|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-541 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 988.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 1 MPTFANIAAHLPRMAQLQPDTTAIIFPKG--------NQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFA 72
Cdd:PRK09274 2 MASMANIARHLPRAAQERPDQLAVAVPGGrgadgklaYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 73 LTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIGIPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQS 152
Cdd:PRK09274 82 LTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGKPSVRRLVTVGGRLLWGGTTLATLLRDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 153 PDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEM 232
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGMTSVIPDM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 233 DFTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGVEIFTP 312
Cdd:PRK09274 242 DPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAEILTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YGATESLPVCSIGSREILGETRVITENGGGVCIGRPVDSIRVELIRISDEPITVWDDDLRVAPGQVGEIVVQGPQVTRGY 392
Cdd:PRK09274 322 YGATEALPISSIESREILFATRAATDNGAGICVGRPVDGVEVRIIAISDAPIPEWDDALRLATGEIGEIVVAGPMVTRSY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 393 FQRPEADLLSKISDPQGGFFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIGPKGS 472
Cdd:PRK09274 402 YNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 473 QQPVICIELEQGITTNQEQLRSELLNIAASHPHTREISTILFHPAFPVDIRHNAKIFREKLAVWAAEEL 541
Cdd:PRK09274 482 QRPVLCVELEPGVACSKSALYQELRALAAAHPHTAGIERFLIHPSFPVDIRHNAKIFREKLAVWAAKQL 550
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
31-537 |
0e+00 |
|
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: 683.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIG 110
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 IPKAqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaaDDQAAILFTSGSTGPPKGAIYSHGNF 190
Cdd:cd05910 81 IPKA--------------------------------------------------DEPAAILFTSGSTGTPKGVVYRHGTF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 191 SAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRS 270
Cdd:cd05910 111 AAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 271 GAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGVEIFTPYGATESLPVCSIGSREILGETRVITENGGGVCIGRPVD 350
Cdd:cd05910 191 CAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSIGSRELLATTTAATSGGAGTCVGRPIP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 351 SIRVELIRISDEPITVWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISDPQGGFFHRMGDLGRQDETGRLWFC 430
Cdd:cd05910 271 GVRVRIIEIDDEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFC 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 431 GRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIGPKGSQQPVICIELEQGITTNQEQLRSELLNIAASHPHTREIS 510
Cdd:cd05910 351 GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTQRIG 430
|
490 500
....*....|....*....|....*..
gi 501446872 511 TILFHPAFPVDIRHNAKIFREKLAVWA 537
Cdd:cd05910 431 RFLIHPSFPVDIRHNAKIFREKLAVWA 457
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
7-542 |
1.33e-101 |
|
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: 313.67 E-value: 1.33e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF--GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIGipkaqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaadd 166
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 167 qAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALFAP-ALGMTAVIPEmdftrpg 238
Cdd:COG0318 103 -ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFhvfgltvGLLAPlLAGATLVLLP------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 SVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATES 318
Cdd:COG0318 175 RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTET 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 319 LPVCSIGSREILGETRvitengggVCIGRPVDSIRVeliRISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRPEA 398
Cdd:COG0318 253 SPVVTVNPEDPGERRP--------GSVGRPLPGVEV---RIVDE------DGRELPPGEVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 399 DLLSKisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRV----ESVhgplFTIPVEAVFNTHPLVYRSALVGI-GPKGSQ 473
Cdd:COG0318 316 TAEAF----RDGWLR-TGDLGRLDEDGYLYIVGRKKDMIisggENV----YPAEVEEVLAAHPGVAEAAVVGVpDEKWGE 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 474 QPVICIELEQGITTNQEQLRSELLNIAASHPHTREistILFHPAFPVdiRHNAKIFREKLAVWAAEELA 542
Cdd:COG0318 387 RVVAFVVLRPGAELDAEELRAFLRERLARYKVPRR---VEFVDELPR--TASGKIDRRALRERYAAGAL 450
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-433 |
1.32e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 250.31 E-value: 1.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:pfam00501 5 AARTPDKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIGIPKAQVARLLFGWAKDSLKTIITVGPRLFWG-GITLDKLIQQSPDKPFEMAVTAADDQAAILFT 173
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLkEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 174 SGSTGPPKGAIYSHGNFSAQVEALQQVY----RIQPGEIDLPTFPLF-------ALFAPAL-GMTAVIPEMDFTRpgsvD 241
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFhdfglslGLLGPLLaGATVVLPPGFPAL----D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 242 PQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLPV 321
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF--GGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 322 CSIGSREILGETRVITengggvcIGRPVDSIRVELIrisDepitvWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEadlL 401
Cdd:pfam00501 318 VTTPLPLDEDLRSLGS-------VGRPLPGTEVKIV---D-----DETGEPVPPGEPGELCVRGPGVMKGYLNDPE---L 379
|
410 420 430
....*....|....*....|....*....|..
gi 501446872 402 SKISDPQGGFFHrMGDLGRQDETGRLWFCGRK 433
Cdd:pfam00501 380 TAEAFDEDGWYR-TGDLGRRDEDGYLEIVGRK 410
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
168-528 |
1.99e-66 |
|
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: 218.69 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF------ALFAP-ALGMTAVIPEMDftrpgsv 240
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFhigglfGLLGAlLAGGTVVLLPKF------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLP 320
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP--GIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 321 VCSIGSREIlgetrvitENGGGVCIGRPVDSIRVELIRisdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADL 400
Cdd:cd04433 154 TVATGPPDD--------DARKPGSVGRPVPGVEVRIVD---------PDGGELPPGEIGELVVRGPSVMKGYWNNPEATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 401 LSKisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRV----ESVHgplfTIPVEAVFNTHPLVYRSALVGI-GPKGSQQP 475
Cdd:cd04433 217 AVD----EDGWYR-TGDLGRLDEDGYLYIVGRLKDMIksggENVY----PAEVEAVLLGHPGVAEAAVVGVpDPEWGERV 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 501446872 476 VICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPvdIRHNAKI 528
Cdd:cd04433 288 VAVVVLRPGADLDAEELRAHV---RERLAPYKVPRRVVFVDALP--RTASGKI 335
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-533 |
2.60e-61 |
|
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: 208.15 E-value: 2.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd05930 1 PDAVAVVD--GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLfgwaKDSlktiitvGPRLfwggitldkliqqspdkpfemAVTAADDQAAILFTSGSTG 178
Cdd:cd05930 72 -------------PAERLAYIL----EDS-------GAKL---------------------VLTDPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFP------LFALFAPAL-GMTAVIPEMDFTRpgsvDPQKIISAITS 251
Cdd:cd05930 107 KPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSfsfdvsVWEIFGALLaGATLVVLPEEVRK----DPEALADLLAE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 252 HKVTTMFGSPALINRVGRSGAEQGikLPTLQRVISAGAPVPAVVMERFSQMLaEGVEIFTPYGATEslpvCSIGSreILG 331
Cdd:cd05930 183 EGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEALPPDLVRRWRELL-PGARLVNLYGPTE----ATVDA--TYY 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 332 ETRVITENGGGVCIGRPVDSIRVElirisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISDP--Q 408
Cdd:cd05930 254 RVPPDDEEDGRVPIGRPIPNTRVY----------VLDENLRpVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPfgP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 409 GGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGIG-PKGSQQPVICIELEQG 484
Cdd:cd05930 324 GERMYRTGDLVRWLPDGNLEFLGRIDDQVK-IRG--YRIelgEIEAALLAHPGVREAAVVAREdGDGEKRLVAYVVPDEG 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 501446872 485 ITTNQEQLRSELLNIAASH--PhtreiSTILFHPAFPVDirHNAKIFREKL 533
Cdd:cd05930 401 GELDEEELRAHLAERLPDYmvP-----SAFVVLDALPLT--PNGKVDRKAL 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
7-493 |
3.80e-60 |
|
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: 205.87 E-value: 3.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLaevqpsafigipkaqvarllfgwaKDSlktiitvGPRLFWGGITLDKLIQQSPDKPFEMAVTAaDD 166
Cdd:cd05936 79 LNPLYTPRELEHIL------------------------NDS-------GAKALIVAVSFTDLLAAGAPLGERVALTP-ED 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 167 QAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVY--RIQPGEIDLPTFPLFALFA--------PALGMTAVIpemdFTR 236
Cdd:cd05936 127 VAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGltvalllpLALGATIVL----IPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 PgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGAT 316
Cdd:cd05936 203 F---RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT--GVPIVEGYGLT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 317 ESLPVCSIGSREilGETRVITengggvcIGRPVDSIRVELIRISDEPitvwdddlrVAPGQVGEIVVQGPQVTRGYFQRP 396
Cdd:cd05936 278 ETSPVVAVNPLD--GPRKPGS-------IGIPLPGTEVKIVDDDGEE---------LPPGEVGELWVRGPQVMKGYWNRP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 397 E--ADLLskisdpQGGFFhRMGDLGRQDETGRLWFCGRKTHRVeSVHGplFTI-P--VEAVFNTHPLVYRSALVGIG-PK 470
Cdd:cd05936 340 EetAEAF------VDGWL-RTGDIGYMDEDGYFFIVDRKKDMI-IVGG--FNVyPreVEEVLYEHPAVAEAAVVGVPdPY 409
|
490 500
....*....|....*....|...
gi 501446872 471 GSQQPVICIELEQGITTNQEQLR 493
Cdd:cd05936 410 SGEAVKAFVVLKEGASLTEEEII 432
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
6-496 |
1.82e-59 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 206.50 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAH-LPRMAQLQPDTTAIIF---PKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVG 81
Cdd:COG0365 9 NIAYNcLDRHAEGRGDKVALIWegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 AIPVLIDPGLGIKNLKSCLAEVQPSAFI----------GIP-KAQVARLLfgwAK-DSLKTIITV---GPRLFWGG-ITL 145
Cdd:COG0365 89 AVHSPVFPGFGAEALADRIEDAEAKVLItadgglrggkVIDlKEKVDEAL---EElPSLEHVIVVgrtGADVPMEGdLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 146 DKLIQQSPDkPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEA-LQQVYRIQPGEI-----DLP--TFPLFA 217
Cdd:COG0365 166 DELLAAASA-EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVfwctaDIGwaTGHSYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 218 LFAP-ALGMTAVIPEmdfTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIK--LPTLQRVISAGAPVPAV 294
Cdd:COG0365 245 VYGPlLNGATVVLYE---GRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 295 VMERFSQMLaeGVEIFTPYGATEslpVCSIgsreilgetrVITENGGGV----CIGRPVDSIRVElirisdepitVWDDD 370
Cdd:COG0365 322 VWEWWYEAV--GVPIVDGWGQTE---TGGI----------FISNLPGLPvkpgSMGKPVPGYDVA----------VVDED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 371 LR-VAPGQVGEIVVQGPQ--VTRGYFQRPEADLLSKISDPQGGFFHrmGDLGRQDETGRLWFCGR-----KT--HRVesv 440
Cdd:COG0365 377 GNpVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFGRFPGWYRT--GDGARRDEDGYFWILGRsddviNVsgHRI--- 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 441 hGPlftIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEqLRSEL 496
Cdd:COG0365 452 -GT---AEIESALVSHPAVAEAAVVGVpDEIRGQVVKAFVVLKPGVEPSDE-LAKEL 503
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
13-467 |
1.04e-58 |
|
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: 201.30 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRtVLMVTP-SPEFFALTFALFKVGAIPVLIDPGL 91
Cdd:cd17631 3 RRARRHPDRTALVF--GGRSLTYAELDERVNRLAHALRALGVAKGDR-VAVLSKnSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 92 GIKNLKSCLAEvqpsafigipkaQVARLLFgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaaDDQAAIL 171
Cdd:cd17631 80 TPPEVAYILAD------------SGAKVLF-------------------------------------------DDLALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFalFAPALGMTAVipeMDFTRPGSV------DPQKI 245
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLF--HIGGLGVFTL---PTLLRGGTVvilrkfDPETV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 246 ISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSqmlAEGVEIFTPYGATESLPVCSIg 325
Cdd:cd17631 180 LDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTETSPGVTF- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 326 sreiLGETRVITENGGgvcIGRPVDSIRVELIRisdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAdllsKIS 405
Cdd:cd17631 256 ----LSPEDHRRKLGS---AGRPVFFVEVRIVD---------PDGREVPPGEVGEIVVRGPHVMAGYWNRPEA----TAA 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501446872 406 DPQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd17631 316 AFRDGWFH-TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGV 376
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
3-496 |
2.63e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 186.16 E-value: 2.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 3 TFANIAAHLprmAQLQPDTTAIIFPKGNqsLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PRK06187 7 TIGRILRHG---ARKHPDKEAVYFDGRR--TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLIdpglgikNLKscLAEVQ---------------PSAFIGIPkAQVARLLfgwakDSLKTIITVGP----RLFWGGI 143
Cdd:PRK06187 82 VLHPI-------NIR--LKPEEiayilndaedrvvlvDSEFVPLL-AAILPQL-----PTVRTVIVEGDgpaaPLAPEVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 144 TLDKLIQQSPDKpFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF---ALFA 220
Cdd:PRK06187 147 EYEELLAAASDT-FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFhvhAWGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 221 P----ALGMTAVIpemdftrPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVM 296
Cdd:PRK06187 226 PylalMAGAKQVI-------PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 297 ERFSQMLaeGVEIFTPYGATESLPVCSIG--SREILGE-TRVITengggvcIGRPVDSirVElIRISdepitvwDDDLRV 373
Cdd:PRK06187 299 REFKEKF--GIDLVQGYGMTETSPVVSVLppEDQLPGQwTKRRS-------AGRPLPG--VE-ARIV-------DDDGDE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 374 AP---GQVGEIVVQGPQVTRGYFQRPEADlLSKIsdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESvhGPLFTIP-- 448
Cdd:PRK06187 360 LPpdgGEVGEIIVRGPWLMQGYWNRPEAT-AETI---DGGWLH-TGDVGYIDEDGYLYITDRIKDVIIS--GGENIYPre 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501446872 449 VEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRSEL 496
Cdd:PRK06187 433 LEDALYGHPAVAEVAVIGVpDEKWGERPVAVVVLKPGATLDAKELRAFL 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
30-493 |
1.86e-49 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 177.40 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 30 NQSLTFQELDRLSDRICHGLIRSGITRGTRtVLMVTP-SPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAF 108
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDV-VGIISPnSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 109 I----GIPKAQ-VARLLFGWAKdslktIITVGPRLFW--GGITLDKLIQQSPDKPFEMA-VTAADDQAAILFTSGSTGPP 180
Cdd:cd05911 87 FtdpdGLEKVKeAAKELGPKDK-----IIVLDDKPDGvlSIEDLLSPTLGEEDEDLPPPlKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 181 KGAIYSHGNFSAQVEALQQVYR--IQPGEIDLPTFPLF-------ALFAPALGMTAVIpemdFTRPgsvDPQKIISAITS 251
Cdd:cd05911 162 KGVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYhiyglftTLASLLNGATVII----MPKF---DSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 252 HKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGVEIFTpYGATESLPVCSIgsreilg 331
Cdd:cd05911 235 YKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQG-YGMTETGGILTV------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 332 etRVITENGGGvCIGRPVDSIRVeliRISDEpitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAdllSKISDPQGGF 411
Cdd:cd05911 307 --NPDGDDKPG-SVGRLLPNVEA---KIVDD-----DGKDSLGPNEPGEICVRGPQVMKGYYNNPEA---TKETFDEDGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 412 FHrMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTIP---VEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITT 487
Cdd:cd05911 373 LH-TGDIGYFDEDGYLYIVDRKKELIK-YKG--FQVApaeLEAVLLEHPGVADAAVIGIpDEVSGELPRAYVVRKPGEKL 448
|
....*.
gi 501446872 488 NQEQLR 493
Cdd:cd05911 449 TEKEVK 454
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
34-465 |
1.32e-48 |
|
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: 173.22 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 34 TFQELDRLSDRICHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGlgiknlksclaevQPS---AFI 109
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-------------YPAerlAFI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 110 gIPKAQVARLLFGWAKDSLKTIITVGPRLFwgGITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGN 189
Cdd:TIGR01733 68 -LEDAGARLLLTDSALASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 190 FSAQVEALQQVYRIQPGEI---------DLPTFPLFAlfAPALGMTAVIPEMDFTRPGSVDPQKIISaitSHKVTTMFGS 260
Cdd:TIGR01733 145 LVNLLAWLARRYGLDPDDRvlqfaslsfDASVEEIFG--ALLAGATLVVPPEDEERDDAALLAALIA---EHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 261 PALINRVgrsGAEQGIKLPTLQRVISAGAPVPAVVMERFSQmLAEGVEIFTPYGATESLPVCSIGSREILGETRVITeng 340
Cdd:TIGR01733 220 PSLLALL---AAALPPALASLRLVILGGEALTPALVDRWRA-RGPGARLINLYGPTETTVWSTATLVDPDDAPRESP--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 341 ggVCIGRPVDSIRVELIrisdepitvwDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEAD----LLSKISDPQGGFFHRM 415
Cdd:TIGR01733 293 --VPIGRPLANTRLYVL----------DDDLRpVPVGVVGELYIGGPGVARGYLNRPELTaerfVPDPFAGGDGARLYRT 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 501446872 416 GDLGRQDETGRLWFCGRKTHRVeSVHGplFTIP---VEAVFNTHPLVyRSALV 465
Cdd:TIGR01733 361 GDLVRYLPDGNLEFLGRIDDQV-KIRG--YRIElgeIEAALLRHPGV-REAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
15-465 |
6.82e-48 |
|
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: 179.28 E-value: 6.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:COG1020 486 AARTPDAVAVVF--GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIGiPKAQVARLlfgwAKDSLKTiitvgprlfwggITLDKL-IQQSPDKPFEMAVTaADDQAAILFT 173
Cdd:COG1020 564 RLAYMLEDAGARLVLT-QSALAARL----PELGVPV------------LALDALaLAAEPATNPPVPVT-PDDLAYVIYT 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 174 SGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL------FALFAPAL-GMTAVIPEMDFTRpgsvDPQKII 246
Cdd:COG1020 626 SGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsfdasvWEIFGALLsGATLVLAPPEARR----DPAALA 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 247 SAITSHKVTTMFGSPALINRVGRSGAEQgikLPTLQRVISAGAPVPAVVMERFSQmLAEGVEIFTPYGATEslpvCSIGS 326
Cdd:COG1020 702 ELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRA-RLPGARLVNLYGPTE----TTVDS 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 327 reILGETRVITENGGGVCIGRPVDSIRVElirisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEadlLSK-- 403
Cdd:COG1020 774 --TYYEVTPPDADGGSVPIGRPIANTRVY----------VLDAHLQpVPVGVPGELYIGGAGLARGYLNRPE---LTAer 838
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 404 -ISDPQGGFFHRM---GDLGRQDETGRLWFCGRK-------THRVEsvhgplftiP--VEAVFNTHPLVyRSALV 465
Cdd:COG1020 839 fVADPFGFPGARLyrtGDLARWLPDGNLEFLGRAddqvkirGFRIE---------LgeIEAALLQHPGV-REAVV 903
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
6-466 |
7.32e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 171.88 E-value: 7.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQLQPDTTAIIFpKGNqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV 85
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRF-LGN-TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 LID----PGLGIKNLKSCLAEVQPSAFIGIPKAQVARLLfgwaKDSLKTIITVGPRLFWGGITLDKLIQQsPDKPFEMAV 161
Cdd:PRK07786 96 PVNfrltPPEIAFLVSDCGAHVVVTEAALAPVATAVRDI----VPLLSTVVVAGGSSDDSVLGYEDLLAE-AGPAHAPVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 162 TAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQ-PGEIDLPTFPLFALfaPALGmtAVIPEMDFTRP--- 237
Cdd:PRK07786 171 IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHI--AGIG--SMLPGLLLGAPtvi 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 238 ---GSVDPQKIISAITSHKVTTMFGSPALINRVgrsGAEQGIKLPTLQ-RVISAG-APVPAVVMERFSQMLAeGVEIFTP 312
Cdd:PRK07786 247 yplGAFDPGQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLAlRVLSWGaAPASDTLLRQMAATFP-EAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YGATESLPVCSIgsreILGETrVITENGGgvcIGRPVDSIRVeliRISDEPItvwDDdlrVAPGQVGEIVVQGPQVTRGY 392
Cdd:PRK07786 323 FGQTEMSPVTCM----LLGED-AIRKLGS---VGKVIPTVAA---RVVDENM---ND---VPVGEVGEIVYRAPTLMSGY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 393 FQRPEAdllskISDP-QGGFFHRmGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:PRK07786 386 WNNPEA-----TAEAfAGGWFHS-GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
4-509 |
6.95e-44 |
|
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: 162.92 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 4 FANIAAHLPRMAQLQPDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAI 83
Cdd:cd05959 3 YNAATLVDLNLNEGRGDKTAFIDDAG--SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 84 PVLI----DPGLGIKNLKSCLAEVqpsAFIGIPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITL--DKLIQQSPDkpF 157
Cdd:cd05959 81 PVPVntllTPDDYAYYLEDSRARV---VVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLlaELVAAEAEQ--L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 158 EMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEAL-QQVYRIQPGEIDLPTFPLF-------ALFAP-ALGMTAV 228
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYaRNVLGIREDDVCFSAAKLFfayglgnSLTFPlSVGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 229 IpemdftRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVE 308
Cdd:cd05959 236 L------MPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF--GLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 309 IFTPYGATESLPV-CSIGSREIlgetrvitENGggvCIGRPVDSIRVELirisdepitVWDDDLRVAPGQVGEIVVQGPQ 387
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPGRV--------RYG---TTGKPVPGYEVEL---------RDEDGGDVADGEPGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 388 VTRGYFQRPEADLLSKisdpQGGFFhRMGDLGRQDETGRLWFCGRkTHRVESVHGpLFTIP--VEAVFNTHPLVYRSALV 465
Cdd:cd05959 368 SATMYWNNRDKTRDTF----QGEWT-RTGDKYVRDDDGFYTYAGR-ADDMLKVSG-IWVSPfeVESALVQHPAVLEAAVV 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501446872 466 GIG-PKGSQQPVICIELEQGITTN---QEQLRSELLNIAASHPHTREI 509
Cdd:cd05959 441 GVEdEDGLTKPKAFVVLRPGYEDSealEEELKEFVKDRLAPYKYPRWI 488
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
13-465 |
1.28e-43 |
|
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: 161.67 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLG 92
Cdd:cd17646 6 EQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 IKNLKSCLAEVQPSAFIGIPkAQVARLLFGWAKDSLKTIITVGPrlfwggitldkliqqSPDKPfemAVTAADDQAA-IL 171
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTA-DLAARLPAGGDVALLGDEALAAP---------------PATPP---LVPPRPDNLAyVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL------FALFAPAL-GMTAVIPEMDftrpGSVDPQK 244
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsfdvsvWELFWPLVaGARLVVARPG----GHRDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMFGSPALINRVGRSGAEQGikLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESlpvcsi 324
Cdd:cd17646 221 LAALIREHGVTTCHFVPSMLRVFLAEPAAGS--CASLRRVFCSGEALPPELAARFLALP--GAELHNLYGPTEA------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 gSREILGETRVITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADLLSK 403
Cdd:cd17646 291 -AIDVTHWPVRGPAETPSVPIGRPVPNTRL----------YVLDDALRPVPvGVPGELYLGGVQLARGYLGRPALTAERF 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501446872 404 ISDP--QGGFFHRMGDLGRQDETGRLWFCGR-------KTHRVEsvhgplftiP--VEAVFNTHPLVYRSALV 465
Cdd:cd17646 360 VPDPfgPGSRMYRTGDLARWRPDGALEFLGRsddqvkiRGFRVE---------PgeIEAALAAHPAVTHAVVV 423
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
6-467 |
1.04e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 159.68 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV 85
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 LIDP-------GLGIKNLKSCLAEVQpSAFIGIPKAQVARLLfgwakdSLKTIITV----GPRLFWGGITLDKLIQQSPD 154
Cdd:PRK07656 84 PLNTrytadeaAYILARGDAKALFVL-GLFLGVDYSATTRLP------ALEHVVICeteeDDPHTEKMKTFTDFLAAGDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 155 KPFEMAVTAaDDQAAILFTSGSTGPPKGAIYSHGN----FSAQVEALQqvyrIQPGEIDLPTFPLFALFAPALGMTA--- 227
Cdd:PRK07656 157 AERAPEVDP-DDVADILFTSGTTGRPKGAMLTHRQllsnAADWAEYLG----LTEGDRYLAANPFFHVFGYKAGVNAplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 228 ----VIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQML 303
Cdd:PRK07656 232 rgatILPLPVF------DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 304 aeGVE-IFTPYGATESLPVCSIgSReiLGETRVITENgggvCIGRPVDSirVElIRISDEpitvwdDDLRVAPGQVGEIV 382
Cdd:PRK07656 306 --GVDiVLTGYGLSEASGVTTF-NR--LDDDRKTVAG----TIGTAIAG--VE-NKIVNE------LGEEVPVGEVGELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 383 VQGPQVTRGYFQRPEADLLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVeSVHGplFTI-P--VEAVFNTHPLV 459
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDAD---GWLH-TGDLGRLDEEGYLYIVDRKKDMF-IVGG--FNVyPaeVEEVLYEHPAV 440
|
....*...
gi 501446872 460 YRSALVGI 467
Cdd:PRK07656 441 AEAAVIGV 448
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
32-466 |
3.21e-42 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 156.77 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 32 SLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIgI 111
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 112 PKAqvarllfgwakdslktiitvgprlfWGGITldklIQQSPDKPfemavtaaddqAAILFTSGSTGPPKGAIYSHGNFS 191
Cdd:cd05903 80 PER-------------------------FRQFD----PAAMPDAV-----------ALLLFTSGTTGEPKGVMHSHNTLS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 192 AQVEALQQVYRIQPGEIDLPTFPL-------FALFAPALGMTAVIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPALI 264
Cdd:cd05903 120 ASIRQYAERLGLGPGDVFLVASPMahqtgfvYGFTLPLLLGAPVVLQDIW------DPDKALALMREHGVTFMMGATPFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 265 NRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESlpvCSIGSREILGEtrvitENGGGVC 344
Cdd:cd05903 194 TDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL--GAKVCSAYGSTEC---PGAVTSITPAP-----EDRRLYT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 345 IGRPVDSIRvelIRISDepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEadlLSKISDPQGGFfhRMGDLGRQDET 424
Cdd:cd05903 264 DGRPLPGVE---IKVVD------DTGATLAPGVEGELLSRGPSVFLGYLDRPD---LTADAAPEGWF--RTGDLARLDED 329
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 501446872 425 GRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-433 |
3.52e-42 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 159.50 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 1 MPTFANIAAHLPRMAQLQPDTTAIIFPKGN--QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALF 78
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 79 KVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIGIPKAQVARLLFGWAK-DSLKTIITVGPRLFWGG---ITLDKLIQQ--- 151
Cdd:COG1022 87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElPSLRHIVVLDPRGLRDDprlLSLDELLALgre 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 152 -SPDKPFEMAVTAA--DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-------FALFAP 221
Cdd:COG1022 167 vADPAELEARRAAVkpDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLahvfertVSYYAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 ALGMTAVIPEmdftrpgsvDPQKIISAITSHKVTTMFGSP--------ALINRVGRSGA--------------------E 273
Cdd:COG1022 247 AAGATVAFAE---------SPDTLAEDLREVKPTFMLAVPrvwekvyaGIQAKAEEAGGlkrklfrwalavgrryararL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 274 QGIKLPTLQRV------------------------ISAGAPVPAVVMERFSQMlaeGVEIFTPYGATESLPVCSIGSrei 329
Cdd:COG1022 318 AGKSPSLLLRLkhaladklvfsklrealggrlrfaVSGGAALGPELARFFRAL---GIPVLEGYGLTETSPVITVNR--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 330 LGETRVITengggvcIGRPVDSIRVeliRISDEpitvwdddlrvapgqvGEIVVQGPQVTRGYFQRPE--ADLLSkisdp 407
Cdd:COG1022 392 PGDNRIGT-------VGPPLPGVEV---KIAED----------------GEILVRGPNVMKGYYKNPEatAEAFD----- 440
|
490 500
....*....|....*....|....*.
gi 501446872 408 QGGFFHrMGDLGRQDETGRLWFCGRK 433
Cdd:COG1022 441 ADGWLH-TGDIGELDEDGFLRITGRK 465
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
13-437 |
1.18e-41 |
|
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: 156.16 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGlg 92
Cdd:cd05918 7 ERARSQPDAPAVCAWDG--SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 iknlksclaevQPsafigipkaqVARLlfgwakdslKTIIT-VGPRLfwggitldkliqqspdkpfeMAVTAADDQAAIL 171
Cdd:cd05918 83 -----------HP----------LQRL---------QEILQdTGAKV--------------------VLTSSPSDAAYVI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDL----PTF--PLFALFAP-ALGMTAVIPEmDFTRPGSvdpqk 244
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfasYTFdvSILEIFTTlAAGGCLCIPS-EEDRLND----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMFGSPALINRVGRSgaeqgiKLPTLQRVISAGAPVPAVVMERFsqmlAEGVEIFTPYGATEslpvCSI 324
Cdd:cd05918 187 LAGFINRLRVTWAFLTPSVARLLDPE------DVPSLRTLVLGGEALTQSDVDTW----ADRVRLINAYGPAE----CTI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 GSReilgeTRVITENGGGVCIGRPVDSirvelirisdepiTVW-----DDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAD 399
Cdd:cd05918 253 AAT-----VSPVVPSTDPRNIGRPLGA-------------TCWvvdpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKT 314
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 501446872 400 LLSKISDP---------QGGFFHRMGDLGRQDETGRLWFCGRKTHRV 437
Cdd:cd05918 315 AAAFIEDPawlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-496 |
1.89e-41 |
|
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: 155.56 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:cd17655 7 AEKTPDHTAVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQpSAFIGIPKAQVARLLFgwakdsLKTIITVGprlfwggitlDKLIQQSPDKPFEmAVTAADDQAAILFTS 174
Cdd:cd17655 85 RIQYILEDSG-ADILLTQSHLQPPIAF------IGLIDLLD----------EDTIYHEESENLE-PVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSAQVEALQQVYrIQpGEIDlpTFPLFA----------LFAP-ALGMTAVI-PEMDFTrpgsvDP 242
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKVI-YQ-GEHL--RVALFAsisfdasvteIFASlLSGNTLYIvRKETVL-----DG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 QKIISAITSHKVTTMFGSPALINRVGRSGAEQGiklPTLQRVISAGAPVPAVVMERFSQMLAEGVEIFTPYGATESLPVC 322
Cdd:cd17655 218 QALTQYIRQNRITIIDLTPAHLKLLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 323 SIGSREilgetrVITENGGGVCIGRPVDSIRVELIrisdepitvwDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEadLL 401
Cdd:cd17655 295 SIYQYE------PETDQQVSVPIGKPLGNTRIYIL----------DQYGRPQPvGVAGELYIGGEGVARGYLNRPE--LT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 402 SK--ISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyRSALVGIGPKGSQQ 474
Cdd:cd17655 357 AEkfVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQVK-IRG--YRIelgEIEARLLQHPDI-KEAVVIARKDEQGQ 432
|
490 500
....*....|....*....|..
gi 501446872 475 PVICIELEQGITTNQEQLRSEL 496
Cdd:cd17655 433 NYLCAYIVSEKELPVAQLREFL 454
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
13-432 |
1.03e-40 |
|
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: 154.70 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIF----PKGNQSLTFQELDRLSDRICHGLIRSGiTRGTRTVLMVTPSPEFFALTFALFKVGAIPVLI- 87
Cdd:cd05931 1 RRAAARPDRPAYTFlddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 88 --DPGLGIKNLKSCLAEVQPSAFIGIPKAQVARLLFGWAKdslktiiTVGPRLFWggITLDkLIQQSPDKPFEMAVTAAD 165
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASR-------PAAGTPRL--LVVD-LLPDTSAADWPPPSPDPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEID---LPTFP----LFALFAPAL-GMTAV-IPEMDFTR 236
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVvswLPLYHdmglIGGLLTPLYsGGPSVlMSPAAFLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 pgsvDPQKIISAITSHKVTTM----FGSPALINRVGRSGAEqGIKLPTLQRVISAGAPVPAVVMERFsqmlaegVEIFTP 312
Cdd:cd05931 230 ----RPLRWLRLISRYRATISaapnFAYDLCVRRVRDEDLE-GLDLSSWRVALNGAEPVRPATLRRF-------AEAFAP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YG--------------AT--------ESLPVCSIGSREILGETRVITENGGG-----VCIGRPVDSIRVeliRISDEpit 365
Cdd:cd05931 298 FGfrpeafrpsyglaeATlfvsggppGTGPVVLRVDRDALAGRAVAVAADDPaarelVSCGRPLPDQEV---RIVDP--- 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 366 vwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAD---LLSKISDPQGGFFhRMGDLGRQDEtGRLWFCGR 432
Cdd:cd05931 372 --ETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetFGALAATDEGGWL-RTGDLGFLHD-GELYITGR 437
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
19-496 |
1.27e-40 |
|
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: 152.83 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:cd12116 1 PDATAVRD--DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAFIgipkaqvarllfgwAKDSLKTiitvgpRLFWGGITLDKLIQQSPDKPFEMAVTAADDQAA-ILFTSGST 177
Cdd:cd12116 79 ILEDAEPALVL--------------TDDALPD------RLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAyVIYTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 178 GPPKGAIYSHGNFSAQVEALQQVYRIQPGE----IDLPTF--PLFALFAPAL-GMTAVIPEMDFTRpgsvDPQKIISAIT 250
Cdd:cd12116 139 GRPKGVVVSHRNLVNFLHSMRERLGLGPGDrllaVTTYAFdiSLLELLLPLLaGARVVIAPRETQR----DPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 251 SHKVTTMFGSPALINRVGRSGAEqgiKLPTLqRVISAGAPVPAVVMERFsqmLAEGVEIFTPYGATESlPVCSIGSReil 330
Cdd:cd12116 215 AHSITVMQATPATWRMLLDAGWQ---GRAGL-TALCGGEALPPDLAARL---LSRVGSLWNLYGPTET-TIWSTAAR--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 331 getrvITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPeaDLLSK--ISDP 407
Cdd:cd12116 284 -----VTAAAGPIPIGRPLANTQV----------YVLDAALRpVPPGVPGELYIGGDGVAQGYLGRP--ALTAErfVPDP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 408 QGGFFHRM---GDLGRQDETGRLWFCGRKTHRVEsVHGplFTIP---VEAVFNTHPLVYRSALVGIGPKGSQQPVICIEL 481
Cdd:cd12116 347 FAGPGSRLyrtGDLVRRRADGRLEYLGRADGQVK-IRG--HRIElgeIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVL 423
|
490
....*....|....*
gi 501446872 482 EQGITTNQEQLRSEL 496
Cdd:cd12116 424 KAGAAPDAAALRAHL 438
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
15-442 |
4.01e-40 |
|
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: 151.25 E-value: 4.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:cd05945 1 AAANPDRPAVVE--GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIGIPkaqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaaDDQAAILFTS 174
Cdd:cd05945 79 RIREILDAAKPALLIADG----------------------------------------------------DDNAYIIFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL------FALF-APALGMTAVIPEMDFTRpgsvDPQKIIS 247
Cdd:cd05945 107 GSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFsfdlsvMDLYpALASGATLVPVPRDATA----DPKQLFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQmLAEGVEIFTPYGATESLPVCSigSR 327
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQ-RFPDARIYNTYGPTEATVAVT--YI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 328 EIlgeTRVITENGGGVCIGRPvdsirvelirISDEPITVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEadllskisD 406
Cdd:cd05945 260 EV---TPEVLDGYDRLPIGYA----------KPGAKLVILDEDGRpVPPGEKGELVISGPSVSKGYLNNPE--------K 318
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 501446872 407 PQGGFF-------HRMGDLGRQDETGRLWFCGRKTHRVEsVHG 442
Cdd:cd05945 319 TAAAFFpdegqraYRTGDLVRLEADGLLFYRGRLDFQVK-LNG 360
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
19-533 |
1.37e-39 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 149.83 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd17649 1 PDAVALVF--GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLfgwaKDSlktiitvgprlfwgGITLdkLIQQSPDKPfemavtaaddqAAILFTSGSTG 178
Cdd:cd17649 72 -------------PAERLRYML----EDS--------------GAGL--LLTHHPRQL-----------AYVIYTSGSTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLP----TFPLFA--LFAPAL-GMTAVIpemdftRPGS--VDPQKIISAI 249
Cdd:cd17649 108 TPKGVAVSHGPLAAHCQATAERYGLTPGDRELQfasfNFDGAHeqLLPPLIcGACVVL------RPDElwASADELAEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 250 TSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGApvPAVVMERFSQMLAEGVEIFTPYGATE---SLPVCSIGS 326
Cdd:cd17649 182 RELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGG--EALSPELLRRWLKAPVRLFNAYGPTEatvTPLVWKCEA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 327 REilgetrviTENGGGVCIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKIS 405
Cdd:cd17649 260 GA--------ARAGASMPIGRPLGGRSA----------YILDADLNpVPVGVTGELYIGGEGLARGYLGRPELTAERFVP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 406 DP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGIGPKGSQQPVICI 479
Cdd:cd17649 322 DPfgaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVK-IRG--FRIelgEIEAALLEHPGVREAAVVALDGAGGKQLVAYV 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 480 ELEQGITTNQ--EQLRSELlniAASHPHTREISTILFHPAFPVDIrhNAKIFREKL 533
Cdd:cd17649 399 VLRAAAAQPElrAQLRTAL---RASLPDYMVPAHLVFLARLPLTP--NGKLDRKAL 449
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
7-466 |
2.41e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 150.47 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:PRK08316 13 IGDILRRSARRYPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIGIPkAQVARLLFGWAKDSLKTII---TVGPRLFWGG-ITLDKLIQQSPDKPFEMAVt 162
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDP-ALAPTAEAALALLPVDTLIlslVLGGREAPGGwLDFADWAEAGSVAEPDVEL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGAIYSHGNFSAQ----VEALqqvyRIQPGEIDLPTFPLF------ALFAP--ALGMTAVIp 230
Cdd:PRK08316 169 ADDDLAQILYTSGTESLPKGAMLTHRALIAEyvscIVAG----DMSADDIPLHALPLYhcaqldVFLGPylYVGATNVI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 231 eMDftrpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAeGVEIF 310
Cdd:PRK08316 244 -LD-----APDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLP-GLRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 311 TPYGATESLPVCSI-GSREILGEtrvitengGGVCiGRPVdsIRVELiRISDepitvwDDDLRVAPGQVGEIVVQGPQVT 389
Cdd:PRK08316 317 NCYGQTEIAPLATVlGPEEHLRR--------PGSA-GRPV--LNVET-RVVD------DDGNDVAPGEVGEIVHRSPQLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 390 RGYFQRPE--ADLLskisdpQGGFFHRmGDLGRQDETGRLWFCGRK------------THRVEsvhgplftipvEAVFnT 455
Cdd:PRK08316 379 LGYWDDPEktAEAF------RGGWFHS-GDLGVMDEEGYITVVDRKkdmiktggenvaSREVE-----------EALY-T 439
|
490
....*....|.
gi 501446872 456 HPLVYRSALVG 466
Cdd:PRK08316 440 HPAVAEVAVIG 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-496 |
2.54e-39 |
|
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: 149.80 E-value: 2.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLG 92
Cdd:cd17651 3 RQAARTPDAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 IKNLKSCLAEVQPSAFIGIPKAQVArllfgwakdslktiitVGPRLFWGGITLDKLIQQSPDKPFEMAvTAADDQAAILF 172
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGE----------------LAVELVAVTLLDQPGAAAGADAEPDPA-LDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 173 TSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-FALFA----PAL--GMTAVIPEmDFTRPgsvDPQKI 245
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLgFDVSVqeifSTLcaGATLVLPP-EEVRT---DPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 246 ISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVpaVVMERFSQMLAE--GVEIFTPYGATE------ 317
Cdd:cd17651 220 AAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQL--VLTEDLREFCAGlpGLRLHNHYGPTEthvvta 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 -SLPVCSIGSREILGetrvitengggvcIGRPVDSIRVElirisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQR 395
Cdd:cd17651 298 lSLPGDPAAWPAPPP-------------IGRPIDNTRVY----------VLDAALRpVPPGVPGELYIGGAGLARGYLNR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 396 PEADLLSKISDPQ--GGFFHRMGDLGRQDETGRLWFCGRKTHRVeSVHGplFTIP---VEAVFNTHPLVYRSA-LVGIGP 469
Cdd:cd17651 355 PELTAERFVPDPFvpGARMYRTGDLARWLPDGELEFLGRADDQV-KIRG--FRIElgeIEAALARHPGVREAVvLAREDR 431
|
490 500
....*....|....*....|....*..
gi 501446872 470 KGSQQPVICIELEQGITTNQEQLRSEL 496
Cdd:cd17651 432 PGEKRLVAYVVGDPEAPVDAAELRAAL 458
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-467 |
3.07e-38 |
|
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: 147.21 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVD--GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIgIP--------KAQVARLLFGWAkdSLKTIITVG-PRLFwggITLDKLIQqsPDKPF 157
Cdd:COG1021 105 ALPAHRRAEISHFAEQSEAVAYI-IPdrhrgfdyRALARELQAEVP--SLRHVLVVGdAGEF---TSLDALLA--APADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 158 EMAVTAADDQAAILFTSGSTGPPKGA-------IYShgnfsaqVEALQQVYRIQPGEIDLPTFPL---FALFAPAL---- 223
Cdd:COG1021 177 SEPRPDPDDVAFFQLSGGTTGLPKLIprthddyLYS-------VRASAEICGLDADTVYLAALPAahnFPLSSPGVlgvl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 224 --GMTAVIPEmdftrpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQ 301
Cdd:COG1021 250 yaGGTVVLAP-------DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 302 ML----------AEGVEIFTPYGATEslpvcsigsreilgETRVITengggvcIGRPV---DSIRVelirisdepitVWD 368
Cdd:COG1021 323 ALgctlqqvfgmAEGLVNYTRLDDPE--------------EVILTT-------QGRPIspdDEVRI-----------VDE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 369 DDLRVAPGQVGEIVVQGPQVTRGYFQRPEADLLSkiSDPQGgfFHRMGDLGRQDETGRLWFCGRKTHRV----ESVHGPl 444
Cdd:COG1021 371 DGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARA--FTPDG--FYRTGDLVRRTPDGYLVVEGRAKDQInrggEKIAAE- 445
|
490 500
....*....|....*....|...
gi 501446872 445 ftiPVEAVFNTHPLVYRSALVGI 467
Cdd:COG1021 446 ---EVENLLLAHPAVHDAAVVAM 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
19-533 |
8.43e-38 |
|
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: 144.76 E-value: 8.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd17643 1 PEAVAVVD--EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLfgwaKDSlktiitvGPRLFwggitldkliqqspdkpfemaVTAADDQAAILFTSGSTG 178
Cdd:cd17643 72 -------------PVERIAFIL----ADS-------GPSLL---------------------LTDPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVYRIQPGEI---------DlptFPLFALFAPAL-GMTAVIPEMDFTRpgsvDPQKIISA 248
Cdd:cd17643 107 RPKGVVVSHANVLALFAATQRWFGFNEDDVwtlfhsyafD---FSVWEIWGALLhGGRLVVVPYEVAR----SPEDFARL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 249 ITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQ-MLAEGVEIFTPYGATEslpVCSIGSR 327
Cdd:cd17643 180 LRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGrFGLDRPQLVNMYGITE---TTVHVTF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 328 EILGETRVitENGGGVCIGRPVDSIRVELIrisdepitvwDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISD 406
Cdd:cd17643 257 RPLDAADL--PAAAASPIGRPLPGLRVYVL----------DADGRpVPPGVVGELYVSGAGVARGYLGRPELTAERFVAN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 407 PQGGFFHRM---GDLGRQDETGRLWFCGRKTHRVEsVHGplFTIP---VEAVFNTHPLVyRSALVGI--GPKGSQQPVIC 478
Cdd:cd17643 325 PFGGPGSRMyrtGDLARRLPDGELEYLGRADEQVK-IRG--FRIElgeIEAALATHPSV-RDAAVIVreDEPGDTRLVAY 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 479 IELEQGITTNQEQLRSELLNIAASHPHTreiSTILFHPAFPVDirHNAKIFREKL 533
Cdd:cd17643 401 VVADDGAAADIAELRALLKELLPDYMVP---ARYVPLDALPLT--VNGKLDRAAL 450
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2-491 |
2.04e-37 |
|
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: 144.68 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 2 PTFANIAAHLPRMAQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGtRTVLMVTP-SPEFFALTFALFKV 80
Cdd:cd05904 2 PTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKG-DVVLLLSPnSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 81 GAIPVLIDPglgiknlKSCLAEVQ-----PSAFIGIPKAQVARLLfgwaKDSLKTIITVGPRLFwGGITLDKLIQQSPDK 155
Cdd:cd05904 81 GAVVTTANP-------LSTPAEIAkqvkdSGAKLAFTTAELAEKL----ASLALPVVLLDSAEF-DSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 156 PFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEID-----LPTF-----PLFALFAPALGM 225
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDvflcvLPMFhiyglSSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 226 TAVIpeMdftrpGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAe 305
Cdd:cd05904 229 TVVV--M-----PRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFP- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 306 GVEIFTPYGATESLPVCSIGSREILGETRVITengggvcIGRPVDsiRVElIRISDepitvWDDDLRVAPGQVGEIVVQG 385
Cdd:cd05904 301 NVDLGQGYGMTESTGVVAMCFAPEKDRAKYGS-------VGRLVP--NVE-AKIVD-----PETGESLPPNQTGELWIRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 386 PQVTRGYFQRPEADLLSKISDpqgGFFHrMGDLGRQDETGRLWFCGR-KthrvESVHGPLFTIP---VEAVFNTHPLVYR 461
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKE---GWLH-TGDLCYIDEDGYLFIVDRlK----ELIKYKGFQVApaeLEALLLSHPEILD 437
|
490 500 510
....*....|....*....|....*....|.
gi 501446872 462 SALVGI-GPKGSQQPVICIELEQGITTNQEQ 491
Cdd:cd05904 438 AAVIPYpDEEAGEVPMAFVVRKPGSSLTEDE 468
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
33-466 |
2.90e-37 |
|
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: 142.86 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVlidPGLGiknlksclaevqpsafigip 112
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYV---PLTT-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 kaqvarlLFGwAKDSLKTIITVGPRlfwggitldkliqqspdkpfeMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSA 192
Cdd:cd05972 58 -------LLG-PKDIEYRLEAAGAK---------------------AIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 193 QVEALQQVYRIQPGEIDLPT-------FPLFALFAP-ALGMTAVIPEMDftrpgSVDPQKIISAITSHKVTTMFGSPALI 264
Cdd:cd05972 109 HIPTAAYWLGLRPDDIHWNIadpgwakGAWSSFFGPwLLGATVFVYEGP-----RFDAERILELLERYGVTSFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 265 NRVGRSGAEQGiKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLPVCsigsreilGETRVITENGGGvc 344
Cdd:cd05972 184 RMLIKQDLSSY-KFSHLRLVVSAGEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTV--------GNFPDMPVKPGS-- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 345 IGRPVDSIRVELIrisdepitvwDDDLR-VAPGQVGEIVVQ--GPQVTRGYFQRPEADlLSKISdpqGGFFHrMGDLGRQ 421
Cdd:cd05972 251 MGRPTPGYDVAII----------DDDGReLPPGEEGDIAIKlpPPGLFLGYVGDPEKT-EASIR---GDYYL-TGDRAYR 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 422 DETGRLWFCGR-----KT--HRVesvhGPLftiPVEAVFNTHPLVYRSALVG 466
Cdd:cd05972 316 DEDGYFWFVGRaddiiKSsgYRI----GPF---EVESALLEHPAVAEAAVVG 360
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
13-455 |
3.62e-37 |
|
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: 142.45 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFPkgNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLg 92
Cdd:cd17653 5 RIAAAHPDAVAVESL--GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 iknlksclaevqPSAFIGIpkaqvarllfgwakdslkTIITVGPRLFwggITLDkliqqspdkpfemavtAADDQAAILF 172
Cdd:cd17653 82 ------------PSARIQA------------------ILRTSGATLL---LTTD----------------SPDDLAYIIF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 173 TSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDL----PTFPLFA--LFApAL--GMTAVIPEMDFTrpgsvdpqk 244
Cdd:cd17653 113 TSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAqvlsIAFDACIgeIFS-TLcnGGTLVLADPSDP--------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMfgSPALINRVGRSGaeqgikLPTLQRVISAGAPVPAVVMERFSqmlaEGVEIFTPYGATEslpvCSI 324
Cdd:cd17653 183 FAHVARTVDALMS--TPSILSTLSPQD------FPNLKTIFLGGEAVPPSLLDRWS----PGRRLYNAYGPTE----CTI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 GS--REILGETRVItengggvcIGRPVDSIRvelIRISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADLLS 402
Cdd:cd17653 247 SStmTELLPGQPVT--------IGKPIPNST---CYILDA------DLQPVPEGVVGEICISGVQVARGYLGNPALTASK 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 403 KISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTIPVEAVFNT 455
Cdd:cd17653 310 FVPDPfwPGSRMYRTGDYGRWTEDGGLEFLGREDNQVK-VRG--FRINLEEIEEV 361
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-533 |
1.19e-36 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 141.42 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 34 TFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIgipk 113
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 114 aqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemaVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQ 193
Cdd:cd05971 84 -----------------------------------------------TDGSDDPALIIYTSGTTGPPKGALHAHRVLLGH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 194 VEALQQVYRIQPGEIDLPTFP--------LFALFAPAL--GMTAVIpemdfTRPGSVDPQKIISAITSHKVTTMFGSPAL 263
Cdd:cd05971 117 LPGVQFPFNLFPRDGDLYWTPadwawiggLLDVLLPSLyfGVPVLA-----HRMTKFDPKAALDLMSRYGVTTAFLPPTA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 264 INRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLPVcsIGSREILGETRviteNGGgv 343
Cdd:cd05971 192 LKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQF--GVEVNEFYGQTECNLV--IGNCSALFPIK----PGS-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 344 cIGRPVDSIRVELIRisdepitvwDDDLRVAPGQVGEIVVQGPQVTR--GYFQRPEADllskiSDPQGGFFHRMGDLGRQ 421
Cdd:cd05971 262 -MGKPIPGHRVAIVD---------DNGTPLPPGEVGEIAVELPDPVAflGYWNNPSAT-----EKKMAGDWLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 422 DETGRLWFCGRKTHRVESVH---GPlftIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEqLRSELL 497
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSSGyriGP---AEIEECLLKHPAVLMAAVVGIpDPIRGEIVKAFVVLNPGETPSDA-LAREIQ 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 501446872 498 N----IAASHPHTREIStilFHPAFPvdIRHNAKIFREKL 533
Cdd:cd05971 403 ElvktRLAAHEYPREIE---FVNELP--RTATGKIRRREL 437
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
7-467 |
1.44e-36 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 141.70 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIfpKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:cd05920 17 LGDLLARSAARHPDRIAVV--DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIGipkaqvarllfgwakdslktiitvgPRlfwggitldkliQQSPDKPFEMAVTAADD 166
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIV-------------------------PD------------RHAGFDHRALARELAES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 167 QAAI---LFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL---FALFAP------ALGMTAVIPemdf 234
Cdd:cd05920 138 IPEValfLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAahnFPLACPgvlgtlLAGGRVVLA---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 trpGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYG 314
Cdd:cd05920 214 ---PDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL--GCTLQQVFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 315 ATESLpVCSI---GSREILGETRvitengggvciGRPVDSirvelirisDEPITVWDDDLR-VAPGQVGEIVVQGPQVTR 390
Cdd:cd05920 289 MAEGL-LNYTrldDPDEVIIHTQ-----------GRPMSP---------DDEIRVVDEEGNpVPPGEEGELLTRGPYTIR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 391 GYFQRPEADllSKISDPQGgfFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd05920 348 GYYRAPEHN--ARAFTPDG--FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-509 |
1.54e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.92 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIfpKGNQSLTFQELDRLSDRICHGLI-RSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV 85
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 LIDPGLGIKNLKSCLAEVQPSAFIGIPKaqvarllFGWAKDSLKTIITVGPRlfwggITLDKLIQQSPDKPFEMAVTAAD 165
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVLFVEKT-------FQNMALSMQKVSYVQRV-----ISITSLKEIEDRKIDNFVEKNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSaqVEALQQVYRI--QPGEIDLPTFPLF-----ALFA-PALGMTAVIpemdfTRP 237
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMF--WNALNNTFAIdlTMHDRSIVLLPLFhiggiGLFAfPTLFAGGVI-----IVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 238 GSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQmlaEGVEIFTPYGATE 317
Cdd:PRK06839 223 RKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID---RGFLFGQGFGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 SLPVCSigsreILGETRVITENGGgvcIGRPVDSIRVELIRisdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPE 397
Cdd:PRK06839 300 TSPTVF-----MLSEEDARRKVGS---IGKPVLFCDYELID---------ENKNKVEVGEVGELLIRGPNVMKEYWNRPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 398 ADlLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPV 476
Cdd:PRK06839 363 AT-EETIQD---GWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRqHVKWGEIPI 437
|
490 500 510
....*....|....*....|....*....|...
gi 501446872 477 ICIELEQGITTNQEQLRSELLNIAASHPHTREI 509
Cdd:PRK06839 438 AFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEI 470
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
34-493 |
6.39e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 138.96 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 34 TFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPsafigipk 113
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGA-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 114 aqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfEMAVTaadDQAAILFTSGSTGPPKGAIYSHGNFSAQ 193
Cdd:cd05934 77 --------------------------------------------QLVVV---DPASILYTSGTTGPPKGVVITHANLTFA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 194 VEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVipemdFTRPGSVDPQKIISA------ITSHKVTTMFGSPALINRV 267
Cdd:cd05934 110 GYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAA-----LSVGATLVLLPRFSAsrfwsdVRRYGATVTNYLGAMLSYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 268 grsgAEQGIKLPTLQ---RVIsAGAPVPAVVMERFSQMLaeGVEIFTPYGATESlPVCSIGSReilGETRVITengggvC 344
Cdd:cd05934 185 ----LAQPPSPDDRAhrlRAA-YGAPNPPELHEEFEERF--GVRLLEGYGMTET-IVGVIGPR---DEPRRPG------S 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 345 IGRPVDSIRVeliRISDepitvwDDDLRVAPGQVGEIVV---QGPQVTRGYFQRPEADLLSKisdpQGGFFHrMGDLGRQ 421
Cdd:cd05934 248 IGRPAPGYEV---RIVD------DDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM----RNGWFH-TGDLGYR 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 422 DETGRLWFCGRKTH----RVESVHgplfTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLR 493
Cdd:cd05934 314 DADGFFYFVDRKKDmirrRGENIS----SAEVERAILRHPAVREAAVVAVpDEVGEDEVKAVVVLRPGETLDPEELF 386
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
19-533 |
1.35e-35 |
|
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: 138.15 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:cd17652 1 PDAPAVVF--GDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAfigipkaqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemAVTAADDQAAILFTSGSTG 178
Cdd:cd17652 79 MLADARPAL----------------------------------------------------LLTTPDNLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVYRIQPGEIDL----PTFPLFAL-FAPAL--GMTAVIPEMDFTRPGsvdpQKIISAITS 251
Cdd:cd17652 107 RPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqfasPSFDASVWeLLMALlaGATLVLAPAEELLPG----EPLADLLRE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 252 HKVTTMFGSPALINRVGRSGaeqgikLPTLQRVISAGAPVPAVVMERFSQmlaeGVEIFTPYGATESlPVCSIGSReilg 331
Cdd:cd17652 183 HRITHVTLPPAALAALPPDD------LPDLRTLVVAGEACPAELVDRWAP----GRRMINAYGPTET-TVCATMAG---- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 332 etrvITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISDPQGG 410
Cdd:cd17652 248 ----PLPGGGVPPIGRPVPGTRV----------YVLDARLRpVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 411 FFHRM---GDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyRSALVGIG--PKGSQQPVICIELE 482
Cdd:cd17652 314 PGSRMyrtGDLARWRADGQLEFLGRADDQVK-IRG--FRIelgEVEAALTEHPGV-AEAVVVVRddRPGDKRLVAYVVPA 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 501446872 483 QGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDIrhNAKIFREKL 533
Cdd:cd17652 390 PGAAPTAAELRAHL---AERLPGYMVPAAFVVLDALPLTP--NGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-533 |
6.85e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 140.86 E-value: 6.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 2 PTFANIAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVG 81
Cdd:PRK12316 508 PLQRGVHRLFEEQVERTPEAPALAF--GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 AIPVLIDPGLgiknlksclaevqpsafigiPKAQVARLLfgwaKDS----LKTIITVGPRL-FWGGIT---LDK---LIQ 150
Cdd:PRK12316 586 GAYVPLDPEY--------------------PAERLAYML----EDSgvqlLLSQSHLGRKLpLAAGVQvldLDRpaaWLE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 151 QSPDKPFEMAVTAaDDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGE---------IDLPTFPLFALFAP 221
Cdd:PRK12316 642 GYSEENPGTELNP-ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDtvlqktpfsFDVSVWEFFWPLMS 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 ALGMTAVIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQgiKLPTLQRVISAGAPVPAVVMERFSQ 301
Cdd:PRK12316 721 GARLVVAAPGDHR------DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFA 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 302 MLAEGvEIFTPYGATESlpvcsigSREILGETRViTENGGGVCIGRPVDSIRVELIrisdepitvwDDDLRVAPGQV-GE 380
Cdd:PRK12316 793 KLPQA-GLYNLYGPTEA-------AIDVTHWTCV-EEGGDSVPIGRPIANLACYIL----------DANLEPVPVGVlGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 381 IVVQGPQVTRGYFQRPEADLLSKISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNT 455
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVK-LRG--LRIelgEIEARLLE 930
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 456 HPLVYRSALVGIgpkGSQQPVICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDirHNAKIFREKL 533
Cdd:PRK12316 931 HPWVREAAVLAV---DGKQLVGYVVLESEGGDWREALKAHL---AASLPEYMVPAQWLALERLPLT--PNGKLDRKAL 1000
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
34-493 |
1.05e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 137.82 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 34 TFQELDRLSDRICHGLIRSGITRGTRtVLMVTPS-PEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEvqPSAFIGIP 112
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDR-VAIVLPNcPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFED--HGARVAIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 KAQVARLLFGWAKDS-LKTIITVG-----PRLFWGGITL---------DKLIQQSPDK-PFEMAVTAA------------ 164
Cdd:PRK05605 136 WDKVAPTVERLRRTTpLETIVSVNmiaamPLLQRLALRLpipalrkarAALTGPAPGTvPWETLVDAAiggdgsdvshpr 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 ---DDQAAILFTSGSTGPPKGAIYSHGNFSA---QVEALQQVYRIQPgEIDLPTFPLF--------ALFAPALGMTAVIp 230
Cdd:PRK05605 216 ptpDDVALILYTSGTTGKPKGAQLTHRNLFAnaaQGKAWVPGLGDGP-ERVLAALPMFhaygltlcLTLAVSIGGELVL- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 231 emdFTRPgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQ----MLAEG 306
Cdd:PRK05605 294 ---LPAP---DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKltggLLVEG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 307 veiftpYGATESLPVcsigsreILGETRVITENGGGVCIGRPvDSIrvelIRISDEPitvwDDDLRVAPGQVGEIVVQGP 386
Cdd:PRK05605 368 ------YGLTETSPI-------IVGNPMSDDRRPGYVGVPFP-DTE----VRIVDPE----DPDETMPDGEEGELLVRGP 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 387 QVTRGYFQRPEADllskisdpqGGFFH----RMGDLGRQDETGRLwfcgRKTHRVESV--HGPLFTIP--VEAVFNTHPL 458
Cdd:PRK05605 426 QVFKGYWNRPEET---------AKSFLdgwfRTGDVVVMEEDGFI----RIVDRIKELiiTGGFNVYPaeVEEVLREHPG 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 501446872 459 VYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLR 493
Cdd:PRK05605 493 VEDAAVVGLpREDGSEEVVAAVVLEPGAALDPEGLR 528
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
32-466 |
1.35e-34 |
|
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: 135.30 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 32 SLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLksclaevqpsAFIgi 111
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL----------EYI-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 112 pkaqvarllfgwAKDSLKTIITVGPRLfwggitldkliqqspdkpfemavtaaDDQAAILFTSGSTGPPKGAIYSHGNFS 191
Cdd:cd05935 69 ------------LNDSGAKVAVVGSEL--------------------------DDLALIPYTSGTTGLPKGCMHTHFSAA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 192 AQVEALQQVYRIQPGEIDLPTFPLF--ALFAPALgMTAVIPEMDFTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGR 269
Cdd:cd05935 111 ANALQSAVWTGLTPSDVILACLPLFhvTGFVGSL-NTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 270 SGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLPVCSIGSREILGETrvitengggvCIGRPV 349
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT--GLRFVEGYGLTETMSQTHTNPPLRPKLQ----------CLGIP* 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 350 DSIRVELIRISdepitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISDpQGGFFHRMGDLGRQDETGRLWF 429
Cdd:cd05935 258 FGVDARVIDIE--------TGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEGYFFF 328
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501446872 430 CGRkTHRVESVHGplFTI---PVEAVFNTHPLVYRSALVG 466
Cdd:cd05935 329 VDR-VKRMINVSG--FKVwpaEVEAKLYKHPAI*EVCVIS 365
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-533 |
1.50e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDP----- 89
Cdd:PRK12316 2013 AARAPEAIAVVF--GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPnypae 2090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 ---------GLGIKNLKSCLAEVQPsafigiPKAQVARLLFgwakdslktiitvgprlfwggiTLDKLIQQSPDKPFEMA 160
Cdd:PRK12316 2091 rlaymledsGAALLLTQRHLLERLP------LPAGVARLPL----------------------DRDAEWADYPDTAPAVQ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 161 vTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLpTFPLFA-------LFAPALGMTAVIpemd 233
Cdd:PRK12316 2143 -LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCEL-QFMSFSfdgaheqWFHPLLNGARVL---- 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 234 fTRPGSV-DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGiKLPTLQRVISAGAPVPAVVMERFSQMLaEGVEIFTP 312
Cdd:PRK12316 2217 -IRDDELwDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCFGGEAVPAASLRLAWEAL-RPVYLFNG 2293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YGATESLPVCSIGSREilgetRVITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVVQGPQVTRG 391
Cdd:PRK12316 2294 YGPTEAVVTPLLWKCR-----PQDPCGAAYVPIGRALGNRRA----------YILDADLNlLAPGMAGELYLGGEGLARG 2358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 392 YFQRPEADLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALV 465
Cdd:PRK12316 2359 YLNRPGLTAERFVPDPfsaSGERLYRTGDLARYRADGVVEYLGRIDHQVK-IRG--FRIelgEIEARLQAHPAVREAVVV 2435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 466 GIGPKGSQQPVICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDirHNAKIFREKL 533
Cdd:PRK12316 2436 AQDGASGKQLVAYVVPDDAAEDLLAELRAWL---AARLPAYMVPAHWVVLERLPLN--PNGKLDRKAL 2498
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
11-467 |
3.94e-34 |
|
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: 134.94 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPG 90
Cdd:cd05923 7 LRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 91 LGIKNLKSCLAEVQPSAFIGIPKAQVARllfgwakdslkTIITVGPRLFWGGITLDKLIQQSPDKPFEMAVTAADDQAAI 170
Cdd:cd05923 87 LKAAELAELIERGEMTAAVIAVDAQVMD-----------AIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 171 LFTSGSTGPPKGAIYSHGNFSAQVEAL--QQVYRIQPGEIDLPTFPL------FALFAPAL--GMTAVIPEMDftrpgsv 240
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLyhvigfFAVLVAALalDGTYVVVEEF------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQML-AEGVEIftpYGATESL 319
Cdd:cd05923 229 DPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLpGEKVNI---YGTTEAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 320 pvcsigsreilgeTRVITENGGGVCIGRPVDSIRVELIRISDEPitvwddDLRVAPGQVGEIVV--QGPQVTRGYFQRPE 397
Cdd:cd05923 306 -------------NSLYMRDARTGTEMRPGFFSEVRIVRIGGSP------DEALANGEEGELIVaaAADAAFTGYLNQPE 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501446872 398 ADlLSKISDPqggfFHRMGDLGRQDETGRLWFCGRKTHRV----ESVHgplfTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd05923 367 AT-AKKLQDG----WYRTGDVGYVDPSGDVRILGRVDDMIisggENIH----PSEIERVLSRHPGVTEVVVIGV 431
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
19-534 |
5.07e-34 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 134.75 E-value: 5.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRtVLMVTPSPEFFALTF-ALFKVGAIPVLIDPGLGIKNLK 97
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDR-VAIALPNGLEFVVAFlAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 98 SCLAEVQPSAFI----GIPKAQVARLLFGWAKDSLKTIITVGPRLF----WGGITLDKLIQQSPDKPFEmavtaaDDQAA 169
Cdd:cd05926 80 FYLADLGSKLVLtpkgELGPASRAASKLGLAILELALDVGVLIRAPsaesLSNLLADKKNAKSEGVPLP------DDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALFAP-ALGMTAVIPEmdftrpgSVD 241
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFhvhglvaSLLSTlAAGGSVVLPP-------RFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 242 PQKIISAITSHKVT------TMfgSPALINrvgRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGA 315
Cdd:cd05926 227 ASTFWPDVRDYNATwytavpTI--HQILLN---RPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF--GAPVLEAYGM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 316 TESLPvcSIGSREILGETRVItengGGVciGRPVDsirVElIRISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQR 395
Cdd:cd05926 300 TEAAH--QMTSNPLPPGPRKP----GSV--GKPVG---VE-VRILDE------DGEILPPGVVGEICLRGPNVTRGYLNN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 396 PEAdllSKISDPQGGFFhRMGDLGRQDETGRLWFCGRKTHRV----ESVhGPLftiPVEAVFNTHPLVYRSALVGI-GPK 470
Cdd:cd05926 362 PEA---NAEAAFKDGWF-RTGDLGYLDADGYLFLTGRIKELInrggEKI-SPL---EVDGVLLSHPAVLEAVAFGVpDEK 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 471 GSQQPVICIELEQGITTNQEQLRSELL-NIAASHPHTReistILFHPAFPvdirHNA--KIFREKLA 534
Cdd:cd05926 434 YGEEVAAAVVLREGASVTEEELRAFCRkHLAAFKVPKK----VYFVDELP----KTAtgKIQRRKVA 492
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-494 |
5.17e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.70 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK03640 12 AFLTPDRTAIEF--EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEvqpsafigipkAQVARLLfgwAKDSLKTIITVGPRlfwggITLDKLIQQSPDKPFEMAVTAADDQAAILFTS 174
Cdd:PRK03640 90 ELLWQLDD-----------AEVKCLI---TDDDFEAKLIPGIS-----VKFAELMNGPKEEAEIQEEFDLDEVATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGN--FSAQVEALQQVYRiqpgEID--LPTFPLFALFAPALGMTAVIPEMDFTRPGSVDPQKIISAIT 250
Cdd:PRK03640 151 GTTGKPKGVIQTYGNhwWSAVGSALNLGLT----EDDcwLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 251 SHKVTTMFGSPA----LINRVGRSGAEqgiklPTLQRVISAGAPVPAVVMErfsQMLAEGVEIFTPYGATE-SLPVCSIG 325
Cdd:PRK03640 227 TGGVTIISVVSTmlqrLLERLGEGTYP-----SSFRCMLLGGGPAPKPLLE---QCKEKGIPVYQSYGMTEtASQIVTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 326 SREILgeTRVitengGGVciGRPVDSIRvelIRISdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAdLLSKIS 405
Cdd:PRK03640 299 PEDAL--TKL-----GSA--GKPLFPCE---LKIE-------KDGVVVPPFEEGEIVVKGPNVTKGYLNREDA-TRETFQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 406 DpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQG 484
Cdd:PRK03640 359 D---GWFK-TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVpDDKWGQVPVAFVVKSGE 434
|
490
....*....|
gi 501446872 485 ITtnQEQLRS 494
Cdd:PRK03640 435 VT--EEELRH 442
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
33-509 |
6.39e-34 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 133.78 E-value: 6.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDpglgiknlksclaevqpSAFIgiP 112
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLF-----------------SAFG--P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 KAQVARLLFGWAKDSLKTiitvgPRLfwggitLDKliqqspdkpfemavTAADDQAAILFTSGSTGPPKGAIYSHGNFSA 192
Cdd:cd05969 62 EAIRDRLENSEAKVLITT-----EEL------YER--------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 193 QVEALQQVYRIQPGEI-----DlP---TFPLFALFAPAL-GMTAVIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPAL 263
Cdd:cd05969 117 YYFTGKYVLDLHPDDIywctaD-PgwvTGTVYGIWAPWLnGVTNVVYEGRF------DAESWYGIIERVKVTVWYTAPTA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 264 INRVGRSGAE--QGIKLPTLQRVISAGAPV-PAVV---MERFsqmlaeGVEIFTPYGATESlpvcsiGSREILGETRVIT 337
Cdd:cd05969 190 IRMLMKEGDElaRKYDLSSLRFIHSVGEPLnPEAIrwgMEVF------GVPIHDTWWQTET------GSIMIANYPCMPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 338 ENGGgvcIGRPVDSIRVELIRISDEPitvwdddlrVAPGQVGEIVVQG--PQVTRGYFQRPEAdllSKISDPQGgfFHRM 415
Cdd:cd05969 258 KPGS---MGKPLPGVKAAVVDENGNE---------LPPGTKGILALKPgwPSMFRGIWNDEER---YKNSFIDG--WYLT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 416 GDLGRQDETGRLWFCGR-----KT--HRVesvhGPlftIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITT 487
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRaddiiKTsgHRV----GP---FEVESALMEHPAVAEAGVIGKpDPLRGEIIKAFISLKEGFEP 393
|
490 500
....*....|....*....|....*.
gi 501446872 488 NqEQLRSELLNIA----ASHPHTREI 509
Cdd:cd05969 394 S-DELKEEIINFVrqklGAHVAPREI 418
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
22-533 |
6.43e-34 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 133.36 E-value: 6.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 22 TAIIFPkgNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPglgiknlkscla 101
Cdd:cd05919 2 TAFYAA--DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 102 EVQPSAFIGIPKAQVARLLfgwakdslktiitvgprlfwggitldkliqqspdkpfemaVTAADDQAAILFTSGSTGPPK 181
Cdd:cd05919 68 LLHPDDYAYIARDCEARLV----------------------------------------VTSADDIAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 182 GAIYSHGNFSAQVEAL-QQVYRIQPGEIDLPTFPLF-------ALFAP-ALGMTAVIpemdftRPGSVDPQKIISAITSH 252
Cdd:cd05919 108 GVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFfgyglgnSLWFPlAVGASAVL------NPGWPTAERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 253 KVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFsqMLAEGVEIFTPYGATESLPVcSIGSREilGE 332
Cdd:cd05919 182 RPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERW--MEHFGGPILDGIGATEVGHI-FLSNRP--GA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 333 TRVitenggGVCiGRPVDSIRVELirisdepitVWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEadllSKISDPQGGFF 412
Cdd:cd05919 257 WRL------GST-GRPVPGYEIRL---------VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPE----KSRATFNGGWY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 413 hRMGDLGRQDETGRLWFCGRkTHRVESVHGpLFTIP--VEAVFNTHPLVYRSALVGIgPKGSQ--QPVICIELEQGITTN 488
Cdd:cd05919 317 -RTGDKFCRDADGWYTHAGR-ADDMLKVGG-QWVSPveVESLIIQHPAVAEAAVVAV-PESTGlsRLTAFVVLKSPAAPQ 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501446872 489 Q---EQLRSELLNIAASHPHTReisTILFHPAFPVDirHNAKIFREKL 533
Cdd:cd05919 393 EslaRDIHRHLLERLSAHKVPR---RIAFVDELPRT--ATGKLQRFKL 435
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
13-496 |
3.53e-33 |
|
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: 132.32 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLg 92
Cdd:cd12117 5 EQAARTPDAVAVVY--GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 iknlksclaevqPsafigipkaqVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMAVTA----ADDQA 168
Cdd:cd12117 82 ------------P----------AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAvpvsPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 169 AILFTSGSTGPPKGAIYSHGNFSAQVeaLQQVYR-IQPGEIDLPTFPL------FALFAPAL-GMTAVIPEMDFTRpgsv 240
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGVVRLV--KNTNYVtLGPDDRVLQTSPLafdastFEIWGALLnGARLVLAPKGTLL---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQgikLPTLQRVISAG--APVPAV--VMERfsqmlAEGVEIFTPYGAT 316
Cdd:cd12117 214 DPDALGALIAEEGVTVLWLTAALFNQLADEDPEC---FAGLRELLTGGevVSPPHVrrVLAA-----CPGLRLVNGYGPT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 317 ESLpVCSIGSReilgeTRVITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLRVAP-GQVGEIVVQGPQVTRGYFQR 395
Cdd:cd12117 286 ENT-TFTTSHV-----VTELDEVAGSIPIGRPIANTRV----------YVLDEDGRPVPpGVPGELYVGGDGLALGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 396 PEADLLSKISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyRSALVGIGPK 470
Cdd:cd12117 350 PALTAERFVADPfgPGERLYRTGDLARWLPDGRLEFLGRIDDQVK-IRG--FRIelgEIEAALRAHPGV-REAVVVVRED 425
|
490 500
....*....|....*....|....*...
gi 501446872 471 GSQQPVIC--IELEQGITTnqEQLRSEL 496
Cdd:cd12117 426 AGGDKRLVayVVAEGALDA--AELRAFL 451
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-466 |
3.54e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 132.95 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFPKGNqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:PRK06087 37 PDKIAVVDNHGA-SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAFIG---IPKAQVARLLFGWAKD--SLKTIITV---GPRLfwGGITLDKLIQQSPdkPFEMAVTA-ADDQAA 169
Cdd:PRK06087 116 VLNKCQAKMFFAptlFKQTRPVDLILPLQNQlpQLQQIVGVdklAPAT--SSLSLSQIIADYE--PLTTAITThGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGN-------FSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTrpgsvdP 242
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNilaseraYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT------P 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 QKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQmlaEGVEIFTPYGATESLPVC 322
Cdd:PRK06087 266 DACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTESSPHA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 323 SIGSREILGETrvitenggGVCIGRPVDSIRVeliRISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRPEadLLS 402
Cdd:PRK06087 343 VVNLDDPLSRF--------MHTDGYAAAGVEI---KVVDE------ARKTLPPGCEGEEASRGPNVFMGYLDEPE--LTA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 403 KISDPQGGFFHrmGDLGRQDETGRLWFCGRKTHRVesVHG--PLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:PRK06087 404 RALDEEGWYYS--GDLCRMDEAGYIKITGRKKDII--VRGgeNISSREVEDILLQHPKIHDACVVA 465
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-534 |
1.17e-32 |
|
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: 130.25 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 53 GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIdpglgiknlkscLAEVQPSAfigipKAQVARLLFgwAKDSLKTII 132
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLV------------FVPLNPTL-----KESVLRYLV--ADAGGRIVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 133 TVGPrlfwGGITLDKLIQQSPD--------------KPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQ 198
Cdd:cd05922 75 ADAG----AADRLRDALPASPDpgtvldadgiraarASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 199 QVYRIQPGEIDLPTFPL-----FALFAPAL--GMTAVIpemdftRPGSVDPQKIISAITSHKVTTMFGSP---ALINRVG 268
Cdd:cd05922 151 EYLGITADDRALTVLPLsydygLSVLNTHLlrGATLVL------TNDGVLDDAFWEDLREHGATGLAGVPstyAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 269 RSGAeqgiKLPTLQRVISAGAPVPAVVMERFSQmLAEGVEIFTPYGATESLPVCSigsreILGETRVITENGGgvcIGRP 348
Cdd:cd05922 225 FDPA----KLPSLRYLTQAGGRLPQETIARLRE-LLPGAQVYVMYGQTEATRRMT-----YLPPERILEKPGS---IGLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 349 VDSIRVELIRisdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADLlskiSDPQGGFFHRMGDLGRQDETGRLW 428
Cdd:cd05922 292 IPGGEFEILD---------DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRR----KEGRGGGVLHTGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 429 FCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIGPKGSQQPVICIELEQGITtnqeqlrsellniaaSHPHTRE 508
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKID---------------PKDVLRS 423
|
490 500 510
....*....|....*....|....*....|....
gi 501446872 509 ISTILFHPAFPVDIR--------HNAKIFREKLA 534
Cdd:cd05922 424 LAERLPPYKVPATVRvvdelpltASGKVDYAALR 457
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
31-466 |
1.20e-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: 130.02 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlksclaevqpsafig 110
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTS------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 iPKAQVARLLfgwaKDSLKTIITVGprlfwggitldkliqqspdkpfemavtAADDQAAILFTSGSTGPPKGAIYSHGNF 190
Cdd:cd05907 65 -SAEQIAYIL----NDSEAKALFVE---------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 191 SAQVEALQQVYRIQPGEIDLPTFPL-------FALFAP-ALGMTAVIPEmdftrpgsvDPQKIISAITSHKVTTMFGSP- 261
Cdd:cd05907 113 LSNALALAERLPATEGDRHLSFLPLahvferrAGLYVPlLAGARIYFAS---------SAETLLDDLSEVRPTVFLAVPr 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 262 ------ALINRVGRSGAEQGI----KLPTLQRVISAGAPVPAVVMERFSQMlaeGVEIFTPYGATESLPVCSIgsreilg 331
Cdd:cd05907 184 vwekvyAAIKVKAVPGLKRKLfdlaVGGRLRFAASGGAPLPAELLHFFRAL---GIPVYEGYGLTETSAVVTL------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 332 eTRVITENGGgvCIGRPVDSIRVeliRISDEpitvwdddlrvapgqvGEIVVQGPQVTRGYFQRPEADLLSKISDpqgGF 411
Cdd:cd05907 254 -NPPGDNRIG--TVGKPLPGVEV---RIADD----------------GEILVRGPNVMLGYYKNPEATAEALDAD---GW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 412 FHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFT-IPVEAVFNTHPLVYRSALVG 466
Cdd:cd05907 309 LH-TGDLGEIDEDGFLHITGRKKDLIITSGGKNISpEPIENALKASPLISQAVVIG 363
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
7-467 |
1.30e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 131.33 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFPKGN----QSLTFQELDRLSDRICHGLIRSGITRGtRTVLMVTPSP-EFFALTFALFKVG 81
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRG-DVVSCQLPNWwEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 AIPVLIDPGLGIKNLKSCLAEVQPSAFIgIPK--------AQVARLLFGWAkdSLKTIITVGPRlfwGGITLDKLI---- 149
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLV-VPKtfrgfdhaAMARRLRPELP--ALRHVVVVGGD---GADSFEALLitpa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 150 -QQSPDKPFEMAVTA--ADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-------FALF 219
Cdd:PRK13295 179 wEQEPDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMahqtgfmYGLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 220 AP-ALGMTAVIPEmdftrpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMER 298
Cdd:PRK13295 259 MPvMLGATAVLQD-------IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 299 FSQMLaeGVEIFTPYGATESLPVCSIG---SREILGETRvitengggvciGRPVDSIRvelIRISDepitvwDDDLRVAP 375
Cdd:PRK13295 332 ARAAL--GAKIVSAWGMTENGAVTLTKlddPDERASTTD-----------GCPLPGVE---VRVVD------ADGAPLPA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 376 GQVGEIVVQGPQVTRGYFQRPEADLlskiSDPQGGFfhRMGDLGRQDETGRLWFCGRkTHRVESVHGPlfTIPV---EAV 452
Cdd:PRK13295 390 GQIGRLQVRGCSNFGGYLKRPQLNG----TDADGWF--DTGDLARIDADGYIRISGR-SKDVIIRGGE--NIPVveiEAL 460
|
490
....*....|....*
gi 501446872 453 FNTHPLVYRSALVGI 467
Cdd:PRK13295 461 LYRHPAIAQVAIVAY 475
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
6-501 |
1.58e-32 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 131.55 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAH-LPRMAQLQPDTTAIIF--PKGNQS--LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKV 80
Cdd:cd17634 53 NLAANaLDRHLRENGDRTAIIYegDDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 81 GAIPVLIDPGLGIKNLKSCLAEVQPSAFI----------GIP-KAQVARLLFGWAKdSLKTIITV----------GPRLF 139
Cdd:cd17634 133 GAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrSVPlKKNVDDALNPNVT-SVEHVIVLkrtgsdidwqEGRDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 140 WggitLDKLIQQSPDKpFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFS-AQVEALQQVYRIQPGEIDLPTFPL--- 215
Cdd:cd17634 212 W----WRDLIAKASPE-HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLvYAATTMKYVFDYGPGDIYWCTADVgwv 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 216 ----FALFAP-ALGMTAVIPEmdfTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSG--AEQGIKLPTLQRVISAG 288
Cdd:cd17634 287 tghsYLLYGPlACGATTLLYE---GVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGddAIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 289 APVPAVVMERFSQMLA-EGVEIFTPYGATE-SLPVCSIgsreilgetRVITENGGGVCIGRPVDSIRVELIRISDEPitv 366
Cdd:cd17634 364 EPINPEAYEWYWKKIGkEKCPVVDTWWQTEtGGFMITP---------LPGAIELKAGSATRPVFGVQPAVVDNEGHP--- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 367 wdddlrVAPGQVGEIVVQG--PQVTRGYFQRPEADLLSKISDPQGGFFHrmGDLGRQDETGRLWFCGRKTHRVESVHGPL 444
Cdd:cd17634 432 ------QPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFSTFKGMYFS--GDGARRDEDGYYWITGRSDDVINVAGHRL 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 445 FTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEqLRSELLNIAA 501
Cdd:cd17634 504 GTAEIESVLVAHPKVAEAAVVGIpHAIKGQAPYAYVVLNHGVEPSPE-LYAELRNWVR 560
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
19-497 |
2.05e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 129.51 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd17650 1 PDAIAVSD--ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLfgwakdslktiitvgprlfwggitldkliqqsPDKPFEMAVTAADDQAAILFTSGSTG 178
Cdd:cd17650 72 -------------PAERLQYML--------------------------------EDSGAKLLLTQPEDLAYVIYTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVY---RIQPGEIDLPTFPL---FALFAPAL--GMTAVIpemdFTRPGSVDPQKIISAIT 250
Cdd:cd17650 107 KPKGVMVEHRNVAHAAHAWRREYeldSFPVRLLQMASFSFdvfAGDFARSLlnGGTLVI----CPDEVKLDPAALYDLIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 251 SHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVI----SAGAPVPAVVMERFSQmlaeGVEIFTPYGATESlpvcSIGS 326
Cdd:cd17650 183 KSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIvgsdGCKAQDFKTLAARFGQ----GMRIINSYGVTEA----TIDS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 327 rEILGETRVITENGGGVCIGRPVDSIRvelirisdepITVWDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADLLSKIS 405
Cdd:cd17650 255 -TYYEEGRDPLGDSANVPIGRPLPNTA----------MYVLDERLQPQPvGVAGELYIGGAGVARGYLNRPELTAERFVE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 406 DP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyRSALVGIGPKGSQQPVICIE 480
Cdd:cd17650 324 NPfaPGERMYRTGDLARWRADGNVELLGRVDHQVK-IRG--FRIelgEIESQLARHPAI-DEAVVAVREDKGGEARLCAY 399
|
490
....*....|....*..
gi 501446872 481 LEQGITTNQEQLRSELL 497
Cdd:cd17650 400 VVAAATLNTAELRAFLA 416
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
20-466 |
2.12e-32 |
|
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: 129.33 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 20 DTTAIIFPkgNQSLTFQELDRLSDRICHGLIRSG-ITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:cd05941 1 DRIAIVDD--GDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAFIgipkaqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaadDQAAILFTSGSTG 178
Cdd:cd05941 79 VITDSEPSLVL--------------------------------------------------------DPALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALFAPALGMTAVIpemdFTRPGSVDPQKIISAits 251
Cdd:cd05941 103 RPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHhvhglvnALLCPLFAGASVE----FLPKFDPKEVAISRL--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 252 HKVTTMF-GSPALINRV-------------GRSGAEQGIKLptlqrVISAGAPVPAVVMERFSQmlAEGVEIFTPYGATE 317
Cdd:cd05941 176 MPSITVFmGVPTIYTRLlqyyeahftdpqfARAAAAERLRL-----MVSGSAALPVPTLEEWEA--ITGHTLLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 SLPVCSIGSReilGETRvitenGGGVciGRPVDSIRVeliRISDEpitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPE 397
Cdd:cd05941 249 IGMALSNPLD---GERR-----PGTV--GMPLPGVQA---RIVDE-----ETGEPLPRGEVGEIQVRGPSVFKEYWNKPE 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 398 AdllSKISDPQGGFFhRMGDLGRQDETGRLWFCGRKTHRVESVHG-PLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:cd05941 311 A---TKEEFTDDGWF-KTGDLGVVDEDGYYWILGRSSVDIIKSGGyKVSALEIERVLLAHPGVSECAVIG 376
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
13-533 |
7.67e-32 |
|
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: 127.82 E-value: 7.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIfpKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPglg 92
Cdd:cd12115 7 AQAARTPDAIALV--CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 iknlksclaevqpsafigipKAQVARLLFgwakdslkTIITVGPRLfwggitldkliqqspdkpfemAVTAADDQAAILF 172
Cdd:cd12115 82 --------------------AYPPERLRF--------ILEDAQARL---------------------VLTDPDDLAYVIY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 173 TSGSTGPPKGAIYSHGN-----------FSAqvEALQQVYRIQPGEIDLPtfpLFALFAP-ALGMTAVIPEmdftrpgsv 240
Cdd:cd12115 113 TSGSTGRPKGVAIEHRNaaaflqwaaaaFSA--EELAGVLASTSICFDLS---VFELFGPlATGGKVVLAD--------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 dpqkiisaitshKVTTMFGSPA-----LINRVGRSGAE--QGIKLPTLQRVIS-AGAPVPAVVMERFsQMLAEGVEIFTP 312
Cdd:cd12115 179 ------------NVLALPDLPAaaevtLINTVPSAAAEllRHDALPASVRVVNlAGEPLPRDLVQRL-YARLQVERVVNL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YGATESLPVCSIgsreilgeTRVITENGGGVCIGRPVDSIRVELIRISDEPitvwdddlrVAPGQVGEIVVQGPQVTRGY 392
Cdd:cd12115 246 YGPSEDTTYSTV--------APVPPGASGEVSIGRPLANTQAYVLDRALQP---------VPLGVPGELYIGGAGVARGY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 393 FQRPEADLLSKISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGI 467
Cdd:cd12115 309 LGRPGLTAERFLPDPfgPGARLYRTGDLVRWRPDGLLEFLGRADNQVK-VRG--FRIelgEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 468 GPK-GSQQPVICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDirHNAKIFREKL 533
Cdd:cd12115 386 GDAaGERRLVAYIVAEPGAAGLVEDLRRHL---GTRLPAYMVPSRFVRLDALPLT--PNGKIDRSAL 447
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
6-520 |
8.28e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 128.62 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV 85
Cdd:PRK07470 8 NLAHFLRQAARRFPDRIALVW--GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 lidPglgiKNLKSCLAEVqpsAFIGipKAQVARLLFGWA--KDSLKTIITVGPRLFW--------GGITLDKLIQQSPDK 155
Cdd:PRK07470 86 ---P----TNFRQTPDEV---AYLA--EASGARAMICHAdfPEHAAAVRAASPDLTHvvaiggarAGLDYEALVARHLGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 156 PFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGnfsaqvealQQVYRIQ-------PG--EID--LPTFPL------FAL 218
Cdd:PRK07470 154 RVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG---------QMAFVITnhladlmPGttEQDasLVVAPLshgagiHQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 219 FAPALGMTAVIPEMDftrpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPvpavvMER 298
Cdd:PRK07470 225 CQVARGAATVLLPSE-----RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAP-----MYR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 299 FSQMLAE---GVEIFTPYGateslpvcsigsreiLGE-TRVIT---------ENGGGVCI---GRPVDSIRVElirisde 362
Cdd:PRK07470 295 ADQKRALaklGKVLVQYFG---------------LGEvTGNITvlppalhdaEDGPDARIgtcGFERTGMEVQ------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 363 pitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKisdpQGGFFhRMGDLGRQDETGRLWFCGRKTHRVESVH 441
Cdd:PRK07470 353 ---IQDDEGReLPPGETGEICVIGPAVFAGYYNNPEANAKAF----RDGWF-RTGDLGHLDARGFLYITGRASDMYISGG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 442 GPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRSELLNIAASHPHTREistILFHPAFPV 520
Cdd:PRK07470 425 SNVYPREIEEKLLTHPAVSEVAVLGVpDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKR---FFFWDALPK 501
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-471 |
1.15e-31 |
|
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: 127.77 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIfpKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd12114 1 PDATAVI--CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQ------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLfgwAKDSLKTIITVGPRLFWGGITLDKLIQ----QSPDKPFEMAVTAADDQAAILFTS 174
Cdd:cd12114 72 -------------PAARREAIL---ADAGARLVLTDGPDAQLDVAVFDVLILdldaLAAPAPPPPVDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEI---------DLPTFPLFALFapALGMTAVIPEMDFTRpgsvDPQKI 245
Cdd:cd12114 136 GSTGTPKGVMISHRAALNTILDINRRFAVGPDDRvlalsslsfDLSVYDIFGAL--SAGATLVLPDEARRR----DPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 246 ISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGvEIFTPYGATESlpvcSIG 325
Cdd:cd12114 210 AELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDA-RLISLGGATEA----SIW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 326 SreILGETRVITENGGGVCIGRPVDSIRVElirisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLLSKI 404
Cdd:cd12114 285 S--IYHPIDEVPPDWRSIPYGRPLANQRYR----------VLDPRGRdCPDWVPGELWIGGRGVALGYLGDPELTAARFV 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 405 SDPQGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTIP---VEAVFNTHPLVYRSALVGIGPKG 471
Cdd:cd12114 353 THPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVK-VRG--YRIElgeIEAALQAHPGVARAVVVVLGDPG 419
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-493 |
1.61e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 128.35 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIGIPK-------AQVARLLFGWAKDS-----------LKTIITVGPRLFWGGITLDKL 148
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICADAfktsdyhAMLQELLPGLAEGQpgalacerlpeLRGVVSLAPAPPPGFLAWHEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 149 IQQ----SPDKPFEM-AVTAADDQAAILFTSGSTGPPKGAIYSHGN------FSAQVEALQQVYRIQpgeIDLPTFPLFA 217
Cdd:PRK12583 180 QARgetvSREALAERqASLDRDDPINIQYTSGTTGFPKGATLSHHNilnngyFVAESLGLTEHDRLC---VPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 218 -----LFAPALGMTAVIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVP 292
Cdd:PRK12583 257 mvlanLGCMTVGACLVYPNEAF------DPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 293 AVVMER-FSQMlaEGVEIFTPYGATESLPVCSIGSREILGETRVITengggvcIGRPVDSIRVELIRISDEPitvwdddl 371
Cdd:PRK12583 331 IEVMRRvMDEM--HMAEVQIAYGMTETSPVSLQTTAADDLERRVET-------VGRTQPHLEVKVVDPDGAT-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 372 rVAPGQVGEIVVQGPQVTRGYFQRPEADLLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVesVHGPLFTIP--V 449
Cdd:PRK12583 394 -VPRGEIGELCTRGYSVMKGYWNNPEATAESIDED---GWMH-TGDLATMDEQGYVRIVGRSKDMI--IRGGENIYPreI 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 501446872 450 EAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLR 493
Cdd:PRK12583 467 EEFLFTHPAVADVQVFGVpDEKYGEEIVAWVRLHPGHAASEEELR 511
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
5-484 |
3.68e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 127.22 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 5 ANIAAHLPRMAQLQPDTTAIIFpkGNQSLTFQEL--DRLSdrICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PLN02860 7 AHICQCLTRLATLRGNAVVTIS--GNRRRTGHEFvdGVLS--LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLIDPGLGIKNLKSCLAEVQPSAFIG-------IPKAQVARL-LFGWA--KDSLKTIITVGPRLFwggITLDKLIQQS 152
Cdd:PLN02860 83 IVAPLNYRWSFEEAKSAMLLVRPVMLVTdetcsswYEELQNDRLpSLMWQvfLESPSSSVFIFLNSF---LTTEMLKQRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 153 PDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQveALQQVYRIQPGEID--LPTFPLFAL--FAPALGMTAV 228
Cdd:PLN02860 160 LGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQ--SLAKIAIVGYGEDDvyLHTAPLCHIggLSSALAMLMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 229 ------IPEMdftrpgsvDPQKIISAITSHKVTTMFGSPAL---INRVGRSgAEQGIKLPTLQRVISAGAPVPAVVMERF 299
Cdd:PLN02860 238 gachvlLPKF--------DAKAALQAIKQHNVTSMITVPAMmadLISLTRK-SMTWKVFPSVRKILNGGGSLSSRLLPDA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 300 SQMLAEGvEIFTPYGATES--------LPVCSIGSREILGETRVITENG-----GGVCIGRPvdSIRVELIRISDEPITv 366
Cdd:PLN02860 309 KKLFPNA-KLFSAYGMTEAcssltfmtLHDPTLESPKQTLQTVNQTKSSsvhqpQGVCVGKP--APHVELKIGLDESSR- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 367 wdddlrvapgqVGEIVVQGPQVTRGYFQRPeadlLSKISDPQGGFFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFT 446
Cdd:PLN02860 385 -----------VGRILTRGPHVMLGYWGQN----SETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYP 449
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 501446872 447 IPVEAVFNTHPLVYRSALVGIgPKG--SQQPVICIELEQG 484
Cdd:PLN02860 450 EEVEAVLSQHPGVASVVVVGV-PDSrlTEMVVACVRLRDG 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-533 |
2.75e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.81 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 2 PTFANIAAHLP------RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTF 75
Cdd:PRK12467 3086 ATAAAYPSERLvhqlieAQVARTPEAPALVF--GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 76 ALFKVGAIPVLIDPGLGIKNLkscLAEVQPSAfIGIPKAQvARLLfgwakDSLKtIITVGPRLFWGGITLDKLIQQSPDk 155
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYPRERL---AYMIEDSG-VKLLLTQ-AHLL-----EQLP-APAGDTALTLDRLDLNGYSENNPS- 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 156 pfemAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLptfpLFALFA---------PAL--G 224
Cdd:PRK12467 3232 ----TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVL----LFMSFSfdgaqerflWTLicG 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 225 MTAVIpemdftRPGSV-DPQKIISAITSHKVTTMFGSPALINRVGRSGaeQGIKLPTLQRVISAGAPVPAVVMERFSQML 303
Cdd:PRK12467 3304 GCLVV------RDNDLwDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKL 3375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 304 AEgVEIFTPYGATESLPVCSigsreilgetrVITENGGGVC------IGRPvdsirvelirISDEPITVWDDDLRVAP-G 376
Cdd:PRK12467 3376 KP-RGLTNGYGPTEAVVTVT-----------LWKCGGDAVCeapyapIGRP----------VAGRSIYVLDGQLNPVPvG 3433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 377 QVGEIVVQGPQVTRGYFQRPEADLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVE 450
Cdd:PRK12467 3434 VAGELYIGGVGLARGYHQRPSLTAERFVADPfsgSGGRLYRTGDLARYRADGVIEYLGRIDHQVK-IRG--FRIelgEIE 3510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 451 AVFNTHPLVYRSALVGIGPKGSQQPVICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDirHNAKIFR 530
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHL---AASLPDYMVPAQLLVLAAMPLG--PNGKVDR 3585
|
...
gi 501446872 531 EKL 533
Cdd:PRK12467 3586 KAL 3588
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
32-492 |
1.09e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 120.91 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 32 SLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlksclaevqpsafigi 111
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 112 pkaqvarllfgwakdslktiitvgprlfwggiTLDKLIQQSPDkpfemAVTAADDQAAILFTSGSTGPPKGAIYSHGNFS 191
Cdd:cd05912 61 --------------------------------TPNELAFQLKD-----SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHW 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 192 AQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPGSVDPQKIISAITSHKVTTMFGSPALINRVgrsg 271
Cdd:cd05912 104 WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL---- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 272 AEQGIKL--PTLQRVISAGAPVPAVVMErfsQMLAEGVEIFTPYGATESlpvCSigsreilgetRVITENgggvcigrPV 349
Cdd:cd05912 180 LEILGEGypNNLRCILLGGGPAPKPLLE---QCKEKGIPVYQSYGMTET---CS----------QIVTLS--------PE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 350 DSirveLIRISDEPITVWDDDLRVA-----PGQVGEIVVQGPQVTRGYFQRPEADLLSKisdpQGGFFHrMGDLGRQDET 424
Cdd:cd05912 236 DA----LNKIGSAGKPLFPVELKIEddgqpPYEVGEILLKGPNVTKGYLNRPDATEESF----ENGWFK-TGDIGYLDEE 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 425 GRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITtnQEQL 492
Cdd:cd05912 307 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIpDDKWGQVPVAFVVSERPIS--EEEL 373
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-496 |
1.12e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.89 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 4 FANIAAH--LPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVG 81
Cdd:PRK12467 509 YAPDCVHqlIEAQARQHPERPALVF--GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 AIPVLIDPGLGIKNLKSCLAEVQPSAFIGIPKaQVARLLFgwaKDSLKTIITVGPrlfwggitlDKLIQQSPDKPFEMAV 161
Cdd:PRK12467 587 GAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH-LLAQLPV---PAGLRSLCLDEP---------ADLLCGYSGHNPEVAL 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 162 tAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDL----PTFPLFA--LFAP-ALGMTAVIPEMDF 234
Cdd:PRK12467 654 -DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLmvstFAFDLGVteLFGAlASGATLHLLPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 TRpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAeqgIKLPTLQRVISAGAPVPAVVMERFSQMLAEGVEIFTPYG 314
Cdd:PRK12467 733 AR----DAEAFAALMADQGVTVLKIVPSHLQALLQASR---VALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 315 ATESLPVCSIgsREILGETRVItengGGVCIGRPvdsirvelirISDEPITVWDDDLRVAPGQV-GEIVVQGPQVTRGYF 393
Cdd:PRK12467 806 PTETTVGVST--YELSDEERDF----GNVPIGQP----------LANLGLYILDHYLNPVPVGVvGELYIGGAGLARGYH 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 394 QRPEADLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGI 467
Cdd:PRK12467 870 RRPALTAERFVPDPfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVK-IRG--FRIelgEIEARLLAQPGVREAVVLAQ 946
|
490 500 510
....*....|....*....|....*....|
gi 501446872 468 GPKGSQQPV-ICIELEQGITTNQEQLRSEL 496
Cdd:PRK12467 947 PGDAGLQLVaYLVPAAVADGAEHQATRDEL 976
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-473 |
1.89e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.30 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDP----- 89
Cdd:PRK12316 4561 ARMTPDAVAVVF--DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPeypre 4638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 --GLGIKNLKSCLAEVQPSAFIGIPKAQVARLLFgwakdslktiitVGPRLFWGGITldkliQQSPDKPfemavTAADDQ 167
Cdd:PRK12316 4639 rlAYMMEDSGAALLLTQSHLLQRLPIPDGLASLA------------LDRDEDWEGFP-----AHDPAVR-----LHPDNL 4696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLpTFPLFA-------LFAP-ALGMTAVIPEmdftrPGS 239
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVL-QFMSFSfdgshegLYHPlINGASVVIRD-----DSL 4770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGiKLPTLQRVISAGAPVPAVVMERFSQMLAEgVEIFTPYGATEsl 319
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTE-- 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 320 pvCSIGSreILGETRVITENGGGVC-IGRPvdsirvelirISDEPITVWDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPE 397
Cdd:PRK12316 4847 --TTVTV--LLWKARDGDACGAAYMpIGTP----------LGNRSGYVLDGQLNPLPvGVAGELYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 398 ADLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGI-GPK 470
Cdd:PRK12316 4913 LTAERFVPDPfgaPGGRLYRTGDLARYRADGVIDYLGRVDHQVK-IRG--FRIelgEIEARLREHPAVREAVVIAQeGAV 4989
|
...
gi 501446872 471 GSQ 473
Cdd:PRK12316 4990 GKQ 4992
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
19-467 |
4.93e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.48 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:PRK06188 26 PDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAFIGIPKAQVARLLFGWAK-DSLKTIITVGPrlFWGGITLDKLIQQSPDKPFEmAVTAADDQAAILFTSGST 177
Cdd:PRK06188 104 VLEDAGISTLIVDPAPFVERALALLARvPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLV-AAALPPDIAGLAYTGGTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 178 GPPKGAIYSHGNFSAQVEalqqvyrIQPGEIDLPTFPLFALFAPA--LGMTAVIPEMdfTRPGSV------DPQKIISAI 249
Cdd:PRK06188 181 GKPKGVMGTHRSIATMAQ-------IQLAEWEWPADPRFLMCTPLshAGGAFFLPTL--LRGGTVivlakfDPAEVLRAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 250 TSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVvmerfsqMLAEGVEIFTP-----YGATES-LPVCS 323
Cdd:PRK06188 252 EEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-------RLAEAIERFGPifaqyYGQTEApMVITY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 324 IGSRE-ILGETRVITEngggvCiGRPVDSIRVELIrisdepitvwDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADLL 401
Cdd:PRK06188 325 LRKRDhDPDDPKRLTS-----C-GRPTPGLRVALL----------DEDGReVAQGEVGEICVRGPLVMDGYWNRPEETAE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 402 SKisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:PRK06188 389 AF----RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
9-494 |
1.55e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 119.38 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 9 AHLPRMAQLQPDTTAIIFPkgNQSLTFQELDRLSDRiCHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLI 87
Cdd:PRK06178 37 EYLRAWARERPQRPAIIFY--GHVITYAELDELSDR-FAALLRQrGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 88 DPGLGIKNLKSCLAEVQPSAFIGI-----------PKAQVARLLFGWAKDSLKTIITV-------GPRLFWGGITLDKLI 149
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALdqlapvveqvrAETSLRHVIVTSLADVLPAEPTLplpdslrAPRLAAAGAIDLLPA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 150 QQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNF---SAQVEALQQVyrIQPGEIDLPTFPLF--------AL 218
Cdd:PRK06178 194 LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvytAAAAYAVAVV--GGEDSVFLSFLPEFwiagenfgLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 219 FAPALGMTAVIpemdFTRpgsVDPQKIISAITSHKVTTMFG---SPALINRVGRSGAEQgikLPTLQ--RVISAGAPVPA 293
Cdd:PRK06178 272 FPLFSGATLVL----LAR---WDAVAFMAAVERYRVTRTVMlvdNAVELMDHPRFAEYD---LSSLRqvRVVSFVKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 294 VVMERFSQmLAEGVEIFTPYGATESLPVCSI------GSREILGETrvitengggVCIGRPVDSIRvelIRISDEpitvw 367
Cdd:PRK06178 342 DYRQRWRA-LTGSVLAEAAWGMTETHTCDTFtagfqdDDFDLLSQP---------VFVGLPVPGTE---FKICDF----- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 368 dDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADLLSKisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVEsVHG-PLF 445
Cdd:PRK06178 404 -ETGELLPlGAEGEIVVRTPSLLKGYWNKPEATAEAL----RDGWLH-TGDIGKIDEQGFLHYLGRRKEMLK-VNGmSVF 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501446872 446 TIPVEAVFNTHPLVYRSALVG-IGPKGSQQPVICIELEQGITTNQEQLRS 494
Cdd:PRK06178 477 PSEVEALLGQHPAVLGSAVVGrPDPDKGQVPVAFVQLKPGADLTAAALQA 526
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
4-467 |
2.47e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 118.44 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 4 FANIAAHLPRmaqlqPDTTAIIFPKGnQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAI 83
Cdd:PRK07514 6 FDALRAAFAD-----RDAPFIETPDG-LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 84 --PVlidpglgikNLKSCLAEVQ-------PSAFIGIPKAqvarllFGW-----AKDSLKTIITVGPRlfwGGITLDKLI 149
Cdd:PRK07514 80 flPL---------NTAYTLAELDyfigdaePALVVCDPAN------FAWlskiaAAAGAPHVETLDAD---GTGSLLEAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 150 QQSPDKpFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-----------AL 218
Cdd:PRK07514 142 AAAPDD-FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFhthglfvatnvAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 219 FAPAlgmtavipEMDFtRPgSVDPQKIISAITshKVTTMFGSPALINRV------GRSgAEQGIKLptlqrVISAGAPVP 292
Cdd:PRK07514 221 LAGA--------SMIF-LP-KFDPDAVLALMP--RATVMMGVPTFYTRLlqeprlTRE-AAAHMRL-----FISGSAPLL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 293 AVVMERFSQMlaEGVEIFTPYGATESlpvCSIGSREILGETRvitenGGGVciGRPVDSIRVeliRISDEpitvwDDDLR 372
Cdd:PRK07514 283 AETHREFQER--TGHAILERYGMTET---NMNTSNPYDGERR-----AGTV--GFPLPGVSL---RVTDP-----ETGAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 373 VAPGQVGEIVVQGPQVTRGYFQRPE-------ADllskisdpqgGFFhRMGDLGRQDETGRLWFCGRKTHRVESvhGPLF 445
Cdd:PRK07514 343 LPPGEIGMIEVKGPNVFKGYWRMPEktaeefrAD----------GFF-ITGDLGKIDERGYVHIVGRGKDLIIS--GGYN 409
|
490 500
....*....|....*....|....
gi 501446872 446 TIP--VEAVFNTHPLVYRSALVGI 467
Cdd:PRK07514 410 VYPkeVEGEIDELPGVVESAVIGV 433
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
168-493 |
3.21e-28 |
|
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: 118.12 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSH-----GNFSAqveALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPG-SVD 241
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHrslvlHAMAA---LLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGpYLD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 242 PQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaeGVEIFTPYGATESLPV 321
Cdd:cd12119 243 PASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER---GVRVIHAWGMTETSPL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 322 CSIG---------SREILGETRVITengggvciGRPVDSIRVELIrisdepitvwDDDLRVAP---GQVGEIVVQGPQVT 389
Cdd:cd12119 320 GTVArppsehsnlSEDEQLALRAKQ--------GRPVPGVELRIV----------DDDGRELPwdgKAVGELQVRGPWVT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 390 RGYFQRPEADLLSKisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-G 468
Cdd:cd12119 382 KSYYKNDEESEALT----EDGWLR-TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVpH 456
|
330 340
....*....|....*....|....*
gi 501446872 469 PKGSQQPVICIELEQGITTNQEQLR 493
Cdd:cd12119 457 PKWGERPLAVVVLKEGATVTAEELL 481
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
10-492 |
4.04e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.21 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 10 HLPRMAQLQPDTTAIIFPkgNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDP 89
Cdd:PRK06710 29 YVEQMASRYPEKKALHFL--GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 GLGIKNLKS-----------CLAEVQP-------------------SAFIGIPKaqvaRLLFGWA-KDSLKTIITVGPRL 138
Cdd:PRK06710 107 LYTERELEYqlhdsgakvilCLDLVFPrvtnvqsatkiehvivtriADFLPFPK----NLLYPFVqKKQSNLVVKVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 139 FwggITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNF-SAQVEALQQVYRIQPGE-IDLPTFPLF 216
Cdd:PRK06710 183 T---IHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 217 ALFapalGMTAV-------------IPEMDFtrpgsvdpQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQR 283
Cdd:PRK06710 260 HVY----GMTAVmnlsimqgykmvlIPKFDM--------KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 284 VISAGAPVPAVVMERFSQMlaEGVEIFTPYGATESLPVCSigsREILGETRVitenGGGVCIGRPVDSIRVELIRISDEp 363
Cdd:PRK06710 328 CISGSAPLPVEVQEKFETV--TGGKLVEGYGLTESSPVTH---SNFLWEKRV----PGSIGVPWPDTEAMIMSLETGEA- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 364 itvwdddlrVAPGQVGEIVVQGPQVTRGYFQRPE--ADLLskisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVH 441
Cdd:PRK06710 398 ---------LPPGEIGEIVVKGPQIMKGYWNKPEetAAVL------QDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASG 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 442 GPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQL 492
Cdd:PRK06710 462 FNVYPREVEEVLYEHEKVQEVVTIGVpDPYRGETVKAFVVLKEGTECSEEEL 513
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
6-493 |
7.46e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.91 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV 85
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVY--RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 LIDPGLGiknlksclaevqPSAFIGIPKAQVARLLFgwAKDSLKTIITVGPRLfwggITLDKLIQQS------PDKPF-E 158
Cdd:PRK06145 81 PINYRLA------------ADEVAYILGDAGAKLLL--VDEEFDAIVALETPK----IVIDAAAQADsrrlaqGGLEIpP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 159 MAVTAADDQAAILFTSGSTGPPKGAIYSHGNFS----AQVEALQqvyrIQPGEIDLPTFPLFALFAPALGMTAVIPEMDF 234
Cdd:PRK06145 143 QAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksiDHVIALG----LTASERLLVVGPLYHVGAFDLPGIAVLWVGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 TR-PGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGVEIfTPY 313
Cdd:PRK06145 219 LRiHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYI-DAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 314 GATESlpvCSigsreilGETrvITENGggvcigRPVDSIRVELIRISDEPITVWDDDLR-VAPGQVGEIVVQGPQVTRGY 392
Cdd:PRK06145 298 GLTET---CS-------GDT--LMEAG------REIEKIGSTGRALAHVEIRIADGAGRwLPPNMKGEICMRGPKVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 393 FQRPEADLLSKIsdpqGGFFhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKG 471
Cdd:PRK06145 360 WKDPEKTAEAFY----GDWF-RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVhDDRW 434
|
490 500
....*....|....*....|..
gi 501446872 472 SQQPVICIELEQGITTNQEQLR 493
Cdd:PRK06145 435 GERITAVVVLNPGATLTLEALD 456
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
29-509 |
1.41e-27 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 115.27 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 29 GNQSLTFQELDRLSDRICHGLIRSGITR-GTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLksclaevqpsA 107
Cdd:cd05958 7 PEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL----------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 FIgIPKAQVARLLFgwakdslktiitvgprlfwggitldkliqqspdkpfEMAVTAADDQAAILFTSGSTGPPKGAIYSH 187
Cdd:cd05958 77 YI-LDKARITVALC------------------------------------AHALTASDDICILAFTSGTTGAPKATMHFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 188 GNFSAQVEAL-QQVYRIQPGEIDLPTFPLFalFAPALGMTAVIP----EMDFTRPGSVdPQKIISAITSHKVTTMFGSPA 262
Cdd:cd05958 120 RDPLASADRYaVNVLRLREDDRFVGSPPLA--FTFGLGGVLLFPfgvgASGVLLEEAT-PDLLLSAIARYKPTVLFTAPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 263 LINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQmlAEGVEIFTPYGATESLPVcSIGSREilGETRVITenggg 342
Cdd:cd05958 197 AYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKE--ATGIPIIDGIGSTEMFHI-FISARP--GDARPGA----- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 343 vcIGRPVDSIRVELIrisdepitvwDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADLLskisdpQGGFFHrMGDLGRQ 421
Cdd:cd05958 267 --TGKPVPGYEAKVV----------DDEGNPVPdGTIGRLAVRGPTGCRYLADKRQRTYV------QGGWNI-TGDTYSR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 422 DETGRLWFCGRKTHRVESvhGPLFTIP--VEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQ---EQLRSE 495
Cdd:cd05958 328 DPDGYFRHQGRSDDMIVS--GGYNIAPpeVEDVLLQHPAVAECAVVGHpDESRGVVVKAFVVLRPGVIPGPvlaRELQDH 405
|
490
....*....|....
gi 501446872 496 LLNIAASHPHTREI 509
Cdd:cd05958 406 AKAHIAPYKYPRAI 419
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
15-496 |
2.82e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.90 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIGIPKAQVARLLfgwakdslktiitvgprlfwgGITLDKLIQQ-SPDKPFEMAVTAADDQAAILFT 173
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAAGRTD---------------------VEDLAAFIASaDALEPADTPSIPPERVSLILFT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 174 SGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFA------PALGMTAVIPEMDFTRPGSV-----DP 242
Cdd:PRK09088 144 SGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGlitsvrPVLAVGGSILVSNGFEPKRTlgrlgDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 qkiisaitSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAvvmERFSQMLAEGVEIFTPYGATESLPVC 322
Cdd:PRK09088 224 --------ALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAA---EDILGWLDDGIPMVDGFGMSEAGTVF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 323 SIGSreilgETRVITENGGGVCIGRPVDSIRVelirisdepitVWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAdlLS 402
Cdd:PRK09088 293 GMSV-----DCDVIRAKAGAAGIPTPTVQTRV-----------VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQA--TA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 403 KISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIG-PKGSQQPVICIEL 481
Cdd:PRK09088 355 RAFTGDGWF--RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAdAQWGEVGYLAIVP 432
|
490
....*....|....*
gi 501446872 482 EQGITTNQEQLRSEL 496
Cdd:PRK09088 433 ADGAPLDLERIRSHL 447
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-542 |
4.07e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 115.23 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 1 MPTFANIAAHLPRMAQLQPDTTAIIfpKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKV 80
Cdd:PRK06164 6 APRADTLASLLDAHARARPDAVALI--DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 81 GAIPVLIDPGLGIKNLKSCLAEVQPS------AFIGIPkaqVARLLFGWAKDSLKT---IITV--------GPrlfWGGI 143
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARwlvvwpGFKGID---FAAILAAVPPDALPPlraIAVVddaadatpAP---APGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 144 TLDKLIQQSPDKPFEMAVTAADDQA-AILFT-SGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPlfalFAP 221
Cdd:PRK06164 158 RVQLFALPDPAPPAAAGERAADPDAgALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALP----FCG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 ALGMTAVIPEmdFTRPGSV------DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGiKLPTLQRV-ISAGAPVPAV 294
Cdd:PRK06164 234 VFGFSTLLGA--LAGGAPLvcepvfDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLFgFASFAPALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 295 VMERfsqMLAEGVEIFTPYGATESLPVCSIGSREILGETRViteNGGGvcigRPVDS-IRVeliRISDEpitvwDDDLRV 373
Cdd:PRK06164 311 LAAL---ARARGVPLTGLYGSSEVQALVALQPATDPVSVRI---EGGG----RPASPeARV---RARDP-----QDGALL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 374 APGQVGEIVVQGPQVTRGYFQRPEADLLSKISDpqgGFFhRMGDLGRQDETGRLWFCGR--KTHRVesvhGPLFTIP--V 449
Cdd:PRK06164 373 PDGESGEIEIRAPSLMRGYLDNPDATARALTDD---GYF-RTGDLGYTRGDGQFVYQTRmgDSLRL----GGFLVNPaeI 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 450 EAVFNTHPLVYRSALVGIGPKGSQQPVICIELEQGITTNQEQLRSELlniAASHPHTREISTILFHPAFPVDIRHN-AKI 528
Cdd:PRK06164 445 EHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDEAGLMAAC---REALAGFKVPARVQVVEAFPVTESANgAKI 521
|
570
....*....|....
gi 501446872 529 FREKLAVWAAEELA 542
Cdd:PRK06164 522 QKHRLREMAQARLA 535
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-476 |
1.39e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.26 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 13 RMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLG 92
Cdd:PRK12467 1582 DQAAATPEAVALVF--GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 IKNLkSCLAEVQPSAFIGIPKAQVARLLFGwakDSLKTIITVGPRlfwggitlDKLIQQSPDKPfemAVTAADDQAA-IL 171
Cdd:PRK12467 1660 RERL-AYMIEDSGIELLLTQSHLQARLPLP---DGLRSLVLDQED--------DWLEGYSDSNP---AVNLAPQNLAyVI 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPlFA-------LFAPAL-GMTAVIpemdfTRPG-SVDP 242
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAfdvsvweLFWPLInGARLVI-----APPGaHRDP 1798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 QKIISAITSHKVTTMFGSPALINRVgRSGAEQGIKLPTLQRVISAGAPVPA----VVMERFSQmlaegVEIFTPYGATES 318
Cdd:PRK12467 1799 EQLIQLIERQQVTTLHFVPSMLQQL-LQMDEQVEHPLSLRRVVCGGEALEVealrPWLERLPD-----TGLFNLYGPTET 1872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 319 lpVCSIGSREIlgeTRVITENGGGVCIGRPVDSIRVELIRISDEPitvwdddlrVAPGQVGEIVVQGPQVTRGYFQRPEA 398
Cdd:PRK12467 1873 --AVDVTHWTC---RRKDLEGRDSVPIGQPIANLSTYILDASLNP---------VPIGVAGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 399 DLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGIGPKGS 472
Cdd:PRK12467 1939 TAERFVADPfgtVGSRLYRTGDLARYRADGVIEYLGRIDHQVK-IRG--FRIelgEIEARLREQGGVREAVVIAQDGANG 2015
|
....
gi 501446872 473 QQPV 476
Cdd:PRK12467 2016 KQLV 2019
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-522 |
2.70e-26 |
|
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: 110.26 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEI---DLPTFPLFALFAPALGMTAVIPEMDFTRP-GSV 240
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVllcGLPLFHVNGSVVTLLTPLASGAHVVLAGPaGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DP---QKIISAITSHKVTTMFGSP----ALINRVGrsgaeqGIKLPTLQRVISAGAPVPAVVMERFSQmlAEGVEIFTPY 313
Cdd:cd05944 82 NPglfDNFWKLVERYRITSLSTVPtvyaALLQVPV------NADISSLRFAMSGAAPLPVELRARFED--ATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 314 GATESLPVCSIGSREilGETRVitengGGVCIGRPVDSIRvelIRISDepiTVWDDDLRVAPGQVGEIVVQGPQVTRGYF 393
Cdd:cd05944 154 GLTEATCLVAVNPPD--GPKRP-----GSVGLRLPYARVR---IKVLD---GVGRLLRDCAPDEVGEICVAGPGVFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 394 QrpeaDLLSKISDPQGGFFhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG-IGPKGS 472
Cdd:cd05944 221 Y----TEGNKNAFVADGWL-NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGqPDAHAG 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 501446872 473 QQPVICIELEQGITTNQEqlrsELLNIAASHPHTReistilfhPAFPVDI 522
Cdd:cd05944 296 ELPVAYVQLKPGAVVEEE----ELLAWARDHVPER--------AAVPKHI 333
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
10-492 |
2.90e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 112.01 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 10 HLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIdp 89
Cdd:cd12118 9 FLERAAAVYPDRTSIVY--GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNAL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 glgikNLKSCLAEVqpsAFIgIPKAQvARLLFgwAKDSLKTIitvgprlfwggitlDKLIQQSPDKPFEMAVTAaDDQAA 169
Cdd:cd12118 85 -----NTRLDAEEI---AFI-LRHSE-AKVLF--VDREFEYE--------------DLLAEGDPDFEWIPPADE-WDPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGnfSAQVEALQQVY--RIQPGEIDLPTFPLF-------ALFAPALGMTAVipemdFTRpgSV 240
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHR--GAYLNALANILewEMKQHPVYLWTLPMFhcngwcfPWTVAAVGGTNV-----CLR--KV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaeGVEIFTPYGATESLP 320
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL---GFDVTHVYGLTETYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 321 VCSIG-----SREILGETRVITENGGGVCIgrpvdsirvelirISDEPITVWDDDLRVA-PG---QVGEIVVQGPQVTRG 391
Cdd:cd12118 286 PATVCawkpeWDELPTEERARLKARQGVRY-------------VGLEEVDVLDPETMKPvPRdgkTIGEIVFRGNIVMKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 392 YFQRPEADLLSKisdpQGGFFHRmGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPK 470
Cdd:cd12118 353 YLKNPEATAEAF----RGGWFHS-GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEK 427
|
490 500
....*....|....*....|..
gi 501446872 471 GSQQPVICIELEQGITTNQEQL 492
Cdd:cd12118 428 WGEVPCAFVELKEGAKVTEEEI 449
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-459 |
3.82e-26 |
|
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: 109.28 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTA-------VIpeMDftrpg 238
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATfhagganVV--ME----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 SVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVisAGAPVPAVVmERFSQMlaEGVEIFTPYGATE- 317
Cdd:cd17637 74 KFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV--LGLDAPETI-QRFEET--TGATFWSLYGQTEt 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 SLPVCSIGSREILGetrvitengggvCIGRPVDSIRVELirisdepitVWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPE 397
Cdd:cd17637 149 SGLVTLSPYRERPG------------SAGRPGPLVRVRI---------VDDNDRPVPAGETGEIVVRGPLVFQGYWNLPE 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 398 ADLLSKisdpQGGfFHRMGDLGRQDETGRLWFCGRKTHRV------ESVhgplFTIPVEAVFNTHPLV 459
Cdd:cd17637 208 LTAYTF----RNG-WHHTGDLGRFDEDGYLWYAGRKPEKElikpggENV----YPAEVEKVILEHPAI 266
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
62-432 |
5.31e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 111.27 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 62 LMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQ------PSAFI---GIPKAQVARLLFGWAK-DSLKTI 131
Cdd:cd05909 36 VMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGiktvltSKQFIeklKLHHLFDVEYDARIVYlEDLRAK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 132 ITVGPRLfWGGITLdKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLP 211
Cdd:cd05909 116 ISKADKC-KAFLAG-KFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 212 TFPLF-------ALFAPAL-GMTAVIpemdftRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQgiKLPTLQR 283
Cdd:cd05909 194 ALPFFhsfgltgCLWLPLLsGIKVVF------HPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHPE--DFSSLRL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 284 VISAGAPVPAVV----MERFsqmlaeGVEIFTPYGATESLPVCSIgsreilgeTRVITENGGGvCIGRPVDSIRVELIRI 359
Cdd:cd05909 266 VVAGAEKLKDTLrqefQEKF------GIRILEGYGTTECSPVISV--------NTPQSPNKEG-TVGRPLPGMEVKIVSV 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501446872 360 sdepitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEadllsKISDPQGGFFHRMGDLGRQDETGRLWFCGR 432
Cdd:cd05909 331 --------ETHEEVPIGEGGLLLVRGPNVMLGYLNEPE-----LTSFAFGDGWYDTGDIGKIDGEGFLTITGR 390
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
20-536 |
8.25e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 111.14 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 20 DTTAIIF--PKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIpvlidpglgiknlk 97
Cdd:PRK04319 59 DKVALRYldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI-------------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 98 sclaeVQP--SAFIgiPKAQVARLLFGWAK-----------------DSLKTIITVGPRLFWGGITLD--KLIQQSPDKp 156
Cdd:PRK04319 125 -----VGPlfEAFM--EEAVRDRLEDSEAKvlittpallerkpaddlPSLKHVLLVGEDVEEGPGTLDfnALMEQASDE- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 157 FEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEI-----DlP---TFPLFALFAPAL-GMTA 227
Cdd:PRK04319 197 FDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVywctaD-PgwvTGTSYGIFAPWLnGATN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 228 VIPEMDFtrpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAE--QGIKLPTLQRVISAGAPV-PAVVmeRFsqmla 304
Cdd:PRK04319 276 VIDGGRF------SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDlvKKYDLSSLRHILSVGEPLnPEVV--RW----- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 305 eGVEIFtpygateSLPVcsigsreilGETRVITENGGGV------------CIGRPVDSIRVELIRisdepitvwDDDLR 372
Cdd:PRK04319 343 -GMKVF-------GLPI---------HDNWWMTETGGIMianypamdikpgSMGKPLPGIEAAIVD---------DQGNE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 373 VAPGQVGEIVVQG--PQVTRGYFQRPEadllsKISDPQGGFFHRMGDLGRQDETGRLWFCGR-----KT--HRVesvhGP 443
Cdd:PRK04319 397 LPPNRMGNLAIKKgwPSMMRGIWNNPE-----KYESYFAGDWYVSGDSAYMDEDGYFWFQGRvddviKTsgERV----GP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 444 LftiPVEAVFNTHPLVYRSALVGIgPkgsqQPVI------CIELEQGITTNqEQLRSELLNIA----ASHPHTREIStil 513
Cdd:PRK04319 468 F---EVESKLMEHPAVAEAGVIGK-P----DPVRgeiikaFVALRPGYEPS-EELKEEIRGFVkkglGAHAAPREIE--- 535
|
570 580
....*....|....*....|....*
gi 501446872 514 FHPAFPvdirHN--AKIFREKLAVW 536
Cdd:PRK04319 536 FKDKLP----KTrsGKIMRRVLKAW 556
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
7-437 |
8.72e-26 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 112.45 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGtRTVLMVTPSPEFFALTF-ALFKVGAIPV 85
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALAD--ARYQFSYREMREQVVALANLLRERGVKPG-DSVAVALPRSVFLTLALhAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 86 LIDPGLGIKNLKSCLAEVQPSAFIGIpKAQVARLlfgwakdslktiiTVGPrlfwGGITLDKLIQQSPDKPFEMAVTAAD 165
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITT-ADQLPRF-------------ADVP----DLTSLCYNAPLAPQGAAPLQLSQPH 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFP------LFALFAPAL-GMTAVIPEMDFTRpg 238
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPcsfdvsVWEFFWPFIaGAKLVMAEPEAHR-- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 svDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLP--TLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGAT 316
Cdd:PRK10252 677 --DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQScaSLRQVFCSGEALPADLCREWQQLT--GAPLHNLYGPT 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 317 ESLPVCSI--GSREILGETRvitenGGGVCIGRPVDSIRVElirisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYF 393
Cdd:PRK10252 753 EAAVDVSWypAFGEELAAVR-----GSSVPIGYPVWNTGLR----------ILDARMRpVPPGVAGDLYLTGIQLAQGYL 817
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 501446872 394 QRPEADLLSKISDP--QGGFFHRMGDLGRQDETGRLWFCGRKTHRV 437
Cdd:PRK10252 818 GRPDLTASRFIADPfaPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
15-467 |
1.61e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.17 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIG-IPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMAVTAADdqaaILFT 173
Cdd:PRK13391 87 EAAYIVDDSGARALITsAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPATPIADESLGTD----MLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 174 SGSTGPPKGaIY---SHGNFSAQV---EALQQVYRIQPGEIDLPTFPLFALfAP--------ALGMTAVIPEmdftrpgS 239
Cdd:PRK13391 163 SGTTGRPKG-IKrplPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLYHS-APqravmlviRLGGTVIVME-------H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAITSHKVT-TMFgSPALINRVGRSGAEQGIK--LPTLQRVISAGAPVPAVVMErfsQMLA-EGVEIFTPYGA 315
Cdd:PRK13391 234 FDAEQYLALIEEYGVThTQL-VPTMFSRMLKLPEEVRDKydLSSLEVAIHAAAPCPPQVKE---QMIDwWGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 316 TESLPVCSIGSREILgetrvitENGGGVciGRPVdsirVELIRISDepitvwDDDLRVAPGQVGEIVVQGPQVTRgYFQR 395
Cdd:PRK13391 310 TEGLGFTACDSEEWL-------AHPGTV--GRAM----FGDLHILD------DDGAELPPGEPGTIWFEGGRPFE-YLND 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501446872 396 PEADLLSKisDPQGGfFHRMGDLGRQDETGRLWFCGRKTHRVESvhGPLFTIPVEA--VFNTHPLVYRSALVGI 467
Cdd:PRK13391 370 PAKTAEAR--HPDGT-WSTVGDIGYVDEDGYLYLTDRAAFMIIS--GGVNIYPQEAenLLITHPKVADAAVFGV 438
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-427 |
3.70e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 109.13 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPG------------LGIKNL------KSC-----LAEVQPSAFIGIPKA-QVARLLFgwakdsLKTIITVGPRLFWGG 142
Cdd:PRK08315 98 INPAyrlseleyalnqSGCKALiaadgfKDSdyvamLYELAPELATCEPGQlQSARLPE------LRRVIFLGDEKHPGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 143 ITLDKLI---QQSPDKPFE--MAVTAADDQAAILFTSGSTGPPKGAIYSHGN------FSAQVEALQQVYRIQpgeidLP 211
Cdd:PRK08315 172 LNFDELLalgRAVDDAELAarQATLDPDDPINIQYTSGTTGFPKGATLTHRNilnngyFIGEAMKLTEEDRLC-----IP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 212 TfPLFALFAPALGM--------TAVIPEMDFtrpgsvDPQKIISAI-----TS-HKVTTMFgspalInrvgrsgAEQGIK 277
Cdd:PRK08315 247 V-PLYHCFGMVLGNlacvthgaTMVYPGEGF------DPLATLAAVeeercTAlYGVPTMF-----I-------AELDHP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 278 ------LPTLQRVISAGAPVPAVVMER-FSQMLAEGVEIftPYGATESLPVCSIGSREILGETRVITengggvcIGRPVD 350
Cdd:PRK08315 308 dfarfdLSSLRTGIMAGSPCPIEVMKRvIDKMHMSEVTI--AYGMTETSPVSTQTRTDDPLEKRVTT-------VGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 351 SIRVeliRISDEpitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEA-----DllskisdpQGGFFHrMGDLGRQDE-- 423
Cdd:PRK08315 379 HLEV---KIVDP-----ETGETVPRGEQGELCTRGYSVMKGYWNDPEKtaeaiD--------ADGWMH-TGDLAVMDEeg 441
|
....*...
gi 501446872 424 ----TGRL 427
Cdd:PRK08315 442 yvniVGRI 449
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
31-433 |
8.23e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 108.14 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLidpglgiknlksclaeVQPSAFIG 110
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAP----------------LTVPPTYD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 IPKAQVARLLFGWA-------------KDSLKTIITVGPRLFWGGITLDKLIQQSPDKPfemAVTA-ADDQAAILFTSGS 176
Cdd:cd05906 102 EPNARLRKLRHIWQllgspvvltdaelVAEFAGLETLSGLPGIRVLSIEELLDTAADHD---LPQSrPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 177 TGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL--------FALFAPALGMTAV-IPEMDFTRpgsvDPQKIIS 247
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLdhvgglveLHLRAVYLGCQQVhVPTEEILA----DPLRWLD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFgSP----ALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAE-GV--EIFTP-YGATESl 319
Cdd:cd05906 255 LIDRYRVTITW-APnfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyGLppDAIRPaFGMTET- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 320 pvCS--IGSREILGETRviTENGGGVCIGRPVDSIRVeliRISDEpitvwDDDLrVAPGQVGEIVVQGPQVTRGYFQRPE 397
Cdd:cd05906 333 --CSgvIYSRSFPTYDH--SQALEFVSLGRPIPGVSM---RIVDD-----EGQL-LPEGEVGRLQVRGPVVTKGYYNNPE 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 501446872 398 ADLLSKISDpqgGFFhRMGDLGRQDEtGRLWFCGRK 433
Cdd:cd05906 400 ANAEAFTED---GWF-RTGDLGFLDN-GNLTITGRT 430
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
145-523 |
1.75e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 107.35 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 145 LDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEI---DLPTFPLFALFAP 221
Cdd:PRK07529 193 DAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTvfcGLPLFHVNALLVT 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 AL-----GMTAVIPemdfTRPGSVDPQ------KIISAitsHKVTTMFGSPALIN---RVGRSGAEqgikLPTLQRVISA 287
Cdd:PRK07529 273 GLaplarGAHVVLA----TPQGYRGPGvianfwKIVER---YRINFLSGVPTVYAallQVPVDGHD----ISSLRYALCG 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 288 GAPVPAVVMERFSQmlAEGVEIFTPYGATESLPVCSIGSREilGETRVitengGGVCIGRPVDSIRvelIRISDEPITVW 367
Cdd:PRK07529 342 AAPLPVEVFRRFEA--ATGVRIVEGYGLTEATCVSSVNPPD--GERRI-----GSVGLRLPYQRVR---VVILDDAGRYL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 368 DDdlrVAPGQVGEIVVQGPQVTRGYFQ-RPEADLLSkisdpQGGFFhRMGDLGRQDETGRLWFCGRKT-------HRVES 439
Cdd:PRK07529 410 RD---CAVDEVGVLCIAGPNVFSGYLEaAHNKGLWL-----EDGWL-NTGDLGRIDADGYFWLTGRAKdliirggHNIDP 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 440 VhgplftiPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEqlrsELLNIAASHPHTReistilfhPAF 518
Cdd:PRK07529 481 A-------AIEEALLRHPAVALAAAVGRpDAHAGELPVAYVQLKPGASATEA----ELLAFARDHIAER--------AAV 541
|
....*
gi 501446872 519 PVDIR 523
Cdd:PRK07529 542 PKHVR 546
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-533 |
2.55e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.12 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK12316 3067 VERTPDAVALAF--GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEvqpsafigipkaqvARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPDkpfemAVTAADDQAAILFTS 174
Cdd:PRK12316 3145 RLAYMLED--------------SGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPA-----IRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLP----TFPLFA--LFAP-ALGMTAVIPEMDFTRpgsvDPQKIIS 247
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQfttfSFDVFVeeLFWPlMSGARVVLAGPEDWR----DPALLVE 3281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFGSPALINRVGRSGAEQgiKLPTLQRVISAGAPVPAVVMERfsqmLAEGVEIFTPYGATESLPVCSIgsr 327
Cdd:PRK12316 3282 LINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQQQ----VFAGLPLYNLYGPTEATITVTH--- 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 328 eilgeTRVITENGGGVCIGRPVDSIRVELIRISDEPITVwdddlrvapGQVGEIVVQGPQVTRGYFQRPEADLLSKISDP 407
Cdd:PRK12316 3353 -----WQCVEEGKDAVPIGRPIANRACYILDGSLEPVPV---------GALGELYLGGEGLARGYHNRPGLTAERFVPDP 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 408 --QGGFFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIgpkGSQQPVICIELEQGI 485
Cdd:PRK12316 3419 fvPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV---DGRQLVAYVVPEDEA 3495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501446872 486 TTNQEQLRSELlniAASHPHTREISTILFHPAFPvdIRHNAKIFREKL 533
Cdd:PRK12316 3496 GDLREALKAHL---KASLPEYMVPAHLLFLERMP--LTPNGKLDRKAL 3538
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
9-467 |
3.31e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.92 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 9 AHLPRM----AQLQPDTTAIIFPKGN---QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVG 81
Cdd:PRK08008 7 QHLRQMwddlADVYGHKTALIFESSGgvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 AIPVLIDPGLG-------IKNLKSCLAEVQPsAFIGIPKAqvarlLFGWAKDSLKTIITVGPRL--FWGGITLDKLIQQS 152
Cdd:PRK08008 87 AIMVPINARLLreesawiLQNSQASLLVTSA-QFYPMYRQ-----IQQEDATPLRHICLTRVALpaDDGVSSFTQLKAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 153 PDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGN--FSAQVEALQQVYRIQpgEIDLPTFPLF--------ALFAPA 222
Cdd:PRK08008 161 PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNlrFAGYYSAWQCALRDD--DVYLTVMPAFhidcqctaAMAAFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 223 LGMTAVIPEMDFTRpgsvdpqKIISAITSHKVTTMFGSPALInrvgrsgaeqgiklptlqRVISAGAPVPAVVMERFSQM 302
Cdd:PRK08008 239 AGATFVLLEKYSAR-------AFWGQVCKYRATITECIPMMI------------------RTLMVQPPSANDRQHCLREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 303 L-------AE--------GVEIFTPYGATESLpVCSIGSREilGETRVITEngggvcIGRPVDSIRVElirISDEpitvw 367
Cdd:PRK08008 294 MfylnlsdQEkdafeerfGVRLLTSYGMTETI-VGIIGDRP--GDKRRWPS------IGRPGFCYEAE---IRDD----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 368 dDDLRVAPGQVGEIVVQG-PQVT--RGYFQRPEADllSKISDPqGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPL 444
Cdd:PRK08008 357 -HNRPLPAGEIGEICIKGvPGKTifKEYYLDPKAT--AKVLEA-DGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500
....*....|....*....|...
gi 501446872 445 FTIPVEAVFNTHPLVYRSALVGI 467
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGI 454
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3-467 |
4.11e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 106.16 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 3 TFANIAAHLPRMAqlqPDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PRK07788 50 PFAGLVAHAARRA---PDRAALIDERG--TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLIDPGLGIKNLKSCLAE------VQPSAFIGIPKAQVARLlfgwakDSLKTIITV---GPRLFWGGITLDKLIQQSP 153
Cdd:PRK07788 125 RIILLNTGFSGPQLAEVAARegvkalVYDDEFTDLLSALPPDL------GRLRAWGGNpddDEPSGSTDETLDDLIAGSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 154 DKPfemAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALqqVYRI--QPGEIDLPTFPLF-------ALFAPALG 224
Cdd:PRK07788 199 TAP---LPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL--LSRVpfRAGETTLLPAPMFhatgwahLTLAMALG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 225 MTAVIPEmDFtrpgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAE--QGIKLPTLQRVISAGAPVPAVVMERFsqM 302
Cdd:PRK07788 274 STVVLRR-RF------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEvlAKYDTSSLKIIFVSGSALSPELATRA--L 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 303 LAEGVEIFTPYGATEsLPVCSIGSREILgetrviTENGGgvCIGRPVDSIRVeliRISDepitvwDDDLRVAPGQVGEIV 382
Cdd:PRK07788 345 EAFGPVLYNLYGSTE-VAFATIATPEDL------AEAPG--TVGRPPKGVTV---KILD------ENGNEVPRGVVGRIF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 383 VQGPQVTRGYF---QRPEAD-LLSkisdpqggffhrMGDLGRQDETGRLWFCGRKTHRV----ESVhgplFTIPVEAVFN 454
Cdd:PRK07788 407 VGNGFPFEGYTdgrDKQIIDgLLS------------SGDVGYFDEDGLLFVDGRDDDMIvsggENV----FPAEVEDLLA 470
|
490
....*....|...
gi 501446872 455 THPLVYRSALVGI 467
Cdd:PRK07788 471 GHPDVVEAAVIGV 483
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-459 |
1.13e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 104.46 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIgIPKAQVARLlfgwakDSLKTIITVGPRLfW-----GGITLDKLIQQSPDKPFEMAV 161
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLV-VEAALLAAL------EAADPGDLPLPAV-WlldapASVSVPAGWSTAPLPPLDAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 162 TAAD----DQAAILFTSGSTGPPKGAIYSHGNF----SAQVEALQqvyrIQPGEIDLPTFPLF-----ALFAPAL--GMT 226
Cdd:PRK06155 173 PAAAvqpgDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLE----IGADDVLYTTLPLFhtnalNAFFQALlaGAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 227 AVIpEMDFTRPGSVDpqkiisAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVV--MERFSQMLA 304
Cdd:PRK06155 249 YVL-EPRFSASGFWP------AVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAafRERFGVDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 305 EGveiftpYGATESLPVCSIgsreilgetrVITENGGGVcIGRPVDSIRvelIRISDEpitvwdDDLRVAPGQVGEIVVQ 384
Cdd:PRK06155 322 DG------YGSTETNFVIAV----------THGSQRPGS-MGRLAPGFE---ARVVDE------HDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 385 GPQ---VTRGYFQRPEAdllsKISDPQGGFFHrMGDLGRQDETGRLWFCGRKT----HRVESVHgplfTIPVEAVFNTHP 457
Cdd:PRK06155 376 ADEpfaFATGYFGMPEK----TVEAWRNLWFH-TGDRVVRDADGWFRFVDRIKdairRRGENIS----SFEVEQVLLSHP 446
|
..
gi 501446872 458 LV 459
Cdd:PRK06155 447 AV 448
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
155-425 |
1.20e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 105.78 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 155 KPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALFAPAL-GMT 226
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFhsfgltvTLWLPLLeGIK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 227 AVipemdfTRPGSVDPQKIISAITSHKVTTMFGSPALIN---RVGRSGAEQGIKLptlqRVISAGApvpavvmERFSQML 303
Cdd:PRK08633 852 VV------YHPDPTDALGIAKLVAKHRATILLGTPTFLRlylRNKKLHPLMFASL----RLVVAGA-------EKLKPEV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 304 AE------GVEIFTPYGATESLPV--CSIGSREILGETRVITENGGGVciGRPVDSIrveLIRISDePITVwdddLRVAP 375
Cdd:PRK08633 915 ADafeekfGIRILEGYGATETSPVasVNLPDVLAADFKRQTGSKEGSV--GMPLPGV---AVRIVD-PETF----EELPP 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 376 GQVGEIVVQGPQVTRGYFQRPE--ADLlskISDPQGGFFHRMGDLGRQDETG 425
Cdd:PRK08633 985 GEDGLILIGGPQVMKGYLGDPEktAEV---IKDIDGIGWYVTGDKGHLDEDG 1033
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
29-498 |
1.37e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 103.68 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 29 GNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSaf 108
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 109 igipkaqvarLLFgwakdslktiitvgprlfwggitldkliqqspdkpfemaVTAADDQAAILFTSGSTGPPKGAIYSHG 188
Cdd:cd05914 82 ----------AIF---------------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 189 NFSAQVEALQQVYRIQPGEID---LP---TFPLFALFAPALGMTAVIPEMDFTrpgsvdPQKIISAITSHKVTTMFGSP- 261
Cdd:cd05914 113 NIVSNVDGVKEVVLLGKGDKIlsiLPlhhIYPLTFTLLLPLLNGAHVVFLDKI------PSAKIIALAFAQVTPTLGVPv 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 262 ----------ALINRVGRSGAEQGIKLPTLQR--------------------VISAGAPVPAVVMERFSQMlaeGVEIFT 311
Cdd:cd05914 187 plviekifkmDIIPKLTLKKFKFKLAKKINNRkirklafkkvheafggnikeFVIGGAKINPDVEEFLRTI---GFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 312 PYGATESLPVCSIG--SREILGETrvitengggvciGRPVDsiRVElIRISDEPITVWDddlrvapgqvGEIVVQGPQVT 389
Cdd:cd05914 264 GYGMTETAPIISYSppNRIRLGSA------------GKVID--GVE-VRIDSPDPATGE----------GEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 390 RGYFQRPEADllSKISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESVHGP-LFTIPVEAVFNTHPLVYRSALVGIG 468
Cdd:cd05914 319 KGYYKNPEAT--AEAFDKDGWF--HTGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVVVQE 394
|
490 500 510
....*....|....*....|....*....|....
gi 501446872 469 PKGSQQPVICIELEQ----GITTNQEQLRSELLN 498
Cdd:cd05914 395 KKLVALAYIDPDFLDvkalKQRNIIDAIKWEVRD 428
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-493 |
4.52e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 100.43 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNF---SAQV-EALqqvyRIQPGEIDLPTFPLFALFAPALGM--------TAVIPEM 232
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIvnnGYFIgERL----GLTEQDRLCIPVPLFHCFGSVLGVlaclthgaTMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 233 DFtrpgsvDPQKIISAITSHKVTTMFGSP----ALINRVGRSGAEqgikLPTLQRVISAGAPVPAVVMER-FSQMLAEGV 307
Cdd:cd05917 78 SF------DPLAVLEAIEKEKCTALHGVPtmfiAELEHPDFDKFD----LSSLRTGIMAGAPCPPELMKRvIEVMNMKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 308 EIftPYGATESLPVCSIGSREILGETRVITengggvcIGRPVDSIRVELIRISDEPItvwdddlrVAPGQVGEIVVQGPQ 387
Cdd:cd05917 148 TI--AYGMTETSPVSTQTRTDDSIEKRVNT-------VGRIMPHTEAKIVDPEGGIV--------PPVGVPGELCIRGYS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 388 VTRGYFQRPEAdllSKISDPQGGFFHrMGDLGRQDETGRLWFCGRKTHRV----ESVHgPLftiPVEAVFNTHPLVYRSA 463
Cdd:cd05917 211 VMKGYWNDPEK---TAEAIDGDGWLH-TGDLAVMDEDGYCRIVGRIKDMIirggENIY-PR---EIEEFLHTHPKVSDVQ 282
|
330 340 350
....*....|....*....|....*....|.
gi 501446872 464 LVGI-GPKGSQQPVICIELEQGITTNQEQLR 493
Cdd:cd05917 283 VVGVpDERYGEEVCAWIRLKEGAELTEEDIK 313
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
22-497 |
8.26e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 101.52 E-value: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 22 TAIIFPKGnQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIdpglgikNLKSCLA 101
Cdd:PRK08276 2 AVIMAPSG-EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI-------NWHLTAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 102 EVqpsAFI----GipkaqvARLLFGWAK--DSLKTIITVGPR------LFWGGIT----LDKLIQQSPDkpfemavTAAD 165
Cdd:PRK08276 74 EI---AYIvddsG------AKVLIVSAAlaDTAAELAAELPAgvplllVVAGPVPgfrsYEEALAAQPD-------TPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAA---ILFTSGSTGPPKGAI---------YSHGNFSAQVEALqqvYRIQPGEIDLPTFPL-------FALFAPALGMT 226
Cdd:PRK08276 138 DETAgadMLYSSGTTGRPKGIKrplpgldpdEAPGMMLALLGFG---MYGGPDSVYLSPAPLyhtaplrFGMSALALGGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 227 AVIpeMD-FtrpgsvDPQKIISAITSHKVTTMFGSPALINRVgrsgaeqgIKLP----------TLQRVISAGAPVPAVV 295
Cdd:PRK08276 215 VVV--MEkF------DAEEALALIERYRVTHSQLVPTMFVRM--------LKLPeevrarydvsSLRVAIHAAAPCPVEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 296 MErfsQMLA-EGVEIFTPYGATESLPVCSIGSREILgetrvitENGGGVciGRPVDSIrvelIRISDEpitvwdDDLRVA 374
Cdd:PRK08276 279 KR---AMIDwWGPIIHEYYASSEGGGVTVITSEDWL-------AHPGSV--GKAVLGE----VRILDE------DGNELP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 375 PGQVGEIVVQGPQVTRGYFQRPEADllSKISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESvhGPLFTIP--VEAV 452
Cdd:PRK08276 337 PGEIGTVYFEMDGYPFEYHNDPEKT--AAARNPHGWV--TVGDVGYLDEDGYLYLTDRKSDMIIS--GGVNIYPqeIENL 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 501446872 453 FNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTnQEQLRSELL 497
Cdd:PRK08276 411 LVTHPKVADVAVFGVpDEEMGERVKAVVQPADGADA-GDALAAELI 455
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
31-541 |
1.11e-22 |
|
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: 101.80 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIG 110
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 ----------IPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLI--QQSPDKPFEMAVTAADDQAAILFTSGSTG 178
Cdd:cd05968 170 adgftrrgreVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSydEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 179 PPKGAIYSHGNFSaqVEALQQVY---RIQPGEIDLPTFPLFALFAP-------ALGMTAVIPEmdfTRPGSVDPQKIISA 248
Cdd:cd05968 250 KPKGTVHVHAGFP--LKAAQDMYfqfDLKPGDLLTWFTDLGWMMGPwlifgglILGATMVLYD---GAPDHPKADRLWRM 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 249 ITSHKVTTMFGSPALINRVGRSGAEQGIK--LPTLQRVISAGAPV-PAVVMERFSQMLAEGVEIFTPYGATESlpvcsig 325
Cdd:cd05968 325 VEDHEITHLGLSPTLIRALKPRGDAPVNAhdLSSLRVLGSTGEPWnPEPWNWLFETVGKGRNPIINYSGGTEI------- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 326 SREILG-----ETRVITENGggvcigrPVDSIRVelirisdepiTVWDDDLRVAPGQVGEIVVQGPQV--TRGYFQRPEA 398
Cdd:cd05968 398 SGGILGnvlikPIKPSSFNG-------PVPGMKA----------DVLDESGKPARPEVGELVLLAPWPgmTRGFWRDEDR 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 399 DLLSKISDPQGGFFHrmGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVI 477
Cdd:cd05968 461 YLETYWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVpHPVKGEAIVC 538
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 478 CIELEQGITTNqEQLRSELLNIAASH---PHTREisTILFHPAFPVDirHNAKIFREKL-AVWAAEEL 541
Cdd:cd05968 539 FVVLKPGVTPT-EALAEELMERVADElgkPLSPE--RILFVKDLPKT--RNAKVMRRVIrAAYLGKEL 601
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
165-467 |
1.58e-22 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 101.28 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYR--IQPGE----IDLPTFPLFALFAPAL-----GMTAVIpemd 233
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKelvvTALPLYHIFALTVNCLlfielGGQNLL---- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 234 FTRPGSVDpqKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaEGVEIFTPY 313
Cdd:PRK08974 282 ITNPRDIP--GFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKL--TGQYLLEGY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 314 GATESLPVCSIGSREILGEtrviteNGGgvcIGRPVDSIrveLIRISDepitvwDDDLRVAPGQVGEIVVQGPQVTRGYF 393
Cdd:PRK08974 358 GLTECSPLVSVNPYDLDYY------SGS---IGLPVPST---EIKLVD------DDGNEVPPGEPGELWVKGPQVMLGYW 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 394 QRPEADlLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVeSVHG-PLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:PRK08974 420 QRPEAT-DEVIKD---GWLA-TGDIAVMDEEGFLRIVDRKKDMI-LVSGfNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
10-425 |
2.10e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 100.80 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 10 HLPRMAQLQPDTTAIIFpKGNqSLTFQELDRLSDRICHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLID 88
Cdd:PRK08314 15 NLEVSARRYPDKTAIVF-YGR-AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 89 PGLGIKNLKS-----------CLAEVQPSAFIGIPKAQVARLLFGWAKDSL--KTIITV---------GPRLFWGGITLD 146
Cdd:PRK08314 93 PMNREEELAHyvtdsgarvaiVGSELAPKVAPAVGNLRLRHVIVAQYSDYLpaEPEIAVpawlraeppLQALAPGGVVAW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 147 KLIQQSPDKPFEMAVTAaDDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALF 219
Cdd:PRK08314 173 KEALAAGLAPPPHTAGP-DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFhvtgmvhSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 220 AP-ALGMTAVI-PEMDftRPGSVDpqkiisAITSHKVT------TM----FGSPALINRvgrsgaeqgiKLPTLQRVISA 287
Cdd:PRK08314 252 APiYAGATVVLmPRWD--REAAAR------LIERYRVThwtnipTMvvdfLASPGLAER----------DLSSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 288 GAPVPAVVMERFSQMLaeGVEIFTPYGATESLPVCSIG--SREILGetrvitengggvCIGRP---VDSirveliRISDe 362
Cdd:PRK08314 314 GAAMPEAVAERLKELT--GLDYVEGYGLTETMAQTHSNppDRPKLQ------------CLGIPtfgVDA------RVID- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501446872 363 PITVWDddlrVAPGQVGEIVVQGPQVTRGYFQRPEADLLSKIsDPQGGFFHRMGDLGRQDETG 425
Cdd:PRK08314 373 PETLEE----LPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI-EIDGKRFFRTGDLGRMDEEG 430
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
27-433 |
3.77e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 100.07 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 27 PKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAipvlidpglgiknlkSCLAEVQPS 106
Cdd:PRK07768 24 PDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGA---------------SLTMLHQPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 107 afigiPKAQVARllfgWAKDSLKTIITVG--------------PRLFWGGITLDKLIQQSPDKPFEMAVTAADDQAAILF 172
Cdd:PRK07768 89 -----PRTDLAV----WAEDTLRVIGMIGakavvvgepflaaaPVLEEKGIRVLTVADLLAADPIDPVETGEDDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 173 TSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPgEID--LPTFPLF-------ALFAP-ALGMTAV-IPEMDFTRpgsvD 241
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDV-ETDvmVSWLPLFhdmgmvgFLTVPmYFGAELVkVTPMDFLR----D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 242 PQKIISAITSHKvTTMFGSP----ALINRVGRSGAEQG-IKLPTLQRVISAGAPVPAVVMERFsqmLAEGV------EIF 310
Cdd:PRK07768 235 PLLWAELISKYR-GTMTAAPnfayALLARRLRRQAKPGaFDLSSLRFALNGAEPIDPADVEDL---LDAGArfglrpEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 311 TP-YGATES------------LPVCSIGSREILGETRVITENGGG----VCIGRPVDSIRVELIrisdepitvwDDDLRV 373
Cdd:PRK07768 311 LPaYGMAEAtlavsfspcgagLVVDEVDADLLAALRRAVPATKGNtrrlATLGPPLPGLEVRVV----------DEDGQV 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501446872 374 -APGQVGEIVVQGPQVTRGYFqrpEADLLSKISDPQGGFFhrMGDLGRQDETGRLWFCGRK 433
Cdd:PRK07768 381 lPPRGVGVIELRGESVTPGYL---TMDGFIPAQDADGWLD--TGDLGYLTEEGEVVVCGRV 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-496 |
4.48e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.01 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK05691 2198 AARTPQAPALTF--AGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKS---------CLAEVQPSAFIGIPKAQVARllfgWAKDSlktiitvgprlfwggiTLDKLIQQSPDKPfeMAVTAAD 165
Cdd:PRK05691 2276 RLHYmiedsgiglLLSDRALFEALGELPAGVAR----WCLED----------------DAAALAAYSDAPL--PFLSLPQ 2333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-F-----ALFAPALGMTAVIpemdFTRPGS 239
Cdd:PRK05691 2334 HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSInFdaaseRLLVPLLCGARVV----LRAQGQ 2409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPtLQRVISAGAPVPAVVMERFSQMLAEGVeIFTPYGATES- 318
Cdd:PRK05691 2410 WGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYGPTETv 2487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 319 -LPVCSIGsreilGETrvITENGGGVCIGRPVDSiRVELIrisdepitvWDDDLRVAP-GQVGEIVVQGPQVTRGYFQRP 396
Cdd:PRK05691 2488 vMPLACLA-----PEQ--LEEGAASVPIGRVVGA-RVAYI---------LDADLALVPqGATGELYVGGAGLAQGYHDRP 2550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 397 EADLLSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALVGIGPK 470
Cdd:PRK05691 2551 GLTAERFVADPfaaDGGRLYRTGDLVRLRADGLVEYVGRIDHQVK-IRG--FRIelgEIESRLLEHPAVREAVVLALDTP 2627
|
490 500
....*....|....*....|....*....
gi 501446872 471 GSQQPV---ICIELEQGITTnQEQLRSEL 496
Cdd:PRK05691 2628 SGKQLAgylVSAVAGQDDEA-QAALREAL 2655
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
170-467 |
4.78e-21 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 94.29 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF---------ALFApaLGMTAVipemdFTRpgSV 240
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFhigtlmftlATFH--AGGTNV-----FVR--RV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISA---GAPVPAVVMERFSQMLAegveiftpYGATE 317
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewNDMATVDTSPWGRKPGG--------YGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 slpvcsigsreILGETRVITENGGGVCI-GRPVDSIRVeliRISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRP 396
Cdd:cd17636 148 -----------VMGLATFAALGGGAIGGaGRPSPLVQV---RILDE------DGREVPDGEVGEIVARGPTVMAGYWNRP 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501446872 397 EADllskiSDPQGGFFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd17636 208 EVN-----ARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
28-432 |
4.79e-21 |
|
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: 95.89 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 28 KGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLidpglgiknlKSCLAEVQPSA 107
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV----------RGSDSSVEELL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 FIgipkaqvarllfgwAKDSLKTIItvgprlfwggitldkLIQQSPDkpfemavtaadDQAAILFTSGSTGPPKGAIYSH 187
Cdd:cd17640 71 YI--------------LNHSESVAL---------------VVENDSD-----------DLATIIYTSGTTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 188 GNFSAQVEALQQVYRIQPGEIDLPTFP-------LFALFAPALGMTAV---IPEM--DFTRpgsVDPQKIIS------AI 249
Cdd:cd17640 111 ANLLHQIRSLSDIVPPQPGDRFLSILPiwhsyerSAEYFIFACGCSQAytsIRTLkdDLKR---VKPHYIVSvprlweSL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 250 TSHKVTTMFGSPALINRVGRSGAEQGIklptLQRVISAGAPVPAVVmERFSQmlAEGVEIFTPYGATESLPVCSIgsrei 329
Cdd:cd17640 188 YSGIQKQVSKSSPIKQFLFLFFLSGGI----FKFGISGGGALPPHV-DTFFE--AIGIEVLNGYGLTETSPVVSA----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 330 lgetRVITENGGGVCiGRPVDSIRvelIRISDEpitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADllSKISDPQG 409
Cdd:cd17640 256 ----RRLKCNVRGSV-GRPLPGTE---IKIVDP-----EGNVVLPPGEKGIVWVRGPQVMKGYYKNPEAT--SKVLDSDG 320
|
410 420
....*....|....*....|...
gi 501446872 410 GFfhRMGDLGRQDETGRLWFCGR 432
Cdd:cd17640 321 WF--NTGDLGWLTCGGELVLTGR 341
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-540 |
4.84e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 96.31 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 29 GNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV--------------LIDPG---- 90
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVpvnwhfkpeeiayiLEDSGarvl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 91 LGIKNLKSCLAEVQPSAF--IGIPKAQVARLLFGWAKDSLKTiitvgPRlfwGGITLDKLIQQSPdkPFEMAVTAAddQA 168
Cdd:PRK12406 88 IAHADLLHGLASALPAGVtvLSVPTPPEIAAAYRISPALLTP-----PA---GAIDWEGWLAQQE--PYDGPPVPQ--PQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 169 AILFTSGSTGPPKG---AIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-------FALFAPALGMTAVIpEMDFtrpg 238
Cdd:PRK12406 156 SMIYTSGTTGHPKGvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLyhsapnaYGLRAGRLGGVLVL-QPRF---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 svDPQKIISAITSHKVTTMFGSPALINRVGRSGAE--QGIKLPTLQRVISAGAPVPAVVMErfsQMLAE-GVEIFTPYGA 315
Cdd:PRK12406 231 --DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKR---AMIEWwGPVIYEYYGS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 316 TESLPVCSIGSREILGETrvitengGGVciGRPVDSIRVELIrisdepitvwDDDLR-VAPGQVGEIVVQ---GPQVTrg 391
Cdd:PRK12406 306 TESGAVTFATSEDALSHP-------GTV--GKAAPGAELRFV----------DEDGRpLPQGEIGEIYSRiagNPDFT-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 392 YFQRPEAdlLSKISdpQGGFFhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIgPKG 471
Cdd:PRK12406 365 YHNKPEK--RAEID--RGGFI-TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGI-PDA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501446872 472 SQQPVIC--IELEQGITTNQEQLRSELLNIAASHPHTREistILFHPAFPvdiRHNA-KIFREKL--AVWAAEE 540
Cdd:PRK12406 439 EFGEALMavVEPQPGATLDEADIRAQLKARLAGYKVPKH---IEIMAELP---REDSgKIFKRRLrdPYWANAG 506
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-438 |
6.23e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPG 90
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGG--SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPD 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 91 LGIKNLKSCLAEVQPSAFIGipkaQVARLlfgwakDSLKTIITVGPrlfwggITLDKLIQQS-PDKPFEMAVTaADDQAA 169
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLT----QSHLL------ERLPQAEGVSA------IALDSLHLDSwPSQAPGLHLH-GDNLAY 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL------FALFAPAL-GMTAVIPEmdftrPGS-VD 241
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsfdvsvWECFWPLItGCRLVLAG-----PGEhRD 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 242 PQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKlpTLQRVISAGAPVPAVVMERFSQMLAeGVEIFTPYGATESlpv 321
Cdd:PRK05691 1353 PQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNRVLQRLP-QVQLHNRYGPTET--- 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 322 cSIGsreiLGETRVITENGGGVCIGRPVDSIrveLIRisdepitVWDDDLR-VAPGQVGEIVVQGPQVTRGYFQRPEADL 400
Cdd:PRK05691 1427 -AIN----VTHWQCQAEDGERSPIGRPLGNV---LCR-------VLDAELNlLPPGVAGELCIGGAGLARGYLGRPALTA 1491
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 501446872 401 LSKISDP---QGGFFHRMGDLGRQDETGRLWFCGRKTHRVE 438
Cdd:PRK05691 1492 ERFVPDPlgeDGARLYRTGDRARWNADGALEYLGRLDQQVK 1532
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
8-506 |
7.10e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.11 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 8 AAHLPRMAQL-------QPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKV 80
Cdd:PRK05852 12 SDFGPRIADLvevaatrLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 81 GAIPVLIDPGLGIKNLKSCLAEVQPSAFIGI---PKAQVARLLFGWAkdslkTIITVGP-RLFWGGI---TLDKLIQQSP 153
Cdd:PRK05852 92 DLVVVPLDPALPIAEQRVRSQAAGARVVLIDadgPHDRAEPTTRWWP-----LTVNVGGdSGPSGGTlsvHLDAATEPTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 154 DKPFEMAVtaADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF-------ALFAP-ALGM 225
Cdd:PRK05852 167 ATSTPEGL--RPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYhghgliaALLATlASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 226 TAVIPEM-DFTRPGSVDPQKIISAitshkvtTMFGSPALINRV--GRSGAEQ-GIKLPTLQRVISAGAPVPAVVMERFSQ 301
Cdd:PRK05852 245 AVLLPARgRFSAHTFWDDIKAVGA-------TWYTAVPTIHQIllERAATEPsGRKPAALRFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 302 MLaeGVEIFTPYGATESlpVCSIGSREILGETRviTENGGgVCIGRPVDSIRVElIRIsdepitVWDDDLRVAPGQVGEI 381
Cdd:PRK05852 318 EF--AAPVVCAFGMTEA--THQVTTTQIEGIGQ--TENPV-VSTGLVGRSTGAQ-IRI------VGSDGLPLPAGAVGEV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 382 VVQGPQVTRGYFQRPeADLLSKISDpqgGFFhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYR 461
Cdd:PRK05852 384 WLRGTTVVRGYLGDP-TITAANFTD---GWL-RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 462 SALVGIGPK--GSQQPVICIELEQGITTNQE---QLRSEL--------LNIAASHPHT 506
Cdd:PRK05852 459 AAVFGVPDQlyGEAVAAVIVPRESAPPTAEElvqFCRERLaafeipasFQEASGLPHT 516
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
166-467 |
9.30e-21 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 93.33 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTA-------VIPEMDFtrpg 238
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVAclltgatVVPVAVF---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 svDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVE-IFTPYGATE 317
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSEL--GFEtVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 318 SlpVCSIGSREILGETRVITengggvCIGRPVDSIRVeliRISDEpitvwdddlrvapgqvGEIVVQGPQVTRGYFQRPE 397
Cdd:cd17638 153 A--GVATMCRPGDDAETVAT------TCGRACPGFEV---RIADD----------------GEVLVRGYNVMQGYLDDPE 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 398 ADLLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd17638 206 ATAEAIDAD---GWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV 271
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
168-492 |
1.48e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.20 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSH-GNF-----SAQVEALQqvyrIQPGEIDLPTFPLF-------ALFAPALGMTAVIPEmdf 234
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVlhalmANNGDALG----TSAADTMLPVVPLFhanswgiAFSAPSMGTKLVMPG--- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 trpGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaeGVEIFTPYG 314
Cdd:PRK06018 253 ---AKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM---GVEVRHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 315 ATESLPVCSIGS-----REILGETRVITEngggVCIGRPvdSIRVELiRISDepitvwDDDLRVA-PGQV-GEIVVQGPQ 387
Cdd:PRK06018 327 MTEMSPLGTLAAlkppfSKLPGDARLDVL----QKQGYP--PFGVEM-KITD------DAGKELPwDGKTfGRLKVRGPA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 388 VTRGYFqRPEADLLSkisdpQGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:PRK06018 394 VAAAYY-RVDGEILD-----DDGFFD-TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGV 466
|
330 340
....*....|....*....|....*.
gi 501446872 468 -GPKGSQQPVICIELEQGITTNQEQL 492
Cdd:PRK06018 467 yHPKWDERPLLIVQLKPGETATREEI 492
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
143-467 |
1.79e-20 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 94.59 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 143 ITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQV----EALQQVYRIQPGEIDLPTFPLFAL 218
Cdd:cd05927 92 YSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 219 FapalgmTAVIPEMDFTRPGSV-----DPQKIISAITSHKVTTMFGSPALINRVgRSGAEQGI-KLPTLQR--------- 283
Cdd:cd05927 172 F------ERVVEALFLYHGAKIgfysgDIRLLLDDIKALKPTVFPGVPRVLNRI-YDKIFNKVqAKGPLKRklfnfalny 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 284 ----------------------------------VISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESLPVCSIGsreI 329
Cdd:cd05927 245 klaelrsgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVAL--GCPVLEGYGQTECTAGATLT---L 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 330 LGETRVitenggGvCIGRPVDSIRVELIRISDEPITVWDDDLRvapgqvGEIVVQGPQVTRGYFQRPEADLLSKISDpqg 409
Cdd:cd05927 320 PGDTSV------G-HVGGPLPCAEVKLVDVPEMNYDAKDPNPR------GEVCIRGPNVFSGYYKDPEKTAEALDED--- 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 410 GFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPlFTIP--VEAVFNTHPLV---------YRSALVGI 467
Cdd:cd05927 384 GWLH-TGDIGEWLPNGTLKIIDRKKNIFKLSQGE-YVAPekIENIYARSPFVaqifvygdsLKSFLVAI 450
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
19-465 |
5.52e-20 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 92.85 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTV-LMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLK 97
Cdd:cd17648 1 PDRVAVVY--GDKRLTYRELNERANRLAHYLLSVAEIRPDDLVgLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 98 SCLAEVQpsafigipkaqvARLLfgwakdslktiitvgprlfwggitldkliqqspdkpfemaVTAADDQAAILFTSGST 177
Cdd:cd17648 79 FILEDTG------------ARVV----------------------------------------ITNSTDLAYAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 178 GPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPAL---------GMTAVIPEMDFtrpgSVDPQKIISA 248
Cdd:cd17648 107 GKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqmtlallnGQKLVVPPDEM----RFDPDRFYAY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 249 ITSHKVTTMFGSPALINRVGRSgaeqgiKLPTLQRVISAG----APVPAVVMERFSQMlaegveIFTPYGATESlpvcSI 324
Cdd:cd17648 183 INREKVTYLSGTPSVLQQYDLA------RLPHLKRVDAAGeeftAPVFEKLRSRFAGL------IINAYGPTET----TV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 GSREILGETRVITENGggvcIGRPVDSIRVelirisdepiTVWDDDL-RVAPGQVGEIVVQGPQVTRGYFQRPEADLLSK 403
Cdd:cd17648 247 TNHKRFFPGDQRFDKS----LGRPVRNTKC----------YVLNDAMkRVPVGAVGELYLGGDGVARGYLNRPELTAERF 312
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 404 ISDP-------QGGFFHRM---GDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVYRSALV 465
Cdd:cd17648 313 LPNPfqteqerARGRNARLyktGDLVRWLPSGELEYLGRNDFQVK-IRG--QRIepgEVEAALASYPGVRECAVV 384
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
34-466 |
5.63e-20 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 93.30 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 34 TFQELDRLSDRICHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAipVLIdPGLGIKNLKSCLAEVQPSAFIGIP 112
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGL--VFI-PGTIQLTAKDILYRLQASKAKCIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 KAQ-VARLLFGWAKD--SLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMAvTAADDQAAILFTSGSTGPPKGAIYSHGN 189
Cdd:cd05928 120 TSDeLAPEVDSVASEcpSLKTKLLVSEKSRDGWLNFKELLNEASTEHHCVE-TGSQEPMAIYFTSGTTGSPKMAEHSHSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 190 FSAQVEALQQVYR-IQPGEIDLPT-------FPLFALFAP-ALGMTAVIPEMdftrpGSVDPQKIISAITSHKVTTMFGS 260
Cdd:cd05928 199 LGLGLKVNGRYWLdLTASDIMWNTsdtgwikSAWSSLFEPwIQGACVFVHHL-----PRFDPLVILKTLSSYPITTFCGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 261 PAlINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaEGVEIFTPYGATESLPVCSigsreilgetrviteNG 340
Cdd:cd05928 274 PT-VYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ--TGLDIYEGYGQTETGLICA---------------NF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 341 GGVCI-----GRPVDSIRVELIrisDEPITVwdddlrVAPGQVGEIVVQ-GPQVTRGYFQRPEADlLSKISDPQGGFFHR 414
Cdd:cd05928 336 KGMKIkpgsmGKASPPYDVQII---DDNGNV------LPPGTEGDIGIRvKPIRPFGLFSGYVDN-PEKTAATIRGDFYL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 415 MGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:cd05928 406 TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVS 457
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
18-492 |
6.12e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.37 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 18 QPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTF-ALFKVGAIPVLIDPGLGIKNL 96
Cdd:PLN02574 52 HNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFlAVLSLGGIVTTMNPSSSLGEI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 97 KS-------CLAEVQPSAFIGIPKAQVARLLFGWAKDsLKTIITVGPRLFWggitldkLIQQSPDkPFEMAVTAADDQAA 169
Cdd:PLN02574 132 KKrvvdcsvGLAFTSPENVEKLSPLGVPVIGVPENYD-FDSKRIEFPKFYE-------LIKEDFD-FVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQ---PG--EIDLPTFPLF-----ALFAP---ALGMTAVIPEmdftr 236
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeyPGsdNVYLAALPMFhiyglSLFVVgllSLGSTIVVMR----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 pgSVDPQKIISAITSHKVTTM-FGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEgVEIFTPYGA 315
Cdd:PLN02574 278 --RFDASDMVKVIDRFKVTHFpVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPH-VDFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 316 TESLPVcsiGSREIlgETRVITENGGgvcIGRPVDSIRVELIRisdepitvWDDDLRVAPGQVGEIVVQGPQVTRGYFQR 395
Cdd:PLN02574 355 TESTAV---GTRGF--NTEKLSKYSS---VGLLAPNMQAKVVD--------WSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 396 PEADLLSKISDpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIGPKGSQQ- 474
Cdd:PLN02574 419 PKATQSTIDKD---GWLR-TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEi 494
|
490
....*....|....*...
gi 501446872 475 PVICIELEQGITTNQEQL 492
Cdd:PLN02574 495 PVAFVVRRQGSTLSQEAV 512
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
31-467 |
1.30e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 92.01 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFI- 109
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 110 ----------GIPKAQVARLLFGWAKDSL--KTIIT----------VGPRLFWGGITLDKLIQQSPDKPFEMAVTAADDQ 167
Cdd:PRK07059 127 lenfattvqqVLAKTAVKHVVVASMGDLLgfKGHIVnfvvrrvkkmVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSA---QVEALQQVYRIQPGEID-------LPTFPLFALFAPAL------GMTAVIPe 231
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVAnvlQMEAWLQPAFEKKPRPDqlnfvcaLPLYHIFALTVCGLlgmrtgGRNILIP- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 232 mdftrpgsvDPQKI---ISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaEGVE 308
Cdd:PRK07059 286 ---------NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEM--TGCP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 309 IFTPYGATESLPVCSIGSREIlgetrviTENGGgvCIGRPVDSIRVElIRisdepitvwDDDLR-VAPGQVGEIVVQGPQ 387
Cdd:PRK07059 355 ITEGYGLSETSPVATCNPVDA-------TEFSG--TIGLPLPSTEVS-IR---------DDDGNdLPLGEPGEICIRGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 388 VTRGYFQRPEADLLSKISDpqgGFFhRMGDLGRQDETGRLWFCGRKTHRVeSVHGplFTI---PVEAVFNTHPLVYRSAL 464
Cdd:PRK07059 416 VMAGYWNRPDETAKVMTAD---GFF-RTGDVGVMDERGYTKIVDRKKDMI-LVSG--FNVypnEIEEVVASHPGVLEVAA 488
|
...
gi 501446872 465 VGI 467
Cdd:PRK07059 489 VGV 491
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
141-493 |
2.11e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 91.36 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 141 GGITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSA---QVEALQQVYRIQPGEIDLPTFPLFA 217
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNEGCEILIAPLPLYH 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 218 LFAPAL--GMTAVIPEMDFTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVV 295
Cdd:PRK05677 263 IYAFTFhcMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLAT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 296 MERFSQMlaEGVEIFTPYGATESLPVCSIGSREILgetRVITengggvcIGRPVDSIRVELIRisdepitvwDDDLRVAP 375
Cdd:PRK05677 343 AERWKEV--TGCAICEGYGMTETSPVVSVNPSQAI---QVGT-------IGIPVPSTLCKVID---------DDGNELPL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 376 GQVGEIVVQGPQVTRGYFQRPEADllSKISDPQGgfFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNT 455
Cdd:PRK05677 402 GEVGELCVKGPQVMKGYWQRPEAT--DEILDSDG--WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAA 477
|
330 340 350
....*....|....*....|....*....|....*....
gi 501446872 456 HPLVYRSALVGIGPKGSQQPV-ICIELEQGITTNQEQLR 493
Cdd:PRK05677 478 LPGVLQCAAIGVPDEKSGEAIkVFVVVKPGETLTKEQVM 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
31-476 |
2.66e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFI 109
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 110 GIPK--AQVARLLfgwAKDSLKTIITVG-------PRLFWGGITLDKLIQQSPDKPFEMAV------------------T 162
Cdd:PRK08751 129 VIDNfgTTVQQVI---ADTPVKQVITTGlgdmlgfPKAALVNFVVKYVKKLVPEYRINGAIrfrealalgrkhsmptlqI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEA----LQQVYRIQPG-EIDLPTFPLFALFApalgMTAviPEMDFTRP 237
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGcEVVITALPLYHIFA----LTA--NGLVFMKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 238 GSV--------DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaEGVEI 309
Cdd:PRK08751 280 GGCnhlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQV--TGLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 310 FTPYGATESLPVCSIGSREIlgetrvITENGGgvcIGRPVDSIRVelirisdepiTVWDDDLRVAP-GQVGEIVVQGPQV 388
Cdd:PRK08751 358 VEAYGLTETSPAACINPLTL------KEYNGS---IGLPIPSTDA----------CIKDDAGTVLAiGEIGELCIKGPQV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 389 TRGYFQRPEADllSKISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIG 468
Cdd:PRK08751 419 MKGYWKRPEET--AKVMDADGWL--HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP 494
|
....*...
gi 501446872 469 PKGSQQPV 476
Cdd:PRK08751 495 DEKSGEIV 502
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
15-498 |
3.13e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.84 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKvgaipvlidPGLGIK 94
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALR---------SGLYIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIGIPKAQVarLLFGWAKDSLKTIITvGP---RLFWGGiTLDKLiqqspdKPFEMAVTAADDQ---- 167
Cdd:PRK13390 78 AINHHLTAPEADYIVGDSGARV--LVASAALDGLAAKVG-ADlplRLSFGG-EIDGF------GSFEAALAGAGPRlteq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 ---AAILFTSGSTGPPKG--------AIYSHGNfsAQVEALQQVYRIQPGEIDLPTFPLFALfAP--------ALGMTAV 228
Cdd:PRK13390 148 pcgAVMLYSSGTTGFPKGiqpdlpgrDVDAPGD--PIVAIARAFYDISESDIYYSSAPIYHA-APlrwcsmvhALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 229 IPEmdftrpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIK--LPTLQRVISAGAPVPAVVMERFSQMLaeG 306
Cdd:PRK13390 225 LAK-------RFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRydVSSLRAVIHAAAPCPVDVKHAMIDWL--G 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 307 VEIFTPYGATESLPVCSIGSREILGETrvitengGGVciGRPVdsirVELIRISDepitvwDDDLRVAPGQVGEIVVQGP 386
Cdd:PRK13390 296 PIVYEYYSSTEAHGMTFIDSPDWLAHP-------GSV--GRSV----LGDLHICD------DDGNELPAGRIGTVYFERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 387 QVTRGYFQRPEADllSKISDPQGGFFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:PRK13390 357 RLPFRYLNDPEKT--AAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
490 500 510
....*....|....*....|....*....|...
gi 501446872 467 I-GPKGSQQPVICIELEQGITTNQEQLRsELLN 498
Cdd:PRK13390 435 VpDPEMGEQVKAVIQLVEGIRGSDELAR-ELID 466
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-188 |
7.52e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.93 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIgIPKAQVARLlfgwakDSLKTIITVGPRLFW-GGIT---------LDKLIQQSPDkp 156
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLI-VGEELVEAF------EEARADLARPPRLWVaGGDTlddpegyedLAAAAAGAPT-- 187
|
170 180 190
....*....|....*....|....*....|....*
gi 501446872 157 FEMAVTA---ADDQAAILFTSGSTGPPKGAIYSHG 188
Cdd:PRK08279 188 TNPASRSgvtAKDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
16-467 |
5.73e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 86.97 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 16 QLQPDTTAIIfpKGNQSLTFQELDRLSDRICHGLIRSGITRGtRTVLMVTPS-PEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK10946 34 HAASDAIAVI--CGERQFSYRELNQASDNLACSLRRQGIKPG-DTALVQLGNvAEFYITFFALLKLGVAPVNALFSHQRS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQPSAFIgipkAQVARLLFGwAKDSLKTIITVGPRLF-------WGGITLDKLIQQsPDKPFEMAVTAADDQ 167
Cdd:PRK10946 111 ELNAYASQIEPALLI----ADRQHALFS-DDDFLNTLVAEHSSLRvvlllndDGEHSLDDAINH-PAEDFTATPSPADEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL---FALFAP-ALGMtavipemdFTRPGSV--- 240
Cdd:PRK10946 185 AFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAahnYPMSSPgALGV--------FLAGGTVvla 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 -DPQKII--SAITSHKVT-TMFGSPAL---INRVGRSGAEQgiKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPY 313
Cdd:PRK10946 257 pDPSATLcfPLIEKHQVNvTALVPPAVslwLQAIAEGGSRA--QLASLKLLQVGGARLSETLARRIPAEL--GCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 314 GATESLpVCSigSREILGETRVITengggvCIGRPVDsirveliriSDEPITVWDDD-LRVAPGQVGEIVVQGPQVTRGY 392
Cdd:PRK10946 333 GMAEGL-VNY--TRLDDSDERIFT------TQGRPMS---------PDDEVWVADADgNPLPQGEVGRLMTRGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 393 FQRPEADllSKISDPQGgfFHRMGDLGRQDETGRLWFCGRKTHRV----ESvhgplftIPVEAVFN---THPLVYRSALV 465
Cdd:PRK10946 395 YKSPQHN--ASAFDANG--FYCSGDLVSIDPDGYITVVGREKDQInrggEK-------IAAEEIENlllRHPAVIHAALV 463
|
..
gi 501446872 466 GI 467
Cdd:PRK10946 464 SM 465
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
165-492 |
8.55e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 86.30 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAA--ILFTSGSTGPPKGAIYSHGN--FSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPG-S 239
Cdd:PRK07008 174 DENQAssLCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGpD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAITSHKVTTMFGSPA----LINRVgrsgAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGA 315
Cdd:PRK07008 254 LDGKSLYELIEAERVTFSAGVPTvwlgLLNHM----REAGLRFSTLRRTVIGGSACPPAMIRTFEDEY--GVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 316 TESLP---VCSIGSREI---LGETRVITENGGGVCIGrpVDsirvelIRISDE-----PitvWDDdlrVApgqVGEIVVQ 384
Cdd:PRK07008 328 TEMSPlgtLCKLKWKHSqlpLDEQRKLLEKQGRVIYG--VD------MKIVGDdgrelP---WDG---KA---FGDLQVR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 385 GPQVTRGYFQRpEADLLSKisdpqgGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSAL 464
Cdd:PRK07008 391 GPWVIDRYFRG-DASPLVD------GWFP-TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAC 462
|
330 340
....*....|....*....|....*....
gi 501446872 465 VGIG-PKGSQQPVICIELEQGITTNQEQL 492
Cdd:PRK07008 463 IACAhPKWDERPLLVVVKRPGAEVTREEL 491
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
144-496 |
8.86e-18 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 86.37 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 144 TLDKLIQQSPdkPFEMAVTAADDQ-AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPA 222
Cdd:cd05932 117 QWDDLIAQHP--PLEERPTRFPEQlATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 223 L--------GMTAVIPEmdftrpgSVDpqKIISAITSHKVTTMFGSPAL--------INRVGRSGAEQGIKLPTLQRVI- 285
Cdd:cd05932 195 FveggslygGVLVAFAE-------SLD--TFVEDVQRARPTLFFSVPRLwtkfqqgvQDKIPQQKLNLLLKIPVVNSLVk 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 286 ----------------SAGAPVPAVVMERFSQMlaeGVEIFTPYGATESLPVCSIgsrEILGETRVITengggvcIGRPV 349
Cdd:cd05932 266 rkvlkglgldqcrlagCGSAPVPPALLEWYRSL---GLNILEAYGMTENFAYSHL---NYPGRDKIGT-------VGNAG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 350 DSIRVeliRISDEpitvwdddlrvapgqvGEIVVQGPQVTRGYFQRPEADLLSKISDpqgGFFHrMGDLGRQDETGRLWF 429
Cdd:cd05932 333 PGVEV---RISED----------------GEILVRSPALMMGYYKDPEATAEAFTAD---GFLR-TGDKGELDADGNLTI 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 430 CGRKTHRVESVHGPLFT-IPVEAVFNTHPLVYRSALVGigpKGSQQPV-ICIELEQGITTNQEQLRSEL 496
Cdd:cd05932 390 TGRVKDIFKTSKGKYVApAPIENKLAEHDRVEMVCVIG---SGLPAPLaLVVLSEEARLRADAFARAEL 455
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
15-438 |
1.02e-17 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 85.68 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgik 94
Cdd:cd17645 8 VERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 nlksclaevqpsafigiPKAQVARLLFgwakDSLKTIItvgprlfwggitldkliqqspdkpfemaVTAADDQAAILFTS 174
Cdd:cd17645 83 -----------------PGERIAYMLA----DSSAKIL----------------------------LTNPDDLAYVIYTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLP----TFPLFAL-FAPALGMTAVIPEMDFTRpgSVDPQKIISAI 249
Cdd:cd17645 114 GSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVyasfSFDASAWeIFPHLTAGAALHVVPSER--RLDLDALNDYF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 250 TSHKVTTMFGSPALinrvgrsgAEQGIKLP--TLQRVISAGApvpavVMERFSQmlaEGVEIFTPYGATESlpvcsigsr 327
Cdd:cd17645 192 NQEGITISFLPTGA--------AEQFMQLDnqSLRVLLTGGD-----KLKKIER---KGYKLVNNYGPTEN--------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 328 EILGETRVITENGGGVCIGRPVDSIRVELIrisdepitvwDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADLLSKISD 406
Cdd:cd17645 247 TVVATSFEIDKPYANIPIGKPIDNTRVYIL----------DEALQLQPiGVAGELCIAGEGLARGYLNRPELTAEKFIVH 316
|
410 420 430
....*....|....*....|....*....|....
gi 501446872 407 PQ--GGFFHRMGDLGRQDETGRLWFCGRKTHRVE 438
Cdd:cd17645 317 PFvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
33-459 |
1.28e-17 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 85.73 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAfigip 112
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 kaqvarllfgwakdslktIITVGprlfwggitldkliqqspdKPfemavtaaDDQAAILFTSGSTGPPKGAIYSHGNFSA 192
Cdd:cd17639 81 ------------------IFTDG-------------------KP--------DDLACIMYTSGSTGNPKGVMLTHGNLVA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 193 QVEALQQVYRIQPGEID--LPTFPLfalfapalgmtAVIPEMDFT--------RPGSVDPQKIISAITSH--------KV 254
Cdd:cd17639 116 GIAGLGDRVPELLGPDDryLAYLPL-----------AHIFELAAEnvclyrggTIGYGSPRTLTDKSKRGckgdltefKP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 255 TTMFGSPALINRVgRSGAEQGI-KLPTLQRVI-----------------------------------------SAGAPVP 292
Cdd:cd17639 185 TLMVGVPAIWDTI-RKGVLAKLnPMGGLKRTLfwtayqsklkalkegpgtplldelvfkkvraalggrlrymlSGGAPLS 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 293 AVVMERFSQMLAEgveIFTPYGATESlpvCSIGSREILGETRVitengggVCIGRPVDSIRVELIRIsdepitvwdDDLR 372
Cdd:cd17639 264 ADTQEFLNIVLCP---VIQGYGLTET---CAGGTVQDPGDLET-------GRVGPPLPCCEIKLVDW---------EEGG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 373 V---APGQVGEIVVQGPQVTRGYFQRPEadLLSKISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLftIP- 448
Cdd:cd17639 322 YstdKPPPRGEILIRGPNVFKGYYKNPE--KTKEAFDGDGWF--HTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY--IAl 395
|
490
....*....|...
gi 501446872 449 --VEAVFNTHPLV 459
Cdd:cd17639 396 ekLESIYRSNPLV 408
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
168-496 |
1.46e-17 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 83.92 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF------ALFAPAL-GMTAVIPEMDftrpgsv 240
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYhvgglaILVRSLLaGAELVLLERN------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 dpQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIkLPTLQRVISAGAPVPAVVMERFSQMlaeGVEIFTPYGATESlp 320
Cdd:cd17630 76 --QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAA-LKSLRAVLLGGAPIPPELLERAADR---GIPLYTTYGMTET-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 321 vcsigsreilgetrvitenGGGVCIGRPVDSIRVELIRISDepitvwDDDLRVAPGqvGEIVVQGPQVTRGYFQRPEADL 400
Cdd:cd17630 148 -------------------ASQVATKRPDGFGRGGVGVLLP------GRELRIVED--GEIWVGGASLAMGYLRGQLVPE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 401 LSKisdpqGGFFHrMGDLGRQDETGRLWFCGRKTHRVESvHGplFTI---PVEAVFNTHPLVYRSALVGIG-PKGSQQPV 476
Cdd:cd17630 201 FNE-----DGWFT-TKDLGELHADGRLTVLGRADNMIIS-GG--ENIqpeEIEAALAAHPAVRDAFVVGVPdEELGQRPV 271
|
330 340
....*....|....*....|
gi 501446872 477 ICIELEQGITTnqEQLRSEL 496
Cdd:cd17630 272 AVIVGRGPADP--AELRAWL 289
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
6-432 |
1.60e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 85.87 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQLQPDTTAIIFPKGN----QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVG 81
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPGhgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 82 --AIPV-----LIDPGLGikNLKSCLAEVQPSAFIGIPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPD 154
Cdd:PRK12582 130 vpAAPVspaysLMSHDHA--KLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLAATPPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 155 KPFE--MAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGE-----ID-LP---TFPLFALFAPAL 223
Cdd:PRK12582 208 AAVAaaIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppvsLDwMPwnhTMGGNANFNGLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 224 --GMTAVIpemDFTRPGSVDPQKIISAITSHKVTTMFGSPA----LINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVME 297
Cdd:PRK12582 288 wgGGTLYI---DDGKPLPGMFEETIRNLREISPTVYGNVPAgyamLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 298 RFsQMLA-----EGVEIFTPYGATESLPVCSigsreilgETRVITENGGgvCIGRPVDSIrvelirisdepitvwddDLR 372
Cdd:PRK12582 365 RM-QALAvrttgHRIPFYTGYGATETAPTTT--------GTHWDTERVG--LIGLPLPGV-----------------ELK 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 373 VAP-GQVGEIVVQGPQVTRGYFQRPEadLLSKISDPQGgfFHRMGDLGR----QDETGRLWFCGR 432
Cdd:PRK12582 417 LAPvGDKYEVRVKGPNVTPGYHKDPE--LTAAAFDEEG--FYRLGDAARfvdpDDPEKGLIFDGR 477
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
164-467 |
1.61e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 85.04 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 164 ADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGmtaVIPEM----DFTRPGS 239
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLG---VLGPLrignRFVHTGR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAItSHKVTTMFGSPALINRVGRSGAEQGiKLPTLQRVISAGAPVPAVVMERFSQmlAEGVEIFTPYGATESL 319
Cdd:PRK07787 204 PTPEAYAQAL-SEGGTLYFGVPTVWSRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAA--LTGHRPVERYGMTETL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 320 PVCSigsreilgeTRVITENGGGVcIGRPVDSIRVELIRISDEPITvWDDDlrvapgQVGEIVVQGPQVTRGYFQRPEAD 399
Cdd:PRK07787 280 ITLS---------TRADGERRPGW-VGLPLAGVETRLVDEDGGPVP-HDGE------TVGELQVRGPTLFDGYLNRPDAT 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501446872 400 LLSKISDpqgGFFhRMGDLGRQDETGRLWFCGRKThrVESVHGPLFTI---PVEAVFNTHPLVYRSALVGI 467
Cdd:PRK07787 343 AAAFTAD---GWF-RTGDVAVVDPDGMHRIVGRES--TDLIKSGGYRIgagEIETALLGHPGVREAAVVGV 407
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
11-492 |
2.74e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.00 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPG 90
Cdd:PRK08162 24 LERAAEVYPDRPAVIH--GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 91 LGIKNLKSCLAEVQPSAFIGIPK-AQVARLLFGWAKDSLKTIITV-------GPRLfwGGITLDKLIQQ-SPDKPFEMAv 161
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEfAEVAREALALLPGPKPLVIDVddpeypgGRFI--GALDYEAFLASgDPDFAWTLP- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 162 taADDQAAIL--FTSGSTGPPKGAIYSH--------GNFSAQVEALQQVYriqpgeidLPTFPLFAL----FAPAlgMTA 227
Cdd:PRK08162 179 --ADEWDAIAlnYTSGTTGNPKGVVYHHrgaylnalSNILAWGMPKHPVY--------LWTLPMFHCngwcFPWT--VAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 228 VIPEMDFTRpgSVDPQKIISAITSHKVTTMFGSP----ALINrvGRSGAEQGIKLPTlqRVISAGAPVPAVVMErfsQML 303
Cdd:PRK08162 247 RAGTNVCLR--KVDPKLIFDLIREHGVTHYCGAPivlsALIN--APAEWRAGIDHPV--HAMVAGAAPPAAVIA---KME 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 304 AEGVEIFTPYGATESL-PVcsigsreilgetrvitenggGVCIGRP-----VDSIRVEL-----IRI-SDEPITVWD-DD 370
Cdd:PRK08162 318 EIGFDLTHVYGLTETYgPA--------------------TVCAWQPewdalPLDERAQLkarqgVRYpLQEGVTVLDpDT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 371 LRVAP--GQ-VGEIVVQGPQVTRGYFQRPEAdllskiSDP--QGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLF 445
Cdd:PRK08162 378 MQPVPadGEtIGEIMFRGNIVMKGYLKNPKA------TEEafAGGWFH-TGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501446872 446 TIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQL 492
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVVAKpDPKWGEVPCAFVELKDGASATEEEI 498
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-493 |
4.66e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.17 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 3 TFANIAAHLprmAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PRK07798 4 NIADLFEAV---ADAVPDRVALVC--GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLID----PGlgikNLKSCLAEVQPSAFI--GIPKAQVARLLFGWAKdsLKTIITV----GPRLFWGGITLDKLI-QQ 151
Cdd:PRK07798 79 VPVNVNyryvED----ELRYLLDDSDAVALVyeREFAPRVAEVLPRLPK--LRTLVVVedgsGNDLLPGAVDYEDALaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 152 SPDKPFEmaVTAADDQAaILFTSGSTGPPKGAIYSH---------------GNFSAQVEALQQVYRIQPGEIDLPTFPLF 216
Cdd:PRK07798 153 SPERDFG--ERSPDDLY-LLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRFPAPPLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 217 ----------ALFApalGMTAVIPEMDftrpgSVDPQKIISAITSHKVTTM------FGSP---ALINRvgrsgaeQGIK 277
Cdd:PRK07798 230 hgagqwaafaALFS---GQTVVLLPDV-----RFDADEVWRTIEREKVNVItivgdaMARPlldALEAR-------GPYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 278 LPTLQRVISAGAPVPAVVMERFSQMLaEGVEIFTPYGATESlpvcsigsreilGETRVITENGGGVCIGRPvdsiRVELi 357
Cdd:PRK07798 295 LSSLFAIASGGALFSPSVKEALLELL-PNVVLTDSIGSSET------------GFGGSGTVAKGAVHTGGP----RFTI- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 358 risDEPITVWDDDLR-VAPGQVGE-IVVQGPQVTRGYFQRPE--ADLLSKIsdpqGGffHRM---GDLGRQDETGRLWFC 430
Cdd:PRK07798 357 ---GPRTVVLDEDGNpVEPGSGEIgWIARRGHIPLGYYKDPEktAETFPTI----DG--VRYaipGDRARVEADGTITLL 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501446872 431 GRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLR 493
Cdd:PRK07798 428 GRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVpDERWGQEVVAVVQLREGARPDLAELR 491
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
19-496 |
4.90e-17 |
|
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: 83.68 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFPkgNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlks 98
Cdd:cd17656 2 PDAVAVVFE--NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 claevqpsafigiPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITL---DKLIQQSPDKPFEMaVTAADDQAAILFTSG 175
Cdd:cd17656 73 -------------PEERRIYIMLDSGVRVVLTQRHLKSKLSFNKSTIlleDPSISQEDTSNIDY-INNSDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 176 STGPPKGAIYSHGNFSAQVEALQQVYRIQPGEiDLPTFPLFA-------LFAPAL-GMTAVIPEMDFTRpgsvDPQKIIS 247
Cdd:cd17656 139 TTGKPKGVQLEHKNMVNLLHFEREKTNINFSD-KVLQFATCSfdvcyqeIFSTLLsGGTLYIIREETKR----DVEQLFD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFGSPALINRVGrsgAEQGIK--LPT-LQRVISAGAPVpaVVMERFSQMLAE-GVEIFTPYGATESLPV-- 321
Cdd:cd17656 214 LVKRHNIEVVFLPVAFLKFIF---SEREFInrFPTcVKHIITAGEQL--VITNEFKEMLHEhNVHLHNHYGPSETHVVtt 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 322 CSIGSREILGETRVItengggvciGRPvdsirvelirISDEPITVWDDDLRVAP-GQVGEIVVQGPQVTRGYFQRPEADL 400
Cdd:cd17656 289 YTINPEAEIPELPPI---------GKP----------ISNTWIYILDQEQQLQPqGIVGELYISGASVARGYLNRQELTA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 401 LSKISDPQGGF--FHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyRSALVGIGPKGSQQP 475
Cdd:cd17656 350 EKFFPDPFDPNerMYRTGDLARYLPDGNIEFLGRADHQVK-IRG--YRIelgEIEAQLLNHPGV-SEAVVLDKADDKGEK 425
|
490 500
....*....|....*....|.
gi 501446872 476 VICIELEQGITTNQEQLRSEL 496
Cdd:cd17656 426 YLCAYFVMEQELNISQLREYL 446
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
152-497 |
4.97e-17 |
|
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: 83.58 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 152 SPDKPFEmAVTAADDqaaILFTSGSTGPPKGAIYSHGNFSAQVEAL-----------QQVYrIQPGeidlptfPLF---- 216
Cdd:cd05929 116 SPETPIE-DEAAGWK---MLYSGGTTGRPKGIKRGLPGGPPDNDTLmaaalgfgpgaDSVY-LSPA-------PLYhaap 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 217 ---ALFAPALGMTAVIPEmdftrpgSVDPQKIISAITSHKVTTMFGSPALINRVgrsgaeqgIKLP----------TLQR 283
Cdd:cd05929 184 frwSMTALFMGGTLVLME-------KFDPEEFLRLIERYRVTFAQFVPTMFVRL--------LKLPeavrnaydlsSLKR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 284 VISAGAPVPAVVMErfsQMLAEGVE-IFTPYGATESLPVCSIGSREILgetrviTENGGgvcIGRPVDSIrvelIRISDE 362
Cdd:cd05929 249 VIHAAAPCPPWVKE---QWIDWGGPiIWEYYGGTEGQGLTIINGEEWL------THPGS---VGRAVLGK----VHILDE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 363 pitvwdDDLRVAPGQVGEIVVQGPQvTRGYFQRPEAdllSKISDPQGGFfHRMGDLGRQDETGRLWFCGRKTHRVESVHG 442
Cdd:cd05929 313 ------DGNEVPPGEIGEVYFANGP-GFEYTNDPEK---TAAARNEGGW-STLGDVGYLDEDGYLYLTDRRSDMIISGGV 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 443 PLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGiTTNQEQLRSELL 497
Cdd:cd05929 382 NIYPQEIENALIAHPKVLDAAVVGVpDEELGQRVHAVVQPAPG-ADAGTALAEELI 436
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
15-510 |
8.22e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 83.27 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIK 94
Cdd:PRK13382 53 AQRCPDRPGLIDELG--TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 NLKSCLAEVQ--------------PSAFIGIPKAqvARLLfGWAKDSlktiitvgprlfwGGITLDKLIqqspDKPFEMA 160
Cdd:PRK13382 131 ALAEVVTREGvdtviydeefsatvDRALADCPQA--TRIV-AWTDED-------------HDLTVEVLI----AAHAGQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 161 VTAADDQA-AILFTSGSTGPPKGAIYSHgnfSAQVEALQQVYRIQPGEIDLPTF---PLF-------ALFAPALGMTAVi 229
Cdd:PRK13382 191 PEPTGRKGrVILLTSGTTGTPKGARRSG---PGGIGTLKAILDRTPWRAEEPTVivaPMFhawgfsqLVLAASLACTIV- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 230 pemdfTRPgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAE-----QGIKLptlqRVISA-GAPV-PAVV---MERF 299
Cdd:PRK13382 267 -----TRR-RFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEvrnrySGRSL----RFAAAsGSRMrPDVViafMDQF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 300 sqmlaeGVEIFTPYGATESLPVCSIGSREIlgetRVITENGggvciGRPVDSIRvelirisdepITVWDDDLRVAP-GQV 378
Cdd:PRK13382 337 ------GDVIYNNYNATEAGMIATATPADL----RAAPDTA-----GRPAEGTE----------IRILDQDFREVPtGEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 379 GEIVVQGPQVTRGYFQrpeadllSKISDPQGGFFHRmGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPL 458
Cdd:PRK13382 392 GTIFVRNDTQFDGYTS-------GSTKDFHDGFMAS-GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 501446872 459 VYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRSELLNIAASHPHTREIS 510
Cdd:PRK13382 464 VAEAAVIGVdDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIV 516
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-466 |
1.28e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 82.18 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIpvlidpglgiknlksclaeVQP--SAFIg 110
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAV-------------------YQPlfTAFG- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 iPKAQVARLlfgwAKDSLKTIITvgprlfwGGITLDKLiqqsPDKPFEMavtaaddqaaiLFTSGSTGPPKGAIYSHGNF 190
Cdd:cd05973 61 -PKAIEHRL----RTSGARLVVT-------DAANRHKL----DSDPFVM-----------MFTSGTTGLPKGVPVPLRAL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 191 SAQVEALQQVYRIQPGEI-----DlPTFP---LFALFAP-ALGMTAVIPEMDFTRPGSVDpqkiisAITSHKVTTMFGSP 261
Cdd:cd05973 114 AAFGAYLRDAVDLRPEDSfwnaaD-PGWAyglYYAITGPlALGHPTILLEGGFSVESTWR------VIERLGVTNLAGSP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 262 ALINRVGRSGAEQGIKLP-TLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATE-SLPVCSIGsreilGETRVITEN 339
Cdd:cd05973 187 TAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAAL--GVPIHDHYGQTElGMVLANHH-----ALEHPVHAG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 340 GggvcIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVV---QGPQVT-RGYFQRPEadllskiSDPQGGFFhR 414
Cdd:cd05973 260 S----AGRAMPGWRV----------AVLDDDGDeLGPGEPGRLAIdiaNSPLMWfRGYQLPDT-------PAIDGGYY-L 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 415 MGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:cd05973 318 TGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
161-496 |
1.68e-16 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 82.10 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 161 VTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIqPGEIDLPTFPLFALFAPA--------LGMTAVIpem 232
Cdd:cd17644 102 LTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGI-TSSDRVLQFASIAFDVAAeeiyvtllSGATLVL--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 233 dftRPGSV--DPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLP-TLQRVISAGAPVPAVVMERFSQMLAEGVEI 309
Cdd:cd17644 178 ---RPEEMrsSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVGNFIQL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 310 FTPYGATEslpvCSIGSrEILGETRVITENGGGVCIGRPVDSIRVelirisdepiTVWDDDLR-VAPGQVGEIVVQGPQV 388
Cdd:cd17644 255 INVYGPTE----ATIAA-TVCRLTQLTERNITSVPIGRPIANTQV----------YILDENLQpVPVGVPGELHIGGVGL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 389 TRGYFQRPEADLLSKISDP----QGGFFHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPLVyR 461
Cdd:cd17644 320 ARGYLNRPELTAEKFISHPfnssESERLYKTGDLARYLPDGNIEYLGRIDNQVK-IRG--FRIelgEIEAVLSQHNDV-K 395
|
330 340 350
....*....|....*....|....*....|....*..
gi 501446872 462 SALVGI--GPKGSQQPVICIELEQGITTNQEQLRSEL 496
Cdd:cd17644 396 TAVVIVreDQPGNKRLVAYIVPHYEESPSTVELRQFL 432
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-471 |
2.68e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.91 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 5 ANIAAHLPRMAQLQPDttaiifpkgnQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIP 84
Cdd:PRK05691 3728 AQVAAHPQRIAASCLD----------QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGY 3797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 85 VLIDPGLGIKNLKSCLaEVQPSAFIGIPKAQVARllfgwAKDSLKTIITVG-PRLF-WGGITLDKLIQQSPDKpfemaVT 162
Cdd:PRK05691 3798 LPLDPGLPAQRLQRII-ELSRTPVLVCSAACREQ-----ARALLDELGCANrPRLLvWEEVQAGEVASHNPGI-----YS 3866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGA-IYSHGNFSAQveaLQQVYRIQPGEIDL------PTFPLFA---LFAPALGMTAVIPEM 232
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVmVEQRGMLNNQ---LSKVPYLALSEADViaqtasQSFDISVwqfLAAPLFGARVEIVPN 3943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 233 DFTRpgsvDPQKIISAITSHKVTTMFGSPALINRVgrsGAEQGIKLPTLQRVISAGAPVPAVV----MERFSQmlaegVE 308
Cdd:PRK05691 3944 AIAH----DPQGLLAHVQAQGITVLESVPSLIQGM---LAEDRQALDGLRWMLPTGEAMPPELarqwLQRYPQ-----IG 4011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 309 IFTPYGATEslpvCSIGS---REILGETRvitenGGGVCIGRPVDSIRVELIrisdepitvwDDDLRVAP-GQVGEIVVQ 384
Cdd:PRK05691 4012 LVNAYGPAE----CSDDVaffRVDLASTR-----GSYLPIGSPTDNNRLYLL----------DEALELVPlGAVGELCVA 4072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 385 GPQVTRGYFQRPEADLLSKISDPQGGF---FHRMGDLGRQDETGRLWFCGRKTHRVEsVHGplFTI---PVEAVFNTHPL 458
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFGAPgerLYRTGDLARRRSDGVLEYVGRIDHQVK-IRG--YRIelgEIEARLHEQAE 4149
|
490
....*....|....*
gi 501446872 459 VyRSALVGI--GPKG 471
Cdd:PRK05691 4150 V-REAAVAVqeGVNG 4163
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
165-476 |
3.35e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 81.41 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQveaLQQVYR------------IQPG-EIDLPTFPLFALFApalgMTAVIPE 231
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVAN---MLQVRAclsqlgpdgqplMKEGqEVMIAPLPLYHIYA----FTANCMC 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 232 MDFTRPGSV---DPQKI---ISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMlaE 305
Cdd:PRK12492 280 MMVSGNHNVlitNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQL--T 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 306 GVEIFTPYGATESLPVCSI---GSREILGEtrvitengggvcIGRPVDSIRVELIRisdepitvwDDDLRVAPGQVGEIV 382
Cdd:PRK12492 358 GCTIVEGYGLTETSPVASTnpyGELARLGT------------VGIPVPGTALKVID---------DDGNELPLGERGELC 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 383 VQGPQVTRGYFQRPEADllSKISDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRS 462
Cdd:PRK12492 417 IKGPQVMKGYWQQPEAT--AEALDAEGWF--KTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
|
330
....*....|....
gi 501446872 463 ALVGIGPKGSQQPV 476
Cdd:PRK12492 493 AAIGVPDERSGEAV 506
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-465 |
4.15e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 80.69 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIpvlidpglgiknlksclaeVQPSAFIGIP 112
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV-------------------VIPATTLLTP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 113 kaqvarllfgwakDSLKTiitvgpRLFWGGITLDKLIQqspdkpfemaVTAADDQAAILFTSGSTGPPKGAIYSHGNFSa 192
Cdd:cd05974 62 -------------DDLRD------RVDRGGAVYAAVDE----------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYP- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 193 qVEALQQVYRI--QPGEIDL----PTFPLFA---LFAPaLGMTAVIPEMDFTRpgsVDPQKIISAITSHKVTTmFGSPAL 263
Cdd:cd05974 112 -VGHLSTMYWIglKPGDVHWnissPGWAKHAwscFFAP-WNAGATVFLFNYAR---FDAKRVLAALVRYGVTT-LCAPPT 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 264 INRVGRSGAEQGIKLPtLQRVISAGAPVPAVVMERFSQmlAEGVEIFTPYGATESlpVCSIGSREilGETRVITEngggv 343
Cdd:cd05974 186 VWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRR--AWGLTIRDGYGQTET--TALVGNSP--GQPVKAGS----- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 344 cIGRPVDSIRVELIrisdepitvwddDLRVAPGQVGEIVV-----QGPQVTRGYFQRPEadllsKISDPQGGFFHRMGDL 418
Cdd:cd05974 254 -MGRPLPGYRVALL------------DPDGAPATEGEVALdlgdtRPVGLMKGYAGDPD-----KTAHAMRGGYYRTGDI 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 501446872 419 GRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALV 465
Cdd:cd05974 316 AMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVV 362
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
18-496 |
6.42e-16 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 80.82 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 18 QPDTTAIIF--PKGN--QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGI 93
Cdd:cd05967 64 RGDQIALIYdsPVTGteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 94 KNLKSCLAEVQP----SAFIGIPKAQV---------ARLLFGWakDSLKTII----TVGPRLFWGGITLD--KLIQQSpd 154
Cdd:cd05967 144 KELASRIDDAKPklivTASCGIEPGKVvpykplldkALELSGH--KPHHVLVlnrpQVPADLTKPGRDLDwsELLAKA-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 155 KPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFS-AQVEALQQVYRIQPGEIDLPTFPL-------FALFAPAL-GM 225
Cdd:cd05967 220 EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAvALNWSMRNIYGIKPGDVWWAASDVgwvvghsYIVYGPLLhGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 226 TAVIPEmdfTRP-GSVDPQKIISAITSHKVTTMFGSPALInRVGRSGAEQG--IK---LPTLQRVISAGAPVPAVVMERF 299
Cdd:cd05967 300 TTVLYE---GKPvGTPDPGAFWRVIEKYQVNALFTAPTAI-RAIRKEDPDGkyIKkydLSSLRTLFLAGERLDPPTLEWA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 300 SQMLaeGVEIFTPYGATES-LPVCS----IGSREI-LGETrvitengggvciGRPVDSIRVELIRisdepitvwDDDLRV 373
Cdd:cd05967 376 ENTL--GVPVIDHWWQTETgWPITAnpvgLEPLPIkAGSP------------GKPVPGYQVQVLD---------EDGEPV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 374 APGQVGEIVVQG---PQVTRGYFQRPEADLLSKISDPQGgfFHRMGDLGRQDETGRLWFCGRkTHRVESVHG-PLFTIPV 449
Cdd:cd05967 433 GPNELGNIVIKLplpPGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGR-TDDVINVAGhRLSTGEM 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501446872 450 EAVFNTHPLVYRSALVGIGP--KGsQQPVICIELEQGITTNQEQLRSEL 496
Cdd:cd05967 510 EESVLSHPAVAECAVVGVRDelKG-QVPLGLVVLKEGVKITAEELEKEL 557
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
15-432 |
2.22e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.78 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA--IPvlIDPGLG 92
Cdd:PRK04813 12 AQTQPDFPAYDY--LGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIP--VDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 IKNLKSCLAEVQPSAFIGIpkaqvarllfgwakDSLKTIITVGPRlfwggITLDKL---IQQSPDKPFEMAVTAaDDQAA 169
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIAT--------------EELPLEILGIPV-----ITLDELkdiFATGNPYDFDHAVKG-DDNYY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-FAL----FAPAL--GMTAVIPEMDFTRpgsvDP 242
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYsFDLsvmdLYPTLasGGTLVALPKDMTA----NF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 QKIISAITSHKVTTMFGSPalinrvgrSGAE--------QGIKLPTLQRVISAGAPVPAVV----MERFSQmlaegVEIF 310
Cdd:PRK04813 224 KQLFETLPQLPINVWVSTP--------SFADmclldpsfNEEHLPNLTHFLFCGEELPHKTakklLERFPS-----ATIY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 311 TPYGATE-SLPVCSIgsrEIlgeTRVITENGGGVCIGRPVDsirvelirisDEPITVWDDDL-RVAPGQVGEIVVQGPQV 388
Cdd:PRK04813 291 NTYGPTEaTVAVTSI---EI---TDEMLDQYKRLPIGYAKP----------DSPLLIIDEEGtKLPDGEQGEIVISGPSV 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 389 TRGYFQRPEADllskisdpQGGFFH-------RMGDLGRQDETgrLWFC-GR 432
Cdd:PRK04813 355 SKGYLNNPEKT--------AEAFFTfdgqpayHTGDAGYLEDG--LLFYqGR 396
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
165-432 |
2.63e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 78.70 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYriQPGEID-----LPTFPLFALFAPAL-GMTAVIPEMDFTRPg 238
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFF--SPKEDDvmmsfLPPFHAYGFNSCTLfPLLSGVPVVFAYNP- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 sVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGapvpavvmERFSQMLAEGVEIFTP------ 312
Cdd:PRK06334 260 -LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGG--------DAFKDSLYQEALKTFPhiqlrq 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 -YGATESLPVCSIGSREILGETRvitengggvCIGRPVDSIRVeLIrISDEpitvwdDDLRVAPGQVGEIVVQGPQVTRG 391
Cdd:PRK06334 331 gYGTTECSPVITINTVNSPKHES---------CVGMPIRGMDV-LI-VSEE------TKVPVSSGETGLVLTRGTSLFSG 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501446872 392 YFQrpeadllskiSDPQGGFFHR-------MGDLGRQDETGRLWFCGR 432
Cdd:PRK06334 394 YLG----------EDFGQGFVELggetwyvTGDLGYVDRHGELFLKGR 431
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
44-400 |
8.43e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 77.38 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 44 RICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgiknlksclaEVQPSAFIGIPKAQVARLLFGW 123
Cdd:PRK06060 42 RLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL----------HRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 124 AKDSLKTIITVGPRlfwggitlDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEAL-QQVYR 202
Cdd:PRK06060 112 LRDRFQPSRVAEAA--------ELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 203 IQPGEIDLPTFPLF--------ALFAPALGMTAVIPEMdftrPGSVDPQKIISaiTSHKVTTMFGSPALINRVgrSGAEQ 274
Cdd:PRK06060 184 LTPEDTGLCSARMYfayglgnsVWFPLATGGSAVINSA----PVTPEAAAILS--ARFGPSVLYGVPNFFARV--IDSCS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 275 GIKLPTLQRVISAGAPVPAVVMERFSQMLAeGVEIFTPYGATEslpvcsigsreiLGETRVitengggvciGRPVDSIRV 354
Cdd:PRK06060 256 PDSFRSLRCVVSAGEALELGLAERLMEFFG-GIPILDGIGSTE------------VGQTFV----------SNRVDEWRL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501446872 355 ELIRISDEPI---TVWDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEADL 400
Cdd:PRK06060 313 GTLGRVLPPYeirVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPV 361
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
7-466 |
1.05e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 76.56 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLP-------RMAQLqPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFfALTF-ALF 78
Cdd:PLN02246 19 IPNHLPlhdycfeRLSEF-SDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEF-VLAFlGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 79 KVGAI-----PVLIDPGLGiKNLKSCLAEVQpsafigIPKAQVARLLFGWAKDSLKTIITVGPRlFWGGITLDKLIQQSP 153
Cdd:PLN02246 97 RRGAVtttanPFYTPAEIA-KQAKASGAKLI------ITQSCYVDKLKGLAEDDGVTVVTIDDP-PEGCLHFSELTQADE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 154 DKPFEMAVtAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEalQQV------YRIQPGEIDLPTFPLFALFA------P 221
Cdd:PLN02246 169 NELPEVEI-SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA--QQVdgenpnLYFHSDDVILCVLPMFHIYSlnsvllC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 AL--GMTAVI-PEMDFTrpgsvdpqKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAP----VPAV 294
Cdd:PLN02246 246 GLrvGAAILImPKFEIG--------ALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPlgkeLEDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 295 VMERFSQ-MLAEGveiftpYGATESLPVCSIgsreILGETRVITENGGGVCiGRPVdsiRVELIRISDEpitvwDDDLRV 373
Cdd:PLN02246 318 FRAKLPNaVLGQG------YGMTEAGPVLAM----CLAFAKEPFPVKSGSC-GTVV---RNAELKIVDP-----ETGASL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 374 APGQVGEIVVQGPQVTRGYFQRPEAdllSKISDPQGGFFHrMGDLGRQDETGRLWFCGR-KthrvESVHGPLFTIP---V 449
Cdd:PLN02246 379 PRNQPGEICIRGPQIMKGYLNDPEA---TANTIDKDGWLH-TGDIGYIDDDDELFIVDRlK----ELIKYKGFQVApaeL 450
|
490
....*....|....*..
gi 501446872 450 EAVFNTHPLVYRSALVG 466
Cdd:PLN02246 451 EALLISHPSIADAAVVP 467
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
172-541 |
1.33e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.36 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQ-------PGEIDLPTFPLFALFAPALGMTaVIPEMDFTrpgsvdPQK 244
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKredsvliAGTLVHSLFLYGAISTLYVGQT-VHLMRKFI------PNQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMFGSPALINRVGRSGA--EQGIKlptlqrVISAGAPVPAVVMERFSQMLAEgVEIFTPYGATESLPVC 322
Cdd:PRK07638 223 VLDKLETENISVMYTVPTMLESLYKENRviENKMK------IISSGAKWEAEAKEKIKNIFPY-AKLYEFYGASELSFVT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 323 SIGSREilgETRVITEngggvcIGRPVDSIRVELIRISDEpitvwdddlRVAPGQVGEIVVQGPQVTRGYFQrpEADLLS 402
Cdd:PRK07638 296 ALVDEE---SERRPNS------VGRPFHNVQVRICNEAGE---------EVQKGEIGTVYVKSPQFFMGYII--GGVLAR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 403 KISDPQggfFHRMGDLGRQDETGRLWFCGRKTHRVesVHGPLFTIP--VEAVFNTHPLVYRSALVGIG-PKGSQQPVICI 479
Cdd:PRK07638 356 ELNADG---WMTVRDVGYEDEEGFIYIVGREKNMI--LFGGINIFPeeIESVLHEHPAVDEIVVIGVPdSYWGEKPVAII 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501446872 480 ELEQgittNQEQLRSELLNIAASHPHTREistILFHPAFPvdIRHNAKIFREKLAVWAAEEL 541
Cdd:PRK07638 431 KGSA----TKQQLKSFCLQRLSSFKIPKE---WHFVDEIP--YTNSGKIARMEAKSWIENQE 483
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
19-534 |
1.51e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.19 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 19 PDTTAIIFPKGnqSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKS 98
Cdd:PRK13383 49 PGRTAIIDDDG--ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 99 CLAEVQPSAFIGIPK--AQVARllfgwAKDSLKTI--ITVGPRlfwggitldkliqQSPDKPfemavTAADDQAAILFTS 174
Cdd:PRK13383 127 ALRAHHISTVVADNEfaERIAG-----ADDAVAVIdpATAGAE-------------ESGGRP-----AVAAPGRIVLLTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 175 GSTGPPKGAIYSHGNFSA---QVEALQQVyRIQPGEIDLPTFPLF-------ALFAPALGMTaVIPEMDFtrpgsvDPQK 244
Cdd:PRK13383 184 GTTGKPKGVPRAPQLRSAvgvWVTILDRT-RLRTGSRISVAMPMFhglglgmLMLTIALGGT-VLTHRHF------DAEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMFGSPALINRV----GRSGAEQgiKLPTLQRVISAGAPVPAVVMERFsqMLAEGVEIFTPYGATEslp 320
Cdd:PRK13383 256 ALAQASLHRADAFTAVPVVLARIlelpPRVRARN--PLPQLRVVMSSGDRLDPTLGQRF--MDTYGDILYNGYGSTE--- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 321 vCSIGSREILGETRVITENgggvcIGRPVDSIRVELIRISDEPitvwdddlrVAPGQVGEIVVQGPQVTRGYFQRPEADL 400
Cdd:PRK13383 329 -VGIGALATPADLRDAPET-----VGKPVAGCPVRILDRNNRP---------VGPRVTGRIFVGGELAGTRYTDGGGKAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 401 LSKISDpqggffhrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGIG-PKGSQQPVICI 479
Cdd:PRK13383 394 VDGMTS--------TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPdERFGHRLAAFV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 480 ELEQGITTNQEQLRSELLNIAASHPHTREISTILFHPAFPVdirhnAKIFREKLA 534
Cdd:PRK13383 466 VLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPT-----GKVLRKELP 515
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
11-533 |
2.31e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.83 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFpkGNQSLTF-QELDRLSdRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDP 89
Cdd:PLN03102 20 LKRASECYPNRTSIIY--GKTRFTWpQTYDRCC-RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 GLGIKNLKSCLAEVQPSA-FIG---IPKAQ-VARLLFGWAKDSLKTIITVG-----PRLFWGGITLDKLIQQSPDKPFEM 159
Cdd:PLN03102 97 RLDATSIAAILRHAKPKIlFVDrsfEPLAReVLHLLSSEDSNLNLPVIFIHeidfpKRPSSEELDYECLIQRGEPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 160 A----VTAADDQAAILFTSGSTGPPKGAIYSHGnfSAQVEALQQVYRIQPGeidlpTFPLFALFAPAL---GMTavIPEM 232
Cdd:PLN03102 177 ArmfrIQDEHDPISLNYTSGTTADPKGVVISHR--GAYLSTLSAIIGWEMG-----TCPVYLWTLPMFhcnGWT--FTWG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 233 DFTRPGS------VDPQKIISAITSHKVTTMFGSPALINRVGR-SGAEQGIKLPTLQrVISAGAPVPAVVMERFSQMlae 305
Cdd:PLN03102 248 TAARGGTsvcmrhVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgNSLDLSPRSGPVH-VLTGGSPPPAALVKKVQRL--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 306 GVEIFTPYGATESL-PV--CsigsrEILGETRVITENGggvcigrpvdsiRVEL-IRISDEPITVWDDDLRVAPGQ---- 377
Cdd:PLN03102 324 GFQVMHAYGLTEATgPVlfC-----EWQDEWNRLPENQ------------QMELkARQGVSILGLADVDVKNKETQesvp 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 378 -----VGEIVVQGPQVTRGYFQRPEADLLSkisdpqggFFH---RMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPV 449
Cdd:PLN03102 387 rdgktMGEIVIKGSSIMKGYLKNPKATSEA--------FKHgwlNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 450 EAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRS------ELLNIAASH-PHTREISTILFHPAFPVD 521
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMpHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerDLIEYCRENlPHFMCPRKVVFLQELPKN 538
|
570
....*....|..
gi 501446872 522 irHNAKIFREKL 533
Cdd:PLN03102 539 --GNGKILKPKL 548
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
11-492 |
3.71e-14 |
|
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: 74.87 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLqPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPG 90
Cdd:cd17642 24 MKRYASV-PGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 91 LGIKNLKSCLAEVQPSaFIGIPKAQVARLLFGWAKDS-LKTIITVGPRLFWGGI-TLDKLIQQSPDKPFEM------AVT 162
Cdd:cd17642 103 YNERELDHSLNISKPT-IVFCSKKGLQKVLNVQKKLKiIKTIIILDSKEDYKGYqCLYTFITQNLPPGFNEydfkppSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGAIYSHGNFSAQVE-ALQQVY--RIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPGS 239
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 240 VDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAP----VPAVVMERFS-QMLAEGveiftpYG 314
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPlskeVGEAVAKRFKlPGIRQG------YG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 315 ATESlpvcsigsreilgETRVITENGGGV---CIGRPVDSIRVELIRIsdepitvwDDDLRVAPGQVGEIVVQGPQVTRG 391
Cdd:cd17642 336 LTET-------------TSAILITPEGDDkpgAVGKVVPFFYAKVVDL--------DTGKTLGPNERGELCVKGPMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 392 YFQRPEADLLSKISDpqgGFFHRmGDLGRQDETGRLWFCGR-------KTHRVESVHgplftipVEAVFNTHPLVYRSAL 464
Cdd:cd17642 395 YVNNPEATKALIDKD---GWLHS-GDIAYYDEDGHFFIVDRlkslikyKGYQVPPAE-------LESILLQHPKIFDAGV 463
|
490 500
....*....|....*....|....*....
gi 501446872 465 VGI-GPKGSQQPVICIELEQGITTNQEQL 492
Cdd:cd17642 464 AGIpDEDAGELPAAVVVLEAGKTMTEKEV 492
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
11-465 |
1.35e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 73.34 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGtRTVLMVTPS-PEFFALTFALFKVGAIPVLIDP 89
Cdd:PLN02479 26 LERAAVVHPTRKSVVH--GSVRYTWAQTYQRCRRLASALAKRSIGPG-STVAVIAPNiPAMYEAHFGVPMAGAVVNCVNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 90 GLGIKNLKSCLAEVQPSAFIgipkaqVARLLFGWAKDSLKTI-------------ITVG-----PR-----LFWGGITLD 146
Cdd:PLN02479 103 RLNAPTIAFLLEHSKSEVVM------VDQEFFTLAEEALKILaekkkssfkppllIVIGdptcdPKslqyaLGKGAIEYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 147 KLIQqSPDKPFEMAVTAADDQA-AILFTSGSTGPPKGAIYSHGnfSAQVEALQQ--VYRIQPGEIDLPTFPLFAL--FAP 221
Cdd:PLN02479 177 KFLE-TGDPEFAWKPPADEWQSiALGYTSGTTASPKGVVLHHR--GAYLMALSNalIWGMNEGAVYLWTLPMFHCngWCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 222 ALGMTAVIPEMDFTRpgSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGI-KLPTLQRVISAGAPVPAVVMERFS 300
Cdd:PLN02479 254 TWTLAALCGTNICLR--QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 301 QmlaEGVEIFTPYGATEslpvcsigsreilgetrviTENGGGVCIGRPV-DSIRVEL---------IR-ISDEPITVWD- 368
Cdd:PLN02479 332 E---KGFRVTHTYGLSE-------------------TYGPSTVCAWKPEwDSLPPEEqarlnarqgVRyIGLEGLDVVDt 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 369 DDLRVAPGQ---VGEIVVQGPQVTRGYFQRPEADLLSKisdpQGGFFHRmGDLGRQDETGRLWFCGRKTHRVESVHGPLF 445
Cdd:PLN02479 390 KTMKPVPADgktMGEIVMRGNMVMKGYLKNPKANEEAF----ANGWFHS-GDLGVKHPDGYIEIKDRSKDIIISGGENIS 464
|
490 500
....*....|....*....|
gi 501446872 446 TIPVEAVFNTHPLVYRSALV 465
Cdd:PLN02479 465 SLEVENVVYTHPAVLEASVV 484
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
43-459 |
7.44e-13 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 71.30 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 43 DRICH---GLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIGIPKaQVARL 119
Cdd:PLN02387 114 ERVCNfasGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK-QLKKL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 120 LFgwAKDSLKTIITV------GPRL--------FWGGIT---LDKLIQQSPDKPfemAVTAADDQAAILFTSGSTGPPKG 182
Cdd:PLN02387 193 ID--ISSQLETVKRViymddeGVDSdsslsgssNWTVSSfseVEKLGKENPVDP---DLPSPNDIAVIMYTSGSTGLPKG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 183 AIYSHGNFSAQVEALQQVY-RIQPGEIDLPTFPL---FALFAPALgMTAVIPEMDFtrpGSvdPQKIISaiTSHKV---- 254
Cdd:PLN02387 268 VMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLahiLELAAESV-MAAVGAAIGY---GS--PLTLTD--TSNKIkkgt 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 255 ---------TTMFGSPALINRVgRSG------AEQGI--KLPTL--QRVISA------GA--------------PVPAVV 295
Cdd:PLN02387 340 kgdasalkpTLMTAVPAILDRV-RDGvrkkvdAKGGLakKLFDIayKRRLAAiegswfGAwglekllwdalvfkKIRAVL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 296 MERFSQMLAE----------------GVEIFTPYGATESlpvCSIGSREILGETRVitengGGVciGRPVDSIRVELI-- 357
Cdd:PLN02387 419 GGRIRFMLSGgaplsgdtqrfiniclGAPIGQGYGLTET---CAGATFSEWDDTSV-----GRV--GPPLPCCYVKLVsw 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 358 -----RISDEPITvwdddlRvapgqvGEIVVQGPQVTRGYFQRPE-ADLLSKIsDPQGGFFHRMGDLGRQDETGRLWFCG 431
Cdd:PLN02387 489 eeggyLISDKPMP------R------GEIVIGGPSVTLGYFKNQEkTDEVYKV-DERGMRWFYTGDIGQFHPDGCLEIID 555
|
490 500
....*....|....*....|....*....
gi 501446872 432 RKTHRVESVHGPLFTI-PVEAVFNTHPLV 459
Cdd:PLN02387 556 RKKDIVKLQHGEYVSLgKVEAALSVSPYV 584
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
11-432 |
8.17e-13 |
|
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: 70.92 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIFPKGN---QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLI 87
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGNggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 88 DPGLGIKN-----LKSCLAEVQPSAFIGIPKAQVARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMAVT 162
Cdd:cd05921 81 SPAYSLMSqdlakLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AA--DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEID-----LP---TFPLFALFAPAL--GMTAVIP 230
Cdd:cd05921 161 AVgpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPvlvdwLPwnhTFGGNHNFNLVLynGGTLYID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 231 EmdftrpGSVDPQKIISAITSHK---VTTMFGSPA----LINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQM- 302
Cdd:cd05921 241 D------GKPMPGGFEETLRNLReisPTVYFNVPAgwemLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALa 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 303 ---LAEGVEIFTPYGATESLPVCSIgsreilgeTRVITENGGgvCIGRPVDSIRVELirisdepitvwdddlrVAPGQVG 379
Cdd:cd05921 315 vatVGERIPMMAGLGATETAPTATF--------THWPTERSG--LIGLPAPGTELKL----------------VPSGGKY 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 380 EIVVQGPQVTRGYFQRPEadLLSKISDPQGgfFHRMGDLGR----QDETGRLWFCGR 432
Cdd:cd05921 369 EVRVKGPNVTPGYWRQPE--LTAQAFDEEG--FYCLGDAAKladpDDPAKGLVFDGR 421
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
163-486 |
1.08e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 70.44 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF------ALFAPALGMTAVIpemdfTR 236
Cdd:PRK13388 148 DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFhsnavmAGWAPAVASGAAV-----AL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 PGSVDPQKIISAITSHKVTTMfgspaliNRVGRSGAeqgIKLPTLQRVISAGAPVPAVV--------MERFSQMLaeGVE 308
Cdd:PRK13388 223 PAKFSASGFLDDVRRYGATYF-------NYVGKPLA---YILATPERPDDADNPLRVAFgneasprdIAEFSRRF--GCQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 309 IFTPYGATEslpvcsigsreilGETRVITENGG--GVcIGRPVDSIR-VELIRISDEPITVWDDDLRVAPGQ--VGEIV- 382
Cdd:PRK13388 291 VEDGYGSSE-------------GAVIVVREPGTppGS-IGRGAPGVAiYNPETLTECAVARFDAHGALLNADeaIGELVn 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 383 VQGPQVTRGYFQRPEADLlSKISDpqgGFFhRMGDLGRQDETGRLWFCGRKTH--RVESVHgpLFTIPVEAVFNTHPLVY 460
Cdd:PRK13388 357 TAGAGFFEGYYNNPEATA-ERMRH---GMY-WSGDLAYRDADGWIYFAGRTADwmRVDGEN--LSAAPIERILLRHPAIN 429
|
330 340
....*....|....*....|....*..
gi 501446872 461 RSALVGI-GPKGSQQPVICIELEQGIT 486
Cdd:PRK13388 430 RVAVYAVpDERVGDQVMAALVLRDGAT 456
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-523 |
1.12e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 69.33 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 164 ADDQAaILFTSGSTGPPKGAIYSHGNF---------SAQVEALQQVYRIQ-----PGEIDLPTFPLF-------ALFAPA 222
Cdd:cd05924 3 ADDLY-ILYTGGTTGMPKGVMWRQEDIfrmlmggadFGTGEFTPSEDAHKaaaaaAGTVMFPAPPLMhgtgswtAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 223 LGMTAVIPEMDFtrpgsvDPQKIISAITSHKVTTM------FGSPaLINRVGRSGAeqgIKLPTLQRVISAGAPVPAVVM 296
Cdd:cd05924 82 GGQTVVLPDDRF------DPEEVWRTIEKHKVTSMtivgdaMARP-LIDALRDAGP---YDLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 297 ERFsQMLAEGVEIFTPYGATESLPVCSIGSREILGETRVITENGGGVCigrpvdsirvelirisdepitVWDDDLRV--- 373
Cdd:cd05924 152 QGL-LELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV---------------------VLDDDGRVvpp 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 374 APGQVGEIVVQGpQVTRGYFQRPE--ADLLSKISDPQGGFfhrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEA 451
Cdd:cd05924 210 GSGGVGWIARRG-HIPLGYYGDEAktAETFPEVDGVRYAV---PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEE 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 452 VFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRSELLNIAASHPHTREI---STILFHPAFPVDIR 523
Cdd:cd05924 286 ALKSHPAVYDVLVVGRpDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVvfvDEIERSPAGKADYR 361
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
164-432 |
1.58e-12 |
|
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: 69.82 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 164 ADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL--------FALfAPAL-GMTA-VIPEMD 233
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLthdmgliaFHL-APLIaGMNQyLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 234 FTRpgsvDPQKIISAITSHKVTTM----FGSPALINRVGRSGAEQgIKLPTLQRVISAGAPVPAVVMERF-SQMLAEGVE 308
Cdd:cd05908 184 FIR----RPILWLKKASEHKATIVsspnFGYKYFLKTLKPEKAND-WDLSSIRMILNGAEPIDYELCHEFlDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 309 ---IFTPYGATE-SLPVC-----------SIGSREIL---GETRVITENGGG---VCIGRPVDSIRvelIRISDEPITVW 367
Cdd:cd05908 259 rnaILPVYGLAEaSVGASlpkaqspfktiTLGRRHVThgePEPEVDKKDSECltfVEVGKPIDETD---IRICDEDNKIL 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 368 DDdlrvapGQVGEIVVQGPQVTRGYFQRPEADllSKISDPQGgfFHRMGDLGRQdETGRLWFCGR 432
Cdd:cd05908 336 PD------GYIGHIQIRGKNVTPGYYNNPEAT--AKVFTDDG--WLKTGDLGFI-RNGRLVITGR 389
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
93-433 |
1.78e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 69.74 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 93 IKNLKSCLAEVqPSAfigipkaqvaRLL--FGWAKDSLKTI-ITVGPRLfwggITLDKLIQQSPDKPFEMAVTAADDQAA 169
Cdd:PLN02736 161 LNTLLSCLSEI-PSV----------RLIvvVGGADEPLPSLpSGTGVEI----VTYSKLLAQGRSSPQPFRPPKPEDVAT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALF--APALGMTAVIPEMDFTRPgsvDPQKIIS 247
Cdd:PLN02736 226 ICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYerVNQIVMLHYGVAVGFYQG---DNLKLMD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFGSPALINR--------VGRSGA-------------EQGI--------------------KLPTLQRVIS 286
Cdd:PLN02736 303 DLAALRPTIFCSVPRLYNRiydgitnaVKESGGlkerlfnaaynakKQALengknpspmwdrlvfnkikaKLGGRVRFMS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 287 AGA-PVPAVVMErFSQmLAEGVEIFTPYGATESlpVCSIGSreilgetrviTENGGGVC--IGRPVDSIRVELIRISDEP 363
Cdd:PLN02736 383 SGAsPLSPDVME-FLR-ICFGGRVLEGYGMTET--SCVISG----------MDEGDNLSghVGSPNPACEVKLVDVPEMN 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 364 ITVWDddlrvAPGQVGEIVVQGPQVTRGYFQrpEADLLSKISDPQgGFFHrMGDLGRQDETGRLWFCGRK 433
Cdd:PLN02736 449 YTSED-----QPYPRGEICVRGPIIFKGYYK--DEVQTREVIDED-GWLH-TGDIGLWLPGGRLKIIDRK 509
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-446 |
1.80e-12 |
|
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: 69.76 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIG 110
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 IPKAQVARLLFGWAK-DSLKTIITVGPR---------------LFWGGITLDKliqQSPDKpFEMAVTAA--DDQAAILF 172
Cdd:cd17641 90 EDEEQVDKLLEIADRiPSVRYVIYCDPRgmrkyddprlisfedVVALGRALDR---RDPGL-YEREVAAGkgEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 173 TSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPL-------FALFAPAL-GMTAVIPE-----MDFTR--- 236
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqmYSVGQALVcGFIVNFPEepetmMEDLReig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 PGSV-DPQKIISAITSHKVTTMFGSPALIN-------RVGRSGAEQG----------------------------IKLPT 280
Cdd:cd17641 246 PTFVlLPPRVWEGIAADVRARMMDATPFKRfmfelgmKLGLRALDRGkrgrpvslwlrlaswladallfrplrdrLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 281 LQRVISAGAPV-PavvmERFSQMLAEGVEIFTPYGATESLPVCSIgSREilGETRVITengggvcIGRPVDSIRVeliRI 359
Cdd:cd17641 326 LRSAATGGAALgP----DTFRFFHAIGVPLKQLYGQTELAGAYTV-HRD--GDVDPDT-------VGVPFPGTEV---RI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 360 SDepitvwdddlrvapgqVGEIVVQGPQVTRGYFQRPEAdllSKISDPQGGFFHrMGDLGRQDETGRLWFCGRKTHRVES 439
Cdd:cd17641 389 DE----------------VGEILVRSPGVFVGYYKNPEA---TAEDFDEDGWLH-TGDAGYFKENGHLVVIDRAKDVGTT 448
|
....*..
gi 501446872 440 VHGPLFT 446
Cdd:cd17641 449 SDGTRFS 455
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-432 |
3.54e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.81 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 7 IAAHLPRMAQLQPDTTAIIF----PKGNQSLTFQELDRLSDRICHGLIRSGITrGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFladdPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLIDPGLGIK-----NLKSCLAEVQP-----SAFIGIPKAQVARLlfgwAKDSLKTIITVGprlfwggiTLDKLIQQS 152
Cdd:PRK05691 90 IAVPAYPPESARrhhqeRLLSIIADAEPrllltVADLRDSLLQMEEL----AAANAPELLCVD--------TLDPALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 153 PDKPfemaVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEID-----LPTFPLFALFAPAL---- 223
Cdd:PRK05691 158 WQEP----ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDvivswLPLYHDMGLIGGLLqpif 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 224 -GMTAVI--PEMDFTRpgsvdPQKIISAItSHKVTTMFGSPAL-----INRVGRSgAEQGIKLPTLQRVISAGAPVPAVV 295
Cdd:PRK05691 234 sGVPCVLmsPAYFLER-----PLRWLEAI-SEYGGTISGGPDFayrlcSERVSES-ALERLDLSRWRVAYSGSEPIRQDS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 296 MERFSQMLA----EGVEIFTPYGATESLPVCSIGSR-----------EILGETRVitENGGG---VCIGRPVDSirvELI 357
Cdd:PRK05691 307 LERFAEKFAacgfDPDSFFASYGLAEATLFVSGGRRgqgipaleldaEALARNRA--EPGTGsvlMSCGRSQPG---HAV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 358 RISD-EPITVWDDdlrvapGQVGEIVVQGPQVTRGYFQRPEADLLSKIsDPQGGFFHRMGDLGRQDEtGRLWFCGR 432
Cdd:PRK05691 382 LIVDpQSLEVLGD------NRVGEIWASGPSIAHGYWRNPEASAKTFV-EHDGRTWLRTGDLGFLRD-GELFVTGR 449
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
157-497 |
7.95e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 67.89 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 157 FEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQV--YRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDF 234
Cdd:PRK05620 173 YDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 TRPG-SVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVM----ERFsqmlaeGVEI 309
Cdd:PRK05620 253 VFPGpDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIkaweERY------GVDV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 310 FTPYGATESLPVCSIgSRE---ILGETRVITEngggVCIGRPVDSIRVELIrisdepitvwdDDLRVAPG---QVGEIVV 383
Cdd:PRK05620 327 VHVWGMTETSPVGTV-ARPpsgVSGEARWAYR----VSQGRFPASLEYRIV-----------NDGQVMEStdrNEGEIQV 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 384 QGPQVTRGYFQRPEADLLSKISDPQG-------------GFFhRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVE 450
Cdd:PRK05620 391 RGNWVTASYYHSPTEEGGGAASTFRGedvedandrftadGWL-RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLE 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 501446872 451 AVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQE---QLRSELL 497
Cdd:PRK05620 470 NYIMAAPEVVECAVIGYpDDKWGERPLAVTVLAPGIEPTREtaeRLRDQLR 520
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
153-467 |
8.77e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.40 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 153 PDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLF------ALFAPALGMT 226
Cdd:PRK07867 140 RDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFhsnavmAGWAVALAAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 227 AVIPemdFTRPGSVdpQKIISAITSHKVTTMfgspaliNRVGRSGAeqgIKLPTLQRVISAGAPV--------PAVVMER 298
Cdd:PRK07867 220 ASIA---LRRKFSA--SGFLPDVRRYGATYA-------NYVGKPLS---YVLATPERPDDADNPLrivygnegAPGDIAR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 299 FSQMLaeGVEIFTPYGATEslpvcsiGSREIlgeTRviTENGGGVCIGRPVDSIRVELIRISDE-PITVWDDDLRV-APG 376
Cdd:PRK07867 285 FARRF--GCVVVDGFGSTE-------GGVAI---TR--TPDTPPGALGPLPPGVAIVDPDTGTEcPPAEDADGRLLnADE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 377 QVGEIV-VQGPQVTRGYFQRPEADLlSKISDpqgGFFHRmGDLGRQDETGRLWFCGRKTHRVEsVHGP-LFTIPVEAVFN 454
Cdd:PRK07867 351 AIGELVnTAGPGGFEGYYNDPEADA-ERMRG---GVYWS-GDLAYRDADGYAYFAGRLGDWMR-VDGEnLGTAPIERILL 424
|
330
....*....|...
gi 501446872 455 THPLVYRSALVGI 467
Cdd:PRK07867 425 RYPDATEVAVYAV 437
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
165-494 |
1.84e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 65.84 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEA----------------------LQQVYR-----IQPGEIDLPT-FPLF 216
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADAthdrlggpgqwllalpahhiagLQVLVRsviagSEPVELDVSAgFDPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 217 ALFAPALGMTAVipemdfTRPGSVDPQKIISAItshkvttmfGSPALINrvgrsgaeqgiKLPTLQRVISAGAPVPAVVM 296
Cdd:PRK07824 115 ALPRAVAELGGG------RRYTSLVPMQLAKAL---------DDPAATA-----------ALAELDAVLVGGGPAPAPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 297 ERFSQMlaeGVEIFTPYGATESlpvcsigsreilgetrviteNGGGVCIGRPVDSIRVeliRISDepitvwdddlrvapg 376
Cdd:PRK07824 169 DAAAAA---GINVVRTYGMSET--------------------SGGCVYDGVPLDGVRV---RVED--------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 377 qvGEIVVQGPQVTRGYFQRPEADLLSkisdpQGGFFhRMGDLGRQDEtGRLWFCGRKTHRVESvhGPLFTIP--VEAVFN 454
Cdd:PRK07824 208 --GRIALGGPTLAKGYRNPVDPDPFA-----EPGWF-RTDDLGALDD-GVLTVLGRADDAIST--GGLTVLPqvVEAALA 276
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 501446872 455 THPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQEQLRS 494
Cdd:PRK07824 277 THPAVADCAVFGLpDDRLGQRVVAAVVGDGGPAPTLEALRA 317
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
75-324 |
4.57e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.76 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 75 FALFKVGAIPVLIDPGLGIKNLKSC--LAEVQ----PSAFIGIPK--AQVARLLFG----WAKDsLKTIITVGPR---LF 139
Cdd:PRK06814 700 FALQSAGRVPAMINFSAGIANILSAckAAQVKtvltSRAFIEKARlgPLIEALEFGiriiYLED-VRAQIGLADKikgLL 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 140 WGGITLDKLIQQSPDKPfemavtaaddqAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALF 219
Cdd:PRK06814 779 AGRFPLVYFCNRDPDDP-----------AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSF 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 220 apalGMTA--VIPEMD----FTRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAeqGIKLPTLQRVISAGAPVPA 293
Cdd:PRK06814 848 ----GLTGglVLPLLSgvkvFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYAH--PYDFRSLRYVFAGAEKVKE 921
|
250 260 270
....*....|....*....|....*....|....*
gi 501446872 294 ----VVMERFsqmlaeGVEIFTPYGATESLPVCSI 324
Cdd:PRK06814 922 etrqTWMEKF------GIRILEGYGVTETAPVIAL 950
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
32-503 |
4.81e-11 |
|
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: 65.06 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 32 SLTFQELDRLSDRICHGLI-RSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLK----SCLAEVQPS 106
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGfllgTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 107 AFI---GIPKAQVARLLFGWAKDSLKTiitvgPRLFWggITLDKLIQQSPDKPF-EMAVTAADDQAAILFTSGSTGPPKG 182
Cdd:cd05905 94 VEAclkGLPKKLLKSKTAAEIAKKKGW-----PKILD--FVKIPKSKRSKLKKWgPHPPTRDGDTAYIEYSFSSDGSLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 183 AIYSHGNFSAQVEALQQVYRIQPGEidlptfPLFALFAPALGM---------------TAVIPEMDFTrpgsVDPQKIIS 247
Cdd:cd05905 167 VAVSHSSLLAHCRALKEACELYESR------PLVTVLDFKSGLglwhgcllsvysghhTILIPPELMK----TNPLLWLQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 248 AITSHKVTTMFGSPALIN----RVGRSGAEQGIKLPTLQRV----ISAGAPVPAVVMERFSQMLAEgveifTPYGATESL 319
Cdd:cd05905 237 TLSQYKVRDAYVKLRTLHwclkDLSSTLASLKNRDVNLSSLrmcmVPCENRPRISSCDSFLKLFQT-----LGLSPRAVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 320 PVcsIGSREIlgetRVITENG-GGVCIGRP-VD--SIRVELIRISDE---------PITVWDDDLRVA-----------P 375
Cdd:cd05905 312 TE--FGTRVN----PFICWQGtSGPEPSRVyLDmrALRHGVVRLDERdkpnslplqDSGKVLPGAQVAivnpetkglckD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 376 GQVGEIVVQGPQVTRGYFQRP-------EADLLSKISDPQGG-FFHRMGDLG----------RQDETGRLWfcgrkthRV 437
Cdd:cd05905 386 GEIGEIWVNSPANASGYFLLDgetndtfKVFPSTRLSTGITNnSYARTGLLGflrptkctdlNVEEHDLLF-------VV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 438 ESVHGPL-------FTIPVEA-VFNTHPLVYRSALVGIGPKgsqqpvICIELEQGITTNQEQLR---SELLNIAASH 503
Cdd:cd05905 459 GSIDETLevrglrhHPSDIEAtVMRVHPYRGRCAVFSITGL------VVVVAEQPPGSEEEALDlvpLVLNAILEEH 529
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
30-229 |
5.01e-11 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 64.75 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 30 NQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSClaevqpsafI 109
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHC---------I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 110 GIPKAqvarllfgwakdslKTIITvgpRLfwggitLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGN 189
Cdd:cd05939 72 TVSKA--------------KALIF---NL------LDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSR 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501446872 190 FSAQVEALQQVYRIQPGEIDLPTFPLFALFAPAL--------GMTAVI 229
Cdd:cd05939 129 YYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMgvgqallhGSTVVI 176
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
166-432 |
2.10e-10 |
|
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: 62.28 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 DQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQ-QVYRIQPGEIDLPTFPLFALFAPALGMTAVIPE------MDFTRPG 238
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGglcvtgGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 SVdpqkiISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLqRVISAGAPVPAVVMERFSQmLAEGVEIFTPYGATES 318
Cdd:cd17635 82 SL-----FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSL-RLIGYGGSRAIAADVRFIE-ATGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 319 LPVCSIGSREILGETRvitengggvCIGRPVDSIRVELIRIsdepitvwdDDLRVAPGQVGEIVVQGPQVTRGYFQRPE- 397
Cdd:cd17635 155 GTALCLPTDDDSIEIN---------AVGRPYPGVDVYLAAT---------DGIAGPSASFGTIWIKSPANMLGYWNNPEr 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 501446872 398 -ADLLSkisdpqGGFFHrMGDLGRQDETGRLWFCGR 432
Cdd:cd17635 217 tAEVLI------DGWVN-TGDLGERREDGFLFITGR 245
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
11-496 |
2.94e-10 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 62.96 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMAQLQPDTTAIIF----PKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVL 86
Cdd:cd05966 59 LDRHLKERGDKVAIIWegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGIKNLKSCLAEVQPSAFIG----------IPKAQVArllfgwakD-------SLKTIITV----------GPRLF 139
Cdd:cd05966 139 VFAGFSAESLADRINDAQCKLVITadggyrggkvIPLKEIV--------DealekcpSVEKVLVVkrtggevpmtEGRDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 140 WggitLDKLIQQSPDkPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEA-LQQVYRIQPGEI-----DLP-- 211
Cdd:cd05966 211 W----WHDLMAKQSP-ECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATtFKYVFDYHPDDIywctaDIGwi 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 212 TFPLFALFAP-ALGMTAVIPEMDFTRPgsvDPQKIISAITSHKVTTMFGSPALINRVGRSGAE--QGIKLPTLqRVI-SA 287
Cdd:cd05966 286 TGHSYIVYGPlANGATTVMFEGTPTYP---DPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEwvKKHDLSSL-RVLgSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 288 GAPV-P--------------AVVMERFSQMLAEGVEIfTPY-GATESLPvcsiGSR---------EILGE-TRVITENGG 341
Cdd:cd05966 362 GEPInPeawmwyyevigkerCPIVDTWWQTETGGIMI-TPLpGATPLKP----GSAtrpffgiepAILDEeGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 342 GV-CIGRPVDSIrvelIRisdepiTVWDDDLRvapgqvgeivvqgpqVTRGYFQRpeadllskisdPQGGFFhrMGDLGR 420
Cdd:cd05966 437 GYlVIKRPWPGM----AR------TIYGDHER---------------YEDTYFSK-----------FPGYYF--TGDGAR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 421 QDETGRLWFCGR-------KTHRvesvhgpLFTIPVEAVFNTHPLVYRSALVGIgP---KGsQQPVICIELEQGITTNQE 490
Cdd:cd05966 479 RDEDGYYWITGRvddvinvSGHR-------LGTAEVESALVAHPAVAEAAVVGR-PhdiKG-EAIYAFVTLKDGEEPSDE 549
|
....*.
gi 501446872 491 qLRSEL 496
Cdd:cd05966 550 -LRKEL 554
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
9-416 |
6.69e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 61.56 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 9 AHLP--------RMAQLQPDTTAIIFPKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKV 80
Cdd:PRK05857 10 PQLPstvldrvfEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 81 GAIPVLIDPGLGIKNLKSCLAEVQPSAFIGIPKAQVarllfgwAKDSLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMA 160
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKM-------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 161 V--TAADDQAAILFTSGSTGPPKGAIYSHGNFSA-----QVEALQQVYRIQpGEIDLPTFP----------LFALFAPAL 223
Cdd:PRK05857 163 NadQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilQKEGLNWVTWVV-GETTYSPLPathigglwwiLTCLMHGGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 224 GMTavipemdftrpGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMeRFSQml 303
Cdd:PRK05857 242 CVT-----------GGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADV-RFIE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 304 AEGVEIFTPYGATES------LPVCSIGSREIlgetrvitENGGgvcIGRPVDSIRVELIRISDEPITVWDDdlrVAPGQ 377
Cdd:PRK05857 308 ATGVRTAQVYGLSETgctalcLPTDDGSIVKI--------EAGA---VGRPYPGVDVYLAATDGIGPTAPGA---GPSAS 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501446872 378 VGEIVVQGPQVTRGYFQRPE-------------ADLLSKISDpqgGFFHRMG 416
Cdd:PRK05857 374 FGTLWIKSPANMLGYWNNPErtaevlidgwvntGDLLERRED---GFFYIKG 422
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
29-467 |
1.10e-09 |
|
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: 60.52 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 29 GNQSLTFQELDRLSDRICHGLIRS-GITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLaevqpsa 107
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 figipKAQVARLLFgwakdslktiitvgprlfwggitldkliqQSPDKPfemavtaaddqAAILFTSGSTGPPKGAIYSH 187
Cdd:cd05937 75 -----KLSGSRFVI-----------------------------VDPDDP-----------AILIYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 188 GNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVipemdftrpgsvdpqkIISAIT---SHKvttmFGSPALI 264
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNC----------------LMSGGTlalSRK----FSASQFW 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 265 NRVGRSGAEQGIKLPTLQRVISAGAPVPAVVMERFSQMLAEGV--EIFTPYgaTESLPVCSIG----SREILGETRVITE 338
Cdd:cd05937 170 KDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLrpDIWERF--RERFNVPEIGefyaATEGVFALTNHNV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 339 NGGGV-CIGRPVDSIR------VELIRISDEPITVWDDD-----LRVAPGQVGEIVVQGPQVTR----GYFQRPEADLLS 402
Cdd:cd05937 248 GDFGAgAIGHHGLIRRwkfenqVVLVKMDPETDDPIRDPktgfcVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATESK 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 403 KISD--PQGGFFHRMGDLGRQDETGRLWFCGR--KTHRVESVHgpLFTIPVEAVFNTHPLVYRSALVGI 467
Cdd:cd05937 328 LVRDvfRKGDIYFRTGDLLRQDADGRWYFLDRlgDTFRWKSEN--VSTTEVADVLGAHPDIAEANVYGV 394
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
20-466 |
1.45e-09 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 60.52 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 20 DTTAIIFPK---GNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNL 96
Cdd:cd05915 9 GRKEVVSRLhtgEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 97 KSCLAEVQPSAFIgipkaqVARLLFGWAKDSLKTI--ITVGPrlfwggitldklIQQSPDKPFEMAVTAAD--------- 165
Cdd:cd05915 89 AYILNHAEDKVLL------FDPNLLPLVEAIRGELktVQHFV------------VMDEKAPEGYLAYEEALgeeadpvrv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 166 ---DQAAILFTSGSTGPPKGAIYSH--GNFSAQVEALQQVYRIQPGEIDLPTFPLF--ALFAPALGMTAVIPEMDFTRPG 238
Cdd:cd05915 151 perAACGMAYTTGTTGLPKGVVYSHraLVLHSLAASLVDGTALSEKDVVLPVVPMFhvNAWCLPYAATLVGAKQVLPGPR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 SVDpQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGAPVPAVVME-----RFSQMLAEGV-EIFTP 312
Cdd:cd05915 231 LDP-ASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIArfermGVEVRQGYGLtETSPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 313 YGATESLPVCSIGSREilgETRVITENGGGVCIGRPVDSIRVELIRISDEPITVwdddlRVapgqvgeIVVQGPQVTRGY 392
Cdd:cd05915 310 VVQNFVKSHLESLSEE---EKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKAL-----GE-------VQLKGPWITGGY 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501446872 393 FQRPEAdllSKISDPQGGFFHRMgDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVG 466
Cdd:cd05915 375 YGNEEA---TRSALTPDGFFRTG-DIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
54-459 |
2.05e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.16 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 54 ITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPS--------------------------A 107
Cdd:cd17632 90 VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRllavsaehldlaveavleggtpprlvV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 FIGIPKAQVARLLFGWAKDSLKTIitvgPRlfwgGITLDKLI-----QQSPDKPFEMAVTAaDDQAAILFTSGSTGPPKG 182
Cdd:cd17632 170 FDHRPEVDAHRAALESARERLAAV----GI----PVTTLTLIavrgrDLPPAPLFRPEPDD-DPLALLIYTSGSTGTPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 183 AIYSHGN---FSAQVEALQQVYriQPGEIDLPTFPL-----------------FALFAPALGMTAVIPEMDFTRPgsvdp 242
Cdd:cd17632 241 AMYTERLvatFWLKVSSIQDIR--PPASITLNFMPMshiagrislygtlarggTAYFAAASDMSTLFDDLALVRP----- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 243 qkiisaitshkvTTMFGSP-----------ALINRVGRSGAEQG-----IKLPTLQRV--------ISAGAPVPAVvMER 298
Cdd:cd17632 314 ------------TELFLVPrvcdmlfqryqAELDRRSVAGADAEtlaerVKAELRERVlggrllaaVCGSAPLSAE-MKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 299 FSQMLAeGVEIFTPYGATESlpvcsiGSREILGEtrvitengggvcIGRPvDSIRVELIRISDEPITVWDddlrvAPGQV 378
Cdd:cd17632 381 FMESLL-DLDLHDGYGSTEA------GAVILDGV------------IVRP-PVLDYKLVDVPELGYFRTD-----RPHPR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 379 GEIVVQGPQVTRGYFQRPEADllSKISDPQGgfFHRMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIP-VEAVFNTHP 457
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVT--AEVFDEDG--FYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVArLEAVFAASP 511
|
..
gi 501446872 458 LV 459
Cdd:cd17632 512 LV 513
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
163-502 |
3.15e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAIL-FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGE-IDLPTFPLFALFAPALGMTAVIPEMDF----TR 236
Cdd:PRK05851 149 PDSGGPAVLqGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAFLLTAALAGAPLwlapTT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 237 PGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAE-QGIKLPTLQRVISAGAPVPAVVMERFSQMLAE-GVE---IFT 311
Cdd:PRK05851 229 AFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRvSDVDLGALRVALNGGEPVDCDGFERFATAMAPfGFDagaAAP 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 312 PYGATES-----LPVCSIGSReilgETRVITENGGGV----CIGRPVDSIRVeliRISDEpitvwDDDLRVAPGQVGEIV 382
Cdd:PRK05851 309 SYGLAEStcavtVPVPGIGLR----VDEVTTDDGSGArrhaVLGNPIPGMEV---RISPG-----DGAAGVAGREIGEIE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 383 VQGPQVTRGYfqRPEADLlskisDPQGGFfhRMGDLGRQDETGrLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRS 462
Cdd:PRK05851 377 IRGASMMSGY--LGQAPI-----DPDDWF--PTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREG 446
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 501446872 463 ALVGIGPK-GSQQPVICIELE-QGitTNQEQLRSELLNIAAS 502
Cdd:PRK05851 447 AVVAVGTGeGSARPGLVIAAEfRG--PDEAGARSEVVQRVAS 486
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
31-459 |
3.77e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 58.90 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 31 QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFIG 110
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 111 ipkaqvarllfgwakdslktiitvgprlfwggitldkliqqspdkpfemavtaadDQAAILFTSGSTGPPKGAIYSHGNF 190
Cdd:cd05940 82 -------------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 191 SAQVEALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIpemdfTRPGSVDPQKIISA------ITSHKVtTMFGSPALI 264
Cdd:cd05940 107 WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACL-----ASGATLVIRKKFSAsnfwddIRKYQA-TIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 265 NR----VGRSGAEQGIKLptlqRVISAGAPVPAV---VMERFsqmlaeGV-EIFTPYGATEslpvCSIGSREILGETRVI 336
Cdd:cd05940 181 CRyllnQPPKPTERKHKV----RMIFGNGLRPDIweeFKERF------GVpRIAEFYAATE----GNSGFINFFGKPGAI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 337 TENGGGVCIGRPVDSIRVELirISDEPITvwDDD---LRVAPGQVGEIVVQGPQVTR--GYFQrPEADLLSKISD--PQG 409
Cdd:cd05940 247 GRNPSLLRKVAPLALVKYDL--ESGEPIR--DAEgrcIKVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDvfKKG 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 501446872 410 GFFHRMGDLGRQDETGRLWFCGR--KTHRV--ESVHgplfTIPVEAVFNTHPLV 459
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRlgDTFRWkgENVS----TTEVAAVLGAFPGV 371
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
33-434 |
4.30e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.86 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 33 LTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPV-LIDP-GLG-----IKNLKSCLAEVQP 105
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVpLPLPmGFGgresyIAQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 106 SAFIGipkaqvARLLFGWAKDslktiITVGPRLFWGGiTLDKLIQQsPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIY 185
Cdd:PRK09192 130 AAIIT------PDELLPWVNE-----ATHGNPLLHVL-SHAWFKAL-PEADVALPRPTPDDIAYLQYSSGSTRFPRGVII 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 186 SHGNFSAQVEALQQV-YRIQPGEIDLPTFPLF-------ALFAPALGMTAV--IPEMDFTRpgsvDPQKIISAITSHKVT 255
Cdd:PRK09192 197 THRALMANLRAISHDgLKVRPGDRCVSWLPFYhdmglvgFLLTPVATQLSVdyLPTRDFAR----RPLQWLDLISRNRGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 256 TMFgSPA----LINRVGRSGAEQGIKLpTLQRVISAGA-PVPAVVMERFSQMLAEG---VEIFTP-YGATESLPVCSI-- 324
Cdd:PRK09192 273 ISY-SPPfgyeLCARRVNSKDLAELDL-SCWRVAGIGAdMIRPDVLHQFAEAFAPAgfdDKAFMPsYGLAEATLAVSFsp 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 ---GSR-EILGETRVItenGGGVCIGRPVDSIRVELIRISDEP-----ITVWDDDLRVAPG-QVGEIVVQGPQVTRGYFQ 394
Cdd:PRK09192 351 lgsGIVvEEVDRDRLE---YQGKAVAPGAETRRVRTFVNCGKAlpgheIEIRNEAGMPLPErVVGHICVRGPSLMSGYFR 427
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501446872 395 RPEAdllSKISDPQGgfFHRMGDLGRQDEtGRLWFCGRKT 434
Cdd:PRK09192 428 DEES---QDVLAADG--WLDTGDLGYLLD-GYLYITGRAK 461
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
29-187 |
4.72e-09 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 58.84 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 29 GNQSLTFQELDRLSDRICHGLIR-SGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSA 107
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 FIGIPKAQ--VARLLFGWAKDSLKTIITVGPRLFWGGITLDKLIQQSPDKPFEMAVTAA---DDQAAILFTSGSTGPPKG 182
Cdd:cd05938 82 LVVAPELQeaVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHvtiKSPALYIYTSGTTGLPKA 161
|
....*
gi 501446872 183 AIYSH 187
Cdd:cd05938 162 ARISH 166
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
156-383 |
1.04e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.47 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 156 PFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYR---IQPGEIDLPTFPlFALFAPALGMT------ 226
Cdd:COG1541 74 PFGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRaagVRPGDRVQNAFG-YGLFTGGLGLHygaerl 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 227 --AVIPEmdftrpGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAEQGIKLP--TLQRVISAGAPVPAVVMERFSQM 302
Cdd:COG1541 153 gaTVIPA------GGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRdlSLKKGIFGGEPWSEEMRKEIEER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 303 LaeGVEIFTPYGATESLPVCSigsreilGETRvitENGGGVCIGrpvDSIRVELIR-ISDEPitvwdddlrVAPGQVGEI 381
Cdd:COG1541 227 W--GIKAYDIYGLTEVGPGVA-------YECE---AQDGLHIWE---DHFLVEIIDpETGEP---------VPEGEEGEL 282
|
..
gi 501446872 382 VV 383
Cdd:COG1541 283 VV 284
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
159-420 |
3.14e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.43 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 159 MAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVY---RIQPGEI-D-LP---TF----------------- 213
Cdd:PRK08180 203 HAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpflAEEPPVLvDwLPwnhTFggnhnlgivlynggtly 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 214 -----PLFALFAPAL-GMTAVIPEMDFTRPgsvdpqKIISAItshkVTTMFGSPALINRVgrsgaeqgikLPTLQRVISA 287
Cdd:PRK08180 283 iddgkPTPGGFDETLrNLREISPTVYFNVP------KGWEML----VPALERDAALRRRF----------FSRLKLLFYA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 288 GAPVPAVVMERFSQM----LAEGVEIFTPYGATESLPVCSIGSREIlgetrviteNGGGvCIGRPVDSIRVELIRIsdep 363
Cdd:PRK08180 343 GAALSQDVWDRLDRVaeatCGERIRMMTGLGMTETAPSATFTTGPL---------SRAG-NIGLPAPGCEVKLVPV---- 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 501446872 364 itvwDDDLrvapgqvgEIVVQGPQVTRGYFQRPEadLLSKISDPQGgfFHRMGDLGR 420
Cdd:PRK08180 409 ----GGKL--------EVRVKGPNVTPGYWRAPE--LTAEAFDEEG--YYRSGDAVR 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
6-188 |
8.31e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 55.19 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQlqPDTTAIIF---PKGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGA 82
Cdd:PRK03584 87 NYAENLLRHRR--DDRPAIIFrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 83 IPVLIDPGLGIKNLKSCLAEVQPSAFIGIP-----------KAQVARLLfgwAK-DSLKTIITVgPRLFW--------GG 142
Cdd:PRK03584 165 IWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafdrRAKVAELR---AAlPSLEHVVVV-PYLGPaaaaaalpGA 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501446872 143 ITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHG 188
Cdd:PRK03584 241 LLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHG 286
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
164-324 |
1.07e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.72 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 164 ADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFALFAPALG-----MTA----------- 227
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGlftplLTGaevflypsplh 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 228 --VIPEMDFTRpgsvdpqkiisaitshKVTTMFGSPALINRVGR--------------SGAEqgiKLPTLQRVIsagapv 291
Cdd:PRK08043 444 yrIVPELVYDR----------------NCTVLFGTSTFLGNYARfanpydfarlryvvAGAE---KLQESTKQL------ 498
|
170 180 190
....*....|....*....|....*....|...
gi 501446872 292 pavVMERFsqmlaeGVEIFTPYGATESLPVCSI 324
Cdd:PRK08043 499 ---WQDKF------GLRILEGYGVTECAPVVSI 522
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-459 |
1.31e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.11 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIFpkGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLgik 94
Cdd:PRK09029 13 AQVRPQAIALRL--NDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 95 nlksclaevqpsafigiPKAQVARLL------FGWAKDSLKTIITvgprlfwggitLDKLIQQSPDKpfEMAVTAADDQA 168
Cdd:PRK09029 88 -----------------PQPLLEELLpsltldFALVLEGENTFSA-----------LTSLHLQLVEG--AHAVAWQPQRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 169 AIL-FTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLFA----------LFApalGMTAVIPEMdftrp 237
Cdd:PRK09029 138 ATMtLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHvsgqgivwrwLYA---GATLVVRDK----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 238 gsvdpQKIISAI--TSHK--VTTmfgspalinRVGRSGAEQGIKLpTLQRVISAGAPVPAVVMErfsQMLAEGVEIFTPY 313
Cdd:PRK09029 210 -----QPLEQALagCTHAslVPT---------QLWRLLDNRSEPL-SLKAVLLGGAAIPVELTE---QAEQQGIRCWCGY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 314 GATE--SlPVCsigSREILGETRVitengGGVCIGRPvdsirvelIRISDepitvwdddlrvapgqvGEIVVQGPQVTRG 391
Cdd:PRK09029 272 GLTEmaS-TVC---AKRADGLAGV-----GSPLPGRE--------VKLVD-----------------GEIWLRGASLALG 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501446872 392 YFQRPEadlLSKISDPQGGFFHRmgDLGR--QDE---TGRL---WFCGRkthrvESVHgplftiP--VEAVFNTHPLV 459
Cdd:PRK09029 318 YWRQGQ---LVPLVNDEGWFATR--DRGEwqNGEltiLGRLdnlFFSGG-----EGIQ------PeeIERVINQHPLV 379
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
6-386 |
3.41e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 53.04 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 6 NIAAHLPRMAQlQPDTTAIIFPKGN--QSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAI 83
Cdd:cd05943 71 NYAENLLRHAD-ADDPAAIYAAEDGerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 84 PVLIDPGLGIKNLKSCLAEVQPSAFIGIPK--------------AQVARLLfgwakDSLKTIITVgPRLFWGG------- 142
Cdd:cd05943 150 WSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdvrekvAELVKGL-----PSLLAVVVV-PYTVAAGqpdlski 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 143 ---ITLDKLIQQSPDKPFEMAVTAADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVY-RIQPGEIdlptfpLF-- 216
Cdd:cd05943 224 akaLTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHcDLRPGDR------LFyy 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 217 -------------ALfapALGMTAVIPEmdfTRPGSVDPQKIISAITSHKVtTMFG-SPALINRVGRSGAEQG--IKLPT 280
Cdd:cd05943 298 ttcgwmmwnwlvsGL---AVGATIVLYD---GSPFYPDTNALWDLADEEGI-TVFGtSAKYLDALEKAGLKPAetHDLSS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 281 LQRVISAGAPVPavvmerfsqmlAEGVEiFTPYGATESLPVCSIGsreilGETRVItengGGVCIGRPVDSI-RVEL-IR 358
Cdd:cd05943 371 LRTILSTGSPLK-----------PESFD-YVYDHIKPDVLLASIS-----GGTDII----SCFVGGNPLLPVyRGEIqCR 429
|
410 420
....*....|....*....|....*...
gi 501446872 359 ISDEPITVWDDDLRVAPGQVGEIVVQGP 386
Cdd:cd05943 430 GLGMAVEAFDEEGKPVWGEKGELVCTKP 457
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-459 |
6.89e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 52.29 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 165 DDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQvyRI-------QPGEIDLPTFPLfalfapalgmtAVIpeMDFTrp 237
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALED--RLndligppEEDETYCSYLPL-----------AHI--MEFG-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 238 gsvdpqkIISAITSHKVTTMFGSPALINR-----------------VG--------RSGAEQgiKLP---TLQRVI---- 285
Cdd:PTZ00216 327 -------VTNIFLARGALIGFGSPRTLTDtfarphgdltefrpvflIGvprifdtiKKAVEA--KLPpvgSLKRRVfdha 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 286 --------SAGAPVP---AVVMERFSQMLAEGVEI-------------------FTP----YGATESlpVCsIGSREILG 331
Cdd:PTZ00216 398 yqsrlralKEGKDTPywnEKVFSAPRAVLGGRVRAmlsgggplsaatqefvnvvFGMviqgWGLTET--VC-CGGIQRTG 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 332 ETRVitengggVCIGRPVDSIRVELIRI-----SDEPitvwddDLRvapgqvGEIVVQGPQVTRGYFQRPEadLLSKISD 406
Cdd:PTZ00216 475 DLEP-------NAVGQLLKGVEMKLLDTeeykhTDTP------EPR------GEILLRGPFLFKGYYKQEE--LTREVLD 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501446872 407 PqGGFFHrMGDLGRQDETGRLWFCGRKTHRVESVHGPLFTIPV-EAVFNTHPLV 459
Cdd:PTZ00216 534 E-DGWFH-TGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEAlEALYGQNELV 585
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
15-432 |
8.53e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 15 AQLQPDTTAIIF------PKG-NQSLTFQELDRLSDRICHGLIRSGITrGTRTVLMVTPSPEFFALTFALFKVGAIPV-L 86
Cdd:PRK05850 11 ASLQPDDAAFTFidyeqdPAGvAETLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAVpL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 87 IDPGLGI--KNLKSCLAEVQPSAFIGIPKA--QVARLLFGWAKDSLKTIITVgprlfwggitlDKLIQQSPDKPfEMAVT 162
Cdd:PRK05850 90 SVPQGGAhdERVSAVLRDTSPSVVLTTSAVvdDVTEYVAPQPGQSAPPVIEV-----------DLLDLDSPRGS-DARPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 163 AADDQAAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVY-RIQPGEIDLPTF-----PLF-------ALFAPAL-GMTAV 228
Cdd:PRK05850 158 DLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfGDTGGVPPPDTTvvswlPFYhdmglvlGVCAPILgGCPAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 229 I--PEMDFTRPG------SVDPQKIISA------ITSHKVTT--MFGSPaLINRVG-RSGAEQgIKLPTLQRVISAGAPV 291
Cdd:PRK05850 238 LtsPVAFLQRPArwmqllASNPHAFSAApnfafeLAVRKTSDddMAGLD-LGGVLGiISGSER-VHPATLKRFADRFAPF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 292 ---PAVVmeRFSQMLAEGVeIFTPYGATESLPVCSIGSREILGETRVI-TENGGG---VCIGRPVDSIrvelIRISDEpi 364
Cdd:PRK05850 316 nlrETAI--RPSYGLAEAT-VYVATREPGQPPESVRFDYEKLSAGHAKrCETGGGtplVSYGSPRSPT----VRIVDP-- 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501446872 365 tvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPEAD---LLSKISDPQ----GGFFHRMGDLGRQDEtGRLWFCGR 432
Cdd:PRK05850 387 ---DTCIECPAGTVGEIWVHGDNVAAGYWQKPEETertFGATLVDPSpgtpEGPWLRTGDLGFISE-GELFIVGR 457
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
172-497 |
1.08e-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: 50.48 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 172 FTSGSTGPPKGAIYSH----GNFSAQVEALQQVYR---IQPGEIDLPTFPLFALFAPALGMTAVIPEMdftrpgsVDPQK 244
Cdd:cd17633 7 FTSGTTGLPKAYYRSErswiESFVCNEDLFNISGEdaiLAPGPLSHSLFLYGAISALYLGGTFIGQRK-------FNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 245 IISAITSHKVTTMFGSPALINRVGRSGAEQGiklpTLQRVISAGAPVPAVVMERFSQMLAEgVEIFTPYGATESlpvcSI 324
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFPK-ANLIEFYGTSEL----SF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 325 GSREILGETRviTENGggvcIGRPVDSIRvelIRISDEpitvwdddlrvAPGQVGEIVVQGPQVTRGYfqrpeadLLSKI 404
Cdd:cd17633 151 ITYNFNQESR--PPNS----VGRPFPNVE---IEIRNA-----------DGGEIGKIFVKSEMVFSGY-------VRGGF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 405 SDPQGGFfhRMGDLGRQDETGRLWFCGRKTHRVesVHGPLFTIP--VEAVFNTHPLVYRSALVGI-GPKGSQQPVICIEl 481
Cdd:cd17633 204 SNPDGWM--SVGDIGYVDEEGYLYLVGRESDMI--IIGGINIFPteIESVLKAIPGIEEAIVVGIpDARFGEIAVALYS- 278
|
330
....*....|....*.
gi 501446872 482 eqGITTNQEQLRSELL 497
Cdd:cd17633 279 --GDKLTYKQLKRFLK 292
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
32-432 |
2.30e-06 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 50.83 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 32 SLTFQELDRLSDRICHGLIRSGITRGTrtVLMVTPSP--EFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSAFI 109
Cdd:TIGR03443 270 SFTYKQINEASNILAHYLLKTGIKRGD--VVMIYAYRgvDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 110 GIPKA-QVARLLFGWAKDSLKTIITVgPRLFW---GGITLDKLIQQSPD--KPFEM-------AVTAADDQAAILFTSGS 176
Cdd:TIGR03443 348 VIEKAgTLDQLVRDYIDKELELRTEI-PALALqddGSLVGGSLEGGETDvlAPYQAlkdtptgVVVGPDSNPTLSFTSGS 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 177 TGPPKGAIYSHgnFS--------AQVEALQQVYRI--------QPGEIDLPTfPLFalfapaLGMTAVIPemdfTRPGSV 240
Cdd:TIGR03443 427 EGIPKGVLGRH--FSlayyfpwmAKRFGLSENDKFtmlsgiahDPIQRDMFT-PLF------LGAQLLVP----TADDIG 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 241 DPQKIISAITSHKVTTMFGSPAlinrvgrsgaeqgiklptLQRVISAGA--PVPAVVMERFS------------QMLAEG 306
Cdd:TIGR03443 494 TPGRLAEWMAKYGATVTHLTPA------------------MGQLLSAQAttPIPSLHHAFFVgdiltkrdclrlQTLAEN 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 307 VEIFTPYGATESLPVCS---IGSRE----ILGETRVITENGGGVcigrpvdsIRVELIRIS--DEPITvwdddlrVAPGQ 377
Cdd:TIGR03443 556 VCIVNMYGTTETQRAVSyfeIPSRSsdstFLKNLKDVMPAGKGM--------KNVQLLVVNrnDRTQT-------CGVGE 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 378 VGEIVVQGPQVTRGYFQRPEA-----------------DLLSKISDPQGGFF-------HRMGDLGRQDETGRLWFCGR 432
Cdd:TIGR03443 621 VGEIYVRAGGLAEGYLGLPELnaekfvnnwfvdpshwiDLDKENNKPEREFWlgprdrlYRTGDLGRYLPDGNVECCGR 699
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
170-496 |
7.94e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.79 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 170 ILFTSGSTGPPKGAIYSHGNFS-AQVEALQQVYRIQPGEidlpTFplFA-------------LFAPAL-GMTAVIPEMDF 234
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAvALATSMDTIFGGKAGE----TF--FCasdigwvvghsyiVYAPLLaGMATIMYEGLP 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 235 TRPgsvDPQKIISAITSHKVTTMFGSPALInRVGRSGAEQGIK---LPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFT 311
Cdd:PRK10524 312 TRP---DAGIWWRIVEKYKVNRMFSAPTAI-RVLKKQDPALLRkhdLSSLRALFLAGEPLDEPTASWISEAL--GVPVID 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 312 PYGATES-LPVCSIGSREILGETRVITEngggvciGRPVDSIRVELIR-ISDEPitvwdddlrVAPGQVGEIVVQGP--- 386
Cdd:PRK10524 386 NYWQTETgWPILAIARGVEDRPTRLGSP-------GVPMYGYNVKLLNeVTGEP---------CGPNEKGVLVIEGPlpp 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 387 ---QVTRGYFQRPEADLLSKISDPQGGFFhrmgDLGRQDETGRLWFCGRkTHRVESVHG-PLFTIPVEAVFNTHPLVYRS 462
Cdd:PRK10524 450 gcmQTVWGDDDRFVKTYWSLFGRQVYSTF----DWGIRDADGYYFILGR-TDDVINVAGhRLGTREIEESISSHPAVAEV 524
|
330 340 350
....*....|....*....|....*....|....*.
gi 501446872 463 ALVGIGP--KGsQQPVICIELEQGITTNQEQLRSEL 496
Cdd:PRK10524 525 AVVGVKDalKG-QVAVAFVVPKDSDSLADREARLAL 559
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
168-433 |
8.99e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 48.24 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 168 AAILFTSGSTGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTFPLfaLFAPAL---------GMTAVIPEMDFtrpg 238
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPL--TFDPSVveiflslssGATLLIVPTSV---- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 239 SVDPQKIISAI-TSHKVTTMFGSPALINRVGrsgaEQGIKLPTLQRVIS------AGAPVPAVVMERFSQMLAEGVEIFT 311
Cdd:cd17654 195 KVLPSKLADILfKRHRITVLQATPTLFRRFG----SQSIKSTVLSATSSlrvlalGGEPFPSLVILSSWRGKGNRTRIFN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 312 PYGATEslpVCSIGSreilgeTRVITENGGGVCIGRPVDSIRVELIRISdepitvwdddlrvapGQVGEIVVQGPQVTRG 391
Cdd:cd17654 271 IYGITE---VSCWAL------AYKVPEEDSPVQLGSPLLGTVIEVRDQN---------------GSEGTGQVFLGGLNRV 326
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 501446872 392 YFQRPEADLLSkisdpqgGFFHRMGDLGRQDEtGRLWFCGRK 433
Cdd:cd17654 327 CILDDEVTVPK-------GTMRATGDFVTVKD-GELFFLGRK 360
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
28-432 |
4.68e-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: 46.20 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 28 KGNQSLTFQELDRLSDRICHGLIRSGITRGTRTVLMVTPSPEFFALTFALFKVGAIPVLIDPGLGIKNLKSCLAEVQPSA 107
Cdd:cd05933 4 DKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 108 FIGIPKAQVARLLFGWAK-DSLKTIITVG-------PRLF-WGGITldKLIQQSPDKPFE--MAVTAADDQAAILFTSGS 176
Cdd:cd05933 84 LVVENQKQLQKILQIQDKlPHLKAIIQYKeplkekePNLYsWDEFM--ELGRSIPDEQLDaiISSQKPNQCCTLIYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 177 TGPPKGAIYSHGNFSAQVEALQQVYRIQPGEIDLPTF----PL-------FALFAPALGMTAVIpemdFTRPgsvDPQKI 245
Cdd:cd05933 162 TGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVvsylPLshiaaqiLDIWLPIKVGGQVY----FAQP---DALKG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 246 ISAITSHKV--TTMFGSPALINRVGRSGAEQGIKLPTLQRVISAGApvPAVVMERFSQMLAEGVEIFTPYGATESLPVCS 323
Cdd:cd05933 235 TLVKTLREVrpTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWA--KGVGLETNLKLMGGESPSPLFYRLAKKLVFKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 324 IgsREILGETRVITENGGGVCIGR-------PVDSIRVELIRISDE--PITVWDDDL-------RVAPG----------- 376
Cdd:cd05933 313 V--RKALGLDRCQKFFTGAAPISRetlefflSLNIPIMELYGMSETsgPHTISNPQAyrllscgKALPGcktkihnpdad 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501446872 377 QVGEIVVQGPQVTRGYFQRPEAdllSKISDPQGGFFHRmGDLGRQDETGRLWFCGR 432
Cdd:cd05933 391 GIGEICFWGRHVFMGYLNMEDK---TEEAIDEDGWLHS-GDLGKLDEDGFLYITGR 442
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
55-517 |
1.18e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.73 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 55 TRGTRTVLMVTPSPEFFALTFALFKVGAIPV-LIDPGLG--IKNLKSCLAEVQPSAFIGIPKAQVArllfgwAKDSLKTI 131
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVpLFAPELPghAERLDTALRDAEPTVVLTTTAAAEA------VEGFLRNL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 132 ITVG-PRLfwggITLDKLiqqsPDKPFEMAVTA---ADDQAAILFTSGSTGPPKGAIYSHGNFSAQVeaLQQVYRIQPGE 207
Cdd:PRK12476 164 PRLRrPRV----IAIDAI----PDSAGESFVPVeldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNL--VQMILSIDLLD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 208 ID------LPTF---PLFALFAPAL--GMTAVIPEMDFTRpgsvDPQKIISAIT--SHKVTTMFGSPaliNRVGRSGAEQ 274
Cdd:PRK12476 234 RNthgvswLPLYhdmGLSMIGFPAVygGHSTLMSPTAFVR----RPQRWIKALSegSRTGRVVTAAP---NFAYEWAAQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 275 GikLPT------LQRV--ISAGAPVPAVVMERFSqmlaegvEIFTPYG------------ATESLPVCSIG--------- 325
Cdd:PRK12476 307 G--LPAegddidLSNVvlIIGSEPVSIDAVTTFN-------KAFAPYGlprtafkpsygiAEATLFVATIApdaepsvvy 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 326 -SREILGETRVITENGGG------VCIGRPvdsIRVELIRISDEpitvwDDDLRVAPGQVGEIVVQGPQVTRGYFQRPE- 397
Cdd:PRK12476 378 lDREQLGAGRAVRVAADApnavahVSCGQV---ARSQWAVIVDP-----DTGAELPDGEVGEIWLHGDNIGRGYWGRPEe 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 398 ------ADLLSKISD-------PQGGFFHRMGDLGRQDEtGRLWFCGRKTHRVE---SVHGPLftiPVEA-VFNTHPLVY 460
Cdd:PRK12476 450 tertfgAKLQSRLAEgshadgaADDGTWLRTGDLGVYLD-GELYITGRIADLIVidgRNHYPQ---DIEAtVAEASPMVR 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 501446872 461 RS--ALVGIGPKGSQQPVICIELEQGITTNQEQLRSELLNIAASHPHTREISTILFHPA 517
Cdd:PRK12476 526 RGyvTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPA 584
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
127-530 |
3.78e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.19 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 127 SLKTIITVGPRLFWggitlDKLIQQSPD---KPFEMAVTAADDQA-AILFTSGSTGPPKGAIYSHG--------NFSAQV 194
Cdd:PTZ00237 217 KIETIPTIPNTLSW-----YDEIKKIKEnnqSPFYEYVPVESSHPlYILYTSGTTGNSKAVVRSNGphlvglkyYWRSII 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 195 EALQQVYRIQPGEIDLPTFPLFALFAPALGMTAVIPEMDFTRPGSVDpQKIISAITSHKVTTMFGSPALINRVGRSGAEQ 274
Cdd:PTZ00237 292 EKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKHIE-DDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 275 GI-----KLPTLQRVISAGAPVPAVVMERFSQMLaeGVEIFTPYGATESlPVCSIGSREILGetrvITENGGGVcigrPV 349
Cdd:PTZ00237 371 TIirskyDLSNLKEIWCGGEVIEESIPEYIENKL--KIKSSRGYGQTEI-GITYLYCYGHIN----IPYNATGV----PS 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 350 DSIRvelirisdePITVWDDDLRVAPGQVGEIVVQ---GPQVTRGYFQRPE--ADLLSKISdpqgGFFHRmGDLGRQDET 424
Cdd:PTZ00237 440 IFIK---------PSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEkfKQLFSKFP----GYYNS-GDLGFKDEN 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 425 GRLWFCGRKTHRVESVHGPLFTIPVEAVFNTHPLVYRSALVGI-GPKGSQQPVICIELEQGITTNQ---EQLRSELLNIA 500
Cdd:PTZ00237 506 GYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIyDPDCYNVPIGLLVLKQDQSNQSidlNKLKNEINNII 585
|
410 420 430
....*....|....*....|....*....|..
gi 501446872 501 AS--HPHTrEISTILFHPAFPvdIRHNAKIFR 530
Cdd:PTZ00237 586 TQdiESLA-VLRKIIIVNQLP--KTKTGKIPR 614
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
164-273 |
9.53e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 41.81 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 164 ADDQAAILFTSGSTGPPKGAIYSHGNFSA-QVEALQQVYRIQPGEIDLPTFPL-------FALFAPAL-GMTAVIPEmdf 234
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVLHTTGGYMVyTATTFKYAFDYKPTDVYWCTADCgwitghsYVTYGPMLnGATVLVFE--- 350
|
90 100 110
....*....|....*....|....*....|....*....
gi 501446872 235 TRPGSVDPQKIISAITSHKVTTMFGSPALINRVGRSGAE 273
Cdd:PLN02654 351 GAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDE 389
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
11-90 |
6.13e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 39.32 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501446872 11 LPRMA---QLQPDT----------TAIIFPKG------NQSLTFQELDRLSDRICHGLIRSGITRGTRT-VLMVTpSPEF 70
Cdd:PRK07868 432 LPRLArlgQINDHTrislgriiaeQARDAPKGefllfdGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVgVLMET-RPSA 510
|
90 100
....*....|....*....|
gi 501446872 71 FALTFALFKVGAIPVLIDPG 90
Cdd:PRK07868 511 LVAIAALSRLGAVAVLMPPD 530
|
|
| |
