ASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILKSRISQ-SHAEGAPDDGMWVKTGDYGTYYKGHLYIAGRIKDL 488
Cdd:PRK12476 421 GAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRLAEgSHADGAADDGTWLRTGDLGVYLDGELYITGRIADL 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 489 VIIDGRNHYPQDLEYSAQEASKALRTGYVAAFSVPANQlpkevfdnphtglkydpddsSEQLVIVAERAAGSHKLDYQPI 568
Cdd:PRK12476 501 IVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAED--------------------NERLVIVAERAAGTSRADPAPA 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 497642598 569 ADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLRS 619
Cdd:PRK12476 561 IDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
27-614 |
0e+00 |
|
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: 734.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 27 KWARVRGDKLAYRFVDFSTERDgeyRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVP 106
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGRE---ETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 107 LFDPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPEADENTIAYLQYT 186
Cdd:cd05931 78 LPPPTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 187 SGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVL-GHNFTFMTPAAFVRRPGRWIRE 265
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYsGGPSVLMSPAAFLRRPLRWLRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 266 MARKPedapdsEVFTVAPNFAFEHAAVRGVPKEGEpPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRETAIKPSYG 345
Cdd:cd05931 238 ISRYR------ATISAAPNFAYDLCVRRVRDEDLE-GLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 346 LAEATLFVSTTPMDQAPTVIHVDRDELNkQRFVEVPADSPKAVPQVSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHG 425
Cdd:cd05931 311 LAEATLFVSGGPPGTGPVVLRVDRDALA-GRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 426 NNLGTGYWGREQETNDIFRnilksrisqshAEGAPDDGMWVKTGDYGTYYKGHLYIAGRIKDLVIIDGRNHYPQDLEYSA 505
Cdd:cd05931 390 PSVASGYWGRPEATAETFG-----------ALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 506 QEASKALRTGYVAAFSVpanqlpkevfdnphtglkydPDDSSEQLVIVAERAAGSHKLDYQPIADDIRAAIAVRHGVTVR 585
Cdd:cd05931 459 EEAHPALRPGCVAAFSV--------------------PDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPA 518
|
570 580
....*....|....*....|....*....
gi 497642598 586 DLLLVQSGTIPRTSSGKIGHRACRAAYLD 614
Cdd:cd05931 519 DVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
33-614 |
0e+00 |
|
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.
Pssm-ID: 468603 [Multi-domain] Cd Length: 613 Bit Score: 647.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 33 GDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAE 112
Cdd:NF040633 42 GDRVCIRFWDYSESREGTAVEYTRAEVNTRIKAVAARLQQVGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLYDPNE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 113 PGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPEADE--------------N 178
Cdd:NF040633 122 PGHADHLRAVLADSGPTVVLTNKTSAPAVRAHFADLPAAERPRILSVDSLPDSLAESWVNPMATIegqpllapagtdpsD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 179 TIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAFVRR 258
Cdd:NF040633 202 DTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAFVTILGLEFELMSPRDFIQQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 259 PGRWIREMARKPEDApdsEVFTVAPNFAFEHAAVRGVPKEGEPpLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRET 338
Cdd:NF040633 282 PKRWVDQLSRREDDV---NVYTVVPNFALELAARYANPEEGED-LDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 339 AIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVEVPADSPKAVPQVSAGTIGVDEWAVIVDPETASELPDGQI 418
Cdd:NF040633 358 ALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAVEVAEDSENAVPFASNGQVVRPQVLAIVDPETGQELPDGTV 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 419 GEIWLHGNNLGTGYWGREQETNDIFRNILKSRISQ-SHAEGAPDDGmWVKTGDYGTYYKGHLYIAGRIKDLVIIDGRNHY 497
Cdd:NF040633 438 GEIWVHGDNMAAGYLDREEETAETFRNTLGERLAEnSRAEGAPEDN-WMATGDLGVIVDGELYITGRLKDLIVIAGRNHY 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 498 PQDLEYSAQEASKALRTGYVAAFSVPAnqlpkevfdnphtglkydpdDSSEQLVIVAERAAGSHKLDYQPIADDIRAAIA 577
Cdd:NF040633 517 PQDIEATVQEASDHIRPDSVAAFAVPG--------------------DDVEKLVILAERDDEADESGDAEAIEAIRAAVT 576
|
570 580 590
....*....|....*....|....*....|....*..
gi 497642598 578 VRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLD 614
Cdd:NF040633 577 SAHGVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
29-615 |
5.67e-178 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 517.19 E-value: 5.67e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLF 108
Cdd:PRK05850 11 ASLQPDDAAFTFIDYEQDPAGVAETLTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQGLEYIVAFLGALQAGLIAVPLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 109 DPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPEADENTIAYLQYTSG 188
Cdd:PRK05850 91 VPQGGAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPSTAYLQYTSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 189 STRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRG------LSWLPFFHDMGLITALLSPVL-GHNFTFMTPAAFVRRPGR 261
Cdd:PRK05850 171 STRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVPppdttvVSWLPFYHDMGLVLGVCAPILgGCPAVLTSPVAFLQRPAR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 262 WIREMARKPedapdsEVFTVAPNFAFEhAAVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRETAIK 341
Cdd:PRK05850 251 WMQLLASNP------HAFSAAPNFAFE-LAVRKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 342 PSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRfvEVPADSPKAVPQVSAGTigVDEWAV-IVDPETASELPDGQIGE 420
Cdd:PRK05850 324 PSYGLAEATVYVATREPGQPPESVRFDYEKLSAGH--AKRCETGGGTPLVSYGS--PRSPTVrIVDPDTCIECPAGTVGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 421 IWLHGNNLGTGYWGREQETNDIFRNILKSRisqshAEGAPdDGMWVKTGDYGTYYKGHLYIAGRIKDLVIIDGRNHYPQD 500
Cdd:PRK05850 400 IWVHGDNVAAGYWQKPEETERTFGATLVDP-----SPGTP-EGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 501 LEYSAQEASKalrtGYVAAFSVpanqlpkevfdnphtglkydPDDSSEQLVIVAE-----RAAGSHKLDYQPIADDIRAA 575
Cdd:PRK05850 474 IEATIQEITG----GRVAAISV--------------------PDDGTEKLVAIIElkkrgDSDEEAMDRLRTVKREVTSA 529
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 497642598 576 IAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLDG 615
Cdd:PRK05850 530 ISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYRQD 569
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
18-613 |
1.99e-134 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 405.80 E-value: 1.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 18 NTNLVKHVEKWARVRGDKLAYRFVDFSTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGA 97
Cdd:NF038337 3 NSSVVSLLRERAGLQPDDVAFRYTDYEQDWAGVTETLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAPQGLPYIVAFLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 98 LYAGRIAVPLFDPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPEADE 177
Cdd:NF038337 83 MQAGLIAVPLSVPQPGSHDERVSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPAVIEIDSLDLDGPNSPSIRISDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 178 NTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVL-------NGLEGKEgDRGLSWLPFFHDMGLITALLSPVLG-HNFTF 249
Cdd:NF038337 163 PSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMaayfpdtNGVAPRD-TTIVSWLPFYHDMGLVLGVIAPILGgYRSEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 250 MTPAAFVRRPGRWIREMARKpedapdSEVFTVAPNFAFEhAAVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEA 329
Cdd:NF038337 242 TSPVAFLQRPARWIHAMANG------SPVFSAAPNFAFE-LAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 330 FSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVEVPADSpkAVPQVSAGTiGVDEWAVIVDPET 409
Cdd:NF038337 315 FAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEGSAQRCEART--GSPLLSYGT-PTSPTVRIVDPDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 410 ASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILksrisqSHAEGAPDDGMWVKTGDYGTYYKGHLYIAGRIKDLV 489
Cdd:NF038337 392 CIECPAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVL------ANPSPGTPEGPWLRTGDLGFISEDEMFIVGRMKDLL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 490 IIDGRNHYPQDLEYSAQEASKalrtGYVAAFSVPAnqlpkevfdnphtglkydpdDSSEQLVIVAE-------RAAGSHK 562
Cdd:NF038337 466 IVYGRNHYPEDIESTVQEITG----GRVAAISVPV--------------------DETEKLVTIIElkkrgdsDEEAMRK 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 497642598 563 LDyqPIADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYL 613
Cdd:NF038337 522 LD--AVKNNVTAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQYR 570
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-619 |
1.78e-107 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 357.17 E-value: 1.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 19 TNLVKHVEKWARVRGDKLAYRFVdfsTERDGEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGAL 98
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFL---ADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 99 YAGRIAVPLFDP--AEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKfIRARSAKERPRVIAVDAVPNEVASTWEPPEAD 176
Cdd:PRK05691 86 YAGVIAVPAYPPesARRHHQERLLSIIADAEPRLLLTVADLRDSLLQ-MEELAAANAPELLCVDTLDPALAEAWQEPALQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 177 ENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNG--LEGKEGDRGLSWLPFFHDMGLITALLSPVL-GHNFTFMTPA 253
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGfgIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 254 AFVRRPGRWIREMARKpedapdSEVFTVAPNFAFEHAAVRgVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPY 333
Cdd:PRK05691 245 YFLERPLRWLEAISEY------GGTISGGPDFAYRLCSER-VSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAAC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 334 GLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRfvevpADSPKAVPQVSAGTIGVDEWAVIVDPETASEL 413
Cdd:PRK05691 318 GFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR-----AEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 414 PDGQIGEIWLHGNNLGTGYWGREQETNDIFRNIlksrisqshaegapDDGMWVKTGDYGTYYKGHLYIAGRIKDLVIIDG 493
Cdd:PRK05691 393 GDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH--------------DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 494 RNHYPQDLEYSAQEASKALRTGYVAAFSVpanqlpkevfdnphtglkydPDDSSEQLVIVAERAAGSHK-LDYQPIADDI 572
Cdd:PRK05691 459 HNLYPQDIEKTVEREVEVVRKGRVAAFAV--------------------NHQGEEGIGIAAEISRSVQKiLPPQALIKSI 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 497642598 573 RAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLRS 619
Cdd:PRK05691 519 RQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
75-619 |
1.24e-100 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 318.10 E-value: 1.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPG----HVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSA 150
Cdd:PRK09192 72 KPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGgresYIAQLRGMLASAQPAAIITPDELLPWVNEATHGNPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 151 KERPRVIAVDAVPnevASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQ-VLNGLEGKEGDRGLSWLPFF 229
Cdd:PRK09192 152 LHVLSHAWFKALP---EADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAiSHDGLKVRPGDRCVSWLPFY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 230 HDMGLITALLSPVLGH-NFTFMTPAAFVRRPGRWIREMARKPEdapdseVFTVAPNFAFEHAAVRgVPKEGEPPLDLSNV 308
Cdd:PRK09192 229 HDMGLVGFLLTPVATQlSVDYLPTRDFARRPLQWLDLISRNRG------TISYSPPFGYELCARR-VNSKDLAELDLSCW 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 309 KAILNGSEPVSPASMRKFYEAFSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDEL-NKQRFVEVPADSPKA 387
Cdd:PRK09192 302 RVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVDRDRLeYQGKAVAPGAETRRV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 388 VPQVSAGTIgVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWgREQETNDIFRnilksrisqshAEGapddgmWVK 467
Cdd:PRK09192 382 RTFVNCGKA-LPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF-RDEESQDVLA-----------ADG------WLD 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 468 TGDYGTYYKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAqEASKALRTGYVAAFSVpanqlpkevfdnphtglkydPDDSS 547
Cdd:PRK09192 443 TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIA-EQEPELRSGDAAAFSI--------------------AQENG 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642598 548 EQLVIVAErAAGSHKLDYQPIADDIRAAIAVRHGVTVrDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLRS 619
Cdd:PRK09192 502 EKIVLLVQ-CRISDEERRGQLIHALAALVRSEFGVEA-AVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
21-619 |
1.63e-90 |
|
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: 287.86 E-value: 1.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 21 LVKHVEKWARVRGDKLAYRFvdfsterdgEYRDIVWSDFSARNRAVGARLQQVT-QPGDRIAVLCPQNLDYLIAFFGALY 99
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF---------GGRRLTYAELDARARRLAAALRALGvGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 100 AGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTttdaaegvrkfirarsakerprviavdavpnevastweppeadent 179
Cdd:COG0318 72 AGAVVVPL-NPRLTAE--ELAYILEDSGARALVT---------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 180 iAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAafvRRP 259
Cdd:COG0318 103 -ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR---FDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 260 GRWIREMARkpEDApdsEVFTVAPNFAFEHAAVrgvpkEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglretA 339
Cdd:COG0318 179 ERVLELIER--ERV---TVLFGVPTMLARLLRH-----PEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV------R 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 IKPSYGLAEATLFVSTTPMDqaptvihvdrdelnkqrfvevpadsPKAVPQVSAGTIGVDEWAVIVDPETAsELPDGQIG 419
Cdd:COG0318 243 IVEGYGLTETSPVVTVNPED-------------------------PGERRPGSVGRPLPGVEVRIVDEDGR-ELPPGEVG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 420 EIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYP 498
Cdd:COG0318 297 EIVVRGPNVMKGYWNDPEATAEAFR-----------------DG-WLRTGDLGRLDEdGYLYIVGRKKDMIISGGENVYP 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 499 QDLEYSAQEASKALRtgyVAAFSVPanqlpkevfdNPHTGlkydpddssEQLVIVAERAAGsHKLDYQPIADDIRAAIAv 578
Cdd:COG0318 359 AEVEEVLAAHPGVAE---AAVVGVP----------DEKWG---------ERVVAFVVLRPG-AELDAEELRAFLRERLA- 414
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 497642598 579 RHGVtVRDLLLVQSgtIPRTSSGKIGHRACRAAYLDGSLRS 619
Cdd:COG0318 415 RYKV-PRRVEFVDE--LPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
56-610 |
1.11e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 256.85 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 56 WSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHA----VLDDCSPST 130
Cdd:PRK07768 32 WGEVHERARRIAGGLAAAgVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEdtlrVIGMIGAKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 131 ILTTT--DAAEGVrkfIRARSAkerpRVIAV-DAVPNEVAstwEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNV 207
Cdd:PRK07768 112 VVVGEpfLAAAPV---LEEKGI----RVLTVaDLLAADPI---DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 208 LQVLNGLEGK-EGDRGLSWLPFFHDMGLITALLSP-VLGHNFTFMTPAAFVRRPGRWIREMARKpedapdSEVFTVAPNF 285
Cdd:PRK07768 182 EAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPmYFGAELVKVTPMDFLRDPLLWAELISKY------RGTMTAAPNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 286 AFEHAA--VRGVPKEGEppLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPT 363
Cdd:PRK07768 256 AYALLArrLRRQAKPGA--FDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 364 VIHVDRDELNKQRFVeVPADSPKAVPQVSAGTIGVDEWAVIVDpETASELPDGQIGEIWLHGNNLGTGYwgreqetndif 443
Cdd:PRK07768 334 VDEVDADLLAALRRA-VPATKGNTRRLATLGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGY----------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 444 rnilksrISQSHAEGAPDDGMWVKTGDYGtYY--KGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASkALRTGYVAAFs 521
Cdd:PRK07768 401 -------LTMDGFIPAQDADGWLDTGDLG-YLteEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVE-GVRPGNAVAV- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 522 vpanqlpkevfdnphtglKYDPDDSSEQLVIVAERAAGSHKLDYQPIADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSG 601
Cdd:PRK07768 471 ------------------RLDAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSG 532
|
....*....
gi 497642598 602 KIGHRACRA 610
Cdd:PRK07768 533 KLRRANAAE 541
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
75-603 |
4.08e-76 |
|
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: 251.64 E-value: 4.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfdpaepghvgrlhavlddcspsTILTTTDAAEGVRKFIRARSakeRP 154
Cdd:cd05908 38 KPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV----------------------SIGSNEEHKLKLNKVWNTLK---NP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 155 RVIAVDAVPNEVAstweppeaDEntIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGL 234
Cdd:cd05908 93 YLITEEEVLCELA--------DE--LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 235 ITALLSPVL-GHNFTFMTPAAFVRRPGRWIREMARKPEDapdsevFTVAPNFAFEHAAVRGVPKEGEpPLDLSNVKAILN 313
Cdd:cd05908 163 IAFHLAPLIaGMNQYLMPTRLFIRRPILWLKKASEHKAT------IVSSPNFGYKYFLKTLKPEKAN-DWDLSSIRMILN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 314 GSEPVSPASMRKFYEAFSPYGLRETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDRDELN-KQRFVEVPADSPKAVPQVS 392
Cdd:cd05908 236 GAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPKAQSPFKTITLGRRHVThGEPEPEVDKKDSECLTFVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 393 AGTiGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegaPDDGmWVKTGDYG 472
Cdd:cd05908 316 VGK-PIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF----------------TDDG-WLKTGDLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 473 TYYKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKALrTGYVAAFSVpanqlpkevfdnphtglkYDPDDSSEQLVI 552
Cdd:cd05908 378 FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE-LGRVVACGV------------------NNSNTRNEEIFC 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497642598 553 VAERAAGSHklDYQPIADDIRAAIAVRHGVTVRDLLLVQsgTIPRTSSGKI 603
Cdd:cd05908 439 FIEHRKSED--DFYPLGKKIKKHLNKRGGWQINEVLPIR--RIPKTTSGKV 485
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
25-491 |
5.92e-67 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 224.88 E-value: 5.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 25 VEKWARVRGDKLAYRfvdfsterDGEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRI 103
Cdd:pfam00501 1 LERQAARTPDKTALE--------VGEGRRLTYRELDERANRLAAGLRALgVGKGDRVAILLPNSPEWVVAFLACLKAGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 104 AVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDA-AEGVRKFIRARSAKERPRVIAVDAVPNEVASTWE----------P 172
Cdd:pfam00501 73 YVPL-NPRLPAE--ELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEakpadvppppP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 173 PEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLN----GLEGKEGDRGLSWLPFFHDMGLITALLSPVL-GHNF 247
Cdd:pfam00501 150 PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLaGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 248 TFMTPAAFvRRPGRWIREMAR-KPEdapdseVFTVAPnfafehAAVRGVPKEGEP-PLDLSNVKAILNGSEPVSPASMRK 325
Cdd:pfam00501 230 VLPPGFPA-LDPAALLELIERyKVT------VLYGVP------TLLNMLLEAGAPkRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 326 FYEAFSPyglretAIKPSYGLAEATLFVSTTPMDQAPTVihvdrdelnkqrfvevpadspkavpqvSAGTIGVDEWAV-- 403
Cdd:pfam00501 297 FRELFGG------ALVNGYGLTETTGVVTTPLPLDEDLR---------------------------SLGSVGRPLPGTev 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 404 -IVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegapDDGMWVKTGDYGTYYK-GHLYI 481
Cdd:pfam00501 344 kIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF-----------------DEDGWYRTGDLGRRDEdGYLEI 406
|
490
....*....|
gi 497642598 482 AGRIKDLVII 491
Cdd:pfam00501 407 VGRKKDQIKL 416
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
48-615 |
7.14e-65 |
|
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: 222.54 E-value: 7.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 48 DGEYRDIVWSDFSARNRAVGARLQQVT-QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDP-------AEPGHVGRL 119
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGLRQLGlRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPptydepnARLRKLRHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 120 HAVLDDCspsTILTTTDAAEGVRKfIRARSAKERPRVIAVDAVPNEVAST-WEPPEADenTIAYLQYTSGSTRTPTGVQI 198
Cdd:cd05906 114 WQLLGSP---VVLTDAELVAEFAG-LETLSGLPGIRVLSIEELLDTAADHdLPQSRPD--DLALLMLTSGSTGFPKAVPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 199 THLNLptnvlqvLNGLEGK-------EGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPA-AFVRRPGRWIREMARKp 270
Cdd:cd05906 188 THRNI-------LARSAGKiqhngltPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTeEILADPLRWLDLIDRY- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 271 edapdSEVFTVAPNFAFEHAAvRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRETAIKPSYGLAE-- 348
Cdd:cd05906 260 -----RVTITWAPNFAFALLN-DLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTEtc 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 349 ATLFVSTTPMDQaptvihvDRDELNkqRFVEVPADSPkavpqvsagtiGVDewAVIVDPETASeLPDGQIGEIWLHGNNL 428
Cdd:cd05906 334 SGVIYSRSFPTY-------DHSQAL--EFVSLGRPIP-----------GVS--MRIVDDEGQL-LPEGEVGRLQVRGPVV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 429 GTGYWGREQETNDIFRnilksrisqshaegapDDGmWVKTGDYGTYYKGHLYIAGRIKDLVIIDGRNHYPQDLEySAQEA 508
Cdd:cd05906 391 TKGYYNNPEANAEAFT----------------EDG-WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIE-AAVEE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 509 SKALRTGYVAAFSVpanqlpkevfdnphtglkYDPDDSSEQLVIV-AERAAGSHKLDyqPIADDIRAAIAVRHGVTVRDL 587
Cdd:cd05906 453 VPGVEPSFTAAFAV------------------RDPGAETEELAIFfVPEYDLQDALS--ETLRAIRSVVSREVGVSPAYL 512
|
570 580
....*....|....*....|....*...
gi 497642598 588 LLVQSGTIPRTSSGKIGHRACRAAYLDG 615
Cdd:cd05906 513 IPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-502 |
3.71e-53 |
|
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: 188.93 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 26 EKWARVRGDKLAYRFVDFSTErdgeYRDIVwsdfsARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIA 104
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLT----YRELD-----ALAEAFAAGLQNLgVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 105 V---PLFDPAEpghvgrLHAVLDDCSPSTILTTTDaaegvrkFIRARSAKERPRviavdavpnevastwEPPEADENTIA 181
Cdd:cd05936 77 VplnPLYTPRE------LEHILNDSGAKALIVAVS-------FTDLLAAGAPLG---------------ERVALTPEDVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 182 YLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEG--KEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAfvrRP 259
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDllEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRF---RP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 260 GRWIREMARKPedapdSEVFTVAPNFafeHAAVRGVPKEGEppLDLSNVKAILNGSEPVSPASMRKFYEAFspyGLReta 339
Cdd:cd05936 206 IGVLKEIRKHR-----VTIFPGVPTM---YIALLNAPEFKK--RDFSSLRLCISGGAPLPVEVAERFEELT---GVP--- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 IKPSYGLAEAtlfvsttpmdqAPtVIHVDRdelnkqrfvevPADSPKavpqvsAGTIGVDEW---AVIVDPETaSELPDG 416
Cdd:cd05936 270 IVEGYGLTET-----------SP-VVAVNP-----------LDGPRK------PGSIGIPLPgteVKIVDDDG-EELPPG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 417 QIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRN 495
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAFV-----------------DG-WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFN 381
|
....*..
gi 497642598 496 HYPQDLE 502
Cdd:cd05936 382 VYPREVE 388
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
54-618 |
3.81e-49 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 180.24 E-value: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 54 IVWSDFSARNRAVGARLQQ--VTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGR-LHAVLDDCSPST 130
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQKkvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFlLGTCKVRVALTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 131 ILTTTDAAEGVRK-FIRARSAKER--PRVIAVDAVPNEVASTWEP----PEADENTIAYLQYTSGSTRTPTGVQITHLNL 203
Cdd:cd05905 95 EACLKGLPKKLLKsKTAAEIAKKKgwPKILDFVKIPKSKRSKLKKwgphPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 204 PTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLI-TALLSPVLGHNFTFMTPAAFVRRPGRWIREMARkpedapdSEVFTVA 282
Cdd:cd05905 175 LAHCRALKEACELYESRPLVTVLDFKSGLGLWhGCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQ-------YKVRDAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 283 PNFAFEHAAVRGVPKEGEP----PLDLSNVKAIL-NGSEPVSPASMRKFYEAFSPYGLRETAIKPSYGlAEATLFVST-T 356
Cdd:cd05905 248 VKLRTLHWCLKDLSSTLASlknrDVNLSSLRMCMvPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFG-TRVNPFICWqG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 357 PMDQAPTVIHVDRDELNKQRFVEVPADSPKAVPQVSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGRE 436
Cdd:cd05905 327 TSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLLD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 437 QETNDIFRNILKSRISqshaEGAPDDGmWVKTGDYG-----------TYYKGHLYIAGRIKDLVIIDGRNHYPQDLEYSA 505
Cdd:cd05905 407 GETNDTFKVFPSTRLS----TGITNNS-YARTGLLGflrptkctdlnVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 506 QEASKAlrTGYVAAFSVpanqlpkevfdnphtglkydpddsSEQLVIVAERAAGSH--KLDYQPIaddIRAAIAVRHGVT 583
Cdd:cd05905 482 MRVHPY--RGRCAVFSI------------------------TGLVVVVAEQPPGSEeeALDLVPL---VLNAILEEHQVI 532
|
570 580 590
....*....|....*....|....*....|....*
gi 497642598 584 VRDLLLVQSGTIPRTSSGKIGHRACRAAYLDGSLR 618
Cdd:cd05905 533 VDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLH 567
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
49-603 |
5.53e-47 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 173.41 E-value: 5.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARLQQVTQPGDRIAVLCPqNLDYLIAFFGALYAGRiAVPLFdpaePGHVgrLHAVLDDCSP 128
Cdd:PRK05851 27 GLWRRHPWPEVHGRAENVAARLLDRDRPGAVGLVGEP-TVELVAAIQGAWLAGA-AVSIL----PGPV--RGADDGRWAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 129 STIltTTDAAEGVRKFI-------RARSAKERPRVIAVDAVPNEVASTWEPPEADEnTIAYLQYTSGSTRTPTGVQIThl 201
Cdd:PRK05851 99 ATL--TRFAGIGVRTVLshgshleRLRAVDSSVTVHDLATAAHTNRSASLTPPDSG-GPAVLQGTAGSTGTPRTAILS-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 202 nlPTNVLQVLNGLEGKEG-----DRGLSWLPFFHDMGLITaLLSPVLGHNFTFMTP-AAFVRRPGRWIREMArkpedapD 275
Cdd:PRK05851 174 --PGAVLSNLRGLNARVGldaatDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPtTAFSASPFRWLSWLS-------D 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 276 SEV-FTVAPNFAFehaAVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRETAIKPSYGLAEATLFVs 354
Cdd:PRK05851 244 SRAtLTAAPNFAY---NLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTCAV- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 355 TTPmdqAP-TVIHVDRDELNKQRFVEVPADSPKAVPqvsagtiGVDewAVIVDPETASELPDGQIGEIWLHGNNLGTGYW 433
Cdd:PRK05851 320 TVP---VPgIGLRVDEVTTDDGSGARRHAVLGNPIP-------GME--VRISPGDGAAGVAGREIGEIEIRGASMMSGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 434 GreqetndifrnilksrisqsHAEGAPDDgmWVKTGDYGTYYKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEAsKALR 513
Cdd:PRK05851 388 G--------------------QAPIDPDD--WFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGVR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 514 TGYVAAFSVpanqlpkevfdnphtglkydpDDSSEQ--LVIVAERAAgshkldyqPIADDIRAA----IAVRHGVTVRDL 587
Cdd:PRK05851 445 EGAVVAVGT---------------------GEGSARpgLVIAAEFRG--------PDEAGARSEvvqrVASECGVVPSDV 495
|
570
....*....|....*.
gi 497642598 588 LLVQSGTIPRTSSGKI 603
Cdd:PRK05851 496 VFVAPGSLPRTSSGKL 511
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-603 |
1.14e-45 |
|
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: 165.15 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 179 TIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPaafvRR 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 259 PGRWIREMAR-KPEdapdsevFTVAPNFAFEHAAVRgvpkEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglre 337
Cdd:cd04433 77 PEAALELIEReKVT-------ILLGVPTLLARLLKA----PESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 338 tAIKPSYGLAEATLFVSTTPMDqaptvihvdrdelnkqRFVEVPADSPKAVPqvsagtiGVDewAVIVDPETAsELPDGQ 417
Cdd:cd04433 141 -KLVNGYGLTETGGTVATGPPD----------------DDARKPGSVGRPVP-------GVE--VRIVDPDGG-ELPPGE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 418 IGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGtyYK---GHLYIAGRIKDLVIIDGR 494
Cdd:cd04433 194 IGELVVRGPSVMKGYWNNPEATAAVDE-----------------DG-WYRTGDLG--RLdedGYLYIVGRLKDMIKSGGE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 495 NHYPQDLEYSAQEASKALRtgyVAAFSVPanqlpkevfdnphtglkyDPDDSSE-QLVIVAERAAGshkldyqPIADDIR 573
Cdd:cd04433 254 NVYPAEVEAVLLGHPGVAE---AAVVGVP------------------DPEWGERvVAVVVLRPGAD-------LDAEELR 305
|
410 420 430
....*....|....*....|....*....|..
gi 497642598 574 AAIAVRHG--VTVRDLLLVqsGTIPRTSSGKI 603
Cdd:cd04433 306 AHVRERLApyKVPRRVVFV--DALPRTASGKI 335
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
52-603 |
1.19e-44 |
|
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: 165.85 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEPGHVgrlhavLDDCS 127
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLgLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAAnpiYTADELAHQ------LKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 128 PSTILTTTDAAEGVRKFirARSAKERPRVI----AVDAVPNEVASTW-----------EPPEADENTIAYLQYTSGSTRT 192
Cdd:cd05911 83 PKVIFTDPDGLEKVKEA--AKELGPKDKIIvlddKPDGVLSIEDLLSptlgeededlpPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 193 PTGVQITHLNLPTNVLQVLNGLEGKEG--DRGLSWLPFFHDMGLITALLSPVLGHNfTFMTPAAFvrrpgrwIREMARKP 270
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLYGNDGsnDVILGFLPLYHIYGLFTTLASLLNGAT-VIIMPKFD-------SELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 271 EDAPDSEVFTVAP--NFAFEHAAvrgVPKEgepplDLSNVKAILNGSEPVSpasmRKFYEAFSPYGLRETaIKPSYGLAE 348
Cdd:cd05911 233 EKYKITFLYLVPPiaAALAKSPL---LDKY-----DLSSLRVILSGGAPLS----KELQELLAKRFPNAT-IKQGYGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 349 ATLFVSTTPmdqaptvihvdrdelnkqRFVEVPAdspkavpqvSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHGNNL 428
Cdd:cd05911 300 TGGILTVNP------------------DGDDKPG---------SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 429 GTGYWGREQETNDIFrnilksrisqshaegapDDGMWVKTGDYGtYYK--GHLYIAGRIKDLVIIDGRNHYPQDLEYSAQ 506
Cdd:cd05911 353 MKGYYNNPEATKETF-----------------DEDGWLHTGDIG-YFDedGYLYIVDRKKELIKYKGFQVAPAELEAVLL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 507 EASKALRTGYVAAFSVPANQLPKE--VfdnphtgLKYDPDDSSEQLV-IVAERAAGSHKLdyqpiaddiraaiavRHGVT 583
Cdd:cd05911 415 EHPGVADAAVIGIPDEVSGELPRAyvV-------RKPGEKLTEKEVKdYVAKKVASYKQL---------------RGGVV 472
|
570 580
....*....|....*....|
gi 497642598 584 VRDlllvqsgTIPRTSSGKI 603
Cdd:cd05911 473 FVD-------EIPKSASGKI 485
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
20-502 |
4.10e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 148.13 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 20 NLVKHVEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGAL 98
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGD---------QRLTYAELNARVRRAAAALAALgIGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 99 YAGRIAVPL---FDPAEPGHV-----GRLHAVLDDCSPsTILTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVAS-- 168
Cdd:PRK07656 77 KAGAVVVPLntrYTADEAAYIlargdAKALFVLGLFLG-VDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAgd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 169 -TWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPvlghnf 247
Cdd:PRK07656 156 pAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 248 tFMTPAAfvrrpgrwireMARKPEDAPDsEVFTVAPNfafEHAAV-RGVPK--------EGEPPLDLSNVKAILNGSEPV 318
Cdd:PRK07656 230 -LMRGAT-----------ILPLPVFDPD-EVFRLIET---ERITVlPGPPTmynsllqhPDRSAEDLSSLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 319 SPASMRKFYEAFsPYGLRETAikpsYGLAEATLFVSTTPMDqaptvihvdrdelnkqrfvevpaDSPKAVpqvsAGTIGV 398
Cdd:PRK07656 294 PVALLERFESEL-GVDIVLTG----YGLSEASGVTTFNRLD-----------------------DDRKTV----AGTIGT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 399 DEWAV---IVDPEtASELPDGQIGEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVKTGDYGTYY 475
Cdd:PRK07656 342 AIAGVenkIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEAT----------------AAAIDADG-WLHTGDLGRLD 403
|
490 500
....*....|....*....|....*...
gi 497642598 476 K-GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK07656 404 EeGYLYIVDRKKDMFIVGGFNVYPAEVE 431
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
15-502 |
1.52e-33 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 134.67 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 15 FPDNTNLVKHVEKWARVRGDKLAyrFVDFSTERDGEYrdivwSDFSARNRAVGARL-QQVTQPGDRIAVLCPQNLDYLIA 93
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPA--LIDAATGRALTY-----AELERRVRRLAAGLaKRGGRKGDVVLLLSPNSIEFPVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 94 FFGALYAGRI---AVPLFDPAEpghvgrLHAVLDDCSPSTILTTTDAAEGVRKFirarsakeRPRVIAVDAVPNEVASTW 170
Cdd:cd05904 74 FLAVLSLGAVvttANPLSTPAE------IAKQVKDSGAKLAFTTAELAEKLASL--------ALPVVLLDSAEFDSLSFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 171 EP-----------PEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNG--LEGKEGDRGLSWLPFFHDMGL--- 234
Cdd:cd05904 140 DLlfeadeaeppvVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGegSNSDSEDVFLCVLPMFHIYGLssf 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 235 ITALLSpvLGhnftfmtpAAFVRRPGRWIREMARKPEdapdsevftvapNFAFEHAAVrgVP--------KEGEPPLDLS 306
Cdd:cd05904 220 ALGLLR--LG--------ATVVVMPRFDLEELLAAIE------------RYKVTHLPV--VPpivlalvkSPIVDKYDLS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 307 NVKAILNGSEPVSPASMRKFYEAFsPyglrETAIKPSYGLAEATLFVSTTpmdqaptvihvdrdelnkqrfvevPADSPK 386
Cdd:cd05904 276 SLRQIMSGAAPLGKELIEAFRAKF-P----NVDLGQGYGMTESTGVVAMC------------------------FAPEKD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 387 AVPQVSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWV 466
Cdd:cd05904 327 RAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEAT----------------AATIDKEG-WL 389
|
490 500 510
....*....|....*....|....*....|....*...
gi 497642598 467 KTGDYGtYY--KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05904 390 HTGDLC-YIdeDGYLFIVDRLKELIKYKGFQVAPAELE 426
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
25-502 |
5.42e-33 |
|
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: 131.96 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 25 VEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRI 103
Cdd:cd17631 1 LRRRARRHPDRTALVFGG---------RSLTYAELDERvNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 104 AVPL---FDPAEpghvgrLHAVLDDCspstiltttdaaegvrkfirarsakeRPRVIAVDavpnevastweppeadentI 180
Cdd:cd17631 72 FVPLnfrLTPPE------VAYILADS--------------------------GAKVLFDD-------------------L 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 181 AYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLsPVLGHNFTFMTPAAFvrRPG 260
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTL-PTLLRGGTVVILRKF--DPE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 261 RWIREMarkpEDAPDSEVFTVaP---NFAFEHAAVRGVpkegepplDLSNVKAILNGSEPvSPASMRKFYEAfspyglRE 337
Cdd:cd17631 178 TVLDLI----ERHRVTSFFLV-PtmiQALLQHPRFATT--------DLSSLRAVIYGGAP-MPERLLRALQA------RG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 338 TAIKPSYGLAEATLFVSTTPMDQAPTVIhvdrdelnkqrfvevpadspkavpqVSAGT--IGVDewAVIVDPETAsELPD 415
Cdd:cd17631 238 VKFVQGYGMTETSPGVTFLSPEDHRRKL-------------------------GSAGRpvFFVE--VRIVDPDGR-EVPP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 416 GQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGR 494
Cdd:cd17631 290 GEVGEIVVRGPHVMAGYWNRPEATAAAFR-----------------DG-WFHTGDLGRLDEdGYLYIVDRKKDMIISGGE 351
|
....*...
gi 497642598 495 NHYPQDLE 502
Cdd:cd17631 352 NVYPAEVE 359
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
75-493 |
1.12e-32 |
|
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: 130.46 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERP 154
Cdd:TIGR01733 23 GPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYP--AERLAFILEDAGARLLLTDSALASRLAGLVLPVILLDPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 155 RVIAVDAVPNEVASTWEPPEADentIAYLQYTSGSTRTPTGVQITHLNLpTNVLQVLNG-LEGKEGDRGLSWLPFFHDMG 233
Cdd:TIGR01733 100 ELAALDDAPAPPPPDAPSGPDD---LAYVIYTSGSTGRPKGVVVTHRSL-VNLLAWLARrYGLDPDDRVLQFASLSFDAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 234 LITALLSPVLGHNFTFMTPA---AFVRRPGRWIREMArkpedapdSEVFTVAPNFaFEHAAvrgvpkeGEPPLDLSNVKA 310
Cdd:TIGR01733 176 VEEIFGALLAGATLVVPPEDeerDDAALLAALIAEHP--------VTVLNLTPSL-LALLA-------AALPPALASLRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 311 ILNGSEPVSPASMRKFYEAFSpyglrETAIKPSYGLAEATLFVSTTPMDQAPTvihvdrdelnkQRFVEVPADSPKAVPQ 390
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGP-----GARLINLYGPTETTVWSTATLVDPDDA-----------PRESPVPIGRPLANTR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 391 vsagtigvdewAVIVDPETaSELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqsHAEGAPDDGMWVKTGD 470
Cdd:TIGR01733 304 -----------LYVLDDDL-RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVP---------DPFAGGDGARLYRTGD 362
|
410 420
....*....|....*....|....
gi 497642598 471 YGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:TIGR01733 363 LVRYLPdGNLEFLGRIDDQVKIRG 386
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
76-607 |
3.32e-32 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 130.51 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPA-EPGHVGRLHA-------VLDDCS--------PSTILTTTDAAE 139
Cdd:cd05926 38 KGDRVAIALPNGLEFVVAFLAAARAGAVVAPL-NPAyKKAEFEFYLAdlgsklvLTPKGElgpasraaSKLGLAILELAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 140 GVRKFIRARSAKERPRVIAVDAVPNEvastwePPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEG 219
Cdd:cd05926 117 DVGVLIRAPSAESLSNLLADKKNAKS------EGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 220 DRGLSWLPFFHDMGLITALLSPvLGHNFTFMTPAAFvrRPGRWIREMARKpedapDSEVFTVAPNFafeHAAVRGVPKEg 299
Cdd:cd05926 191 DRTLVVMPLFHVHGLVASLLST-LAAGGSVVLPPRF--SASTFWPDVRDY-----NATWYTAVPTI---HQILLNRPEP- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 300 EPPLDLSNVKAILNGSEPVSPASMRKFYEAFspyglrETAIKPSYGLAEATLFVSTTPMDQAPtvihvdrdelnkqrfve 379
Cdd:cd05926 259 NPESPPPKLRFIRSCSASLPPAVLEALEATF------GAPVLEAYGMTEAAHQMTSNPLPPGP----------------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 380 vpaDSPKAVPQVSagtiGVDewAVIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqshaega 459
Cdd:cd05926 316 ---RKPGSVGKPV----GVE--VRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFK-------------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 460 pdDGmWVKTGDYGtYYK--GHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKALRtgyVAAFSVPANQLPKEVfdnpht 537
Cdd:cd05926 372 --DG-WFRTGDLG-YLDadGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLE---AVAFGVPDEKYGEEV------ 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 538 glkydpddsseQLVIVAEraaGSHKLDYQPIADDIRAAIAvRHGVTvRDLLLVQSgtIPRTSSGKIGHRA 607
Cdd:cd05926 439 -----------AAAVVLR---EGASVTEEELRAFCRKHLA-AFKVP-KKVYFVDE--LPKTATGKIQRRK 490
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
13-502 |
3.98e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 131.28 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 13 IKFPDNTnLVKHVEKWARVRGDKLAYRFvdFSTErdgeyrdIVWSDFSARNRAVGARLQQV-TQPGDRIAVL---CPQNL 88
Cdd:PRK05605 27 LDYGDTT-LVDLYDNAVARFGDRPALDF--FGAT-------TTYAELGKQVRRAAAGLRALgVRPGDRVAIVlpnCPQHI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 89 dylIAFFGALYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDDCSPSTILTT--TDAAEGVRKFI-- 145
Cdd:PRK05605 97 ---VAFYAVLRLGAVVVehnPLYTAHELEHpfedhgarvaivwdkvAPTVERLRRTTPLETIVSVnmIAAMPLLQRLAlr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 146 ----RARSAKE---------RPRVIAVDAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQV-- 210
Cdd:PRK05605 174 lpipALRKARAaltgpapgtVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGka 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 211 -LNGLeGKEGDRGLSWLPFFHDMGL-ITALLSPVLGHNFTFMtPA--------AFVRRPGRWIremarkpedapdSEVFT 280
Cdd:PRK05605 254 wVPGL-GDGPERVLAALPMFHAYGLtLCLTLAVSIGGELVLL-PApdidlildAMKKHPPTWL------------PGVPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 281 VAPNFAfEHAAVRGVpkegepplDLSNVKAILNGSEPVSPASMRKfYEAFSPYGLREtaikpSYGLAEATLFVSTTPMdq 360
Cdd:PRK05605 320 LYEKIA-EAAEERGV--------DLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVE-----GYGLTETSPIIVGNPM-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 361 aptvihvdrdelNKQRfvevpadspkavpqvSAGTIGV---DEWAVIVDPETASE-LPDGQIGEIWLHGNNLGTGYWGRE 436
Cdd:PRK05605 383 ------------SDDR---------------RPGYVGVpfpDTEVRIVDPEDPDEtMPDGEEGELLVRGPQVFKGYWNRP 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 437 QETNDIFRnilksrisqshaegapdDGmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK05605 436 EETAKSFL-----------------DG-WFRTGDVVVMEEdGFIRIVDRIKELIITGGFNVYPAEVE 484
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-528 |
4.15e-32 |
|
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: 129.64 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDpaepghvgrlhavlddcs 127
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALgVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYP------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 128 pstilttTDAAEGVRkFIRARSAkerPRVIAVDAvPNEVAStweppeadentiayLQYTSGSTRTPTGVQITHLNLPTNV 207
Cdd:cd05907 63 -------TSSAEQIA-YILNDSE---AKALFVED-PDDLAT--------------IIYTSGTTGRPKGVMLSHRNILSNA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 208 LQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAfvrrpgRWIREMAR--KPEdapdseVFTVAPNF 285
Cdd:cd05907 117 LALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSA------ETLLDDLSevRPT------VFLAVPRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 286 aFE--HAAVRGVpkeGEPPLD--------LSNVKAILNGSEPVSPASMRkFYEAFspyGLretAIKPSYGLAEatlfvsT 355
Cdd:cd05907 185 -WEkvYAAIKVK---AVPGLKrklfdlavGGRLRFAASGGAPLPAELLH-FFRAL---GI---PVYEGYGLTE------T 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 356 TPmdqaptVIHVDRDELNKqrfvevpadspkavpqvsAGTIGvdewAVIVDPETaselpdgQI---GEIWLHGNNLGTGY 432
Cdd:cd05907 248 SA------VVTLNPPGDNR------------------IGTVG----KPLPGVEV-------RIaddGEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 433 WGREQETndifrnilksrisqshAEGAPDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIID-GRNHYPQDLEysaqeaSK 510
Cdd:cd05907 293 YKNPEAT----------------AEALDADG-WLHTGDLGEIdEDGFLHITGRKKDLIITSgGKNISPEPIE------NA 349
|
490
....*....|....*...
gi 497642598 511 ALRTGYVAAFSVPANQLP 528
Cdd:cd05907 350 LKASPLISQAVVIGDGRP 367
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-615 |
4.58e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 127.61 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 20 NLVKHV-EKWARVRGDKLAYRFvdfsTERDGEYRDivwsdFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGA 97
Cdd:PRK06187 6 LTIGRIlRHGARKHPDKEAVYF----DGRRTTYAE-----LDERvNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 98 LYAGRIAVPL-FdpaepghvgRLHA-----VLDDCSPSTILTTTD----------AAEGVRKFIRA---RSAKERPRVIA 158
Cdd:PRK06187 77 PKIGAVLHPInI---------RLKPeeiayILNDAEDRVVLVDSEfvpllaailpQLPTVRTVIVEgdgPAAPLAPEVGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 159 VDAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITAL 238
Cdd:PRK06187 148 YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 239 LSpvlghnftFMTPAAFV--RR--PGRWIREMAR-KPedapdsEVFTVAPnfafehAAVRGVPKEGEP-PLDLSNVKAIL 312
Cdd:PRK06187 228 LA--------LMAGAKQVipRRfdPENLLDLIETeRV------TFFFAVP------TIWQMLLKAPRAyFVDFSSLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 313 NGSEPVSPASMRKFYEAFspyGLRETAIkpsYGLAEATLFVSTTPmdqaptvihvdrdeLNKQrfveVPADSPKAvpqVS 392
Cdd:PRK06187 288 YGGAALPPALLREFKEKF---GIDLVQG---YGMTETSPVVSVLP--------------PEDQ----LPGQWTKR---RS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 393 AGTI--GVDewAVIVDPETAsELP--DGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegapDDGmWVKT 468
Cdd:PRK06187 341 AGRPlpGVE--ARIVDDDGD-ELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETI-----------------DGG-WLHT 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 469 GDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLE--YSAQEAskalrtgyVAAFSVpanqlpkevfdnphTGLkydPDD 545
Cdd:PRK06187 400 GDVGYIDEdGYLYITDRIKDVIISGGENIYPRELEdaLYGHPA--------VAEVAV--------------IGV---PDE 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 546 SSEQ----LVIVAEraagshklDYQPIADDIRA---------AIAVRhgVTVRDlllvqsgTIPRTSSGKIGHRACRAAY 612
Cdd:PRK06187 455 KWGErpvaVVVLKP--------GATLDAKELRAflrgrlakfKLPKR--IAFVD-------ELPRTSVGKILKRVLREQY 517
|
...
gi 497642598 613 LDG 615
Cdd:PRK06187 518 AEG 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-607 |
5.32e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 127.84 E-value: 5.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 1 MAYHNPFIVNGKIKFP-----DNTNLVKHVEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQQV-T 74
Cdd:PRK06710 1 MKVEKPWLKSYPEEIPstisyDIQPLHKYVEQMASRYPEKKALHFLG---------KDITFSVFHDKVKRFANYLQKLgV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEpghvgrLHAVLDDCSPSTIL---------TTTDAAEGVR 142
Cdd:PRK06710 72 EKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTERE------LEYQLHDSGAKVILcldlvfprvTNVQSATKIE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 143 KFIRARSA----------------KERPRVIAV---------DAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQ 197
Cdd:PRK06710 146 HVIVTRIAdflpfpknllypfvqkKQSNLVVKVsesetihlwNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 198 ITHLNLPTNVLQ----VLNGLEGKEGDRGLswLPFFHDMGLiTALLspvlghNFTFMTPAAFVRRPgRWIREMARKPEDA 273
Cdd:PRK06710 226 LTHKNLVSNTLMgvqwLYNCKEGEEVVLGV--LPFFHVYGM-TAVM------NLSIMQGYKMVLIP-KFDMKMVFEAIKK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 274 PDSEVFTVAPNFafeHAAVRGVPKEGEppLDLSNVKAILNGSEPVsPASMRKFYEAFSPYGLREtaikpSYGLAEatlfv 353
Cdd:PRK06710 296 HKVTLFPGAPTI---YIALLNSPLLKE--YDISSIRACISGSAPL-PVEVQEKFETVTGGKLVE-----GYGLTE----- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 354 sTTPMDQAPTVIHvdrdelnkqrfvevpadspKAVPqvsaGTIGV---DEWAVIVDPETASELPDGQIGEIWLHGNNLGT 430
Cdd:PRK06710 360 -SSPVTHSNFLWE-------------------KRVP----GSIGVpwpDTEAMIMSLETGEALPPGEIGEIVVKGPQIMK 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 431 GYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEAS 509
Cdd:PRK06710 416 GYWNKPEETAAVLQ-----------------DG-WLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 510 KALRtgyVAAFSVPanqlpkevfdNPHTG--------LKYDPDDSSEQLVIVAERAAGSHKLdyqPIADDIRAaiavrhg 581
Cdd:PRK06710 478 KVQE---VVTIGVP----------DPYRGetvkafvvLKEGTECSEEELNQFARKYLAAYKV---PKVYEFRD------- 534
|
650 660
....*....|....*....|....*.
gi 497642598 582 vtvrdlllvqsgTIPRTSSGKIGHRA 607
Cdd:PRK06710 535 ------------ELPKTTVGKILRRV 548
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
16-502 |
7.68e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.44 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 16 PDNTNLVKHVEKWARVRGDKLAYRFVDfsterDGEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAF 94
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKE-----DGIWQSLTWAEFAERVRALAAGLLALgVKPGDRVAILSDNRPEWVIAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 95 FGALYAGRIAVPLFDPAEPGHVgrlHAVLDDCSPS-----------TILTTTDAAEGVRK--FIRARSAKERPRVIAVDA 161
Cdd:COG1022 83 LAILAAGAVTVPIYPTSSAEEV---AYILNDSGAKvlfvedqeqldKLLEVRDELPSLRHivVLDPRGLRDDPRLLSLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 162 V---------PNEVASTWEppEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFH-- 230
Cdd:COG1022 160 LlalgrevadPAELEARRA--AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHvf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 231 ---------DMGLITALLSPV--LGHNF-----TFMT--PA-----------------AFVRRPGRWIREMARKPEDAPD 275
Cdd:COG1022 238 ertvsyyalAAGATVAFAESPdtLAEDLrevkpTFMLavPRvwekvyagiqakaeeagGLKRKLFRWALAVGRRYARARL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 276 SEVfTVAPNFAFEHA--------AVR---GvpkegeppldlSNVKAILNGSEPVSPASMRkFYEAFspyGLRetaIKPSY 344
Cdd:COG1022 318 AGK-SPSLLLRLKHAladklvfsKLRealG-----------GRLRFAVSGGAALGPELAR-FFRAL---GIP---VLEGY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 345 GLAEatlfvsTTPmdqaptVIHVDRDELNKqrfvevpadspkavpqvsAGTIGVdewavivdPetaseLPDGQI-----G 419
Cdd:COG1022 379 GLTE------TSP------VITVNRPGDNR------------------IGTVGP--------P-----LPGVEVkiaedG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 420 EIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapDDGmWVKTGDYGTY-YKGHLYIAGRIKDLvII--DGRNH 496
Cdd:COG1022 416 EILVRGPNVMKGYYKNPEATAEAFD----------------ADG-WLHTGDIGELdEDGFLRITGRKKDL-IVtsGGKNV 477
|
....*.
gi 497642598 497 YPQDLE 502
Cdd:COG1022 478 APQPIE 483
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
25-523 |
1.04e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.05 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 25 VEKWARVRGDKLAYrfvdFSTERDGEYRDIvwSDFSAR-NRAVGARLQqvTQPGDRIAVLCPQNLDYLIAFFGALYAGRI 103
Cdd:PRK06839 8 IEKRAYLHPDRIAI----ITEEEEMTYKQL--HEYVSKvAAYLIYELN--VKKGERIAILSQNSLEYIVLLFAIAKVECI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 104 AVPL---FDPAEpghvgrLHAVLDDcSPSTILTTTDAAEGVRKFIRARSAKERP-RVIAVDAVPNEVASTWEPPEADENT 179
Cdd:PRK06839 80 AVPLnirLTENE------LIFQLKD-SGTTVLFVEKTFQNMALSMQKVSYVQRViSITSLKEIEDRKIDNFVEKNESASF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 180 IayLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHdMGLITALLSPVLGHNFTFMTPAAFvrRP 259
Cdd:PRK06839 153 I--ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH-IGGIGLFAFPTLFAGGVIIVPRKF--EP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 260 GRWIREMarkpedapDSEVFTVAPNFAFEHAAVRGVPKEGEPplDLSNVKAILNGSEPVSPASMRKFYEAFSPYGlreta 339
Cdd:PRK06839 228 TKALSMI--------EKHKVTVVMGVPTIHQALINCSKFETT--NLQSVRWFYNGGAPCPEELMREFIDRGFLFG----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 ikPSYGLAEAtlfvsttpmdqAPTVIHVDRDELNKQrfvevpadspkavpqvsAGTIG----VDEWAVIvDPETaSELPD 415
Cdd:PRK06839 293 --QGFGMTET-----------SPTVFMLSEEDARRK-----------------VGSIGkpvlFCDYELI-DENK-NKVEV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 416 GQIGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqshaegapddgMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGR 494
Cdd:PRK06839 341 GEVGELLIRGPNVMKEYWNRPDATEETIQD------------------GWLCTGDLARVdEDGFVYIVGRKKEMIISGGE 402
|
490 500
....*....|....*....|....*....
gi 497642598 495 NHYPQDLEYSAQEASKALRtgyVAAFSVP 523
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYE---VAVVGRQ 428
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
19-486 |
3.01e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 122.38 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 19 TNLVKHVEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQQVT--QPGDRIAVL---CPQnldYLIA 93
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIVFYG---------RAISYRELLEEAERLAGYLQQECgvRKGDRVLLYmqnSPQ---FVIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 94 FFGALYAGRIAVP---LFDPAEPGHVgrlhavLDDCSPSTILTTTDAAEGVRKFIRA----------------------- 147
Cdd:PRK08314 78 YYAILRANAVVVPvnpMNREEELAHY------VTDSGARVAIVGSELAPKVAPAVGNlrlrhvivaqysdylpaepeiav 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 148 ----RSAKERPRVIAVDAVPNE--VASTWEPP--EADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEG 219
Cdd:PRK08314 152 pawlRAEPPLQALAPGGVVAWKeaLAAGLAPPphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 220 DRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPaafvrrpgRWIREMARK-------------PEDAPDsevFTVAPNFA 286
Cdd:PRK08314 232 SVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP--------RWDREAAARlieryrvthwtniPTMVVD---FLASPGLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 287 fehaavrgvpkegepPLDLSNVKAILNGSEPVSPASMRKFYEAF-----SPYGLRETAikpsyglaeatlfvsttpmdqA 361
Cdd:PRK08314 301 ---------------ERDLSSLRYIGGGGAAMPEAVAERLKELTgldyvEGYGLTETM---------------------A 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 362 PTviHVDrdelnkqrfvevPADSPK----AVPqvsagTIGVDewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQ 437
Cdd:PRK08314 345 QT--HSN------------PPDRPKlqclGIP-----TFGVD--ARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPE 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497642598 438 ETNDIFRNIlksrisqshaegapdDGM-WVKTGDYGTY-YKGHLYIAGRIK 486
Cdd:PRK08314 404 ATAEAFIEI---------------DGKrFFRTGDLGRMdEEGYFFITDRLK 439
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
77-502 |
2.46e-27 |
|
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: 115.27 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 77 GDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGR-LHAVLDDcSPSTILTTTdaaegvrkfirarsakerpr 155
Cdd:cd05935 26 GDRVGICLQNSPQYVIAYFAIWRANAVVVPI----NPMLKEReLEYILND-SGAKVAVVG-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 viavdavpnevastweppeADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLI 235
Cdd:cd05935 81 -------------------SELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 236 TALLSPVLGHNFTFMTpaafvrrpGRWIREMARKPEDAPDSEVFTVAPNFAFEHAAVRGVPKEgepplDLSNVKAILNGS 315
Cdd:cd05935 142 GSLNTAVYVGGTYVLM--------ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTR-----DLSSLKVLTGGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 316 EPVSPASMRKFYEAFspyGLRETAIkpsYGLAEATLFVSTTPMdQAPtvihvdrdelnKQRFVEVPAdspkavpqvsagt 395
Cdd:cd05935 209 APMPPAVAEKLLKLT---GLRFVEG---YGLTETMSQTHTNPP-LRP-----------KLQCLGIP*------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 396 IGVDewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILKSRisqshaegapddgmWVKTGDYGtyY 475
Cdd:cd05935 258 FGVD--ARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRR--------------FFRTGDLG--Y 319
|
410 420 430
....*....|....*....|....*....|
gi 497642598 476 ---KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05935 320 mdeEGYFFFVDRVKRMINVSGFKVWPAEVE 349
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
75-502 |
5.90e-27 |
|
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: 114.46 E-value: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEpgHVGRLHAVLDDCSPSTILTTtdaaegvrkfirarsakerp 154
Cdd:cd05914 30 GTGDRVALMGENRPEWGIAFFAIWTYGAIAVPI-LAEF--TADEVHHILNHSEAKAIFVS-------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 155 rviavdavpnevastweppeaDENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGL 234
Cdd:cd05914 87 ---------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 235 ITALLSPVL-GHNFTFM----------------TPAAFVRRPgrWIREMARKPEDAPDSEV----FTVAP---NFAFEHA 290
Cdd:cd05914 146 TFTLLLPLLnGAHVVFLdkipsakiialafaqvTPTLGVPVP--LVIEKIFKMDIIPKLTLkkfkFKLAKkinNRKIRKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 291 AVRGVPKE-GeppldlSNVKAILNGSEPVSPASMRKFYEAFSPYGLretaikpSYGLAEATLFVSTTPMdqaptvihvdr 369
Cdd:cd05914 224 AFKKVHEAfG------GNIKEFVIGGAKINPDVEEFLRTIGFPYTI-------GYGMTETAPIISYSPP----------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 370 delNKQRFvevpADSPKAVPqvsagtigvdewavIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilks 449
Cdd:cd05914 280 ---NRIRL----GSAGKVID--------------GVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAF------ 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 450 risqshaegapDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVII-DGRNHYPQDLE 502
Cdd:cd05914 333 -----------DKDGWFHTGDLGKIdAEGYLYIRGRKKEMIVLsSGKNIYPEEIE 376
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
62-523 |
1.42e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 114.38 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 62 RNRAVGARLQQ--VTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVgrlhavLDDCSPSTILTTTD 136
Cdd:PRK08974 57 RSRAFAAYLQNglGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYTPRELEHQ------LNDSGAKAIVIVSN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 137 AAEGVRKFIRARSAKE-----------RPRVIAVDAV-------------PNEVA----------STWEPPEADENTIAY 182
Cdd:PRK08974 131 FAHTLEKVVFKTPVKHviltrmgdqlsTAKGTLVNFVvkyikrlvpkyhlPDAISfrsalhkgrrMQYVKPELVPEDLAF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 183 LQYTSGSTRTPTGVQITHLNLPTNVLQ-------VLNglEGKEgdRGLSWLPFFHDMGL-ITALLSPVLGHNFTFMTPAA 254
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRNMLANLEQakaaygpLLH--PGKE--LVVTALPLYHIFALtVNCLLFIELGGQNLLITNPR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 255 FVrrPGrWIREMARKPedapdsevFTvapnfafehaAVRGV--------PKEGEPPLDLSNVKAILNGSEPVSPASMRKF 326
Cdd:PRK08974 287 DI--PG-FVKELKKYP--------FT----------AITGVntlfnallNNEEFQELDFSSLKLSVGGGMAVQQAVAERW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 327 YEafspygLRETAIKPSYGLAEATLFVSTTPmdqaptvihVDRDELNKQRFVEVPADSPKavpqvsagtigvdewavIVD 406
Cdd:PRK08974 346 VK------LTGQYLLEGYGLTECSPLVSVNP---------YDLDYYSGSIGLPVPSTEIK-----------------LVD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 407 PEtASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRI 485
Cdd:PRK08974 394 DD-GNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIK-----------------DG-WLATGDIAVMdEEGFLRIVDRK 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 497642598 486 KDLVIIDGRNHYPQDLEYSAQEASKALRtgyVAAFSVP 523
Cdd:PRK08974 455 KDMILVSGFNVYPNEIEDVVMLHPKVLE---VAAVGVP 489
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
52-502 |
3.95e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 112.93 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQVT--QPGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGH----------- 115
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHTdlKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYTAREMEHqfndsgakalv 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 116 ---------------VGRLHAVL----DDCSPSTILTTTDAAEGVRKFIRARSAkerPRVIAV-DAVPNEVASTWEPPEA 175
Cdd:PRK05677 128 clanmahlaekvlpkTGVKHVIVtevaDMLPPLKRLLINAVVKHVKKMVPAYHL---PQAVKFnDALAKGAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 176 DENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQV--LNGLEGKEGDRGL-SWLPFFHDMGLITALLSPVL--GHNFTFM 250
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCraLMGSNLNEGCEILiAPLPLYHIYAFTFHCMAMMLigNHNILIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 251 TP---AAFVRRPGRWiremarkpedapdseVFT--VAPNFAFehaaVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRK 325
Cdd:PRK05677 285 NPrdlPAMVKELGKW---------------KFSgfVGLNTLF----VALCNNEAFRKLDFSALKLTLSGGMALQLATAER 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 326 FYEafspygLRETAIKPSYGLAEATLFVSTTPMDQaptvihvdrdelnkqrfvevpadspkavpqVSAGTIGV---DEWA 402
Cdd:PRK05677 346 WKE------VTGCAICEGYGMTETSPVVSVNPSQA------------------------------IQVGTIGIpvpSTLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 403 VIVDPEtASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegapDDGMWVKTGDYGTYYK-GHLYI 481
Cdd:PRK05677 390 KVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL-----------------DSDGWLKTGDIALIQEdGYMRI 451
|
490 500
....*....|....*....|.
gi 497642598 482 AGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK05677 452 VDRKKDMILVSGFNVYPNELE 472
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
16-629 |
1.87e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 110.97 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 16 PDNTNLVKH-VEKWARVRGDKLAYRFVDfsteRDGEYRDIVWSDFSARNRAVGARLQQ--VtQPGDRIAVLCPQNLDYLI 92
Cdd:COG0365 5 GGRLNIAYNcLDRHAEGRGDKVALIWEG----EDGEERTLTYAELRREVNRFANALRAlgV-KKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 93 AFFGALYAGRIAVP---LFDPAEpghvgrLHAVLDDCSPSTILTTTDAAEGVRKF--------IRARSAKERpRVIAVDA 161
Cdd:COG0365 80 AMLACARIGAVHSPvfpGFGAEA------LADRIEDAEAKVLITADGGLRGGKVIdlkekvdeALEELPSLE-HVIVVGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 162 VPNEV---------------ASTWEPPEADENTIAYLQYTSGSTRTPTGVQITH----LNLPTNVLQVLNgleGKEGDRg 222
Cdd:COG0365 153 TGADVpmegdldwdellaaaSAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHggylVHAATTAKYVLD---LKPGDV- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 223 lswlpFFH--DMGLITALLSPVLG-HNF---TFMTPAAFVRR-PGRWIREMAR-KPedapdsEVFTVAPnfafehAAVRG 294
Cdd:COG0365 229 -----FWCtaDIGWATGHSYIVYGpLLNgatVVLYEGRPDFPdPGRLWELIEKyGV------TVFFTAP------TAIRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 VPKEGEPPL---DLSNVKAILNGSEPVSPASMRKFYEAFspyG--LRETaikpsYGLAEAT-LFVSTTPMDqaptvihvd 368
Cdd:COG0365 292 LMKAGDEPLkkyDLSSLRLLGSAGEPLNPEVWEWWYEAV---GvpIVDG-----WGQTETGgIFISNLPGL--------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 369 rdelnkqrfvEVPADSP-KAVPqvsagtiGVDewAVIVDpETASELPDGQIGEIWLHGNNLG--TGYWGREQETNDIFRN 445
Cdd:COG0365 355 ----------PVKPGSMgKPVP-------GYD--VAVVD-EDGNPVPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 446 ilksrisqshaegaPDDGMWVkTGDYgtYYK---GHLYIAGRIKDLVIIDGRNHYPQDLEySA-------QEA-----SK 510
Cdd:COG0365 415 --------------RFPGWYR-TGDG--ARRdedGYFWILGRSDDVINVSGHRIGTAEIE-SAlvshpavAEAavvgvPD 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 511 ALRTGYVAAFSVPANQlpkevfdnphtglkYDPDDSseqlvIVAEraagshkldyqpIADDIRAAIAVRHgvTVRDLLLV 590
Cdd:COG0365 477 EIRGQVVKAFVVLKPG--------------VEPSDE-----LAKE------------LQAHVREELGPYA--YPREIEFV 523
|
650 660 670
....*....|....*....|....*....|....*....
gi 497642598 591 QSgtIPRTSSGKIGHRACRAAYLDGSLrsgvGSPTAFAN 629
Cdd:COG0365 524 DE--LPKTRSGKIMRRLLRKIAEGRPL----GDTSTLED 556
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-502 |
2.47e-25 |
|
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: 107.75 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 183 LQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSpVLGHNFTFMTPaafvrrpgrw 262
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLA-CLTHGATMVFP---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 263 iremarkpedapdSEVFTVAPNFAFEH----AAVRGVP----KEGEPPL----DLSNVK-AILNGSePVSPASMRKFYEA 329
Cdd:cd05917 76 -------------SPSFDPLAVLEAIEkekcTALHGVPtmfiAELEHPDfdkfDLSSLRtGIMAGA-PCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 330 FspyGLRETAIkpSYGLAEAT-LFVSTTPMDQAPTVIhvdrdelnkqrfvevpadspkavpqVSAGTIGVDEWAVIVDPE 408
Cdd:cd05917 142 M---NMKDVTI--AYGMTETSpVSTQTRTDDSIEKRV-------------------------NTVGRIMPHTEAKIVDPE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 409 TASELPDGQIGEIWLHGNNLGTGYWGREQETNDifrnilksrisqshaegAPDDGMWVKTGDYGTYYK-GHLYIAGRIKD 487
Cdd:cd05917 192 GGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE-----------------AIDGDGWLHTGDLAVMDEdGYCRIVGRIKD 254
|
330
....*....|....*
gi 497642598 488 LVIIDGRNHYPQDLE 502
Cdd:cd05917 255 MIIRGGENIYPREIE 269
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
65-523 |
5.22e-25 |
|
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: 108.96 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 65 AVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHvgrLHAVLDDCSPSTILTTtdaaegvRKF 144
Cdd:cd05909 19 ALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRE---LRACIKLAGIKTVLTS-------KQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 145 IR------ARSAKERPRVIAVDAVPNEVaSTWE----------PPE----------ADENTIAYLQYTSGSTRTPTGVQI 198
Cdd:cd05909 89 IEklklhhLFDVEYDARIVYLEDLRAKI-SKADkckaflagkfPPKwllrifgvapVQPDDPAVILFTSGSEGLPKGVVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 199 THLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAFvrrPGRWIREMARKPEdapdSEV 278
Cdd:cd05909 168 SHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPL---DYKKIPELIYDKK----ATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 279 FTVAPNFafehaaVRGVPKEGEPPlDLSNVKAILNGSEPVSPASMRKFYEAFspyGLRetaIKPSYGLAEATLFVS-TTP 357
Cdd:cd05909 241 LLGTPTF------LRGYARAAHPE-DFSSLRLVVAGAEKLKDTLRQEFQEKF---GIR---ILEGYGTTECSPVISvNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 358 mdQAPtvihvdrdelNKQRFVEVPadspkaVPqvsagtiGVDewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQ 437
Cdd:cd05909 308 --QSP----------NKEGTVGRP------LP-------GME--VKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 438 ETNDIFRnilksrisqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNhypQDLEYSAQEASKALRT-G 515
Cdd:cd05909 361 LTSFAFG-----------------DG-WYDTGDIGKIdGEGFLTITGRLSRFAKIAGEM---VSLEAIEDILSEILPEdN 419
|
....*...
gi 497642598 516 YVAAFSVP 523
Cdd:cd05909 420 EVAVVSVP 427
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
78-609 |
6.63e-25 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 109.15 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 78 DRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVgrLHAvLDDCSPSTILTTTDAAEGVRKFirARSAKERPRVI 157
Cdd:cd17642 70 DRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNEREL--DHS-LNISKPTIVFCSKKGLQKVLNV--QKKLKIIKTII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 158 AVDAV------------------PNEVASTWEPPEAD-ENTIAYLQYTSGSTRTPTGVQITHLNL---------PTNVLQ 209
Cdd:cd17642 145 ILDSKedykgyqclytfitqnlpPGFNEYDFKPPSFDrDEQVALIMNSSGSTGLPKGVQLTHKNIvarfshardPIFGNQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 210 VLnglegkEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTpaafvrrpgRWIREM-ARKPEDAPDSEVFTVAPNFAF- 287
Cdd:cd17642 225 II------PDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY---------KFEEELfLRSLQDYKVQSALLVPTLFAFf 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 288 -EHAAVRgvpkegepPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLREtaikpSYGLAEATLFVSTTPmdqaptvih 366
Cdd:cd17642 290 aKSTLVD--------KYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ-----GYGLTETTSAILITP--------- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 367 vdrDELNKqrfvevPADSPKAVPQVSAGtigvdewavIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIfrnI 446
Cdd:cd17642 348 ---EGDDK------PGAVGKVVPFFYAK---------VVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKAL---I 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 447 LKsrisqshaegapdDGmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLEysaqeaSKALrtgyvaafsvpan 525
Cdd:cd17642 407 DK-------------DG-WLHSGDIAYYDEdGHFFIVDRLKSLIKYKGYQVPPAELE------SILL------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 526 QLPKeVFDNPHTGLkydPDDSSEQL----VIVAERAAGSHKLDYQPIADDIRAAIAVRHGVTVRDlllvqsgTIPRTSSG 601
Cdd:cd17642 454 QHPK-IFDAGVAGI---PDEDAGELpaavVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVD-------EVPKGLTG 522
|
....*...
gi 497642598 602 KIGHRACR 609
Cdd:cd17642 523 KIDRRKIR 530
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
29-493 |
7.65e-25 |
|
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: 107.72 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL 107
Cdd:cd05945 1 AAANPDRPAVVEGG---------RTLTYRELKERADALAAALAsLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 108 fDPAEPghVGRLHAVLDDCSPSTILtttdaaegvrkfirarsakerprviavdavpnevastweppeADENTIAYLQYTS 187
Cdd:cd05945 72 -DASSP--AERIREILDAAKPALLI------------------------------------------ADGDDNAYIIFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 188 GSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHD---MGLITALLSP----VLGHNFTfmtpaAFVRRPG 260
Cdd:cd05945 107 GSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDlsvMDLYPALASGatlvPVPRDAT-----ADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 261 RWIREMarkpedapDSEVFTVAPNFAfeHAAVRgvpkegEPPLD---LSNVKAILNGSEPVSPASMRKFYEAFsPyglrE 337
Cdd:cd05945 182 RFLAEH--------GITVWVSTPSFA--AMCLL------SPTFTpesLPSLRHFLFCGEVLPHKTARALQQRF-P----D 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 338 TAIKPSYGLAEATLFVsttpmdqapTVIHVDRDelnkqrfvevPADSPKAVPqvsagtIGV---DEWAVIVDpETASELP 414
Cdd:cd05945 241 ARIYNTYGPTEATVAV---------TYIEVTPE----------VLDGYDRLP------IGYakpGAKLVILD-EDGRPVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 415 DGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegaPDDGMWV-KTGDYGTYY-KGHLYIAGRIKDLVIID 492
Cdd:cd05945 295 PGEKGELVISGPSVSKGYLNNPEKTAAAFF---------------PDEGQRAyRTGDLVRLEaDGLLFYRGRLDFQVKLN 359
|
.
gi 497642598 493 G 493
Cdd:cd05945 360 G 360
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
51-493 |
2.14e-24 |
|
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: 106.61 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 51 YRDIVWSDFSARNRAVGARlqqVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPST 130
Cdd:cd05941 14 YADLVARAARLANRLLALG---KDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPL-NPSYPLA--ELEYVITDSEPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 131 ILtttdaaegvrkfirarsakeRPRVIAvdavpnevastweppeadentiaylqYTSGSTRTPTGVQITHLNLPTNVLQV 210
Cdd:cd05941 88 VL--------------------DPALIL--------------------------YTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 211 LNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAFVRRPGRWIREmarkpedaPDSEVFTVAPNF----- 285
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLM--------PSITVFMGVPTIytrll 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 286 -AFEHAAVRGVPKEGEPPldlSNVKAILNGSEPVSPASMRKFYEAFspyGLRetaIKPSYGLAEaTLFVSTTPmdqaptv 364
Cdd:cd05941 194 qYYEAHFTDPQFARAAAA---ERLRLMVSGSAALPVPTLEEWEAIT---GHT---LLERYGMTE-IGMALSNP------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 365 IHVDRdelnkqrfveVPADSPKAVPQVSAgtigvdewaVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFR 444
Cdd:cd05941 257 LDGER----------RPGTVGMPLPGVQA---------RIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFT 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 497642598 445 nilksrisqshaegapDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDG 493
Cdd:cd05941 318 ----------------DDG-WFKTGDLGVVdEDGYYWILGRSSVDIIKSG 350
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
15-443 |
2.46e-24 |
|
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: 108.79 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 15 FPDNTNLVKHVEKWARVRGDKLAYRFvdfsteRDGE--YRDivwsdFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYL 91
Cdd:COG1020 472 YPADATLHELFEAQAARTPDAVAVVF------GDQSltYAE-----LNARANRLAHHLRALgVGPGDLVGVCLERSLEMV 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 92 IAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAEGVrkfirarsAKERPRVIAVDAVPNEVASTWE 171
Cdd:COG1020 541 VALLAVLKAGAAYVPL-DPAYP--AERLAYMLEDAGARLVLTQSALAARL--------PELGVPVLALDALALAAEPATN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 172 PP-EADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMG---LITALLSpvlGHnf 247
Cdd:COG1020 610 PPvPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASvweIFGALLS---GA-- 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 248 T-FMTPAAFVRRPGRWIREMARKPEDapdseVFTVAPnfafehAAVRGVPKEGepPLDLSNVKAILNGSEPVSPASMRKF 326
Cdd:COG1020 685 TlVLAPPEARRDPAALAELLARHRVT-----VLNLTP------SLLRALLDAA--PEALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 327 YEAFSPYGLRETaikpsYGLAEATLFVSTTPMDQAPtvihvdrdelnkqrfvevpaDSPKAVPqvsagtIG--------- 397
Cdd:COG1020 752 RARLPGARLVNL-----YGPTETTVDSTYYEVTPPD--------------------ADGGSVP------IGrpiantrvy 800
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 497642598 398 -VDEWAVIVdpetaselPDGQIGEIWLHGNNLGTGYWGREQETNDIF 443
Cdd:COG1020 801 vLDAHLQPV--------PVGVPGELYIGGAGLARGYLNRPELTAERF 839
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
76-493 |
3.29e-23 |
|
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: 102.99 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTttdaaegvrkfirarsakerpr 155
Cdd:cd05930 36 PGDLVAVLLERSLEMVVAILAVLKAGAAYVPL-DPSYP--AERLAYILEDSGAKLVLT---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 viavdavpnevastweppeaDENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGlI 235
Cdd:cd05930 91 --------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 236 TALLSPVL-GHnfT-FMTPAAFVRRPGRWIREMARKpedapDSEVFTVAPnfafehAAVRGVPKEGEPPlDLSNVKAILN 313
Cdd:cd05930 150 WEIFGALLaGA--TlVVLPEEVRKDPEALADLLAEE-----GITVLHLTP------SLLRLLLQELELA-ALPSLRLVLV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 314 GSEPVSPASMRKFYEAFSPYGLRETaikpsYGLAEATLFVSTTpmdqaptviHVDRDELNKQRfveVPADSPkaVPQVSa 393
Cdd:cd05930 216 GGEALPPDLVRRWRELLPGARLVNL-----YGPTEATVDATYY---------RVPPDDEEDGR---VPIGRP--IPNTR- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 394 gtigvdewAVIVDPETAsELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNIlksrisqshaegAPDDGMWV-KTGDYG 472
Cdd:cd05930 276 --------VYVLDENLR-PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN------------PFGPGERMyRTGDLV 334
|
410 420
....*....|....*....|..
gi 497642598 473 TY-YKGHLYIAGRIKDLVIIDG 493
Cdd:cd05930 335 RWlPDGNLEFLGRIDDQVKIRG 356
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-609 |
1.73e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 100.98 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 63 NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGR-LHAVLDDCSPSTILTTTDAAEGV 141
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESvLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 142 RK-FIRARSAKErprVIAVDAVPNEVASTWEPPEADENTiAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGD 220
Cdd:cd05922 84 RDaLPASPDPGT---VLDADGIRAARASAPAHEVSHEDL-ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 221 RGLSWLPFFHDMG---LITALL---SPVLghNFTFMTPAAFVrrpgrwiremarkpEDAPDSEVFTVApnfafehaavrG 294
Cdd:cd05922 160 RALTVLPLSYDYGlsvLNTHLLrgaTLVL--TNDGVLDDAFW--------------EDLREHGATGLA-----------G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 VP-------KEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFspyglRETAIKPSYGLAEATLFVSTTPMDQAptvihv 367
Cdd:cd05922 213 VPstyamltRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELL-----PGAQVYVMYGQTEATRRMTYLPPERI------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 368 drdelnkqrfvevpADSPKAVPQVSAGTigvdewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDifrnil 447
Cdd:cd05922 282 --------------LEKPGSIGLAIPGG------EFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK------ 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 448 ksrisqshaEGAPDDGMWvkTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKalrTGYVAAFSvpanq 526
Cdd:cd05922 336 ---------EGRGGGVLH--TGDLARRdEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL---IIEAAAVG----- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 527 lpkevfdnphtglkyDPDDSSEQLVIVAERAAGShkldyqpIADDIRAAIAVRHGVTVRDLLLVQSGTIPRTSSGKIGHR 606
Cdd:cd05922 397 ---------------LPDPLGEKLALFVTAPDKI-------DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
...
gi 497642598 607 ACR 609
Cdd:cd05922 455 ALR 457
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
25-493 |
8.66e-22 |
|
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: 98.81 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 25 VEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRI 103
Cdd:cd12117 3 FEEQAARTPDAVAVVYGD---------RSLTYAELNERANRLARRLRAAgVGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 104 AVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAegvrkfirARSAKERPRVIAVDAVPNEVASTWEPPeADENTIAYL 183
Cdd:cd12117 74 YVPL-DPELP--AERLAFMLADAGAKVLLTDRSLA--------GRAGGLEVAVVIDEALDAGPAGNPAVP-VSPDDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 184 QYTSGSTRTPTGVQITHLNLPTNVLQVlNGLEGKEGDRGLSWLPFFHDMGLI---TALLSP---VLGHNFTFMTPAAFvr 257
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVKNT-NYVTLGPDDRVLQTSPLAFDASTFeiwGALLNGarlVLAPKGTLLDPDAL-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 258 rpGRWIREmarkpEDApdSEVFTVAPNFafeHAAVRGVPKEgeppldLSNVKAILNGSEPVSPASMRKFYEAFSPyglre 337
Cdd:cd12117 219 --GALIAE-----EGV--TVLWLTAALF---NQLADEDPEC------FAGLRELLTGGEVVSPPHVRRVLAACPG----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 338 TAIKPSYGLAEATLFVSTTPMDQAPTVIHvdrdelnkqrfvEVPADSPkavpqvSAGTIgvdewAVIVDpETASELPDGQ 417
Cdd:cd12117 276 LRLVNGYGPTENTTFTTSHVVTELDEVAG------------SIPIGRP------IANTR-----VYVLD-EDGRPVPPGV 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 418 IGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshAEGAPDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:cd12117 332 PGELYVGGDGLALGYLNRPALTAERFV-----------ADPFGPGERLYRTGDLARWLPdGRLEFLGRIDDQVKIRG 397
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
51-502 |
1.45e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.81 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 51 YRDIVW--SDFSARNRAVGARlqqvtqPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEP--------GHVGRLH 120
Cdd:PRK05852 46 YRDLARlvDDLAGQLTRSGLL------PGDRVALRMGSNAEFVVALLAASRADLVVVPL-DPALPiaeqrvrsQAAGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 121 AVLDDCSPS-TILTTTDAAEGVRKFIRARSAKERPRVIAVDAV--PNEVASTWEPPEADEntiAYLQYTSGSTRTPTGVQ 197
Cdd:PRK05852 119 VLIDADGPHdRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAAtePTPATSTPEGLRPDD---AMIMFTGGTTGLPKMVP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 198 ITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSpVLGHNFTFMTPAAfvrrpGRWIREMARKPEDAPDSE 277
Cdd:PRK05852 196 WTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLA-TLASGGAVLLPAR-----GRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 278 VFTVAPNFafeHAAVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSpyglreTAIKPSYGLAEATLFVSTTP 357
Cdd:PRK05852 270 WYTAVPTI---HQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA------APVVCAFGMTEATHQVTTTQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 358 MDQAptvihvDRDelnkqrfvEVPADSPKAVPQVSAGTIGvdewavIVDPEtASELPDGQIGEIWLHGNNLGTGYWGREQ 437
Cdd:PRK05852 341 IEGI------GQT--------ENPVVSTGLVGRSTGAQIR------IVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642598 438 ETNDIFrnilksrisqshaegapDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK05852 400 ITAANF-----------------TDG-WLRTGDLGSLsAAGDLSIRGRIKELINRGGEKISPERVE 447
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
65-502 |
1.47e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 98.74 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 65 AVGARLQQVTQ--PGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHV----------------GRLHAVL 123
Cdd:PRK12492 61 AFAAYLQQHTDlvPGDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLYTAREMRHQfkdsgaralvylnmfgKLVQEVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 124 DDCSPSTILTTT-----DAAEG------VRKFIRARSAKERPRVIAVDAVPNEVA-STWEPPEADENTIAYLQYTSGSTR 191
Cdd:PRK12492 141 PDTGIEYLIEAKmgdllPAAKGwlvntvVDKVKKMVPAYHLPQAVPFKQALRQGRgLSLKPVPVGLDDIAVLQYTGGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 192 TPTGVQITHLNLPTNVLQVLNGLeGKEGDRGLSW-----------LPFFHdmglITALLSPVL------GHNFTFMTP-- 252
Cdd:PRK12492 221 LAKGAMLTHGNLVANMLQVRACL-SQLGPDGQPLmkegqevmiapLPLYH----IYAFTANCMcmmvsgNHNVLITNPrd 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 253 -AAFVRRPGRWiremarkpedapdseVFTVAPNFAFEHAAVRGVPkeGEPPLDLSNVKAILNGSEPVSPASMRKFyeafs 331
Cdd:PRK12492 296 iPGFIKELGKW---------------RFSALLGLNTLFVALMDHP--GFKDLDFSALKLTNSGGTALVKATAERW----- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 332 pYGLRETAIKPSYGLAEATLFVSTTPMDQaptvihvdrdelnkqrfvevpadspkavpQVSAGTIG--VDEWAVIVDPET 409
Cdd:PRK12492 354 -EQLTGCTIVEGYGLTETSPVASTNPYGE-----------------------------LARLGTVGipVPGTALKVIDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 410 ASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqsHAEGapddgmWVKTGDYGTY-YKGHLYIAGRIKDL 488
Cdd:PRK12492 404 GNELPLGERGELCIKGPQVMKGYWQQPEATAEAL-----------DAEG------WFKTGDIAVIdPDGFVRIVDRKKDL 466
|
490
....*....|....
gi 497642598 489 VIIDGRNHYPQDLE 502
Cdd:PRK12492 467 IIVSGFNVYPNEIE 480
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
76-493 |
5.38e-21 |
|
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: 96.22 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAegvrkfirarsakerpr 155
Cdd:cd17643 36 PGDRVALALPRSAELIVALLAILKAGGAYVPI-DPAYP--VERIAFILADSGPSLLLTDPDDL----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 viavdavpnevastweppeadentiAYLQYTSGSTRTPTGVQITHlnlpTNVLQVLNGLEgkegdrglSWLPFFHDMgli 235
Cdd:cd17643 96 -------------------------AYVIYTSGSTGRPKGVVVSH----ANVLALFAATQ--------RWFGFNEDD--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 236 tallSPVLGHNFTF-----------MTPAAFVRRPgrwiREMARKPEDAPD---SEVFTV---APNfAFEH--AAVRGvp 296
Cdd:cd17643 136 ----VWTLFHSYAFdfsvweiwgalLHGGRLVVVP----YEVARSPEDFARllrDEGVTVlnqTPS-AFYQlvEAADR-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 297 kEGEPPLDLSNVkaILnGSEPVSPASMRKFYEAFspyGLRETAIKPSYGLAEATLFVSTTPMDqaptvihvdrdelnkqr 376
Cdd:cd17643 205 -DGRDPLALRYV--IF-GGEALEAAMLRPWAGRF---GLDRPQLVNMYGITETTVHVTFRPLD----------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 377 fvevPADspkaVPQVSAGTIG--VDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqS 454
Cdd:cd17643 261 ----AAD----LPAAAASPIGrpLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFV---------A 323
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497642598 455 HAEGAPDDGMWvKTGDYGTYY-KGHLYIAGRIKDLVIIDG 493
Cdd:cd17643 324 NPFGGPGSRMY-RTGDLARRLpDGELEYLGRADEQVKIRG 362
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
50-493 |
9.28e-21 |
|
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: 95.82 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 50 EYRDIVWS--DFSARNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDC 126
Cdd:cd12116 7 RDDDRSLSyaELDERANRLAARLRaRGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYP--ADRLRYILEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 127 SPSTILTTTDAAEGVRKFIRARsakerPRVIAVDAVPNEVAstwePPEADENTIAYLQYTSGSTRTPTGVQITHLNLpTN 206
Cdd:cd12116 84 EPALVLTDDALPDRLPAGLPVL-----LLALAAAAAAPAAP----RTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNL-VN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 207 VLQVLNGLEG-KEGDRGLSWLPFFHDMGLItALLSPVlghnftfMTPAAFVRRPgrwiREMARKPE------DAPDSEVF 279
Cdd:cd12116 154 FLHSMRERLGlGPGDRLLAVTTYAFDISLL-ELLLPL-------LAGARVVIAP----RETQRDPEalarliEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 280 TVAPnfafehAAVRGVPKEGEPPLDlsNVKAiLNGSEPVSPASMRKFYEafspyglRETAIKPSYGLAEATLFVSTTPMD 359
Cdd:cd12116 222 QATP------ATWRMLLDAGWQGRA--GLTA-LCGGEALPPDLAARLLS-------RVGSLWNLYGPTETTIWSTAARVT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 360 QAPTVIHVDRDELNKQrfvevpadspkavpqvsagtigvdewAVIVDPETASeLPDGQIGEIWLHGNNLGTGYWGREQET 439
Cdd:cd12116 286 AAAGPIPIGRPLANTQ--------------------------VYVLDAALRP-VPPGVPGELYIGGDGVAQGYLGRPALT 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 440 NDIFRnilksrisqsHAEGAPDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:cd12116 339 AERFV----------PDPFAGPGSRLYRTGDLVRRRAdGRLEYLGRADGQVKIRG 383
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
29-502 |
1.83e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 94.87 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYrfVDFSTERDgeyrdivWSdFSARNRAVGaRLQQVTQ-----PGDRIAVLCPQNLDYLIAFFGALYAGRI 103
Cdd:PRK09088 5 ARLQPQRLAA--VDLALGRR-------WT-YAELDALVG-RLAAVLRrrgcvDGERLAVLARNSVWLVALHFACARVGAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 104 AVPL---FDPAEpghvgrLHAVLDDCSPSTILTTTDAAEGvrkfirarsakeRPRVIAVDAVPNEV--ASTWEPPEADEN 178
Cdd:PRK09088 74 YVPLnwrLSASE------LDALLQDAEPRLLLGDDAVAAG------------RTDVEDLAAFIASAdaLEPADTPSIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 179 TIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVlnGLEGKEGDRG--LSWLPFFHDMGLITAlLSPVLGHNFTFMTPAAFv 256
Cdd:PRK09088 136 RVSLILFTSGTSGQPKGVMLSERNLQQTAHNF--GVLGRVDAHSsfLCDAPMFHIIGLITS-VRPVLAVGGSILVSNGF- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 257 rRPGRWIREMARkpedaPDSEV--FTVAPNFAfehAAVRGVPkeGEPPLDLSNVKAILNGSEPVSPASMRKFyeafspyg 334
Cdd:PRK09088 212 -EPKRTLGRLGD-----PALGIthYFCVPQMA---QAFRAQP--GFDAAALRHLTALFTGGAPHAAEDILGW-------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 335 lretaikpsygLAEATLFVSTTPMDQAPTVIHvdrdelnkqrfveVPADSpkAVPQVSAGTIGVDEWAV---IVDpETAS 411
Cdd:PRK09088 273 -----------LDDGIPMVDGFGMSEAGTVFG-------------MSVDC--DVIRAKAGAAGIPTPTVqtrVVD-DQGN 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 412 ELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshAEGapddgmWVKTGDYGTY-YKGHLYIAGRIKDLVI 490
Cdd:PRK09088 326 DCPAGVPGELLLRGPNLSPGYWRRPQATARAFT-----------GDG------WFRTGDIARRdADGFFWVVDRKKDMFI 388
|
490
....*....|..
gi 497642598 491 IDGRNHYPQDLE 502
Cdd:PRK09088 389 SGGENVYPAEIE 400
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
52-551 |
2.29e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.09 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGH------------ 115
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRgLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTPRELEHqlkdsgaeaivv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 116 ----VGRLHAVLDDCSPSTILTttdAAEG-------------VRKFIRARSAKERPRVIAVDAVPNEVAS-TWEPPEADE 177
Cdd:PRK07059 127 lenfATTVQQVLAKTAVKHVVV---ASMGdllgfkghivnfvVRRVKKMVPAWSLPGHVRFNDALAEGARqTFKPVKLGP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 178 NTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQV---LN-GLEGKEGDRGLSW---LPFFHDMGL-ITALLSPVLG-HNFT 248
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawLQpAFEKKPRPDQLNFvcaLPLYHIFALtVCGLLGMRTGgRNIL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 249 FMTPaafvRRPGRWIREMARKPedapdsevFTVAPNFAFEHAAVRGVPkeGEPPLDLSNVKAILNGSEPVSPASMRKFYE 328
Cdd:PRK07059 284 IPNP----RDIPGFIKELKKYQ--------VHIFPAVNTLYNALLNNP--DFDKLDFSKLIVANGGGMAVQRPVAERWLE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 329 afspygLRETAIKPSYGLAEatlfvsTTPMdqaPTVIHVDRDELNkqrfvevpadspkavpqvsaGTIGV---DEWAVIV 405
Cdd:PRK07059 350 ------MTGCPITEGYGLSE------TSPV---ATCNPVDATEFS--------------------GTIGLplpSTEVSIR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 406 DpETASELPDGQIGEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGMWvKTGDYGTY-YKGHLYIAGR 484
Cdd:PRK07059 395 D-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDET----------------AKVMTADGFF-RTGDVGVMdERGYTKIVDR 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642598 485 IKDLVIIDGRNHYPQDLEYSAQEASKALRtgyVAAFSVPanqlpkevfdNPHTG-------LKYDPDDSSEQLV 551
Cdd:PRK07059 457 KKDMILVSGFNVYPNEIEEVVASHPGVLE---VAAVGVP----------DEHSGeavklfvVKKDPALTEEDVK 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
19-502 |
7.28e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 93.30 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 19 TNLVKHVEKWARVRGDKLAYRFVDFSTerdgeyrdiVWSDFSARNRAVGARL-QQVTQPGDRIAVLCPQNLDYLIAFFGA 97
Cdd:PRK07786 17 QNWVNQLARHALMQPDAPALRFLGNTT---------TWRELDDRVAALAGALsRRGVGFGDRVLILMLNRTEFVESVLAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 98 LYAGRIAVPLFDPAEPGHVGRLhavLDDCSPSTILTT---TDAAEGVRKFIRARS------AKERPRVIAVDAVPNEVAS 168
Cdd:PRK07786 88 NMLGAIAVPVNFRLTPPEIAFL---VSDCGAHVVVTEaalAPVATAVRDIVPLLStvvvagGSSDDSVLGYEDLLAEAGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 169 TWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLptnVLQVLNGLEGKEGDR----GLSWLPFFHDMGLITALLSPVLG 244
Cdd:PRK07786 165 AHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL---TGQAMTCLRTNGADInsdvGFVGVPLFHIAGIGSMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 245 HNFTFMTPAAFvrRPGRWIremarkpeDAPDSEVFTVAPNFAFEHAAVRGVPKegEPPLDLSnVKAILNGSEPVSPASMR 324
Cdd:PRK07786 242 APTVIYPLGAF--DPGQLL--------DVLEAEKVTGIFLVPAQWQAVCAEQQ--ARPRDLA-LRVLSWGAAPASDTLLR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 325 KFYEAFSpyglrETAIKPSYGLAEatlfvsTTPMdqapTVIHVDRDELNKQRFVevpadsPKAVPQVSAGtigvdewavI 404
Cdd:PRK07786 309 QMAATFP-----EAQILAAFGQTE------MSPV----TCMLLGEDAIRKLGSV------GKVIPTVAAR---------V 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 405 VDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegapdDGMWVKTGDY-GTYYKGHLYIAG 483
Cdd:PRK07786 359 VD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------------------AGGWFHSGDLvRQDEEGYVWVVD 419
|
490
....*....|....*....
gi 497642598 484 RIKDLVIIDGRNHYPQDLE 502
Cdd:PRK07786 420 RKKDMIISGGENIYCAEVE 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
29-502 |
1.43e-19 |
|
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: 92.43 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYrfvdfsterDGEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVP- 106
Cdd:cd05959 14 NEGRGDKTAF---------IDDAGSLTYAELEAEARRVAGALRALgVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 107 --LFDPAEPGHV------------GRLHAVLDDcspstilTTTDAAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEP 172
Cdd:cd05959 85 ntLLTPDDYAYYledsrarvvvvsGELAPVLAA-------ALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 173 PEADENTIAYLQYTSGSTRTPTGVQITHLNL-PTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPV-LGHNFTFM 250
Cdd:cd05959 158 AATHADDPAFWLYSSGSTGRPKGVVHLHADIyWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLsVGATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 251 ----TPAAFVRRpgrwIREmaRKPedapdsEVFTVAPNFafeHAAVRGVPkeGEPPLDLSNVKAILNGSEPVsPASMrkf 326
Cdd:cd05959 238 perpTPAAVFKR----IRR--YRP------TVFFGVPTL---YAAMLAAP--NLPSRDLSSLRLCVSAGEAL-PAEV--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 327 YEAFSP-YGLRetaIKPSYGLAEAT-LFVSTTPMDqaptvihvdrdelnkqrfVEvPADSPKAVP--QVSagtigvdewa 402
Cdd:cd05959 297 GERWKArFGLD---ILDGIGSTEMLhIFLSNRPGR------------------VR-YGTTGKPVPgyEVE---------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 403 vIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapddGMWVKTGDygTYYK---GHL 479
Cdd:cd05959 345 -LRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------------------GEWTRTGD--KYVRdddGFY 402
|
490 500
....*....|....*....|...
gi 497642598 480 YIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVE 425
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
48-502 |
3.14e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.09 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 48 DGEYrdIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVL 123
Cdd:PRK07514 25 DGLR--YTYGDLDAASARLANLLVALgVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLntaYTLAE------LDYFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 124 DDCSPSTILTTTDAAEGVRKFIRARSAkerPRVIAVDA--------VPNEVASTWEPPEADENTIAYLQYTSGSTRTPTG 195
Cdd:PRK07514 97 GDAEPALVVCDPANFAWLSKIAAAAGA---PHVETLDAdgtgslleAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 196 VQITHLNLPTNVlQVLNGLEG-KEGDRGLSWLPFFHDMGLITALlspvlghNFTFMTPAA--FVRR--PGRWIREMarkp 270
Cdd:PRK07514 174 AMLSHGNLLSNA-LTLVDYWRfTPDDVLIHALPIFHTHGLFVAT-------NVALLAGASmiFLPKfdPDAVLALM---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 271 edaPDSEVFTVAPNF--------AFEHAAVRgvpkegeppldlsNVKAILNGSEPVSPASMRKFYEafspyglrET--AI 340
Cdd:PRK07514 242 ---PRATVMMGVPTFytrllqepRLTREAAA-------------HMRLFISGSAPLLAETHREFQE--------RTghAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 341 KPSYGLAEATLFVSTtPMDQaptvihvDRdelnkqrfveVPADSPKAVPQVSAgtigvdewaVIVDPETASELPDGQIGE 420
Cdd:PRK07514 298 LERYGMTETNMNTSN-PYDG-------ER----------RAGTVGFPLPGVSL---------RVTDPETGAELPPGEIGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 421 IWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQ 499
Cdd:PRK07514 351 IEVKGPNVFKGYWRMPEKTAEEFR----------------ADG-FFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPK 413
|
...
gi 497642598 500 DLE 502
Cdd:PRK07514 414 EVE 416
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
77-611 |
4.00e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 77 GDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVgrlhavLDDCSPSTILTTTDAAEGVRKFIRARSAKE- 152
Cdd:PRK08751 76 GDRVALMMPNCLQYPIATFGVLRAGLTVVnvnPLYTPRELKHQ------LIDSGASVLVVIDNFGTTVQQVIADTPVKQv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 153 ----------RPRVIAVDAVPNEVAS-----------------------TWEPPEADENTIAYLQYTSGSTRTPTGVQIT 199
Cdd:PRK08751 150 ittglgdmlgFPKAALVNFVVKYVKKlvpeyringairfrealalgrkhSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 200 HLNLPTNVLQVLNGLEG----KEGDRG-LSWLPFFHDMGLiTA---LLSPVLGHNFTFMTPAAFvrrPGrWIREMARKPe 271
Cdd:PRK08751 230 HRNLVANMQQAHQWLAGtgklEEGCEVvITALPLYHIFAL-TAnglVFMKIGGCNHLISNPRDM---PG-FVKELKKTR- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 272 dapdsevFTVAPNFAFEHAAVRGVPkeGEPPLDLSNVKAILNGSEPVSpASMRKFYEAFSPYGLREtaikpSYGLAEATL 351
Cdd:PRK08751 304 -------FTAFTGVNTLFNGLLNTP--GFDQIDFSSLKMTLGGGMAVQ-RSVAERWKQVTGLTLVE-----AYGLTETSP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 352 FVSTTPMDQaptvihvdrDELNKQrfVEVPADSPKAVPQVSAGTIgvdewavivdpetaseLPDGQIGEIWLHGNNLGTG 431
Cdd:PRK08751 369 AACINPLTL---------KEYNGS--IGLPIPSTDACIKDDAGTV----------------LAIGEIGELCIKGPQVMKG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 432 YWGREQETNDIFrnilksrisqsHAEGapddgmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASK 510
Cdd:PRK08751 422 YWKRPEETAKVM-----------DADG------WLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 511 ALRtgyVAAFSVP---ANQLPKEVFdnphtgLKYDPDDSSEQlviVAERAAGSHKLDYQPIADDIRAaiavrhgvtvrdl 587
Cdd:PRK08751 485 VLE---VAAVGVPdekSGEIVKVVI------VKKDPALTAED---VKAHARANLTGYKQPRIIEFRK------------- 539
|
570 580
....*....|....*....|....
gi 497642598 588 llvqsgTIPRTSSGKIGHRACRAA 611
Cdd:PRK08751 540 ------ELPKTNVGKILRRELRDA 557
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
69-502 |
7.11e-19 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 89.43 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 69 RLQQVTQpGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHvgrLHAVLDDCSPSTILTTTDAAEgvrKFIRAR 148
Cdd:TIGR01923 17 KAQGIRS-GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENE---RTNQLEDLDVQLLLTDSLLEE---KDFQAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 149 SAkerPRVIAVDAVPNEVaSTWEPPEAdentIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPF 228
Cdd:TIGR01923 90 SL---DRIEAAGRYETSL-SASFNMDQ----IATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 229 FHDMGLiTALLSPVLGhnftfmtpAAFVRRPgrwiremarkpedAPDSEVFTVAPNFAFEHAAVrgVP-------KEGEP 301
Cdd:TIGR01923 162 YHISGL-SILFRWLIE--------GATLRIV-------------DKFNQLLEMIANERVTHISL--VPtqlnrllDEGGH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 302 PLdlsNVKAILNGSEPVSPASMRKFYEafspYGLretAIKPSYGLAEA--TLFVSTTPMDQAPTvihvdrdelnkqrfve 379
Cdd:TIGR01923 218 NE---NLRKILLGGSAIPAPLIEEAQQ----YGL---PIYLSYGMTETcsQVTTATPEMLHARP---------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 380 vpaDSPKAVPQVSAgTIGVDEWAvivdpetaselpdgQIGEIWLHGNNLGTGYWGREQetndifrnilksrisqshAEGA 459
Cdd:TIGR01923 272 ---DVGRPLAGREI-KIKVDNKE--------------GHGEIMVKGANLMKGYLYQGE------------------LTPA 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 497642598 460 PDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:TIGR01923 316 FEQQGWFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIE 359
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-495 |
9.27e-19 |
|
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: 88.89 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHVgrLHAVLDDCspst 130
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALgIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPI-NTALRGDE--LAYIIDHS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 131 iltttdaaegvrkfirarsakeRPRVIAVDavpnevastweppeadentIAYLQYTSGSTRTPTGVQITHLNLPTNVLQV 210
Cdd:cd05934 75 ----------------------GAQLVVVD-------------------PASILYTSGTTGPPKGVVITHANLTFAGYYS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 211 LNGLEGKEGDRGLSWLPFFHDMGLITALLsPVLGHNFTFmtpaAFVRR--PGRWIREMARKpedapDSEVFTVAPnfafe 288
Cdd:cd05934 114 ARRFGLGEDDVYLTVLPLFHINAQAVSVL-AALSVGATL----VLLPRfsASRFWSDVRRY-----GATVTNYLG----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 289 hAAVRGVPKEGEPPLDLSN-VKAIlnGSEPVSPASMRKFYEAFspyGLRetaIKPSYGLAEATlfvsttpmdqaptvihv 367
Cdd:cd05934 179 -AMLSYLLAQPPSPDDRAHrLRAA--YGAPNPPELHEEFEERF---GVR---LLEGYGMTETI----------------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 368 drdelnkqrfVEVPADSPKAVPQVSAGTIGVDEWAVIVDPETaSELPDGQIGEIWL---HGNNLGTGYWGREQETNDIFR 444
Cdd:cd05934 233 ----------VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDG-QELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMR 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 497642598 445 NilksrisqshaegapddgMWVKTGDYGtyYK---GHLYIAGRIKDLVIIDGRN 495
Cdd:cd05934 302 N------------------GWFHTGDLG--YRdadGFFYFVDRKKDMIRRRGEN 335
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
51-622 |
1.66e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.89 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 51 YRD---IVWSDFSARNRAVGARLQQVTQ--------PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfdpaepgH-VGR 118
Cdd:PRK06188 25 YPDrpaLVLGDTRLTYGQLADRISRYIQafealglgTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL-------HpLGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 119 L--HA-VLDDCSPSTILTttDAAegvrKFI-RARSAKER----PRVIAVDAVP-----NEVASTWEP----PEADENTIA 181
Cdd:PRK06188 98 LddHAyVLEDAGISTLIV--DPA----PFVeRALALLARvpslKHVLTLGPVPdgvdlLAAAAKFGPaplvAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 182 YLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGlitALLSPVLGHNFTFMTPAAFvrRPGR 261
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG---AFFLPTLLRGGTVIVLAKF--DPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 262 WIREMARKPEDApdseVFTVaPNFAF---EHAAVRGVpkegepplDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLRet 338
Cdd:PRK06188 247 VLRAIEEQRITA----TFLV-PTMIYallDHPDLRTR--------DLSSLETVYYGASPMSPVRLAEAIERFGPIFAQ-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 339 aikpSYGLAEATLFVSTTPMDQaptviHVDRDElnkQRFVevpadspkavpqvSAG--TIGVDewAVIVDPEtASELPDG 416
Cdd:PRK06188 312 ----YYGQTEAPMVITYLRKRD-----HDPDDP---KRLT-------------SCGrpTPGLR--VALLDED-GREVAQG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 417 QIGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqshaeGapddgmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRN 495
Cdd:PRK06188 364 EVGEICVRGPLVMDGYWNRPEETAEAFRD------------G------WLHTGDVAREDEdGFYYIVDRKKDMIVTGGFN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 496 HYPQDLEYS-AQEASKALrtgyVAAFSVpanqlpkevfdnphtglkydPDDSSEQLV--IVAERAagshklDYQPIADDI 572
Cdd:PRK06188 426 VFPREVEDVlAEHPAVAQ----VAVIGV--------------------PDEKWGEAVtaVVVLRP------GAAVDAAEL 475
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 573 RAAIAVRHG-------VTVRDlllvqsgTIPRTSSGKIGHRACRAAYLDGSLRsGVG 622
Cdd:PRK06188 476 QAHVKERKGsvhapkqVDFVD-------SLPLTALGKPDKKALRARYWEGRGR-AVG 524
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
48-493 |
3.13e-18 |
|
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: 87.36 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 48 DGEYRDIVWSDFSARNRAVGARL-QQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDC 126
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLlQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL-DAKLPS--ARIQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 127 SPSTILTTTDAaegvrkfirarsakerprviavdavpnevastweppeadeNTIAYLQYTSGSTRTPTGVQITHLNLPTN 206
Cdd:cd17653 94 GATLLLTTDSP----------------------------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 207 VLQVLNGLEGKEGDRGLSWLPFFHDMGlITALLSpVLGHNFTFMtpaafVRRPGRWIREMARKpedapdSEVFTVAPNFA 286
Cdd:cd17653 134 VSQPPARLDVGPGSRVAQVLSIAFDAC-IGEIFS-TLCNGGTLV-----LADPSDPFAHVART------VDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 287 fehAAVrgvpkegePPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGlretaikpSYGLAEATLFVSTTPM-DQAPTVI 365
Cdd:cd17653 201 ---STL--------SPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYN--------AYGPTECTISSTMTELlPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 366 HvdrdelnkqrfvevpadspKAVPQVSAgtigvdewaVIVDPETaSELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRN 445
Cdd:cd17653 262 G-------------------KPIPNSTC---------YILDADL-QPVPEGVVGEICISGVQVARGYLGNPALTASKFVP 312
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 497642598 446 ILK---SRIsqshaegapddgmwVKTGDYGTY-YKGHLYIAGRIKDLVIIDG 493
Cdd:cd17653 313 DPFwpgSRM--------------YRTGDYGRWtEDGGLEFLGREDNQVKVRG 350
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
49-607 |
5.26e-18 |
|
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: 87.40 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCS 127
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARgVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-DPAYPAE--RLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 128 PSTILTTTDAAEgvrkfiraRSAKERPRVIAVDAVPNEVASTWEP-PEADENTIAYLQYTSGSTRTPTGVQITHLNLpTN 206
Cdd:cd17651 93 PVLVLTHPALAG--------ELAVELVAVTLLDQPGAAAGADAEPdPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-AN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 207 VLQVLNG-LEGKEGDRGLSWLPFFHDMGLITALlsPVLGHNFTFMTPAAFVRRPgrwIREMARKPEDAPDSEVFtvAPNF 285
Cdd:cd17651 164 LVAWQARaSSLGPGARTLQFAGLGFDVSVQEIF--STLCAGATLVLPPEEVRTD---PPALAAWLDEQRISRVF--LPTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 286 AFEHAAVRGVPKEGEPPLdlsnVKAILNGSEPVSPAS-MRKFyeafsPYGLRETAIKPSYGLAEATLFvsttpmdqapTV 364
Cdd:cd17651 237 ALRALAEHGRPLGVRLAA----LRYLLTGGEQLVLTEdLREF-----CAGLPGLRLHNHYGPTETHVV----------TA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 365 IHVDRDelnkqrfvevPADSPKAVPqvsagtIG--VDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDI 442
Cdd:cd17651 298 LSLPGD----------PAAWPAPPP------IGrpIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAER 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 443 FrnilksrisqsHAEGAPDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLEySAQEASKALRTGYVAAfs 521
Cdd:cd17651 362 F-----------VPDPFVPGARMYRTGDLARWLPdGELEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVVLA-- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 522 vpanqlpkevfdnphtglkyDPDDSSE-QLV--IVAERAAGshkldyqPIADDIRAAIAVR---HGVTVRDLLLvqsGTI 595
Cdd:cd17651 428 --------------------REDRPGEkRLVayVVGDPEAP-------VDAAELRAALATHlpeYMVPSAFVLL---DAL 477
|
570
....*....|..
gi 497642598 596 PRTSSGKIGHRA 607
Cdd:cd17651 478 PLTPNGKLDRRA 489
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-502 |
5.42e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 84.44 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEP----GHVG-------------RLHAVLDDCSPSTiltt 134
Cdd:PRK12583 68 QPGDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRASELeyalGQSGvrwvicadafktsDYHAMLQELLPGL---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 135 tdaAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPEADENTIAY-----------------LQYTSGSTRTPTGVQ 197
Cdd:PRK12583 144 ---AEGQPGALACERLPELRGVVSLAPAPPPGFLAWHELQARGETVSRealaerqasldrddpinIQYTSGTTGFPKGAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 198 ITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITAllspvlghNFTFMTPAAFVRRPGRWIRemarkpedaPDSE 277
Cdd:PRK12583 221 LSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLA--------NLGCMTVGACLVYPNEAFD---------PLAT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 278 VFTVAPNFAfehAAVRGVP----KEGEPP----LDLSNVKAILNGSEPVSPASMRKFYEAfspygLRETAIKPSYGLAEA 349
Cdd:PRK12583 284 LQAVEEERC---TALYGVPtmfiAELDHPqrgnFDLSSLRTGIMAGAPCPIEVMRRVMDE-----MHMAEVQIAYGMTET 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 350 T-LFVSTTPMDQAPT-VIHVDRDelnkQRFVEVPadspkavpqvsagtigvdewavIVDPETASeLPDGQIGEIWLHGNN 427
Cdd:PRK12583 356 SpVSLQTTAADDLERrVETVGRT----QPHLEVK----------------------VVDPDGAT-VPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642598 428 LGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK12583 409 VMKGYWNNPEAT----------------AESIDEDG-WMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIE 467
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
64-502 |
5.46e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 84.26 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 64 RAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRI---AVPLFDPAEpghvgrLHAVLDDCSPSTILTTTDAAE 139
Cdd:PLN02246 61 RRVAAGLHKLgIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttANPFYTPAE------IAKQAKASGAKLIITQSCYVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 140 GVRKFIRARSAKerprVIAVDAVPNEVASTWEPPEADENTI----------AYLQYTSGSTRTPTGVQITHLNLPTNVLQ 209
Cdd:PLN02246 135 KLKGLAEDDGVT----VVTIDDPPEGCLHFSELTQADENELpeveispddvVALPYSSGTTGLPKGVMLTHKGLVTSVAQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 210 VLNG----LEGKEGDRGLSWLPFFHDMGLITALLSP-------VLGHNFTFMTPAAFVRRPGrwiremarkpedapdsev 278
Cdd:PLN02246 211 QVDGenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGlrvgaaiLIMPKFEIGALLELIQRHK------------------ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 279 FTVAPnFAfehaavrgvpkegePPL-------------DLSNVKAILNGSEPVSP----ASMRKFYEAFSPYGlretaik 341
Cdd:PLN02246 273 VTIAP-FV--------------PPIvlaiakspvvekyDLSSIRMVLSGAAPLGKeledAFRAKLPNAVLGQG------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 342 psYGLAEATLFVSttpMDQAptvihvdrdelnkqrFvevpADSPKAVPQVSAGTIGVDEWAVIVDPETASELPDGQIGEI 421
Cdd:PLN02246 331 --YGMTEAGPVLA---MCLA---------------F----AKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 422 WLHGNNLGTGYwgreqeTNDIfrnilksrisQSHAEGAPDDGmWVKTGDYGtYYKG--HLYIAGRIKDLVIIDGRNHYPQ 499
Cdd:PLN02246 387 CIRGPQIMKGY------LNDP----------EATANTIDKDG-WLHTGDIG-YIDDddELFIVDRLKELIKYKGFQVAPA 448
|
...
gi 497642598 500 DLE 502
Cdd:PLN02246 449 ELE 451
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
61-493 |
9.39e-17 |
|
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: 83.47 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 61 ARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAE 139
Cdd:cd12114 20 ERARRVAGALKAAgVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV-DIDQP--AARREAILADAGARLVLTDGPDAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 140 GVrkfirarsaKERPRVIAVDAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEG 219
Cdd:cd12114 97 LD---------VAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 220 DRGLSWLPFFHDMGL--ITALLSpvLGHNFTFMTPAAfVRRPGRWIREMARKPedapdsevFTV---APnfAFEHAAVRG 294
Cdd:cd12114 168 DRVLALSSLSFDLSVydIFGALS--AGATLVLPDEAR-RRDPAHWAELIERHG--------VTLwnsVP--ALLEMLLDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 VPKEGEPPLDLSNVkaILNGSE-PVS-PASMRKFY---EAFSPYGLRETAIKPSYglaeatlfVSTTPMDQAPTVIHVDR 369
Cdd:cd12114 235 LEAAQALLPSLRLV--LLSGDWiPLDlPARLRALApdaRLISLGGATEASIWSIY--------HPIDEVPPDWRSIPYGR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 370 DELNKQRFVevpadspkavpqvsagtigVDEWavivdpetASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNIlks 449
Cdd:cd12114 305 PLANQRYRV-------------------LDPR--------GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH--- 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 497642598 450 risqshaegaPDDGMWVKTGDYGTYY-KGHLYIAGRIKDLVIIDG 493
Cdd:cd12114 355 ----------PDGERLYRTGDLGRYRpDGTLEFLGRRDGQVKVRG 389
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
58-200 |
1.01e-16 |
|
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: 83.09 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 58 DFSARNRAVGARL-QQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDCSPSTILTTTD 136
Cdd:cd17646 28 ELDERANRLAHLLrARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPA--DRLAYMLADAGPAVVLTTAD 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642598 137 AAegvrkfirARSAKERPRVIAVDAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITH 200
Cdd:cd17646 105 LA--------ARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
69-479 |
1.16e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 84.21 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 69 RLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL-FDPAEPGhvgrLHAVLDDCSPSTILTTtdaaegvRKFIRA 147
Cdd:PRK08633 657 LLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLnYTASEAA----LKSAIEQAQIKTVITS-------RKFLEK 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 148 RSAK-------ERPRVIAVDAV-------------------PNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHL 201
Cdd:PRK08633 726 LKNKgfdlelpENVKVIYLEDLkakiskvdkltallaarllPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHH 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 202 NLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLgHNFtfmtPAAFVRRP--GRWIREMARKpedapdsevF 279
Cdd:PRK08633 806 NILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLL-EGI----KVVYHPDPtdALGIAKLVAK---------H 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 280 TVAPNFA---FEHAAVRGVPKEgepPLDLSNVKAILNGSEPVSPASMRKFYEAFspyGLRetaIKPSYGLAEatlfvsTT 356
Cdd:PRK08633 872 RATILLGtptFLRLYLRNKKLH---PLMFASLRLVVAGAEKLKPEVADAFEEKF---GIR---ILEGYGATE------TS 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 357 PmdqaptVIHVD-RDELNKQrFVEVPADSPKAVPQVSAGTIgvdewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGR 435
Cdd:PRK08633 937 P------VASVNlPDVLAAD-FKRQTGSKEGSVGMPLPGVA-----VRIVDPETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 497642598 436 EQETNDIFRNILKSRisqshaegapddgmWVKTGDygtyyKGHL 479
Cdd:PRK08633 1005 PEKTAEVIKDIDGIG--------------WYVTGD-----KGHL 1029
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
56-502 |
1.74e-16 |
|
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: 82.04 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 56 WSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFdPAEPGHvgRLHAVLDDCSPSTILTT 134
Cdd:cd05903 4 YSELDTRADRLAAGLAALgVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPIL-PFFREH--ELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 135 tdaaegvRKFIRARsakerprviavdavpnevastwepPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGL 214
Cdd:cd05903 81 -------ERFRQFD------------------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 215 EGKEGDRGLSWLPFFHDMGLITALLSPVLghnftFMTPAAFVRRpgrWirEMARKPEDAPDSEVFTVAPNFAFEHAAVRG 294
Cdd:cd05903 130 GLGPGDVFLVASPMAHQTGFVYGFTLPLL-----LGAPVVLQDI---W--DPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 VPKEGEPPLDLsnvKAILNGSEPVSPASMRKFYEAFspyglrETAIKPSYGLAEATLFVSTTPMDQAPTVIHVDrdelnk 374
Cdd:cd05903 200 VEEAGEPLSRL---RTFVCGGATVPRSLARRAAELL------GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 375 qrfvevpaDSPKAvpqvsagtiGVDewaVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREqetndifrnilksrisqs 454
Cdd:cd05903 265 --------GRPLP---------GVE---IKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRP------------------ 306
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 497642598 455 HAEGAPDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05903 307 DLTADAAPEGWFRTGDLARLDEdGYLRITGRSKDIIIRGGENIPVLEVE 355
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
21-502 |
1.22e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 80.09 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 21 LVKHVEKWARVRGDKLAYRFvdfsterdgeY-RDIVWSDFSARNRAVGARLQQV-TQPGDRIAVL---CPQnldYLIAFF 95
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIF----------YgHVITYAELDELSDRFAALLRQRgVGAGDRVAVFlpnCPQ---FHIVFF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 96 GALYAGRIAV---PLFDPAEPGHvgrlhaVLDDCSPSTILTTTDAAEGVRKfIRARSAKER------------------- 153
Cdd:PRK06178 102 GILKLGAVHVpvsPLFREHELSY------ELNDAGAEVLLALDQLAPVVEQ-VRAETSLRHvivtsladvlpaeptlplp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 154 -----PRVIA---VDAVPNEVASTWEPPE--ADENTIAYLQYTSGSTRTPTGVQITHLNLP-TNVLQVLNGLEGKEGDRG 222
Cdd:PRK06178 175 dslraPRLAAagaIDLLPALRACTAPVPLppPALDALAALNYTGGTTGMPKGCEHTQRDMVyTAAAAYAVAVVGGEDSVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 223 LSWLPFF----HDMGLITALLSpvlGHNFTFMTpaafvrrpgRWIRE--MARKPEDAPDSEVFTVaPNFA--FEHaavrg 294
Cdd:PRK06178 255 LSFLPEFwiagENFGLLFPLFS---GATLVLLA---------RWDAVafMAAVERYRVTRTVMLV-DNAVelMDH----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 vPKEGEppLDLSNVKAILNGS--EPVSPAsMRKFYEAFSPYGLRETAikpsYGLAEA-TLFVSTTPMDQAptvihvDRDE 371
Cdd:PRK06178 317 -PRFAE--YDLSSLRQVRVVSfvKKLNPD-YRQRWRALTGSVLAEAA----WGMTEThTCDTFTAGFQDD------DFDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 372 LNKQRFVEVPadspkaVPqvsaGTIgvdewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksri 451
Cdd:PRK06178 383 LSQPVFVGLP------VP----GTE-----FKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR------- 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 497642598 452 sqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK06178 441 ----------DG-WLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
76-443 |
1.77e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDAAE------GVRKFIRARS 149
Cdd:PRK12316 2052 PEVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAE--RLAYMLEDSGAALLLTQRHLLErlplpaGVARLPLDRD 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 150 AKERprviavdavpnEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFF 229
Cdd:PRK12316 2129 AEWA-----------DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFS 2197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 230 HDmGLITALLSPVLGHNFTFMTPAAfVRRPGRWIREMARKP---EDAPDSEVFTVApnfafEHAAVrgvpkEGEPPldls 306
Cdd:PRK12316 2198 FD-GAHEQWFHPLLNGARVLIRDDE-LWDPEQLYDEMERHGvtiLDFPPVYLQQLA-----EHAER-----DGRPP---- 2261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 307 NVKAILNGSEPVSPASMRKFYEAFSPYGLRETaikpsYGLAEATLfvsttpmdqAPTVIHVDRDElnkqrfvevpadsPK 386
Cdd:PRK12316 2262 AVRVYCFGGEAVPAASLRLAWEALRPVYLFNG-----YGPTEAVV---------TPLLWKCRPQD-------------PC 2314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 387 AVPQVSAGTIGVDEWAVIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIF 443
Cdd:PRK12316 2315 GAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERF 2370
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
16-609 |
2.96e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 78.87 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 16 PDNTNLVKHVEKWARVRGDKLAyrFVDFSTERDGEYRDIVWSD--FSARNRAVGARLQQVtqpgdrIAVLCPQNLDYLIA 93
Cdd:PLN02330 25 PDKLTLPDFVLQDAELYADKVA--FVEAVTGKAVTYGEVVRDTrrFAKALRSLGLRKGQV------VVVVLPNVAEYGIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 94 FFGALYAGRIavplFDPAEP-GHVGRLHAVLDDCSPSTILTTTDAAEGVRKFirarsakERPrVIAVDAVPNEVASTW-- 170
Cdd:PLN02330 97 ALGIMAAGGV----FSGANPtALESEIKKQAEAAGAKLIVTNDTNYGKVKGL-------GLP-VIVLGEEKIEGAVNWke 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 171 --EPPEADENTIAY----------LQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLE----GKEGDRGLswLPFFHDMGl 234
Cdd:PLN02330 165 llEAADRAGDTSDNeeilqtdlcaLPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGpemiGQVVTLGL--IPFFHIYG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 235 ITALLSPVLGHNFTFMTPAAFVRRP---GRWIREMARKPEDAPDseVFTVAPNFAFEHaavrgvpkegeppLDLSNVK-- 309
Cdd:PLN02330 242 ITGICCATLRNKGKVVVMSRFELRTflnALITQEVSFAPIVPPI--ILNLVKNPIVEE-------------FDLSKLKlq 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 310 AILNGSEPVSPASMRKFYEAFSPYGLREtaikpSYGLAEATLFvsttpmdqapTVIHVDrdelnkqrfvevPADSPKAVP 389
Cdd:PLN02330 307 AIMTAAAPLAPELLTAFEAKFPGVQVQE-----AYGLTEHSCI----------TLTHGD------------PEKGHGIAK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 390 QVSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNdifRNIlksrisqshaegapDDGMWVKTG 469
Cdd:PLN02330 360 KNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD---RTI--------------DEDGWLHTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 470 DYGtYY--KGHLYIAGRIKDLVIIDGRNHYPQDLEysaqeaskALRTGYVAAFSVPANQLPKEvfdnphtglkyDPDDSS 547
Cdd:PLN02330 423 DIG-YIddDGDIFIVDRIKELIKYKGFQVAPAELE--------AILLTHPSVEDAAVVPLPDE-----------EAGEIP 482
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642598 548 EQLVIVAERAAGSHKLDYQPIADDiraaiaVRHGVTVRDLLLVQSgtIPRTSSGKIGHRACR 609
Cdd:PLN02330 483 AACVVINPKAKESEEDILNFVAAN------VAHYKKVRVVQFVDS--IPKSLSGKIMRRLLK 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
77-606 |
9.98e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.19 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 77 GDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEpghvgrLHAVLDDCSPSTILTTTDAAEgvrkfirarsaKER 153
Cdd:PLN02574 92 GDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnPSSSLGE------IKKRVVDCSVGLAFTSPENVE-----------KLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 154 PRVIAVDAVP-----NEVASTWEP--------------PEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVlQVLNGL 214
Cdd:PLN02574 155 PLGVPVIGVPenydfDSKRIEFPKfyelikedfdfvpkPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV-ELFVRF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 215 EGKEGDRG------LSWLPFFHDMGL---ITALLSpvLGHNFTFMtpaafvrrpgrwiremarKPEDApdSEVFTVAPNF 285
Cdd:PLN02574 234 EASQYEYPgsdnvyLAALPMFHIYGLslfVVGLLS--LGSTIVVM------------------RRFDA--SDMVKVIDRF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 286 AFEHAAVrgVP---------KEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPYGLREtaikpSYGLAEATLfvstt 356
Cdd:PLN02574 292 KVTHFPV--VPpilmaltkkAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ-----GYGMTESTA----- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 357 pmdqaptvihVDRDELNKQRFVEVPadspkavpqvSAGTIGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGRE 436
Cdd:PLN02574 360 ----------VGTRGFNTEKLSKYS----------SVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 437 QETNdifrnilkSRISQshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKALRTG 515
Cdd:PLN02574 420 KATQ--------STIDK--------DG-WLRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 516 YVAAFSVPANQLPKE-VFDNPHTGLkydpddsSEQLVI--VAERAAGSHKldyqpiaddiraaiavrhgvtVRDLLLVQS 592
Cdd:PLN02574 483 VTAVPDKECGEIPVAfVVRRQGSTL-------SQEAVInyVAKQVAPYKK---------------------VRKVVFVQS 534
|
570
....*....|....
gi 497642598 593 gtIPRTSSGKIGHR 606
Cdd:PLN02574 535 --IPKSPAGKILRR 546
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
29-502 |
1.14e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 77.30 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYRFVDFSTERDgEYRDIVWSDFSAR-----N--RAVGARlqqvtqPGDRIAVLCPQNLDYLIAFFGALYAG 101
Cdd:PRK07529 35 AARHPDAPALSFLLDADPLD-RPETWTYAELLADvtrtaNllHSLGVG------PGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 102 rIAVPLFDPAEPGHVG------------------------RLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAKERP--- 154
Cdd:PRK07529 108 -IANPINPLLEPEQIAellraagakvlvtlgpfpgtdiwqKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRkah 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 155 -RVIAVDAV----PNEVASTWEPPEADEntIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFF 229
Cdd:PRK07529 187 aRILDFDAElarqPGDRLFSGRPIGPDD--VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 230 HDMGLITALLSPVL-GHNFTFMTPAAFvRRPG----------RW-IREMarkpedapdSEVFTVapnfafeHAAVRGVPK 297
Cdd:PRK07529 265 HVNALLVTGLAPLArGAHVVLATPQGY-RGPGvianfwkiveRYrINFL---------SGVPTV-------YAALLQVPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 298 EGEpplDLSNVKAILNGSEPVSPASMRKFYEAfspYGLRetaIKPSYGLAEATLFVSTTPmdqaptvihvdrdelnkqrf 377
Cdd:PRK07529 328 DGH---DISSLRYALCGAAPLPVEVFRRFEAA---TGVR---IVEGYGLTEATCVSSVNP-------------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 378 vevpADSPKAVpqvsaGTIGV-----DEWAVIVDPETA--SELPDGQIGEIWLHGNNLGTGYwgreqetndifrnilksr 450
Cdd:PRK07529 379 ----PDGERRI-----GSVGLrlpyqRVRVVILDDAGRylRDCAVDEVGVLCIAGPNVFSGY------------------ 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 497642598 451 ISQSHAEGAPDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK07529 432 LEAAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
60-507 |
2.25e-14 |
|
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: 75.46 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 60 SARNRAVGARLQQVTQP-GDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfdpaepghvgrlhavlddcspSTILTttdaa 138
Cdd:cd05912 8 FEEVSRLAEHLAALGVRkGDRVALLSKNSIEMILLIHALWLLGAEAVLL---------------------NTRLT----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 139 egvrkfirarsakerprviavdavPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVL-QVLN-GLEg 216
Cdd:cd05912 62 ------------------------PNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIgSALNlGLT- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 217 kEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTP--AAFVRrpgrwiremarkpEDAPDSEVFTVA--PNFAFEHAAV 292
Cdd:cd05912 117 -EDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKfdAEQVL-------------HLINSGKVTIISvvPTMLQRLLEI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 293 RGvpkEGEPPldlsNVKAILNGSEPVSPASMRKFYEafspYGLretAIKPSYGLAE-ATLFVSTTPmdqaptvihvdRDE 371
Cdd:cd05912 183 LG---EGYPN----NLRCILLGGGPAPKPLLEQCKE----KGI---PVYQSYGMTEtCSQIVTLSP-----------EDA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 372 LNKqrfvevPADSPKAVPQVSAGtigvdewavIVDPETaselPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNilksri 451
Cdd:cd05912 238 LNK------IGSAGKPLFPVELK---------IEDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESFEN------ 292
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 497642598 452 sqshaegapddgMWVKTGDYGtyY---KGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQE 507
Cdd:cd05912 293 ------------GWFKTGDIG--YldeEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
76-502 |
4.08e-14 |
|
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: 74.81 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAV---PLFDPAEpghvgrLHAVLDDCSPSTILTTTDAaegvrkfirarsake 152
Cdd:cd05919 34 SGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDD------YAYIARDCEARLVVTSADD--------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 153 rprviavdavpnevastweppeadentIAYLQYTSGSTRTPTGVQITHLNLPTNV-LQVLNGLEGKEGDRGLSWLPFFHD 231
Cdd:cd05919 93 ---------------------------IAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 232 MGLitallspvlGHNFTF--MTPAAFVRRPGRWIRE--MARKPEDAPdsEVFTVAPNFafeHAAVRgvPKEGEPPLDLSN 307
Cdd:cd05919 146 YGL---------GNSLWFplAVGASAVLNPGWPTAErvLATLARFRP--TVLYGVPTF---YANLL--DSCAGSPDALRS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 308 VKAILNGSEPVSpasmRKFYEAFSPYGLREtaIKPSYGLAEAT-LFVSTTPmdqaptvihvdrdelnkqrfvevpadspk 386
Cdd:cd05919 210 LRLCVSAGEALP----RGLGERWMEHFGGP--ILDGIGATEVGhIFLSNRP----------------------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 387 avPQVSAGTIG-VDEWAVI--VDPEtASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapddG 463
Cdd:cd05919 255 --GAWRLGSTGrPVPGYEIrlVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------------------G 313
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497642598 464 MWVKTGD-YGTYYKGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05919 314 GWYRTGDkFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
19-485 |
6.27e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 74.55 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 19 TNLVKHVEKWARVRGDKLAYRfvdfsterdgeYRD--IVWSDFSARNRAVGARLQQVTQPGDR-IAVLCPQNLDYLIAFF 95
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYD-----------YLGekLTYGQLKEDSDALAAFIDSLKLPDKSpIIVFGHMSPEMLATFL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 96 GALYAGR--IAVPLFDPAEpghvgRLHAVLDDCSPSTILTTTDAAEGVrKFIRARSAKERPRVIAVDAVPNEVASTwepp 173
Cdd:PRK04813 71 GAVKAGHayIPVDVSSPAE-----RIEMIIEVAKPSLIIATEELPLEI-LGIPVITLDELKDIFATGNPYDFDHAV---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 174 EADENtiAYLQYTSGSTRTPTGVQITHLNLP--TNVLQVLNGLEgkEGDRGLSWLPFFHD---MGLITALLSpvlGHNFt 248
Cdd:PRK04813 141 KGDDN--YYIIFTSGTTGKPKGVQISHDNLVsfTNWMLEDFALP--EGPQFLNQAPYSFDlsvMDLYPTLAS---GGTL- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 249 FMTPAAFVRRPGRWIREMARKPEDapdseVFTVAPNFAfEHAAVrgvpkegEPPLD---LSNVKAIL-NGSE-PVSPAsm 323
Cdd:PRK04813 213 VALPKDMTANFKQLFETLPQLPIN-----VWVSTPSFA-DMCLL-------DPSFNeehLPNLTHFLfCGEElPHKTA-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 324 RKFYEAFsPyglrETAIKPSYGLAEATLfvsttpmdqAPTVIHVDRDELNK-QRfveVPADSPKAvpqvsagtigvDEWA 402
Cdd:PRK04813 278 KKLLERF-P----SATIYNTYGPTEATV---------AVTSIEITDEMLDQyKR---LPIGYAKP-----------DSPL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 403 VIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegAPDDGMWV-KTGDYGTYYKGHLYI 481
Cdd:PRK04813 330 LIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF---------------FTFDGQPAyHTGDAGYLEDGLLFY 393
|
....
gi 497642598 482 AGRI 485
Cdd:PRK04813 394 QGRI 397
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
17-502 |
8.79e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.16 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 17 DNTNLVKHVEKWARVRGDKLAYRFVDfSTERDG--EYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDY--- 90
Cdd:PRK09274 4 SMANIARHLPRAAQERPDQLAVAVPG-GRGADGklAYDELSFAELDARSDAIAHGLNAAgIGRGMRAVLMVTPSLEFfal 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 91 LIAFFGAlyaGriAVP-LFDPAepghVGR--LHAVLDDCSPSTILTTTDAAEGVRKFIRA-RSAKerpRVIAVD------ 160
Cdd:PRK09274 83 TFALFKA---G--AVPvLVDPG----MGIknLKQCLAEAQPDAFIGIPKAHLARRLFGWGkPSVR---RLVTVGgrllwg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 161 ----AVPNEV--ASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLpTNVLQVLNGLEGKE-GDRGLSWLPFFhdmg 233
Cdd:PRK09274 151 gttlATLLRDgaAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMF-EAQIEALREDYGIEpGEIDLPTFPLF---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 234 litALLSPVLGhnftfMTPAafvrrpgrwIREM-ARKPEDApdsevftvapNFAFEHAAVRG---------------VPK 297
Cdd:PRK09274 226 ---ALFGPALG-----MTSV---------IPDMdPTRPATV----------DPAKLFAAIERygvtnlfgspallerLGR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 298 EGEP-PLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglrETAIKPSYGLAEAtLFVSTTPMdqaptvihvdRDELNKQR 376
Cdd:PRK09274 279 YGEAnGIKLPSLRRVISAGAPVPIAVIERFRAMLPP----DAEILTPYGATEA-LPISSIES----------REILFATR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 377 fvEVPADSP-----KAVPQVSAGTIGVDEwAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETndifrniLKSRI 451
Cdd:PRK09274 344 --AATDNGAgicvgRPVDGVEVRIIAISD-APIPEWDDALRLATGEIGEIVVAGPMVTRSYYNRPEAT-------RLAKI 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 497642598 452 SqshaegAPDDGMWVKTGDYGtyY---KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK09274 414 P------DGQGDVWHRMGDLG--YldaQGRLWFCGRKAHRVETAGGTLYTIPCE 459
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
184-502 |
1.26e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 73.69 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 184 QYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLitallspVLGhNFTFMTPAAFVRRPGrwi 263
Cdd:PRK08315 205 QYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGM-------VLG-NLACVTHGATMVYPG--- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 264 remarkpedapdsEVF-------TVAPnfafEHA-AVRGVPK----EGEPPL----DLSNVK-AILNGS---EPVspasM 323
Cdd:PRK08315 274 -------------EGFdplatlaAVEE----ERCtALYGVPTmfiaELDHPDfarfDLSSLRtGIMAGSpcpIEV----M 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 324 RKFYEAFspyGLRETAIkpSYGLAEatlfvsTTPmdqaptVIH---VDrDELNK--------QRFVEVpadspKavpqvs 392
Cdd:PRK08315 333 KRVIDKM---HMSEVTI--AYGMTE------TSP------VSTqtrTD-DPLEKrvttvgraLPHLEV-----K------ 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 393 agtigvdewavIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDifrnilksrisqshaegAPDDGMWVKTGDYG 472
Cdd:PRK08315 384 -----------IVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE-----------------AIDADGWMHTGDLA 435
|
330 340 350
....*....|....*....|....*....|....*
gi 497642598 473 T-----YYKghlyIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK08315 436 VmdeegYVN----IVGRIKDMIIRGGENIYPREIE 466
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-443 |
1.62e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.61 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 14 KFPDNTNLVKHVEKWARVRGDKLAYRFvdfsterdgEYRDIVWSDFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLI 92
Cdd:PRK12316 4546 GYPATRCVHQLVAERARMTPDAVAVVF---------DEEKLTYAELNRRaNRLAHALIARGVGPEVLVGIAMERSAEMMV 4616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 93 AFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDAAEGVrkfirarsakerPRVIAVDAVPNEVASTWEP 172
Cdd:PRK12316 4617 GLLAVLKAGGAYVPL-DPEYPRE--RLAYMMEDSGAALLLTQSHLLQRL------------PIPDGLASLALDRDEDWEG 4681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 173 -PEAD-------ENtIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITalLSPVLG 244
Cdd:PRK12316 4682 fPAHDpavrlhpDN-LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEG--LYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 245 HNFTFMTPAAFVRRPGRWIREMARKpedapdsEVFTVAPNFAFEHAAVRGVPKEGEPPldlsNVKAILNGSEPVSPASMR 324
Cdd:PRK12316 4759 NGASVVIRDDSLWDPERLYAEIHEH-------RVTVLVFPPVYLQQLAEHAERDGEPP----SLRVYCFGGEAVAQASYD 4827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 325 KFYEAFSPYGLRETaikpsYGLAEATLfvsttpmdqapTVIHVDrdelnkqrfveVPADSPKAVPQVSAGTIGVDEWAVI 404
Cdd:PRK12316 4828 LAWRALKPVYLFNG-----YGPTETTV-----------TVLLWK-----------ARDGDACGAAYMPIGTPLGNRSGYV 4880
|
410 420 430
....*....|....*....|....*....|....*....
gi 497642598 405 VDPEtASELPDGQIGEIWLHGNNLGTGYWGREQETNDIF 443
Cdd:PRK12316 4881 LDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERF 4918
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
29-495 |
2.38e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 72.66 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 29 ARVRGDKLAYRFvdfsterdgeyRDIVWS--DFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAV 105
Cdd:PRK08316 21 ARRYPDKTALVF-----------GDRSWTyaELDAAvNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 106 P---------------------LFdpAEPGHVGRLHAVLDDCSPSTI-----LTTTDAAEGVRKFIRARSAKErprviav 159
Cdd:PRK08316 90 PvnfmltgeelayildhsgaraFL--VDPALAPTAEAALALLPVDTLilslvLGGREAPGGWLDFADWAEAGS------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 160 DAVPNevastwepPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLitall 239
Cdd:PRK08316 161 VAEPD--------VELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQL----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 240 spvlgHNftFMTPAAFVrrpGRWIREMarkpeDAPDsevftvaPNFAFEHAAVRGVPKEGEPP---LDLSNVKAIlngsE 316
Cdd:PRK08316 228 -----DV--FLGPYLYV---GATNVIL-----DAPD-------PELILRTIEAERITSFFAPPtvwISLLRHPDF----D 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 317 PVSPASMRKFYeafspYG--------LRETAIK-PS------YGLAE-ATLFVSTTPMDQAptvihvdrdelnkqrfvEV 380
Cdd:PRK08316 282 TRDLSSLRKGY-----YGasimpvevLKELRERlPGlrfyncYGQTEiAPLATVLGPEEHL-----------------RR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 381 PAdspkavpqvSAGTIGVDEWAVIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegap 460
Cdd:PRK08316 340 PG---------SAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR---------------- 393
|
490 500 510
....*....|....*....|....*....|....*.
gi 497642598 461 ddGMWVKTGDYGTYY-KGHLYIAGRIKDLVIIDGRN 495
Cdd:PRK08316 394 --GGWFHSGDLGVMDeEGYITVVDRKKDMIKTGGEN 427
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
75-612 |
2.94e-13 |
|
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: 72.19 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTdaaegvrkfirarsakerp 154
Cdd:cd05918 47 GPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL-DPSHP--LQRLQEILQDTGAKVVLTSS------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 155 rviavdavPNEVAstweppeadentiaYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRglsWLPF----Fh 230
Cdd:cd05918 105 --------PSDAA--------------YVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESR---VLQFasytF- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 231 DMGLITALLspVLGHNFTFMTPAAFVRRPG--RWIREMArkpedapdsevftvaPNFAFEHAAV-RGVPkegepPLDLSN 307
Cdd:cd05918 159 DVSILEIFT--TLAAGGCLCIPSEEDRLNDlaGFINRLR---------------VTWAFLTPSVaRLLD-----PEDVPS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 308 VKAILNGSEPVSPasmrkfyEAFSPYGLRETAIKpSYGLAEATLFVSTTPMdqaptvihvdrdelnkqrfvevpadspka 387
Cdd:cd05918 217 LRTLVLGGEALTQ-------SDVDTWADRVRLIN-AYGPAECTIAATVSPV----------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 388 VPQVSAGTIGvdeWAV-----IVDPETASEL-PDGQIGEIWLHGNNLGTGYWGREQETNDIFRNILKSRisqsHAEGAPD 461
Cdd:cd05918 260 VPSTDPRNIG---RPLgatcwVVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWL----KQEGSGR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 462 DGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGrnhypQDLEYSAQEAskALRTGYVAAFSVPAnqlpkEVfdnphtglk 540
Cdd:cd05918 333 GRRLYRTGDLVRYNPdGSLEYVGRKDTQVKIRG-----QRVELGEIEH--HLRQSLPGAKEVVV-----EV--------- 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 541 YDPDDSSEQLVIVA--------ERAAGSHKLDYQPIADDIRAAIAVRHGVT-------VRDLLLVQSgTIPRTSSGKIGH 605
Cdd:cd05918 392 VKPKDGSSSPQLVAfvvldgssSGSGDGDSLFLEPSDEFRALVAELRSKLRqrlpsymVPSVFLPLS-HLPLTASGKIDR 470
|
....*..
gi 497642598 606 RACRAAY 612
Cdd:cd05918 471 RALRELA 477
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-528 |
3.18e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.11 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 173 PEADEntIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFhdmglitALLSPVLGhnftfMTP 252
Cdd:cd05910 82 PKADE--PAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALG-----LTS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 253 AafvrrpgrwIREM-ARKPEDAPDSEVFTVAPNFAFEH-----AAVRGVPKEGEP-PLDLSNVKAILNGSEPVSPASMRK 325
Cdd:cd05910 148 V---------IPDMdPTRPARADPQKLVGAIRQYGVSIvfgspALLERVARYCAQhGITLPSLRRVLSAGAPVPIALAAR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 326 FYEAFSPyglrETAIKPSYGLAEA---------TLFVSTTPMDQAPTVIHVDRdelnkqrfvevpadspkAVPQVSAGTI 396
Cdd:cd05910 219 LRKMLSD----EAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCVGR-----------------PIPGVRVRII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 397 GVDEwAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETndifrnilksRISQSHaegAPDDGMWVKTGDYGtYY- 475
Cdd:cd05910 278 EIDD-EPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVAT----------ALAKID---DNSEGFWHRMGDLG-YLd 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497642598 476 -KGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKALRTGYVaAFSVPANQLP 528
Cdd:cd05910 343 dEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV-GVGKPGCQLP 395
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-443 |
3.36e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 73.27 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 80 IAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTtdaaegvrkfirARSAKERPRVIAV 159
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPL-DPEYPRE--RLAYMIEDSGVKLLLTQ------------AHLLEQLPAPAGD 3212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 160 DAVPNEVASTWEPPE------ADENTIAYLQYTSGSTRTPTGVQITH--LNLPTNVLQVLNGLEGkeGDRGLSWLPFFHD 231
Cdd:PRK12467 3213 TALTLDRLDLNGYSEnnpstrVMGENLAYVIYTSGSTGKPKGVGVRHgaLANHLCWIAEAYELDA--NDRVLLFMSFSFD 3290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 232 mGLITALLSPVlghnftfMTPAAFVRRPGR-WIREMARKPEDAPDSEVFTVAPnfafehAAVRGVPKEGEPPlDLSNVKA 310
Cdd:PRK12467 3291 -GAQERFLWTL-------ICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPP------AYLQQFAEDAGGA-DCASLDI 3355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 311 ILNGSEPVSPASMRKFYEAFSPYGLRETaikpsYGLAEATLfvsttpmdqapTVIHVDrdelnkqrfveVPADspkAVPQ 390
Cdd:PRK12467 3356 YVFGGEAVPPAAFEQVKRKLKPRGLTNG-----YGPTEAVV-----------TVTLWK-----------CGGD---AVCE 3405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 391 VSAGTIG--VDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIF 443
Cdd:PRK12467 3406 APYAPIGrpVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERF 3460
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
174-502 |
6.81e-13 |
|
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: 71.24 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 174 EADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFH------DMGLITALLS------P 241
Cdd:cd17640 84 ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHsyersaEYFIFACGCSqaytsiR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 242 VLGHNFTFMTPAAFVRRPGRW------IREMARKpEDAPDSEVFtvapnfafeHAAVRGvpkegeppldlSNVKAILNGS 315
Cdd:cd17640 164 TLKDDLKRVKPHYIVSVPRLWeslysgIQKQVSK-SSPIKQFLF---------LFFLSG-----------GIFKFGISGG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 316 EPVsPASMRKFYEAFspyGLRetaIKPSYGLAEatlfvsTTPMdqaptvihvdrdelnkqrfveVPADSPKAVPQVSAGT 395
Cdd:cd17640 223 GAL-PPHVDTFFEAI---GIE---VLNGYGLTE------TSPV---------------------VSARRLKCNVRGSVGR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 396 IGVDEWAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIfrnilksrISQshaegapdDGmWVKTGDYGTYY 475
Cdd:cd17640 269 PLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV--------LDS--------DG-WFNTGDLGWLT 331
|
330 340
....*....|....*....|....*....
gi 497642598 476 K-GHLYIAGRIKD-LVIIDGRNHYPQDLE 502
Cdd:cd17640 332 CgGELVLTGRAKDtIVLSNGENVEPQPIE 360
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
37-523 |
8.38e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 71.33 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 37 AYRFVDFSTERDGEYRdivWSDFSARNRA--VGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEP 113
Cdd:PRK06155 31 AERYPDRPLLVFGGTR---WTYAEAARAAaaAAHALAAAgVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI-NTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 114 GhvGRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAkeRPRVIAVDAVPNEVA----STWEPPEADE----------NT 179
Cdd:PRK06155 107 G--PQLEHILRNSGARLLVVEAALLAALEAADPGDLP--LPAVWLLDAPASVSVpagwSTAPLPPLDApapaaavqpgDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 180 IAYLqYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGL---ITALLSP---VLGHNFTFMTPA 253
Cdd:PRK06155 183 AAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALnafFQALLAGatyVLEPRFSASGFW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 254 AFVRRPGR----WIREMA----RKPEDAPDSEvftvapnfafehaavrgvpkegeppldlSNVKAILNGSepVSPASMRK 325
Cdd:PRK06155 262 PAVRRHGAtvtyLLGAMVsillSQPARESDRA----------------------------HRVRVALGPG--VPAALHAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 326 FYEAFSpYGLREtaikpSYGLAEATLFVSTTPMDQAPTvihvdrdelnkqrfvevpadspkavpqvSAGTIGVDEWAVIV 405
Cdd:PRK06155 312 FRERFG-VDLLD-----GYGSTETNFVIAVTHGSQRPG----------------------------SMGRLAPGFEARVV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 406 DpETASELPDGQIGEIWLHGNN---LGTGYWGREQETNDIFRNilksrisqshaegapddgMWVKTGDYGTY-YKGHLYI 481
Cdd:PRK06155 358 D-EHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRN------------------LWFHTGDRVVRdADGWFRF 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 497642598 482 AGRIKDLVIIDGRNhypqdleYSAQEASKALRT----GYVAAFSVP 523
Cdd:PRK06155 419 VDRIKDAIRRRGEN-------ISSFEVEQVLLShpavAAAAVFPVP 457
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
75-493 |
8.95e-13 |
|
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: 70.82 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAEGV--RKFIRArsake 152
Cdd:cd17655 45 GPDTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYP--EERIQYILEDSGADILLTQSHLQPPIafIGLIDL----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 153 rprvIAVDAVPNEVASTWEPPEADENtIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDM 232
Cdd:cd17655 117 ----LDEDTIYHEESENLEPVSKSDD-LAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 233 GlITALLSPVLGHNFTFMTPAAfVRRPGRWIREMARKPEdapdSEVFTVAPNFAFEHAAVRGVPKegeppldlSNVKAIL 312
Cdd:cd17655 192 S-VTEIFASLLSGNTLYIVRKE-TVLDGQALTQYIRQNR----ITIIDLTPAHLKLLDAADDSEG--------LSLKHLI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 313 NGSEPVSPASMRKFYEAFSP-------YGLRETAIKPSYGLAEatlfvsttPMDQAPTVIHVDRDELNKQRFVevpadsp 385
Cdd:cd17655 258 VGGEALSTELAKKIIELFGTnptitnaYGPTETTVDASIYQYE--------PETDQQVSVPIGKPLGNTRIYI------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 386 kavpqvsagtigVDEWAVIVdpetaselPDGQIGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqshAEGAPDDGMW 465
Cdd:cd17655 323 ------------LDQYGRPQ--------PVGVAGELYIGGEGVARGYLNRPELTAEKFVD----------DPFVPGERMY 372
|
410 420
....*....|....*....|....*....
gi 497642598 466 vKTGDYGTYY-KGHLYIAGRIKDLVIIDG 493
Cdd:cd17655 373 -RTGDLARWLpDGNIEFLGRIDHQVKIRG 400
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
24-531 |
1.06e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.88 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 24 HVEKWARVRGDKLAyrFVDFSTERDGEYRDivwsdFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGR 102
Cdd:PRK13391 2 YPGIHAQTTPDKPA--VIMASTGEVVTYRE-----LDERSNRLAHLFRSLgLKRGDHVAIFMENNLRYLEVCWAAERSGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 103 IAVPL---FDPAEPGHVgrlhavLDDCSpSTILTTTDAAEGVRKFIRARSAKERPRVIA--------VDAVPNEVASTWE 171
Cdd:PRK13391 75 YYTCVnshLTPAEAAYI------VDDSG-ARALITSAAKLDVARALLKQCPGVRHRLVLdgdgelegFVGYAEAVAGLPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 172 PPEADENTIAYLQYTSGSTRTPTGV--QITHLNL--PTNVLQVLNGLEG-KEGDRGLSWLPFFHD-----MGLITAL--- 238
Cdd:PRK13391 148 TPIADESLGTDMLYSSGTTGRPKGIkrPLPEQPPdtPLPLTAFLQRLWGfRSDMVYLSPAPLYHSapqraVMLVIRLggt 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 239 ------------LSPVLGHNFTF--MTPAAFVRrpgrwireMARKPEDAPDSevftvapnfafehaavrgvpkegeppLD 304
Cdd:PRK13391 228 vivmehfdaeqyLALIEEYGVTHtqLVPTMFSR--------MLKLPEEVRDK--------------------------YD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 305 LSNVKAILNGSEPVSPASMRKFYEAFSPyglretAIKPSYGLAEATLFvstTPMDQAPTVIHvdrdelnkqrfvevpads 384
Cdd:PRK13391 274 LSSLEVAIHAAAPCPPQVKEQMIDWWGP------IIHEYYAATEGLGF---TACDSEEWLAH------------------ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 385 PKAVPQVSAGTIgvdewaVIVDPETAsELPDGQIGEIWLHGnnlgtgywGREQEtndIFRNILKSRISQShaegapDDGM 464
Cdd:PRK13391 327 PGTVGRAMFGDL------HILDDDGA-ELPPGEPGTIWFEG--------GRPFE---YLNDPAKTAEARH------PDGT 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642598 465 WVKTGDYGtyY---KGHLYIAGRIKDLVIIDGRNHYPqdleysaQEASKALRT----GYVAAFSVPANQLPKEV 531
Cdd:PRK13391 383 WSTVGDIG--YvdeDGYLYLTDRAAFMIISGGVNIYP-------QEAENLLIThpkvADAAVFGVPNEDLGEEV 447
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
77-502 |
1.56e-12 |
|
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: 69.67 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 77 GDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFdpaepghvgrlhavlddcspsTILTTTDaaegvrkfIRARSAKERPRV 156
Cdd:cd05972 25 GDRVAVLLPRVPELWAVILAVIKLGAVYVPLT---------------------TLLGPKD--------IEYRLEAAGAKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 157 IAVDAvpnevastweppeadeNTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDrgLSWLPffHDMGLIT 236
Cdd:cd05972 76 IVTDA----------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD--IHWNI--ADPGWAK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 237 ALLSPVLG------HNFTFMTPaAFVrrPGRWIREMARKPedapdSEVFTVAPnfafehAAVRGVPKEGEPPLDLSNVKA 310
Cdd:cd05972 136 GAWSSFFGpwllgaTVFVYEGP-RFD--AERILELLERYG-----VTSFCGPP------TAYRMLIKQDLSSYKFSHLRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 311 ILNGSEPVSPASMRKFYEAFSPYglretaIKPSYGLAEATLFVSTTPmdqaptvihvdrdelnkqrFVEV-PADSPKAVP 389
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAATGLP------IRDGYGQTETGLTVGNFP-------------------DMPVkPGSMGRPTP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 390 qvsagtiGVDewAVIVDPEtASELPDGQIGEIWLHGNNLG--TGYWGREQETNDIFRnilksrisqshaegapddGMWVK 467
Cdd:cd05972 257 -------GYD--VAIIDDD-GRELPPGEEGDIAIKLPPPGlfLGYVGDPEKTEASIR------------------GDYYL 308
|
410 420 430
....*....|....*....|....*....|....*...
gi 497642598 468 TGDYGtyYK---GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05972 309 TGDRA--YRdedGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
26-233 |
1.61e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 70.29 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 26 EKWARVRGDKLayrfvdFSTER--DGEYRDIVWSDFSARNRAVG-ARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGR 102
Cdd:PRK08180 46 VHWAQEAPDRV------FLAERgaDGGWRRLTYAEALERVRAIAqALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 103 IAVPLfDPAE---PGHVGRLHAVLDDCSPSTILtttdAAEGVRkFIRARSA--KERPRVIAVDAVPN--------EVAST 169
Cdd:PRK08180 120 PYAPV-SPAYslvSQDFGKLRHVLELLTPGLVF----ADDGAA-FARALAAvvPADVEVVAVRGAVPgraatpfaALLAT 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642598 170 WEPPEADE-------NTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGL--EGKEGDRGLSWLPFFHDMG 233
Cdd:PRK08180 194 PPTAAVDAahaavgpDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpfLAEEPPVLVDWLPWNHTFG 266
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
44-489 |
2.00e-12 |
|
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: 69.97 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 44 STERDGEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIavplfdpaepghvgrLHAV 122
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLgVKPGDRVATLAWNTHRHLELYYAVPGMGAV---------------LHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 123 LDDCSPSTILTTTDAAEG----------------------VRKFIRARSAKERP-----RVIAVDAVPNEVASTWEPPEA 175
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDrvvfvdrdflplleaiaprlptVEHVVVMTDDAAMPepagvGVLAYEELLAAESPEYDWPDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 176 DENTIAYLQYTSGSTRTPTGVQITHLNLptnVLQVL-----NGLEGKEGDRGLSWLPFFHdmglITALLSPVLghnfTFM 250
Cdd:cd12119 161 DENTAAAICYTSGTTGNPKGVVYSHRSL---VLHAMaalltDGLGLSESDVVLPVVPMFH----VNAWGLPYA----AAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 251 TPAAFVrRPGrwiremarkPEDAPDSEVFTVA---PNFAfehAAV----RGVPKEGE-PPLDLSNVKAILNGSEPVSPAS 322
Cdd:cd12119 230 VGAKLV-LPG---------PYLDPASLAELIEregVTFA---AGVptvwQGLLDHLEaNGRDLSSLRRVVIGGSAVPRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 323 MRKFYEAFSP----YGLRETaikpsyglaEATLFVSTTPMDQAPTVIHVDRDELNKQ-RFVevpadspkavpqvsagtIG 397
Cdd:cd12119 297 IEAFEERGVRvihaWGMTET---------SPLGTVARPPSEHSNLSEDEQLALRAKQgRPV-----------------PG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 398 VDewAVIVDPETaSELP-DGQ-IGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTYY 475
Cdd:cd12119 351 VE--LRIVDDDG-RELPwDGKaVGELQVRGPWVTKSYYKNDEESEALTE-----------------DG-WLRTGDVATID 409
|
490
....*....|....*
gi 497642598 476 -KGHLYIAGRIKDLV 489
Cdd:cd12119 410 eDGYLTITDRSKDVI 424
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
76-493 |
2.11e-12 |
|
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: 69.59 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDAAegvrkfirarsakerpr 155
Cdd:cd17652 36 PERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYPAE--RIAYMLADARPALLLTTPDNL----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 viavdavpnevastweppeadentiAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLi 235
Cdd:cd17652 96 -------------------------AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASV- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 236 tALLSPVLGHNFTFMTPAAFVRRPGRWIREMARkpedapDSEVFTVA--PnfafehAAVRGVPKEGEPPLDlsnvkAILN 313
Cdd:cd17652 150 -WELLMALLAGATLVLAPAEELLPGEPLADLLR------EHRITHVTlpP------AALAALPPDDLPDLR-----TLVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 314 GSEPVSP------ASMRKFYEAfspyglretaikpsYGLAEATLFVSTTPMDQAPTVIHVDRDELNKQRFVevpadspka 387
Cdd:cd17652 212 AGEACPAelvdrwAPGRRMINA--------------YGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYV--------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 388 vpqvsagtigVDEWAVIVdpetaselPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisQSHAEGAPDDGMWvK 467
Cdd:cd17652 269 ----------LDARLRPV--------PPGVPGELYIAGAGLARGYLNRPGLTAERF---------VADPFGAPGSRMY-R 320
|
410 420
....*....|....*....|....*..
gi 497642598 468 TGDYGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:cd17652 321 TGDLARWRAdGQLEFLGRADDQVKIRG 347
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
62-443 |
2.85e-12 |
|
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: 69.32 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 62 RNRAVGarlqqvtqPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTttdaaegv 141
Cdd:cd17649 30 RALGVG--------PEVRVGIALERSLEMVVALLAILKAGGAYVPL-DPEYP--AERLRYMLEDSGAGLLLT-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 142 rkfirarsakERPRviavdavpnevastweppeadenTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDR 221
Cdd:cd17649 91 ----------HHPR-----------------------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 222 GLSWLPFFHDmGLITALLSPVlghnftfMTPAAFVRRP-GRWI--REMARKPEDAPDSeVFTVAPNFAFEHAAVRGVPKE 298
Cdd:cd17649 138 ELQFASFNFD-GAHEQLLPPL-------ICGACVVLRPdELWAsaDELAEMVRELGVT-VLDLPPAYLQQLAEEADRTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 299 GEPPldlsNVKAILNGSEPVSPasmrKFYEAFSPYGLRetaIKPSYGLAEATLfvsttpmdqAPTVIHVDRDElnkqrfV 378
Cdd:cd17649 209 GRPP----SLRLYIFGGEALSP----ELLRRWLKAPVR---LFNAYGPTEATV---------TPLVWKCEAGA------A 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 379 EVPADSP--KAVPQVSagtigvdewAVIVDPETAsELPDGQIGEIWLHGNNLGTGYWGREQETNDIF 443
Cdd:cd17649 263 RAGASMPigRPLGGRS---------AYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAERF 319
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
23-196 |
4.37e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 68.77 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 23 KHVEKWarvRGDKLAYRFVDFSTERDGEYRDIvwSDFSarNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGR 102
Cdd:PRK04319 51 RHADGG---RKDKVALRYLDASRKEKYTYKEL--KELS--NKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 103 IAVPLFDPAEPGHVgrlHAVLDDCSPSTILTTTDAAEgvRK-----------FIRARSAKERPRVIAVDAVPNEVASTWE 171
Cdd:PRK04319 124 IVGPLFEAFMEEAV---RDRLEDSEAKVLITTPALLE--RKpaddlpslkhvLLVGEDVEEGPGTLDFNALMEQASDEFD 198
|
170 180
....*....|....*....|....*
gi 497642598 172 PPEADENTIAYLQYTSGSTRTPTGV 196
Cdd:PRK04319 199 IEWTDREDGAILHYTSGSTGKPKGV 223
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
68-502 |
6.87e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 68.07 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 68 ARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDDCSPSTILTTTDAAEGVRK 143
Cdd:PRK03640 42 GKLAALgVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLntrLSREE------LLWQLDDAEVKCLITDDDFEAKLIP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 144 FIRARSAKerprVIAVDAVPNEVASTWeppeaDENTIAYLQYTSGSTRTPTGVQITHLN-LPTNVLQVLN-GLegKEGDR 221
Cdd:PRK03640 116 GISVKFAE----LMNGPKEEAEIQEEF-----DLDEVATIMYTSGTTGKPKGVIQTYGNhWWSAVGSALNlGL--TEDDC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 222 GLSWLPFFHDMGLITALLSPVLGHNFTFMTP--AAFVRRpgrWIREmarkpedapdSEVFTVAPNFAFEHAAVRGVPKEG 299
Cdd:PRK03640 185 WLAAVPIFHISGLSILMRSVIYGMRVVLVEKfdAEKINK---LLQT----------GGVTIISVVSTMLQRLLERLGEGT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 300 EPpldlSNVKAILNGSEPVSPASM----RKFYEAFSPYGLRETA-----IKPSY-----GLAEATLFvsttpmdqaPTVI 365
Cdd:PRK03640 252 YP----SSFRCMLLGGGPAPKPLLeqckEKGIPVYQSYGMTETAsqivtLSPEDaltklGSAGKPLF---------PCEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 366 HVDRDElnkqrfvevpadspkavpqvsagtigvdewavivdpetaSELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRn 445
Cdd:PRK03640 319 KIEKDG---------------------------------------VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ- 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 497642598 446 ilksrisqshaegapdDGmWVKTGDYGtYY--KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK03640 359 ----------------DG-WFKTGDIG-YLdeEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
51-364 |
1.16e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.07 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 51 YRDIVwsdfsARNRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHV-------------- 116
Cdd:PRK06814 661 YRKLL-----TGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANIlsackaaqvktvlt 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 117 -------GRLHAVLDDCSPS-TILTTTDAAEGVRKF--IRARSAKERPRViavdavpnevastwEPPEADENTIAYLQYT 186
Cdd:PRK06814 736 srafiekARLGPLIEALEFGiRIIYLEDVRAQIGLAdkIKGLLAGRFPLV--------------YFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 187 SGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPAAfvrRPGRWIREM 266
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSP---LHYRIIPEL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 267 ARkpeDAPDSEVF---TVAPNFA-FEHaavrgvpkegepPLDLSNVKAILNGSEPVSpASMRKFYeaFSPYGLRetaIKP 342
Cdd:PRK06814 879 IY---DTNATILFgtdTFLNGYArYAH------------PYDFRSLRYVFAGAEKVK-EETRQTW--MEKFGIR---ILE 937
|
330 340
....*....|....*....|....
gi 497642598 343 SYGLAEATLFVS-TTPM-DQAPTV 364
Cdd:PRK06814 938 GYGVTETAPVIAlNTPMhNKAGTV 961
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
46-502 |
1.22e-11 |
|
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: 67.45 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 46 ERD-GEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVG------ 117
Cdd:cd17641 3 EKDfGIWQEFTWADYADRVRAFALGLLALgVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAyllnyt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 118 --RLHAVLDDCSPSTILTTTDAAEGVRKFI----RARSAKERPRVIAV-DAVPNEVASTWEPPEADENTI--------AY 182
Cdd:cd17641 83 gaRVVIAEDEEQVDKLLEIADRIPSVRYVIycdpRGMRKYDDPRLISFeDVVALGRALDRRDPGLYEREVaagkgedvAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 183 LQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVlghnftfmtpaafvrrpgrW 262
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQAL-------------------V 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 263 IREMARKPEDAPD--SEVFTVAPNFAFehAAVRgvPKEGEppldLSNVKAILNGSEPVSPA----SMRKFYEAfSPYGLR 336
Cdd:cd17641 224 CGFIVNFPEEPETmmEDLREIGPTFVL--LPPR--VWEGI----AADVRARMMDATPFKRFmfelGMKLGLRA-LDRGKR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 337 ----ETAIKPSYGLAEATLFvstTPMdqaptvihvdRDELNkQRFVEVPADSPKAV-PQVSA--GTIGVD--------EW 401
Cdd:cd17641 295 grpvSLWLRLASWLADALLF---RPL----------RDRLG-FSRLRSAATGGAALgPDTFRffHAIGVPlkqlygqtEL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 402 AVI--------VDPETAS-ELPDGQI-----GEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVK 467
Cdd:cd17641 361 AGAytvhrdgdVDPDTVGvPFPGTEVridevGEILVRSPGVFVGYYKNPEAT----------------AEDFDEDG-WLH 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 497642598 468 TGDYGtYYK--GHLYIAGRIKDL-VIIDGRNHYPQDLE 502
Cdd:cd17641 424 TGDAG-YFKenGHLVVIDRAKDVgTTSDGTRFSPQFIE 460
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
57-619 |
2.06e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 66.65 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 57 SDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEPGHVgrlhavLDDCSPSTIL 132
Cdd:PRK12406 15 DELAQRAARAAGGLAALgVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVnwhFKPEEIAYI------LEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 133 TTTDAAEGVRKFIRARSA----------KERPRVIAVDAVPNEVASTWEPPEADENTIAYLQ--------YTSGSTRTPT 194
Cdd:PRK12406 89 AHADLLHGLASALPAGVTvlsvptppeiAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGPPvpqpqsmiYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 195 GVQIThlnlPTNVLQVLNGlegkEGDRGLSwlpffhdMGL---ITALLSPVLGHNftfmTPAAFVRRPGRWIREMARKPE 271
Cdd:PRK12406 169 GVRRA----APTPEQAAAA----EQMRALI-------YGLkpgIRALLTGPLYHS----APNAYGLRAGRLGGVLVLQPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 272 DAPD-----------SEVFTVAPNFafehaaVR--GVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglret 338
Cdd:PRK12406 230 FDPEellqlierhriTHMHMVPTMF------IRllKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 339 AIKPSYGLAEATLFVSTTPmdqaptvihvdRDELNKqrfvevpadsPKAVPQVSAGTigvdEWAVIvdPETASELPDGQI 418
Cdd:PRK12406 298 VIYEYYGSTESGAVTFATS-----------EDALSH----------PGTVGKAAPGA----ELRFV--DEDGRPLPQGEI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 419 GEIWLH--GNNLGTgYWGREQETNDIfrnilksrisqshaegapDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRN 495
Cdd:PRK12406 351 GEIYSRiaGNPDFT-YHNKPEKRAEI------------------DRGGFITSGDVGYLDAdGYLFLCDRKRDMVISGGVN 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 496 HYPQDLEysaQEASKALRTGYVAAFSVPanqlpkevfdnphtglkyDPdDSSEQLVIVAERAAGShKLDyqpiADDIRAA 575
Cdd:PRK12406 412 IYPAEIE---AVLHAVPGVHDCAVFGIP------------------DA-EFGEALMAVVEPQPGA-TLD----EADIRAQ 464
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 497642598 576 IAVR-HGVTVRDLLLVQSGtIPRTSSGKIGHRACRAAYLDGSLRS 619
Cdd:PRK12406 465 LKARlAGYKVPKHIEIMAE-LPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
178-489 |
2.53e-11 |
|
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: 66.47 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 178 NTIAYLQYTSGSTRTPTGVQITHLNLP---TNVLQVLNGLEGKEgDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTP-- 252
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVagiAGLGDRVPELLGPD-DRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPrt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 253 --AAFVRRPGRWIRE-----MARKPE------DAPDSEVFTVAPNF--AFEHA------AVRGVPkeGEPPLDL------ 305
Cdd:cd17639 167 ltDKSKRGCKGDLTEfkptlMVGVPAiwdtirKGVLAKLNPMGGLKrtLFWTAyqsklkALKEGP--GTPLLDElvfkkv 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 306 -----SNVKAILNGSEPVSPASMRKFYEAFSP----YGLRETAikpsyglAEATLfvsTTPMDQAPTVIH---------- 366
Cdd:cd17639 245 raalgGRLRYMLSGGAPLSADTQEFLNIVLCPviqgYGLTETC-------AGGTV---QDPGDLETGRVGpplpcceikl 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 367 VDRDELNKQrfvevpADSPKavPQvsagtigvdewavivdpetaselpdgqiGEIWLHGNNLGTGYWGREQETNDIFrni 446
Cdd:cd17639 315 VDWEEGGYS------TDKPP--PR----------------------------GEILIRGPNVFKGYYKNPEKTKEAF--- 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 497642598 447 lksrisqshaegapDDGMWVKTGDYGTYYK-GHLYIAGRIKDLV 489
Cdd:cd17639 356 --------------DGDGWFHTGDIGEFHPdGTLKIIDRKKDLV 385
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
173-495 |
5.17e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 65.46 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 173 PEADEntIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPV-LGHNFTFM- 250
Cdd:PRK13295 194 PGPDD--VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVmLGATAVLQd 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 251 --TPAAFVRRpgrwIREmarkpedapDSEVFTVAPNfAFEHAAVRGVpkeGEPPLDLSNVKAILNGSEPVSPASMRKFYE 328
Cdd:PRK13295 272 iwDPARAAEL----IRT---------EGVTFTMAST-PFLTDLTRAV---KESGRPVSSLRTFLCAGAPIPGALVERARA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 329 AFSpyglreTAIKPSYGLAEatlfvsttpmDQAPTVIHVDRDelnkqrfvevpadspkavPQVSAGTIGVDEWAV---IV 405
Cdd:PRK13295 335 ALG------AKIVSAWGMTE----------NGAVTLTKLDDP------------------DERASTTDGCPLPGVevrVV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 406 DPETAsELPDGQIGEIWLHGNNLGTGYWGREQETNDifrnilksrisqsHAEGapddgmWVKTGDYGTY-YKGHLYIAGR 484
Cdd:PRK13295 381 DADGA-PLPAGQIGRLQVRGCSNFGGYLKRPQLNGT-------------DADG------WFDTGDLARIdADGYIRISGR 440
|
330
....*....|.
gi 497642598 485 IKDLVIIDGRN 495
Cdd:PRK13295 441 SKDVIIRGGEN 451
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
76-493 |
6.50e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.95 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 76 PGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTttdaaegvrkfiRARSAKERPR 155
Cdd:PRK12467 561 PDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL-DPEYP--QDRLAYMLDDSGVRLLLT------------QSHLLAQLPV 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 VIAVDAVP-NEVASTWE-------PPEADENTIAYLQYTSGSTRTPTGVQITHLNLpTNVLQVLNGLEGKEGD-RGLSWL 226
Cdd:PRK12467 626 PAGLRSLClDEPADLLCgysghnpEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADdSMLMVS 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 227 PFFHDMG---LITALLSPVLGHnftfMTPAAFVRRPGRWIREMARKPEDAPDsevftvapnfaFEHAAVRGVPKEGEPPL 303
Cdd:PRK12467 705 TFAFDLGvteLFGALASGATLH----LLPPDCARDAEAFAALMADQGVTVLK-----------IVPSHLQALLQASRVAL 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 304 DLSnVKAILNGSEPVSPASMRKFYEaFSPyglrETAIKPSYGLAEATLFVSTTPMDQAPTVIhvdrdelnkqrfvevpAD 383
Cdd:PRK12467 770 PRP-QRALVCGGEALQVDLLARVRA-LGP----GARLINHYGPTETTVGVSTYELSDEERDF----------------GN 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 384 SPKAVPQVSAGTigvdewaVIVDPETASeLPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqSHAEGAPDDG 463
Cdd:PRK12467 828 VPIGQPLANLGL-------YILDHYLNP-VPVGVVGELYIGGAGLARGYHRRPALTAERF----------VPDPFGADGG 889
|
410 420 430
....*....|....*....|....*....|.
gi 497642598 464 MWVKTGDYGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:PRK12467 890 RLYRTGDLARYRAdGVIEYLGRMDHQVKIRG 920
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
180-502 |
1.31e-10 |
|
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: 63.29 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 180 IAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLgHNFTFMTPAAFvrrp 259
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLL-TGATVVPVAVF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 260 grwireMARKPEDAPDSEVFTVAPNFAFEHAAVRGVPkeGEPPLDLSNVKAILNGSEPVSPASMRKFYEAfspygLRETA 339
Cdd:cd17638 77 ------DVDAILEAIERERITVLPGPPTLFQSLLDHP--GRKKFDLSSLRAAVTGAATVPVELVRRMRSE-----LGFET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 IKPSYGLAEATLFVSTTPMDQAPTVihvdrdelnkqrfvevPADSPKAVPQVSAGtigvdewavIVDPetaselpdgqiG 419
Cdd:cd17638 144 VLTAYGLTEAGVATMCRPGDDAETV----------------ATTCGRACPGFEVR---------IADD-----------G 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 420 EIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYP 498
Cdd:cd17638 188 EVLVRGYNVMQGYLDDPEAT----------------AEAIDADG-WLHTGDVGELdERGYLRITDRLKDMYIVGGFNVYP 250
|
....
gi 497642598 499 QDLE 502
Cdd:cd17638 251 AEVE 254
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-493 |
3.09e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPST 130
Cdd:PRK12467 1598 QELTYGELNRRaNRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL-DPEYPRE--RLAYMIEDSGIEL 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 131 ILTTTDAAEGVrkfirarSAKERPRVIAVDAvPNEVASTWEP--PE---ADENtIAYLQYTSGSTRTPTGVQITHLNLPT 205
Cdd:PRK12467 1675 LLTQSHLQARL-------PLPDGLRSLVLDQ-EDDWLEGYSDsnPAvnlAPQN-LAYVIYTSGSTGRPKGAGNRHGALVN 1745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 206 NVLQVLNGLEGKEGDRGLSWLPFFHDM---GLITALLSpvlGHNFTFMTPAAFvRRPGRWIREMARkpedapdsEVFTVA 282
Cdd:PRK12467 1746 RLCATQEAYQLSAADVVLQFTSFAFDVsvwELFWPLIN---GARLVIAPPGAH-RDPEQLIQLIER--------QQVTTL 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 283 pNF---AFEhAAVRGVPKEGEPPldlsNVKAILNGSEPVSPASMRKFYEAFSPYGLRETaikpsYGLAEATLFVSTTPMD 359
Cdd:PRK12467 1814 -HFvpsMLQ-QLLQMDEQVEHPL----SLRRVVCGGEALEVEALRPWLERLPDTGLFNL-----YGPTETAVDVTHWTCR 1882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 360 qaptviHVDrdelnkqrfVEVPADSPKAVPQVSAGTIGVDewavivdpETASELPDGQIGEIWLHGNNLGTGYWGREQET 439
Cdd:PRK12467 1883 ------RKD---------LEGRDSVPIGQPIANLSTYILD--------ASLNPVPIGVAGELYLGGVGLARGYLNRPALT 1939
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 440 NDIFrnilksrISQSHAEGapdDGMWVKTGDYGTYY-KGHLYIAGRIKDLVIIDG 493
Cdd:PRK12467 1940 AERF-------VADPFGTV---GSRLYRTGDLARYRaDGVIEYLGRIDHQVKIRG 1984
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
56-495 |
4.06e-10 |
|
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: 62.32 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 56 WSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDDCSPSTI 131
Cdd:cd12118 32 WRQTYDRCRRLASALAALgISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALntrLDAEE------IAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 132 LTTTD------AAEGVRKFirarsakerprviavdavpnevasTWEPPEADENTIAyLQYTSGSTRTPTGVQITHLNLPT 205
Cdd:cd12118 106 FVDREfeyedlLAEGDPDF------------------------EWIPPADEWDPIA-LNYTSGTTGRPKGVVYHHRGAYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 206 NVLQvlNGLEGKEGDRG--LSWLPFFHDMGlitallspvlghnFTFM-TPAAF---------VRRPG--RWIREmarkpe 271
Cdd:cd12118 161 NALA--NILEWEMKQHPvyLWTLPMFHCNG-------------WCFPwTVAAVggtnvclrkVDAKAiyDLIEK------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 272 dapdSEV--FTVAPNFafeHAAVRGVPKEGEPPLDlSNVKAILNGSEPvsPASMrkfYEAFSPYGLRETAikpSYGLAEA 349
Cdd:cd12118 220 ----HKVthFCGAPTV---LNMLANAPPSDARPLP-HRVHVMTAGAPP--PAAV---LAKMEELGFDVTH---VYGLTET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 350 TlfvsttpmdqAPTVIHVDRDELNkqrfvEVPADSP---KAVPQVsaGTIGVDEWAVIvDPETASELP-DGQ-IGEIWLH 424
Cdd:cd12118 284 Y----------GPATVCAWKPEWD-----ELPTEERarlKARQGV--RYVGLEEVDVL-DPETMKPVPrDGKtIGEIVFR 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642598 425 GNNLGTGYWGREQETNDIFRnilksrisqshaegapddGMWVKTGDYGTYY-KGHLYIAGRIKDLVIIDGRN 495
Cdd:cd12118 346 GNIVMKGYLKNPEATAEAFR------------------GGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGEN 399
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
75-502 |
6.26e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.12 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVlCPQNLD-YLIAFFGALYAGRIAVPL-----FDPAEPG--HVGRLHAVLDD-CSPSTILTTTDAAEGVRKFI 145
Cdd:PLN02860 55 RNGDVVAI-AALNSDlYLEWLLAVACAGGIVAPLnyrwsFEEAKSAmlLVRPVMLVTDEtCSSWYEELQNDRLPSLMWQV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 146 RARSAKERPRVIAVDAVPNEVASTWE--PPEAD----ENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEG 219
Cdd:PLN02860 134 FLESPSSSVFIFLNSFLTTEMLKQRAlgTTELDyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 220 DRGLSWLPFFHDMGLITALLSPVLG--HNF--TFMTPAAFVRRPGRWIREMARKPEDAPDsevfTVAPNFAFEHAAVRgv 295
Cdd:PLN02860 214 DVYLHTAPLCHIGGLSSALAMLMVGacHVLlpKFDAKAALQAIKQHNVTSMITVPAMMAD----LISLTRKSMTWKVF-- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 296 pkegeppldlSNVKAILNGSEPVS----PASMRKFYEA--FSPYGLRETAIKPSYglaeATLFVsttPMDQAPTVIHVDR 369
Cdd:PLN02860 288 ----------PSVRKILNGGGSLSsrllPDAKKLFPNAklFSAYGMTEACSSLTF----MTLHD---PTLESPKQTLQTV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 370 DELNKQrfvevPADSP------KAVPQVSAGtIGVDEwavivdpetaselpDGQIGEIWLHGNNLGTGYWGREQETndif 443
Cdd:PLN02860 351 NQTKSS-----SVHQPqgvcvgKPAPHVELK-IGLDE--------------SSRVGRILTRGPHVMLGYWGQNSET---- 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 444 rnilksrisqshAEGAPDDGmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PLN02860 407 ------------ASVLSNDG-WLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVE 453
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
48-488 |
6.64e-10 |
|
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: 61.72 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 48 DGEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRL--HAVLD 124
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALgLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVleHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 125 DCSPSTILTTTDAAEGVrkfirarsAKERPRVIAVDAVPNEVASTWE------PPEADENT-----IAYLQYTSGSTRTP 193
Cdd:cd05932 81 ALFVGKLDDWKAMAPGV--------PEGLISISLPPPSAANCQYQWDdliaqhPPLEERPTrfpeqLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 194 TGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHdmglITALLSPVLGHNFTFMTpAAFVRRPGRWIREMAR-KPed 272
Cdd:cd05932 153 KGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAH----VTERVFVEGGSLYGGVL-VAFAESLDTFVEDVQRaRP-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 273 apdsEVFTVAPNF--AFEHAAVRGVPKEG-----EPP-------------LDLSNVKAILNGSEPVSPASMrkfyEAFSP 332
Cdd:cd05932 226 ----TLFFSVPRLwtKFQQGVQDKIPQQKlnlllKIPvvnslvkrkvlkgLGLDQCRLAGCGSAPVPPALL----EWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 333 YGLRetaIKPSYGLAEaTLFVSTtpmdqaptvihvdrdelnkqrfVEVPADSpkavpqvSAGTIGvdewavivDPETASE 412
Cdd:cd05932 298 LGLN---ILEAYGMTE-NFAYSH----------------------LNYPGRD-------KIGTVG--------NAGPGVE 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642598 413 LPDGQIGEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVKTGDYGTY-YKGHLYIAGRIKDL 488
Cdd:cd05932 337 VRISEDGEILVRSPALMMGYYKDPEAT----------------AEAFTADG-FLRTGDKGELdADGNLTITGRVKDI 396
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
61-200 |
8.34e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 61.98 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 61 ARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDaae 139
Cdd:PRK10252 491 EQVVALANLLRERgVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DTGYP--DDRLKMMLEDARPSLLITTAD--- 564
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642598 140 gvrkfirarsakERPRVIAV-DAVPNEVASTWEPPEADENTI------AYLQYTSGSTRTPTGVQITH 200
Cdd:PRK10252 565 ------------QLPRFADVpDLTSLCYNAPLAPQGAAPLQLsqphhtAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
63-508 |
9.95e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.28 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 63 NRAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTD----AA 138
Cdd:PRK12316 3093 NRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--RLAYMLEDSGAQLLLSQSHlrlpLA 3169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 139 EGVRkfirarsakerprVIAVDAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKE 218
Cdd:PRK12316 3170 QGVQ-------------VLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV 3236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 219 GDRGLSWLPFFHDMGLITAllspvlghnFTFMTPAAFVRRPGRWIREMARKPEDAPDSEVFTVAPNFAFEHAAVRgvpkE 298
Cdd:PRK12316 3237 GDRVLQFTTFSFDVFVEEL---------FWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----E 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 299 GEPPLDLSNVKAILNGSEPVSPASMRKFY---EAFSPYGLRETAIKPSyglaeatlfvSTTPMDQAPTVIHVDRDELNKQ 375
Cdd:PRK12316 3304 EEDAHRCTSLKRIVCGGEALPADLQQQVFaglPLYNLYGPTEATITVT----------HWQCVEEGKDAVPIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 376 RFVEVPADSPKavpqvsagtigvdewavivdpetaselPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrISQSH 455
Cdd:PRK12316 3374 CYILDGSLEPV---------------------------PVGALGELYLGGEGLARGYHNRPGLTAERF-------VPDPF 3419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 497642598 456 AEGapddGMWVKTGDYGTYY-KGHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEA 508
Cdd:PRK12316 3420 VPG----ERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH 3469
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
53-502 |
1.93e-09 |
|
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: 60.22 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 53 DIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDDCSpsti 131
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARgLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTA---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 132 LTTTDAAEGVRKFIRARSakerpRVIAVDAVP----NEVAS-TWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTN 206
Cdd:cd05923 104 AVIAVDAQVMDAIFQSGV-----RVLALSDLVglgePESAGpLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 207 VLQVLN--GLEGKEGDRGLSWLPFFHDMGLItALLSPVLGHNFTFMTPAAFvrRPG---RWIREmarkpEDApdSEVFTV 281
Cdd:cd05923 179 VLFMSTqaGLRHGRHNVVLGLMPLYHVIGFF-AVLVAALALDGTYVVVEEF--DPAdalKLIEQ-----ERV--TSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 282 APNF-AFEHAAVRGvpkegepPLDLSNV-KAILNGSepVSPASMRKFYEAFSPygLRETAIkpsYGLAEATLFVsttpMD 359
Cdd:cd05923 249 PTHLdALAAAAEFA-------GLKLSSLrHVTFAGA--TMPDAVLERVNQHLP--GEKVNI---YGTTEAMNSL----YM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 360 QAPTVIHVDRDELNKQ-RFVEVPADSPKAVPQVSAGTIGVDewavivdpetaselpdgqigeiwLHGNNLGTGYWGREQE 438
Cdd:cd05923 311 RDARTGTEMRPGFFSEvRIVRIGGSPDEALANGEEGELIVA-----------------------AAADAAFTGYLNQPEA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 439 TndifrnilksriSQSHAEGapddgmWVKTGDYGTYY-KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd05923 368 T------------AKKLQDG------WYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIE 414
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-502 |
2.56e-09 |
|
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: 59.42 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 180 IAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVL-GHNFTFMTPAAFvRR 258
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAGPAGY-RN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 259 PGRW--IREMARKPEDAPDSEVFTVapnfafeHAAVRGVPKEGepplDLSNVKAILNGSEPVsPASMRKFYEAFSPYGLR 336
Cdd:cd05944 83 PGLFdnFWKLVERYRITSLSTVPTV-------YAALLQVPVNA----DISSLRFAMSGAAPL-PVELRARFEDATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 337 EtaikpSYGLAEATLFVSTTPMDQAptvihvdrdelnkQRFVEVPADSPKAVPQVsagtigvdewaVIVDPETASELPDG 416
Cdd:cd05944 151 E-----GYGLTEATCLVAVNPPDGP-------------KRPGSVGLRLPYARVRI-----------KVLDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 417 --QIGEIWLHGNNLGTGYwgreqetndifrnilksrISQSHAEGAPDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDG 493
Cdd:cd05944 202 pdEVGEICVAGPGVFGGY------------------LYTEGNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGG 263
|
....*....
gi 497642598 494 RNHYPQDLE 502
Cdd:cd05944 264 HNIDPALIE 272
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
52-241 |
2.64e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 60.00 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQVtqpgDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfdPAEPGHVGRLHaVLDDCSPSTI 131
Cdd:PRK07787 24 RVLSRSDLAGAATAVAERVAGA----RRVAVLATPTLATVLAVVGALIAGVPVVPV--PPDSGVAERRH-ILADSGAQAW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 132 LTTTDAAEGvrkfirarsakERPRViavdAVPNEVASTWEPPEADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVL 211
Cdd:PRK07787 97 LGPAPDDPA-----------GLPHV----PVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
|
170 180 190
....*....|....*....|....*....|
gi 497642598 212 NGLEGKEGDRGLSWLPFFHDMGLITALLSP 241
Cdd:PRK07787 162 EAWQWTADDVLVHGLPLFHVHGLVLGVLGP 191
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
185-502 |
2.75e-09 |
|
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: 59.21 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 185 YTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLspvlghnfTFMTPAAFVRRPgRWIR 264
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALA--------TFHAGGANVVME-KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 265 EMARKPEDAPDSEVFtvapnFAFEHAAVRGVPKEGEPPLDLSNVKAILnGSEpvSPASMRKFyEAFSP---YGLretaik 341
Cdd:cd17637 78 AEALELIEEEKVTLM-----GSFPPILSNLLDAAEKSGVDLSSLRHVL-GLD--APETIQRF-EETTGatfWSL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 342 psYGLAEATLFVSTTPMDQAPTvihvdrdelnkqrfvevpadspkavpqvSAGTIGVDEWAVIVDpETASELPDGQIGEI 421
Cdd:cd17637 143 --YGQTETSGLVTLSPYRERPG----------------------------SAGRPGPLVRVRIVD-DNDRPVPAGETGEI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 422 WLHGNNLGTGYWGREQETNDIFRNilksrisqshaeGapddgmWVKTGDYGTYYK-GHLYIAGRI--KDLVIIDGRNHYP 498
Cdd:cd17637 192 VVRGPLVFQGYWNLPELTAYTFRN------------G------WHHTGDLGRFDEdGYLWYAGRKpeKELIKPGGENVYP 253
|
....
gi 497642598 499 QDLE 502
Cdd:cd17637 254 AEVE 257
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
62-493 |
4.47e-09 |
|
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: 58.87 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 62 RNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAaeg 140
Cdd:cd12115 33 RANRLAARLRaAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL-DPAYP--PERLRFILEDAQARLVLTDPDD--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 141 vrkfirarsakerprviavdavpnevastweppeadentIAYLQYTSGSTRTPTGVQITHLNlPTNVLQVLNGLEGKEGD 220
Cdd:cd12115 107 ---------------------------------------LAYVIYTSGSTGRPKGVAIEHRN-AAAFLQWAAAAFSAEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 221 RG-LSWLPFFHDMGLITALLspvlghnfTFMTPAAFVrrpgrwIREMARKPEDAPDSEVFTV---APNFAFEHAAVRGVP 296
Cdd:cd12115 147 AGvLASTSICFDLSVFELFG--------PLATGGKVV------LADNVLALPDLPAAAEVTLintVPSAAAELLRHDALP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 297 KegeppldlsNVKAILNGSEPVSPASMRKFYEAfspygLRETAIKPSYGLAEATLFvSTtpmdqaptvihvdrdelnkqr 376
Cdd:cd12115 213 A---------SVRVVNLAGEPLPRDLVQRLYAR-----LQVERVVNLYGPSEDTTY-ST--------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 377 FVEVPADSPKAVpqvsagTIGV---DEWAVIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksriSQ 453
Cdd:cd12115 257 VAPVPPGASGEV------SIGRplaNTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFL-------PD 322
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 497642598 454 SHAEGAPddgMWvKTGDYGTYY-KGHLYIAGRIKDLVIIDG 493
Cdd:cd12115 323 PFGPGAR---LY-RTGDLVRWRpDGLLEFLGRADNQVKVRG 359
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
49-492 |
1.48e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 57.80 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARL-QQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRL--HAVLDD 125
Cdd:PLN02736 74 GEYKWMTYGEAGTARTAIGSGLvQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIvnHAEVAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 126 --CSP---STILTTTDAAEGVRKFIRARSAKER-P--------RVIAVDAVPNEVASTWEPPEADENT-IAYLQYTSGST 190
Cdd:PLN02736 154 ifCVPqtlNTLLSCLSEIPSVRLIVVVGGADEPlPslpsgtgvEIVTYSKLLAQGRSSPQPFRPPKPEdVATICYTSGTT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 191 RTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFH---DMGLITALLSPVL-----GHNFTFM------TPAAFV 256
Cdd:PLN02736 234 GTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyeRVNQIVMLHYGVAvgfyqGDNLKLMddlaalRPTIFC 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 257 RRPGRWIREMAR-----KPEDAPDSEVFTVApnfafeHAAVRGVPKEGEPP------LDLSNVKA--------ILNGSEP 317
Cdd:PLN02736 314 SVPRLYNRIYDGitnavKESGGLKERLFNAA------YNAKKQALENGKNPspmwdrLVFNKIKAklggrvrfMSSGASP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 318 VSPASMRKFYEAFSPYglretaIKPSYGLAEATLFVSTtpMDQAPTVI-HVdrdelnkqrfvevpaDSPKAVPQVSagti 396
Cdd:PLN02736 388 LSPDVMEFLRICFGGR------VLEGYGMTETSCVISG--MDEGDNLSgHV---------------GSPNPACEVK---- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 397 gvdewavIVD-PE---TASELPDGQiGEIWLHGNNLGTGYWGREQETNDIFrnilksrisqshaegapDDGMWVKTGDYG 472
Cdd:PLN02736 441 -------LVDvPEmnyTSEDQPYPR-GEICVRGPIIFKGYYKDEVQTREVI-----------------DEDGWLHTGDIG 495
|
490 500
....*....|....*....|
gi 497642598 473 TYYKGhlyiaGRIKdlvIID 492
Cdd:PLN02736 496 LWLPG-----GRLK---IID 507
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
20-243 |
1.62e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 57.75 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 20 NLVKHVEKWARVRGDK--LAYRfvdfsTERDGEYRDIVWSDFSARNRAVG-ARLQQVTQPGDRIAVLCPQNLDYLIAFFG 96
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRpwLAQR-----EPGHGQWRKVTYGEAKRAVDALAqALLDLGLDPGRPVMILSGNSIEHALMTLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 97 ALYAGRIAVPLfDPAE---PGHVGRLHAVLDDCSPSTILtttdAAEGVRkFIRARSA--KERPRVIAVDAVPN------- 164
Cdd:PRK12582 125 AMQAGVPAAPV-SPAYslmSHDHAKLKHLFDLVKPRVVF----AQSGAP-FARALAAldLLDVTVVHVTGPGEgiasiaf 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 165 -EVASTwePPEAD---------ENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLnGLEGKEGDRG----LSWLPFFH 230
Cdd:PRK12582 199 aDLAAT--PPTAAvaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQE-QLRPREPDPPppvsLDWMPWNH 275
|
250
....*....|...
gi 497642598 231 DMGLiTALLSPVL 243
Cdd:PRK12582 276 TMGG-NANFNGLL 287
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
25-233 |
2.25e-08 |
|
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: 57.06 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 25 VEKWARVRGDKLayrfvdFSTERDGE--YRDIVWSDFSARNRAVG-ARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAG 101
Cdd:cd05921 1 LAHWARQAPDRT------WLAEREGNggWRRVTYAEALRQVRAIAqGLLDLGLSAERPLLILSGNSIEHALMALAAMYAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 102 RIAVP-----------------LFDPAEPGHV---------GRLHAVLDDCSPstILTTTDAAEGVRKFIRARSAkERPR 155
Cdd:cd05921 75 VPAAPvspayslmsqdlaklkhLFELLKPGLVfaqdaapfaRALAAIFPLGTP--LVVSRNAVAGRGAISFAELA-ATPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 156 VIAVDAVPNEVAStweppeadeNTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLN--GLEGKEGDRGLSWLPFFHDMG 233
Cdd:cd05921 152 TAAVDAAFAAVGP---------DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQtyPFFGEEPPVLVDWLPWNHTFG 222
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
7-617 |
5.63e-08 |
|
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: 55.96 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 7 FIVNGKIKFPDNTnlvkhVEKWARVRGDKLAYRFvdfSTErDGEYRDIVWSDFSAR-NRAVGARLQQVTQPGDRIAVLCP 85
Cdd:cd05968 54 WFVGGRMNIVEQL-----LDKWLADTRTRPALRW---EGE-DGTSRTLTYGELLYEvKRLANGLRALGVGKGDRVGIYLP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 86 QNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGrlhAVLDDCSPSTILTT------------TDAAE-------GVRKFIR 146
Cdd:cd05968 125 MIPEIVPAFLAVARIGGIVVPIFSGFGKEAAA---TRLQDAEAKALITAdgftrrgrevnlKEEADkacaqcpTVEKVVV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 147 ARSAK-ERPRVIAVDAVPNEVASTwEPPEADENTI---AYLQYTSGSTRTPTGVQITHLNLPTNVLQVL-NGLEGKEGDR 221
Cdd:cd05968 202 VRHLGnDFTPAKGRDLSYDEEKET-AGDGAERTESedpLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMyFQFDLKPGDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 222 gLSWlpfFHDMG------LITALLspVLGHNFTFMTPAAFVRRPGRwIREMArkpeDAPDSEVFTVAPNFafehaaVRGV 295
Cdd:cd05968 281 -LTW---FTDLGwmmgpwLIFGGL--ILGATMVLYDGAPDHPKADR-LWRMV----EDHEITHLGLSPTL------IRAL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 296 PKEGEPPL---DLSNVKAILNGSEPVSPASMRKFYEafspyglretaikpsyglaeatlfvsTTPMDQAPTVIHVDRDEL 372
Cdd:cd05968 344 KPRGDAPVnahDLSSLRVLGSTGEPWNPEPWNWLFE--------------------------TVGKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 373 NKQRFVEVPADSPKAVpQVSAGTIGVDewAVIVDpETASELPDgQIGEIWLHGNNLGT--GYWGREqetnDIFRNILKSR 450
Cdd:cd05968 398 SGGILGNVLIKPIKPS-SFNGPVPGMK--ADVLD-ESGKPARP-EVGELVLLAPWPGMtrGFWRDE----DRYLETYWSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 451 IsqshaegapdDGMWVKtGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEySAQEASKALRTGyvAAFSVPanqlpk 529
Cdd:cd05968 469 F----------DNVWVH-GDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIE-SVLNAHPAVLES--AAIGVP------ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 530 evfdnphtglkyDPDDSSEQLVIVAERAagshklDYQP---IADDIRAAIAVRHG--VTVRDLLLVQSgtIPRTSSGKIG 604
Cdd:cd05968 529 ------------HPVKGEAIVCFVVLKP------GVTPteaLAEELMERVADELGkpLSPERILFVKD--LPKTRNAKVM 588
|
650
....*....|...
gi 497642598 605 HRACRAAYLDGSL 617
Cdd:cd05968 589 RRVIRAAYLGKEL 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
64-493 |
5.87e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.59 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 64 RAVGARLQQVTQ-PGDRIAVLCPQNLDYLIAFFGALYAGRIAV---------PLFDPAEPGHVGR----------LHAVL 123
Cdd:PRK06334 53 KAVIALATKVSKyPDQHIGIMMPASAGAYIAYFATLLSGKIPVminwsqglrEVTACANLVGVTHvltskqlmqhLAQTH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 124 DDCS--PSTILTTtdaaEGVRKFIrarSAKERPRVIAVDAVPNEVASTW-EPPEADENTIAYLQYTSGSTRTPTGVQITH 200
Cdd:PRK06334 133 GEDAeyPFSLIYM----EEVRKEL---SFWEKCRIGIYMSIPFEWLMRWfGVSDKDPEDVAVILFTSGTEKLPKGVPLTH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 201 LNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHnftfmTPAAFVRRP--GRWIREMArkpeDAPDSEV 278
Cdd:PRK06334 206 ANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG-----VPVVFAYNPlyPKKIVEMI----DEAKVTF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 279 FTVAPNFaFEHaAVRGVPKEGEpplDLSNVKAILNGSEpVSPASMRKFYEAFSPYglreTAIKPSYGLAEATlfvsttpm 358
Cdd:PRK06334 277 LGSTPVF-FDY-ILKTAKKQES---CLPSLRFVVIGGD-AFKDSLYQEALKTFPH----IQLRQGYGTTECS-------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 359 dqaPTVIHVDRDELNKQRFVEVPADspkavpqvsagtiGVDewAVIVDPETASELPDGQIGEIWLHGNNLGTGYWGREQe 438
Cdd:PRK06334 339 ---PVITINTVNSPKHESCVGMPIR-------------GMD--VLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDF- 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497642598 439 tndifrnilksriSQSHAEGAPDdgMWVKTGDYGTYYK-GHLYIAGRIKDLVIIDG 493
Cdd:PRK06334 400 -------------GQGFVELGGE--TWYVTGDLGYVDRhGELFLKGRLSRFVKIGA 440
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
52-502 |
7.75e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 55.43 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVP----------------------LF 108
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAaRGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPtnfrqtpdevaylaeasgaramIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 109 DPAEPGHVGRLHAVLDDCSPSTILTTTDAAEGVRKFIrARSAKERPRVIAVDAvpnevastweppeadeNTIAYLQYTSG 188
Cdd:PRK07470 111 HADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALV-ARHLGARVANAAVDH----------------DDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 189 STRTPTGVQITHLNLP---TNVL-QVLNGLegKEGDRGLSWLPFFHDMGlITALLSPVLGhnftfmtpAAFVRRPGRW-- 262
Cdd:PRK07470 174 TTGRPKAAVLTHGQMAfviTNHLaDLMPGT--TEQDASLVVAPLSHGAG-IHQLCQVARG--------AATVLLPSERfd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 263 IREMARKPEDAPDSEVFTVaPNFA---FEHAAVRGvpkegeppLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglretA 339
Cdd:PRK07470 243 PAEVWALVERHRVTNLFTV-PTILkmlVEHPAVDR--------YDHSSLRYVIYAGAPMYRADQKRALAKLGK------V 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 IKPSYGLAEATLFVSTTPmdqaptvihvdrdelnkqrfvevPAD-SPKAVPQVSAGTIGVDEWAV---IVDPEtASELPD 415
Cdd:PRK07470 308 LVQYFGLGEVTGNITVLP-----------------------PALhDAEDGPDARIGTCGFERTGMevqIQDDE-GRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 416 GQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapdDGmWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGR 494
Cdd:PRK07470 364 GETGEICVIGPAVFAGYYNNPEANAKAFR-----------------DG-WFRTGDLGHLdARGFLYITGRASDMYISGGS 425
|
....*...
gi 497642598 495 NHYPQDLE 502
Cdd:PRK07470 426 NVYPREIE 433
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
20-612 |
7.93e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 55.28 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 20 NLVKHVEKWARVRGDKLAYRFVDfsterdgeyRDIVWSDFSARNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGAL 98
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRD---------QEISYAEFHQRILQAAGMLHaRGIGQGDVVALLMKNSAAFLELAFAAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 99 YAGRIAVPLFDPAEPGHVGRlhaVLDDCSPSTILTTTD----AAEGVRKFIRARSAKERPRVIAVDAVPNEVASTWEPPE 174
Cdd:PRK06145 74 YLGAVFLPINYRLAADEVAY---ILGDAGAKLLLVDEEfdaiVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 175 adentIAYLQYTSGSTRTPTGVQITHLNLptnvlqvlnglegkegdrglSWLPFFHDMGL-ITA----LLSPVLGHNFTF 249
Cdd:PRK06145 151 -----LVRLMYTSGTTDRPKGVMHSYGNL--------------------HWKSIDHVIALgLTAserlLVVGPLYHVGAF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 250 MTPAAFVRRPGRWIREMAR-KPE---DAPDSEVFTVAPNFAFEHAAVRGVPKEGEppLDLSNVKAILNGSEPVSPASMRK 325
Cdd:PRK06145 206 DLPGIAVLWVGGTLRIHREfDPEavlAAIERHRLTCAWMAPVMLSRVLTVPDRDR--FDLDSLAWCIGGGEKTPESRIRD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 326 FYEAFspyglRETAIKPSYGLAEATlfVSTTPMDQAptvihvdrdelnkqRFVEVPADSPKAVPQVSagtigvdewaVIV 405
Cdd:PRK06145 284 FTRVF-----TRARYIDAYGLTETC--SGDTLMEAG--------------REIEKIGSTGRALAHVE----------IRI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 406 DPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapddGMWVKTGDYGTY-YKGHLYIAGR 484
Cdd:PRK06145 333 ADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY------------------GDWFRSGDVGYLdEEGFLYLTDR 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 485 IKDLVIIDGRNHYPQDLEYSAQEASKALRTGYVAAfsvpanqlpkevfdnphtglkydPDDS-SEQLVIVAERAAGShKL 563
Cdd:PRK06145 395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGV-----------------------HDDRwGERITAVVVLNPGA-TL 450
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 497642598 564 DYQPIADDIRAAIAVRHgvTVRDLLLVQSgtIPRTSSGKIGHRACRAAY 612
Cdd:PRK06145 451 TLEALDRHCRQRLASFK--VPRQLKVRDE--LPRNPSGKVLKRVLRDEL 495
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
52-495 |
1.02e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 54.95 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDDCS 127
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRgIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLntrLDAAS------IAFMLRHGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 128 PSTILTTTDAAEGVRkfiRARSAKERPRVIAVDAVPNE---------------VAS-----TWEPPEADENTIAyLQYTS 187
Cdd:PRK08162 116 AKVLIVDTEFAEVAR---EALALLPGPKPLVIDVDDPEypggrfigaldyeafLASgdpdfAWTLPADEWDAIA-LNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 188 GSTRTPTGVqITH-----LNLPTNVLqvlnglegkEGDRG-----LSWLPFFHDMGlitallspvLGHNFTfMTPAAFVR 257
Cdd:PRK08162 192 GTTGNPKGV-VYHhrgayLNALSNIL---------AWGMPkhpvyLWTLPMFHCNG---------WCFPWT-VAARAGTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 258 RPGRWIRemARKPEDA-PDSEV--FTVAPnfaFEHAAVRGVPKEGEPPLDlSNVKAILNGSEPvsPAS----MRKF-YEA 329
Cdd:PRK08162 252 VCLRKVD--PKLIFDLiREHGVthYCGAP---IVLSALINAPAEWRAGID-HPVHAMVAGAAP--PAAviakMEEIgFDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 330 FSPYGLRETaikpsYGlaEATLFVSTTPMDQAPtviHVDRDELNKQRFVEVPADSPKAVpqvsagtigvdewaviVDPET 409
Cdd:PRK08162 324 THVYGLTET-----YG--PATVCAWQPEWDALP---LDERAQLKARQGVRYPLQEGVTV----------------LDPDT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 410 ASELP-DGQ-IGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapddGMWVKTGDYGTYYK-GHLYIAGRIK 486
Cdd:PRK08162 378 MQPVPaDGEtIGEIMFRGNIVMKGYLKNPKATEEAFA------------------GGWFHTGDLAVLHPdGYIKIKDRSK 439
|
....*....
gi 497642598 487 DLVIIDGRN 495
Cdd:PRK08162 440 DIIISGGEN 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-493 |
1.30e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 15 FPDNTNLVKHVEKWARVRGDKLAYRFvdfsterdGEYRdIVWSDFSAR-NRAVGARLQQVTQPGDRIAVLCPQNLDYLIA 93
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAF--------GEET-LDYAELNRRaNRLAHALIERGVGPDVLVGVAMERSIEMVVA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 94 FFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDC------SPSTILTTTDAAEGVRkfirarsakerprVIAVDAVPNEVA 167
Cdd:PRK12316 578 LLAILKAGGAYVPL-DPEYPAE--RLAYMLEDSgvqlllSQSHLGRKLPLAAGVQ-------------VLDLDRPAAWLE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 168 STWEPP---EADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGlITALLSPVLG 244
Cdd:PRK12316 642 GYSEENpgtELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMS 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 245 HNFTFMTPAAFVRRPGRWIREMARKPEDapdseVFTVAPNF--AFEHAAvrGVPkegepplDLSNVKAILNGSEPVSPAS 322
Cdd:PRK12316 721 GARLVVAAPGDHRDPAKLVELINREGVD-----TLHFVPSMlqAFLQDE--DVA-------SCTSLRRIVCSGEALPADA 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 323 MRKFYEAFSPYGLRETaikpsYGLAEATLFVSttpmdqaptviHVDRDElnkqrfvEVPADSPKAVPQVSAGTIGVDEWA 402
Cdd:PRK12316 787 QEQVFAKLPQAGLYNL-----YGPTEAAIDVT-----------HWTCVE-------EGGDSVPIGRPIANLACYILDANL 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 403 VIVdpetaselPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrISQSHAEGApddgMWVKTGDYGTYYK-GHLYI 481
Cdd:PRK12316 844 EPV--------PVGVLGELYLAGRGLARGYHGRPGLTAERF-------VPSPFVAGE----RMYRTGDLARYRAdGVIEY 904
|
490
....*....|..
gi 497642598 482 AGRIKDLVIIDG 493
Cdd:PRK12316 905 AGRIDHQVKLRG 916
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-496 |
4.12e-07 |
|
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: 52.99 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARLQQV---TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVgrlHAVLDD 125
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLggkPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAI---EYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 126 CSPSTILtttdAAEGVR-----KFIRARSAKERPrviavdavpnevastwePPEADENTIAYLQYTSGSTRTPTGVQITH 200
Cdd:cd05927 78 AEISIVF----CDAGVKvysleEFEKLGKKNKVP-----------------PPPPKPEDLATICYTSGTTGNPKGVMLTH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 201 LNLPTNVLQVLNGLEGK----EGDRGLSWLP---------------------FFHdmGLITAL------LSPvlghnfTF 249
Cdd:cd05927 137 GNIVSNVAGVFKILEILnkinPTDVYISYLPlahifervvealflyhgakigFYS--GDIRLLlddikaLKP------TV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 250 --MTPAAFVRRPGRWIREMARKPedAPDSEVFtvapNFAFEH--AAVRGVPKEGEPPLD-----------LSNVKAILNG 314
Cdd:cd05927 209 fpGVPRVLNRIYDKIFNKVQAKG--PLKRKLF----NFALNYklAELRSGVVRASPFWDklvfnkikqalGGNVRLMLTG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 315 SEPVSPASMRKFYEAFSpyglreTAIKPSYGLAEATlfvsttpmdqAPTvihvdrdelnkqrFVEVPADSpkavpqvSAG 394
Cdd:cd05927 283 SAPLSPEVLEFLRVALG------CPVLEGYGQTECT----------AGA-------------TLTLPGDT-------SVG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 395 TIGVDEWAVIVDPETASEL------PDGQiGEIWLHGNNLGTGYWGREQETndifrnilksrisqshAEGAPDDGmWVKT 468
Cdd:cd05927 327 HVGGPLPCAEVKLVDVPEMnydakdPNPR-GEVCIRGPNVFSGYYKDPEKT----------------AEALDEDG-WLHT 388
|
490 500
....*....|....*....|....*...
gi 497642598 469 GDYGTYYKGhlyiaGRIKdlvIIDGRNH 496
Cdd:cd05927 389 GDIGEWLPN-----GTLK---IIDRKKN 408
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
55-238 |
7.20e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 52.46 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 55 VWSDFSARnrAVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAEpghVGRLHAVLDDCSPSTILTT 134
Cdd:cd17632 73 LWERVGAV--AAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGAS---AAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 135 TDAAEGVRKFIRA-------------------RSAKERPR-----------VIAVDAVPNEVASTWEPPEADENT--IAY 182
Cdd:cd17632 148 AEHLDLAVEAVLEggtpprlvvfdhrpevdahRAALESARerlaavgipvtTLTLIAVRGRDLPPAPLFRPEPDDdpLAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 183 LQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDR-GLSWLPFFHDMG---LITAL 238
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASiTLNFMPMSHIAGrisLYGTL 287
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
121-531 |
7.90e-07 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 51.99 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 121 AVLDDCSPSTILTTTDAAEGvrkfirARSAKERPRVIAVDAVPN----------EVASTWEPPEADENTIAYLQYTSGST 190
Cdd:cd05929 64 KCGACPAYKSSRAPRAEACA------IIEIKAAALVCGLFTGGGaldgledyeaAEGGSPETPIEDEAAGWKMLYSGGTT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 191 RTPTGVQITHLNLPTNVLQVLN---GLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMT---PAAFVRRPGRW-- 262
Cdd:cd05929 138 GRPKGIKRGLPGGPPDNDTLMAaalGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEkfdPEEFLRLIERYrv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 263 ---------IREMARKPEDAPDSEvftvapnfafehaavrgvpkegepplDLSNVKAILNGSEPVSPASMRKFYEAFSPy 333
Cdd:cd05929 218 tfaqfvptmFVRLLKLPEAVRNAY--------------------------DLSSLKRVIHAAAPCPPWVKEQWIDWGGP- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 334 glretAIKPSYGLAEAtlfvsttpmdQAPTVIhvdrdelNKQRFVEvpadSPKAVPQVSAGTIGvdewavIVDpETASEL 413
Cdd:cd05929 271 -----IIWEYYGGTEG----------QGLTII-------NGEEWLT----HPGSVGRAVLGKVH------ILD-EDGNEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 414 PDGQIGEIWLHGNnlgtgywgreqETNDIFRNILKsrisqshAEGAPDDGMWVKTGDYGTYYK-GHLYIAGRIKDLVIID 492
Cdd:cd05929 318 PPGEIGEVYFANG-----------PGFEYTNDPEK-------TAAARNEGGWSTLGDVGYLDEdGYLYLTDRRSDMIISG 379
|
410 420 430
....*....|....*....|....*....|....*....
gi 497642598 493 GRNHYPQDLEySAQEASKALRTgyVAAFSVPANQLPKEV 531
Cdd:cd05929 380 GVNIYPQEIE-NALIAHPKVLD--AAVVGVPDEELGQRV 415
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
49-472 |
1.04e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 51.67 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 49 GEYRDIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEPGHV---GR--- 118
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQgVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVntrYRSHEVAHIlgrGRarw 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 119 -----------LHAVLDDCSPSTILTttdaAEGVRKFIRARSAKERP----RVIAVDAVPNEVASTWEPPEADENTIAYL 183
Cdd:PRK06164 111 lvvwpgfkgidFAAILAAVPPDALPP----LRAIAVVDDAADATPAPapgaRVQLFALPDPAPPAAAGERAADPDAGALL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 184 QYTSGSTRTPTGV---QITHLNLPTNVLQVLnGLEgkEGDRGLSWLPFFHDMGLITALLSpvLGHNFTFMTPAAFvrRPG 260
Cdd:PRK06164 187 FTTSGTTSGPKLVlhrQATLLRHARAIARAY-GYD--PGAVLLAALPFCGVFGFSTLLGA--LAGGAPLVCEPVF--DAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 261 RWIREMARKpedapdsevfTVAPNFAFEHAAVRGVPKEGEPPlDLSnvkailngsepvspaSMRKF-YEAFSPyGLRETA 339
Cdd:PRK06164 260 RTARALRRH----------RVTHTFGNDEMLRRILDTAGERA-DFP---------------SARLFgFASFAP-ALGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 340 IKP-SYGLAEATLFVSTTPmdQAPTVIHvdrdelnkqrfvevPADSPKAVPQVSAGTIGVDEWAV-IVDPETASELPDGQ 417
Cdd:PRK06164 313 ALArARGVPLTGLYGSSEV--QALVALQ--------------PATDPVSVRIEGGGRPASPEARVrARDPQDGALLPDGE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 418 IGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapDDGmWVKTGDYG 472
Cdd:PRK06164 377 SGEIEIRAPSLMRGYLDNPDATARALT----------------DDG-YFRTGDLG 414
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
380-616 |
2.41e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 50.39 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 380 VPADSpKAVPQVSAGTIGVDEWAVIV--------DPETASELPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksri 451
Cdd:PRK05857 329 LPTDD-GSIVKIEAGAVGRPYPGVDVylaatdgiGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVL-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 452 sqshAEGapddgmWVKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLEYSAQEASKalrTGYVAAFSVPanqlpke 530
Cdd:PRK05857 400 ----IDG------WVNTGDLLERREdGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSG---VREAACYEIP------- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 531 vfdNPHTGlkydpddSSEQLVIVAE---RAAGSHKLDYQPIADDIRAAIAVrhgvtVRDLLLVQSGTIPRTSSGKIgHRA 607
Cdd:PRK05857 460 ---DEEFG-------ALVGLAVVASaelDESAARALKHTIAARFRRESEPM-----ARPSTIVIVTDIPRTQSGKV-MRA 523
|
....*....
gi 497642598 608 CRAAYLDGS 616
Cdd:PRK05857 524 SLAAAATAD 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
412-509 |
3.09e-06 |
|
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: 49.57 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 412 ELPDGQIGEIWLHGNNLGTGYWGREQETNDIFRnilksrisqshaegapddGMWVKTGDYGTYYK-GHLYIAGRIKDLVI 490
Cdd:cd17635 190 AGPSASFGTIWIKSPANMLGYWNNPERTAEVLI------------------DGWVNTGDLGERREdGFLFITGRSSESIN 251
|
90
....*....|....*....
gi 497642598 491 IDGRNHYPQDLEYSAQEAS 509
Cdd:cd17635 252 CGGVKIAPDEVERIAEGVS 270
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
75-502 |
3.22e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 49.90 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEPGHvgrlhaVLDDCSPSTILTTTDAAEGVRKFIRARSAK 151
Cdd:PRK08276 34 REGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhLTAAEIAY------IVDDSGAKVLIVSAALADTAAELAAELPAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 152 ERPRVIAVDAVP------NEVASTWEPPEADENTIAYLQYTSGSTRTPTGV--QITHL----NLPTNVLQVLNGLEGKEG 219
Cdd:PRK08276 108 VPLLLVVAGPVPgfrsyeEALAAQPDTPIADETAGADMLYSSGTTGRPKGIkrPLPGLdpdeAPGMMLALLGFGMYGGPD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 220 DRGLSWLPFFHDMGLITALLSPVLGHNFTFMT----------------------PAAFVRrpgrwireMARKPEDapdse 277
Cdd:PRK08276 188 SVYLSPAPLYHTAPLRFGMSALALGGTVVVMEkfdaeealalieryrvthsqlvPTMFVR--------MLKLPEE----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 278 vftvapnfafehaaVRGvpkegepPLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglretAIKPSYGLAEATLFvsttp 357
Cdd:PRK08276 255 --------------VRA-------RYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP------IIHEYYASSEGGGV----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 358 mdqapTVIhvdrdelNKQRFVEVPADSPKAVpqvsagtIGVdewAVIVDpETASELPDGQIGEIWLHGNNLGTGYWGREQ 437
Cdd:PRK08276 303 -----TVI-------TSEDWLAHPGSVGKAV-------LGE---VRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPE 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642598 438 ETNDIFRnilksrisqshaegapdDGMWVKTGDYGtyY---KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK08276 360 KTAAARN-----------------PHGWVTVGDVG--YldeDGYLYLTDRKSDMIISGGVNIYPQEIE 408
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
75-603 |
4.90e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 75 QPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEPGHVgrlhaVLDdcSPSTILTTTDAAEGVRkfirARSAK 151
Cdd:PRK13390 47 RTGDVVALLSDNSPEALVVLWAALRSGLYITAInhhLTAPEADYI-----VGD--SGARVLVASAALDGLA----AKVGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 152 ERPRVIAVDAVPNEVAStWE-------PPEADENTIAYLQYTSGSTRTPTGVQIthlNLPTN--------VLQVLNGLEG 216
Cdd:PRK13390 116 DLPLRLSFGGEIDGFGS-FEaalagagPRLTEQPCGAVMLYSSGTTGFPKGIQP---DLPGRdvdapgdpIVAIARAFYD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 217 -KEGDRGLSWLPFFHDM-----GLITALLSPV-----------LGH------NFTFMTPAAFVRrpgrwireMARKpeda 273
Cdd:PRK13390 192 iSESDIYYSSAPIYHAAplrwcSMVHALGGTVvlakrfdaqatLGHveryriTVTQMVPTMFVR--------LLKL---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 274 pDSEVFTvapnfAFEHAAVRGVPKEGEP-PLDLSnvKAILNGSEPVspasMRKFYEAFSPYGLretaikpsyglaeatlf 352
Cdd:PRK13390 260 -DADVRT-----RYDVSSLRAVIHAAAPcPVDVK--HAMIDWLGPI----VYEYYSSTEAHGM----------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 353 vstTPMDQAPTVIHvdrdelnkqrfvevpadsPKAVPQVSAGTIGVDEwavivdpETASELPDGQIGEIWLHGNNLGTGY 432
Cdd:PRK13390 311 ---TFIDSPDWLAH------------------PGSVGRSVLGDLHICD-------DDGNELPAGRIGTVYFERDRLPFRY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 433 WGREQETNdifrnilksrisqshAEGAPDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDGRNHYPQDLEySAQEASKA 511
Cdd:PRK13390 363 LNDPEKTA---------------AAQHPAHPFWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETE-NALTMHPA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 512 LRTgyVAAFSVPANQLPKEVfdnphtglkydpddssEQLVIVAERAAGSHKLDYQPIaDDIRAAIAvrHGVTVRDLLLVQ 591
Cdd:PRK13390 427 VHD--VAVIGVPDPEMGEQV----------------KAVIQLVEGIRGSDELARELI-DYTRSRIA--HYKAPRSVEFVD 485
|
570
....*....|..
gi 497642598 592 SgtIPRTSSGKI 603
Cdd:PRK13390 486 E--LPRTPTGKL 495
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
170-495 |
5.39e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 49.46 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 170 WEPPEADENTIAyLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMG-LITALLSPVLGHNFT 248
Cdd:PLN02479 188 WKPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGwCFTWTLAALCGTNIC 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 249 fmtpaafvrrpgrwIREMARKpedapdsEVFTVAPNFAFEHAAVRGV--------PKEgEPPLDLSNVKAILN-GSEPvs 319
Cdd:PLN02479 267 --------------LRQVTAK-------AIYSAIANYGVTHFCAAPVvlntivnaPKS-ETILPLPRVVHVMTaGAAP-- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 320 PASMrkfYEAFSPYGLRETAikpSYGLAE----ATLFVSTTPMDQAPTvihVDRDELNKQRFVEVpadspkavpqvsAGT 395
Cdd:PLN02479 323 PPSV---LFAMSEKGFRVTH---TYGLSEtygpSTVCAWKPEWDSLPP---EEQARLNARQGVRY------------IGL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 396 IGVDewavIVDPETASELP-DGQ-IGEIWLHGNNLGTGYWGREQETNDIFRNilksrisqshaegapddgMWVKTGDYGT 473
Cdd:PLN02479 382 EGLD----VVDTKTMKPVPaDGKtMGEIVMRGNMVMKGYLKNPKANEEAFAN------------------GWFHSGDLGV 439
|
330 340
....*....|....*....|...
gi 497642598 474 YY-KGHLYIAGRIKDLVIIDGRN 495
Cdd:PLN02479 440 KHpDGYIEIKDRSKDIIISGGEN 462
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
435-502 |
7.31e-06 |
|
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: 48.56 E-value: 7.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642598 435 REQETNDIFRNILKS--RISQSHAEGAPDDGMWVKTGDYGtYYK--GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd17633 177 RNADGGEIGKIFVKSemVFSGYVRGGFSNPDGWMSVGDIG-YVDeeGYLYLVGRESDMIIIGGINIFPTEIE 247
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-220 |
1.25e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 72 QVTQPgdrIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDAAEGVRKFIRARSAK 151
Cdd:PRK05691 3768 GVDQP---VALLAERGLDLLGMIVGSFKAGAGYLPL-DPGLPAQ--RLQRIIELSRTPVLVCSAACREQARALLDELGCA 3841
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 152 ERPRVIAVDAVPNEVASTWEPP-EADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGD 220
Cdd:PRK05691 3842 NRPRLLVWEEVQAGEVASHNPGiYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEAD 3911
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
89-493 |
2.09e-05 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 47.74 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 89 DYLIAFFGALYAGRIAVPLFDPAEPGHVgrlHAVLDDCSPSTILTTTDaaegvRKFIRARSAKER-PRVIAV----DAVP 163
Cdd:cd05933 45 EWFIAAVGAIFAGGIAVGIYTTNSPEAC---QYVAETSEANILVVENQ-----KQLQKILQIQDKlPHLKAIiqykEPLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 164 NEVAS--TWEP--------PEADENTI---------AYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRG-- 222
Cdd:cd05933 117 EKEPNlySWDEfmelgrsiPDEQLDAIissqkpnqcCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGqe 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 223 --LSWLPFFHDMGLITALLSPVL-GHNFTF----------------MTPAAFVRRPGRWIREMARKPEDAPDS-----EV 278
Cdd:cd05933 197 svVSYLPLSHIAAQILDIWLPIKvGGQVYFaqpdalkgtlvktlreVRPTAFMGVPRVWEKIQEKMKAVGAKSgtlkrKI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 279 FTVA----------------PNFAFEHAAVRGVPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYeafspyGLrETAIKP 342
Cdd:cd05933 277 ASWAkgvgletnlklmggesPSPLFYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFL------SL-NIPIME 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 343 SYGLAEATlfvsttpmdqAPTVIHVdrdelnkqrfvevpadsPKAVPQVSAGTigvdewaVIVDPETASELPDGQ-IGEI 421
Cdd:cd05933 350 LYGMSETS----------GPHTISN-----------------PQAYRLLSCGK-------ALPGCKTKIHNPDADgIGEI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642598 422 WLHGNNLGTGYWGREQETndifrnilksrisqshaEGAPDDGMWVKTGDYGTY-YKGHLYIAGRIKDLVIIDG 493
Cdd:cd05933 396 CFWGRHVFMGYLNMEDKT-----------------EEAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIITAG 451
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
65-253 |
2.96e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.01 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 65 AVGARLQQVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLFDPAepGHVGrLHAVLDDCSPSTILTT---------T 135
Cdd:PRK08043 243 FVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTA--GVKG-LTSAITAAEIKTIFTSrqfldkgklW 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 136 DAAEGVRKfirAR-----------SAKERPRVIAVDAVPNEVASTWEPPEAdentiAYLQYTSGSTRTPTGVQITHLNLP 204
Cdd:PRK08043 320 HLPEQLTQ---VRwvyledlkddvTTADKLWIFAHLLMPRLAQVKQQPEDA-----ALILFTSGSEGHPKGVVHSHKSLL 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497642598 205 TNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNFTFMTPA 253
Cdd:PRK08043 392 ANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
69-502 |
3.05e-05 |
|
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: 47.08 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 69 RLQQVTqPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCSPSTILTTTDAAEGVrKFIRAR 148
Cdd:cd17656 31 REKGVK-KDSIVAIMMERSAEMIVGILGILKAGGAFVPI-DPEYPEE--RRIYIMLDSGVRVVLTQRHLKSKL-SFNKST 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 149 SAKERPRVIAVDAvpNEVAStweppEADENTIAYLQYTSGSTRTPTGVQITHLNLpTNVLQVLNGLEGKE-GDRGLSWLP 227
Cdd:cd17656 106 ILLEDPSISQEDT--SNIDY-----INNSDDLLYIIYTSGTTGKPKGVQLEHKNM-VNLLHFEREKTNINfSDKVLQFAT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 228 FFHDMG---LITALLSpvlGHNFTFMTPAAfvrrpGRWIREMARKPEDAPDSEVF--TVAPNFAFEHaavrgvpKEGEPP 302
Cdd:cd17656 178 CSFDVCyqeIFSTLLS---GGTLYIIREET-----KRDVEQLFDLVKRHNIEVVFlpVAFLKFIFSE-------REFINR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 303 LdLSNVK-AILNGSEPVSPASMRKFYEAfspyglRETAIKPSYGLAEATLfVSTTPMDQAPtvihvdrdelnkqrfvEVP 381
Cdd:cd17656 243 F-PTCVKhIITAGEQLVITNEFKEMLHE------HNVHLHNHYGPSETHV-VTTYTINPEA----------------EIP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 382 ADSPKAVPQVSAgtigvdeWAVIVDPETASElPDGQIGEIWLHGNNLGTGYWGREQETNDIFrnilksrISQSHaegAPD 461
Cdd:cd17656 299 ELPPIGKPISNT-------WIYILDQEQQLQ-PQGIVGELYISGASVARGYLNRQELTAEKF-------FPDPF---DPN 360
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 497642598 462 DGMWvKTGDYGTYYK-GHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:cd17656 361 ERMY-RTGDLARYLPdGNIEFLGRADHQVKIRGYRIELGEIE 401
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
295-502 |
5.29e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.29 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 295 VPKEGEPPLDLSNVKAILNGSEPVSPASMRKFYEAFSPyglretAIKPSYGLAEATLFVSTTPMDQaptvihvdrdelnk 374
Cdd:PRK13382 301 LPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD------VIYNNYNATEAGMIATATPADL-------------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 375 qrfvevpadspKAVPQvSAGTIGVDEWAVIVDPEtASELPDGQIGEIWLHGNNLGTGYW-GREQETNDIFrnilksrisq 453
Cdd:PRK13382 361 -----------RAAPD-TAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGF---------- 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497642598 454 shaegapddgmwVKTGDYGtYY--KGHLYIAGRIKDLVIIDGRNHYPQDLE 502
Cdd:PRK13382 418 ------------MASGDVG-YLdeNGRLFVVGRDDEMIVSGGENVYPIEVE 455
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
62-200 |
7.07e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 62 RNRAVGarlqqvtqPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCSPSTILTTTDAAEGV 141
Cdd:PRK05691 1174 RDKGVG--------PDVCVAIAAERSPQLLVGLLAILKAGGAYVPL-DPDYP--AERLAYMLADSGVELLLTQSHLLERL 1242
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642598 142 rkfirarsakerPRVIAVDAVPNEV--ASTW--EPP--EADENTIAYLQYTSGSTRTPTGVQITH 200
Cdd:PRK05691 1243 ------------PQAEGVSAIALDSlhLDSWpsQAPglHLHGDNLAYVIYTSGSTGQPKGVGNTH 1295
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
24-200 |
5.99e-04 |
|
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: 42.83 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 24 HVEKWARVRGDKLAyrFVDfsterdGEYRdIVWSDFSARNRAVGARLQQV-TQPGDRIAVLCPQNLDYLIAFFGALYAGr 102
Cdd:COG1021 30 LLRRRAERHPDRIA--VVD------GERR-LSYAELDRRADRLAAGLLALgLRPGDRVVVQLPNVAEFVIVFFALFRAG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 103 iAVPLFdpAEPGHvgRLH----------AVLddcspstiLTTTDAAEGV--RKFIRA-RSAKERPRVIAVDAVPNEVAS- 168
Cdd:COG1021 100 -AIPVF--ALPAH--RRAeishfaeqseAVA--------YIIPDRHRGFdyRALARElQAEVPSLRHVLVVGDAGEFTSl 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497642598 169 --------TWEPPEADENTIAYLQYTSGSTRTPTGVQITH 200
Cdd:COG1021 167 dallaapaDLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTH 206
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
178-230 |
7.26e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 42.80 E-value: 7.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 497642598 178 NTIAYLQYTSGSTRTPTGVQITHLNL---PTNVLQVLNGLEGKegDRGLSWLPFFH 230
Cdd:PLN02387 250 NDIAVIMYTSGSTGLPKGVMMTHGNIvatVAGVMTVVPKLGKN--DVYLAYLPLAH 303
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
175-248 |
2.43e-03 |
|
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: 40.88 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 175 ADENTIAYLQYTSGSTRTPTGVQITHLNLPTNVLQVLNGLEGKEGDRGLSWLPFFHDMGLITALLSPV-------LGHNF 247
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLmsggtlaLSRKF 163
|
.
gi 497642598 248 T 248
Cdd:cd05937 164 S 164
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
176-489 |
3.17e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 40.51 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 176 DENTIAYLQYTSGSTRTPTGVQITHlnlPTNVLQVL-----NGLEGKEGDRGLSWLPFFHDMGLITALLSPVLGHNftFM 250
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSH---RSNVLHALmanngDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTK--LV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 251 TPAAfvRRPGRWIREMArkpedapDSEVFTVApnfafehAAVRGV--------PKEGeppLDLSNVKAILNGSEpvspAS 322
Cdd:PRK06018 250 MPGA--KLDGASVYELL-------DTEKVTFT-------AGVPTVwlmllqymEKEG---LKLPHLKMVVCGGS----AM 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 323 MRKFYEAFSPYGLRetaIKPSYGLAE----ATLFVSTTPMDQAPTVIHVDRdeLNKQRFvevpadSPKAVPQvsagtigv 398
Cdd:PRK06018 307 PRSMIKAFEDMGVE---VRHAWGMTEmsplGTLAALKPPFSKLPGDARLDV--LQKQGY------PPFGVEM-------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 399 dewaVIVDPEtASELP-DGQ-IGEIWLHGNNLGTGYWGREQETNDifrnilksrisqshaegapDDGmWVKTGDYGTYYK 476
Cdd:PRK06018 368 ----KITDDA-GKELPwDGKtFGRLKVRGPAVAAAYYRVDGEILD-------------------DDG-FFDTGDVATIDA 422
|
330
....*....|....
gi 497642598 477 -GHLYIAGRIKDLV 489
Cdd:PRK06018 423 yGYMRITDRSKDVI 436
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-196 |
3.85e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 40.25 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 52 RDIVWSDFSARNRAVGARLQ-QVTQPGDRIAVLCPQNLDYLIAFFGALYAGRIAVPL---FDPAEpghvgrLHAVLDDCS 127
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIaQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVEDE------LRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642598 128 PSTILTTTDAAEGVRKfIRARSAKERpRVIAVD----------AVPNEVASTWEPPEADENTIA----YLQYTSGSTRTP 193
Cdd:PRK07798 101 AVALVYEREFAPRVAE-VLPRLPKLR-TLVVVEdgsgndllpgAVDYEDALAAGSPERDFGERSpddlYLLYTGGTTGMP 178
|
...
gi 497642598 194 TGV 196
Cdd:PRK07798 179 KGV 181
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
404-444 |
6.59e-03 |
|
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: 39.21 E-value: 6.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 497642598 404 IVDPEtASELPDGQIGEIWLHGNNLGTGYWGREQE-----------TNDIFR 444
Cdd:cd17636 176 ILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVnarrtrggwhhTNDLGR 226
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