|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
20-566 |
0e+00 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 1113.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 20 KVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQ 99
Cdd:PRK06087 1 KVTLTFNEQRRAAYRQQGYWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 100 LPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLA 179
Cdd:PRK06087 81 LPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 180 PATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA 259
Cdd:PRK06087 161 PATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 260 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVAR 339
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 340 ECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPE 419
Cdd:PRK06087 321 ECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 420 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVV 499
Cdd:PRK06087 401 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 500 LKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDVCEEIE 566
Cdd:PRK06087 481 LKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEEIE 547
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
68-551 |
0e+00 |
|
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: 682.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 68 SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 147
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 TLFKQTRPVDLilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthGDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05903 81 ERFRQFDPAAM----------------------------------------------PDAVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVY 307
Cdd:cd05903 115 HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 308 DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGI-KLLSVYGSTEsSPHAVVNLDDPLS-RFMHTDGYAAAGVEI 385
Cdd:cd05903 195 DLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGaKVCSAYGSTE-CPGAVTSITPAPEdRRLYTDGRPLPGVEI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 386 KVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAlDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSR 465
Cdd:cd05903 274 KVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 466 EVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQ 545
Cdd:cd05903 353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....*.
gi 1489134476 546 KFLLRK 551
Cdd:cd05903 432 KFRLRE 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
25-550 |
2.28e-168 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 489.18 E-value: 2.28e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 25 FNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVD---NHGAS--YTYSALDHAASCLANWMLAKGIESGDRIAFQ 99
Cdd:PRK13295 7 LLPPRRAASIAAGHWHDRTINDDLDACVASCPDKTAVTAvrlGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 100 LPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLA 179
Cdd:PRK13295 87 LPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELPALRHVVVVGGDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 180 PATSSLSLS----QIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAP 255
Cdd:PRK13295 167 ADSFEALLItpawEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 256 LGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPK 335
Cdd:PRK13295 247 MAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 336 KVARECQQR-GIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGY 414
Cdd:PRK13295 327 ALVERARAAlGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 415 FDEPELTarALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERS 494
Cdd:PRK13295 407 LKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489134476 495 CAYVVLKaPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK13295 485 CAFVVPR-PGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
44-551 |
2.25e-167 |
|
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: 482.77 E-value: 2.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 44 LADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPL 123
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 124 LPSWREAELVWVLNKCQAKMFFAptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitt 203
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 hgdelAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 283
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 284 PDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAV 362
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 VNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEA 442
Cdd:COG0318 258 VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDED 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFFsRKRVA 522
Cdd:COG0318 337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR-PGAELDAEELRAFL-RERLA 414
|
490 500
....*....|....*....|....*....
gi 1489134476 523 KYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-553 |
9.74e-139 |
|
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: 412.62 E-value: 9.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 27 EQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEF 106
Cdd:COG1021 10 EEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGER-RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 107 TVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSsls 186
Cdd:COG1021 89 VIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGDAGEFTS--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 187 LSQIIADNTSLTTAiTTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH-ATGFLHG 265
Cdd:COG1021 166 LDALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnFPLSSPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 266 VTAPFLIGARSVLLDIFTPDACLALLEQQRCTcMLGATPFVYDL-LNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR 344
Cdd:COG1021 245 VLGVLYAGGTVVLAPDPSPDTAFPLIERERVT-VTALVPPLALLwLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 -GIKLLSVYGSTEssphAVVN---LDDPLSRFMHTDGYA-AAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPE 419
Cdd:COG1021 324 lGCTLQQVFGMAE----GLVNytrLDDPEEVILTTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 420 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVV 499
Cdd:COG1021 400 HNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1489134476 500 LKAPhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDI 553
Cdd:COG1021 480 PRGE--PLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
49-553 |
1.08e-127 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 384.15 E-value: 1.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 49 QQTARAMPDKIAVVDNHGAsYTYSALDHAASCLANWMLAKGIESGDRIAfqLPGW--CEFTVIYLACLKIGAVSVPLlpS 126
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRR-TTYAELDERVNRLANALRALGVKKGDRVA--VFDWnsHEYLEAYFAVPKIGAVLHPI--N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 127 WR--EAELVWVLNKCQAKMFFAPTLFkqtrpVDLILPLQNQLPQLQQIVGV---DKLAPATSSLSLSQIIADNTSLTTAI 201
Cdd:PRK06187 88 IRlkPEEIAYILNDAEDRVVLVDSEF-----VPLLAAILPQLPTVRTVIVEgdgPAAPLAPEVGEYEELLAAASDTFDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAtgflHGVTAP---FLIGARSVL 278
Cdd:PRK06187 163 DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHV----HAWGLPylaLMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 LDIFTPDACLALLEQQRCTcMLGATPFVY-DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTE 356
Cdd:PRK06187 239 PRRFDPENLLDLIETERVT-FFFAVPTIWqMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 SSPHAVVNL----DDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCE--GEEASRGPNVFMGYFDEPELTARALDEeGW 430
Cdd:PRK06187 318 TSPVVSVLPpedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETIDG-GW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLE 510
Cdd:PRK06187 397 LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK-PGATLDAK 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1489134476 511 EVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDI 553
Cdd:PRK06187 476 ELRA-FLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
44-550 |
4.69e-124 |
|
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: 372.67 E-value: 4.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 44 LADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPL 123
Cdd:cd05936 1 LADLLEEAARRFPDKTALI-FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 124 LPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplqnqlpqlqqivgvDKLAPATSSLSLSQIiadntslttaitt 203
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT------------------------DLLAAGAPLGERVAL------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN--LTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI 281
Cdd:cd05936 123 TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 FTPDACLALLEQQRCTCMLGA-TPFVYdLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSP 359
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGVpTMYIA-LLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAVVN-LDDPlsRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEeGWYYSGDLCR 438
Cdd:cd05936 282 VVAVNpLDGP--RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 439 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSR 518
Cdd:cd05936 359 MDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK-EGASLTEEEIIA-FCR 436
|
490 500 510
....*....|....*....|....*....|..
gi 1489134476 519 KRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05936 437 EQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
50-551 |
5.73e-124 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 374.24 E-value: 5.73e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWRE 129
Cdd:PRK07656 13 RAARRFGDKEAYVFG-DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 130 AELVWVLNKCQAKMFFAPTLFkqtRPVDLILPLQNQLPQLQQIVGVDKLAPATSS-LSLSQIIADNTSLTTAITTHGDEL 208
Cdd:PRK07656 92 DEAAYILARGDAKALFVLGLF---LGVDYSATTRLPALEHVVICETEEDDPHTEKmKTFTDFLAAGDPAERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACL 288
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 289 ALLEQQRCTcMLGATPFVYD-LLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIK-LLSVYGSTESSPHAVVN- 364
Cdd:PRK07656 249 RLIETERIT-VLPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESElGVDiVLTGYGLSEASGVTTFNr 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 365 LDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGY 444
Cdd:PRK07656 328 LDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 445 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKY 524
Cdd:PRK07656 408 LYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLK-PGAELTEEELIA-YCREHLAKY 485
|
490 500
....*....|....*....|....*..
gi 1489134476 525 KYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK07656 486 KVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-458 |
1.41e-122 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 367.41 E-value: 1.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 48 WQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSW 127
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 128 REAELVWVLNKCQAKMFFAPTLFKqtrpVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDE 207
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK----LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 208 LAAVLFTSGTEGLPKGVMLTHNNILASERAYC----ARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 283
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 284 ---PDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSP 359
Cdd:pfam00501 237 aldPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAV--VNLDDPLSRFMHTdGYAAAGVEIKVVDDAR-KTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDL 436
Cdd:pfam00501 317 VVTtpLPLDEDLRSLGSV-GRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDL 395
|
410 420
....*....|....*....|..
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRG 458
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
50-546 |
1.68e-114 |
|
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: 347.29 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWRE 129
Cdd:cd17631 3 RRARRHPDRTALVFG-GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 130 AELVWVLNKCQAKMFFaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgDELA 209
Cdd:cd17631 82 PEVAYILADSGAKVLF------------------------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 210 AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLA 289
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 290 LLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPL 369
Cdd:cd17631 182 LIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 370 SRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITG 449
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 450 RKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEH 529
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR-PGAELDEDELIA-HCRERLARYKIPKS 418
|
490
....*....|....*..
gi 1489134476 530 IVVIEKLPRTTSGKIQK 546
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-545 |
7.92e-111 |
|
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: 334.25 E-value: 7.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLhGVTAPFLIGARSVLLDIFTPDA 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNL 365
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 366 DDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTArALDEEGWYYSGDLCRMDEAGYI 445
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 446 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYK 525
Cdd:cd04433 239 YIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR-PGADLDAEELRA-HVRERLAPYK 316
|
330 340
....*....|....*....|
gi 1489134476 526 YPEHIVVIEKLPRTTSGKIQ 545
Cdd:cd04433 317 VPRRVVFVDALPRTASGKID 336
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
41-557 |
2.41e-108 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 335.24 E-value: 2.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNH-GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDqGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLIlplqnqlpqlqqivgvDKLAP--ATSS------------- 184
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAML----------------YELAPelATCEpgqlqsarlpelr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 185 -------------LSLSQIIADntslttAITTHGDELAAVL------------FTSGTEGLPKGVMLTHNNILASERAYC 239
Cdd:PRK08315 159 rviflgdekhpgmLNFDELLAL------GRAVDDAELAARQatldpddpiniqYTSGTTGFPKGATLTHRNILNNGYFIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 240 ARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL-LDIFTPDACLALLEQQRCTCMLGA-TPFVYDLlNVLEKQP 317
Cdd:PRK08315 233 EAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYpGEGFDPLATLAAVEEERCTALYGVpTMFIAEL-DHPDFAR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 318 ADLSALRFFLCGGTTIPKKVARECQQR-GIK-LLSVYGSTESSPhavVNL----DDPLSRFMHTDGYAAAGVEIKVVD-D 390
Cdd:PRK08315 312 FDLSSLRTGIMAGSPCPIEVMKRVIDKmHMSeVTIAYGMTETSP---VSTqtrtDDPLEKRVTTVGRALPHLEVKIVDpE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 391 ARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDI 470
Cdd:PRK08315 389 TGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 471 LLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK08315 469 LYTHPKIQDVQVVGVPDEKYGEEVCAWIILR-PGATLTEEDVRD-FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
....*..
gi 1489134476 551 kDIMRRL 557
Cdd:PRK08315 547 -EMMIEE 552
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
29-546 |
4.94e-107 |
|
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: 329.67 E-value: 4.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 29 RRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTV 108
Cdd:cd05920 2 FARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDG-DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 109 IYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPtlfKQTRPVDlilplqnqlpqlqqivgvdklapatsslsls 188
Cdd:cd05920 81 LFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVP---DRHAGFD------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 189 qiiadntSLTTAITTHGD--ELAAVLFTSGTEGLPKGVMLTHNNILASERAyCARL-NLTWQDVFMMPAPLGHatGFLH- 264
Cdd:cd05920 127 -------HRALARELAESipEVALFLLSGGTTGTPKLIPRTHNDYAYNVRA-SAEVcGLDQDTVYLAVLPAAH--NFPLa 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 265 --GVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQ 342
Cdd:cd05920 197 cpGVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 343 QR-GIKLLSVYGSTEssphAVVN---LDDPLSRFMHTDGY-AAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDE 417
Cdd:cd05920 277 PVlGCTLQQVFGMAE----GLLNytrLDDPDEVIIHTQGRpMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 418 PELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAY 497
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAF 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1489134476 498 VVLKAPhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd05920 433 VVLRDP--PPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
41-561 |
3.06e-103 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 322.11 E-value: 3.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNH-GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQ----------IVGVDKLAPATSS--LSL 187
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPgalacerlpeLRGVVSLAPAPPPgfLAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 188 SQIIADNTSLT-------TAITTHGDELAaVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT 260
Cdd:PRK12583 177 HELQARGETVSrealaerQASLDRDDPIN-IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 261 GFLHGVTAPFLIGARSVL-LDIFTPDACLALLEQQRCTCMLGA-TPFVYDLLNVlEKQPADLSALRFFLCGGTTIPKKVA 338
Cdd:PRK12583 256 GMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVpTMFIAELDHP-QRGNFDLSSLRTGIMAGAPCPIEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 339 REC--QQRGIKLLSVYGSTESSPhavVNL----DDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFM 412
Cdd:PRK12583 335 RRVmdEMHMAEVQIAYGMTETSP---VSLqttaADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 413 GYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGE 492
Cdd:PRK12583 412 GYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 493 RSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDV 561
Cdd:PRK12583 492 EIVAWVRLH-PGHAASEEELRE-FCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELALPV 558
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
43-552 |
2.69e-101 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 316.10 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVP 122
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGD-RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 123 LLPSWREAELVWVLNKCQAKMFFA-PTLFKQTRPVdlilPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAI 201
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVdPALAPTAEAA----LALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAP-FLIGARSVLLD 280
Cdd:PRK08316 167 ELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQ-LDVFLGPyLYVGATNVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDACLALLEQQRCTcMLGATPFVY-DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTES 357
Cdd:PRK08316 246 APDPELILRTIEAERIT-SFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 358 SP-HAVVNLDDPLSRfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDL 436
Cdd:PRK08316 325 APlATVLGPEEHLRR-PGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKApHHSLSLEEVVAfF 516
Cdd:PRK08316 403 GVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA-GATVTEDELIA-H 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 1489134476 517 SRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK08316 481 CRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
56-551 |
8.91e-95 |
|
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: 298.07 E-value: 8.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIA-VVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVW 134
Cdd:cd05926 1 PDAPAlVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 135 VLNKCQAKMFFAPtlfKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVLFT 214
Cdd:cd05926 81 YLADLGSKLVLTP---KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 215 SGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQ 294
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 295 RCTcMLGATPFVYD-LLNVLEKQPAD-LSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLDDPLSR 371
Cdd:cd05926 238 NAT-WYTAVPTIHQiLLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 372 FMHTDGyAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRK 451
Cdd:cd05926 317 KPGSVG-KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 452 KDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSlEEVVAFFsRKRVAKYKYPEHIV 531
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE-EELRAFC-RKHLAAFKVPKKVY 473
|
490 500
....*....|....*....|
gi 1489134476 532 VIEKLPRTTSGKIQKFLLRK 551
Cdd:cd05926 474 FVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
56-561 |
2.04e-93 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 297.02 E-value: 2.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVV----DNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAE 131
Cdd:COG0365 23 GDKVALIwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 LVWVLNKCQAKMFF-APTLFKQTRPVDL---ILPLQNQLPQLQQIVGVDKLAPATSS---LSLSQIIADNTSLTTAITTH 204
Cdd:COG0365 103 LADRIEDAEAKVLItADGGLRGGKVIDLkekVDEALEELPSLEHVIVVGRTGADVPMegdLDWDELLAAASAEFEPEPTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 205 GDELAAVLFTSGTEGLPKGVMLTHNNILAsERAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD-- 280
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHGGYLV-HAATTAKyvLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEgr 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 -IF-TPDACLALLEQQRCTcMLGATPFVYD-LLNVLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGS 354
Cdd:COG0365 262 pDFpDPGRLWELIEKYGVT-VFFTAPTAIRaLMKAGDEPLKkyDLSSLRLLGSAGEPLNPEVWEWWYEAvGVPIVDGWGQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 355 TESSpHAVVNLddplsrFMHTD------GYAAAGVEIKVVDDARKTLPPGCEGEEASRG--PNVFMGYFDEPELTARAL- 425
Cdd:COG0365 341 TETG-GIFISN------LPGLPvkpgsmGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYf 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 -DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPH 504
Cdd:COG0365 414 gRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 505 H-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDV 561
Cdd:COG0365 494 EpSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDT 551
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
66-545 |
4.29e-93 |
|
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: 293.74 E-value: 4.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFF 145
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 146 APTLFKQTrpvdlILPLQNQLPQLQQIVGVDKLAPATSSLslsQIIADNTSLTTAIT------THGDELAAVLFTSGTEG 219
Cdd:cd05911 88 TDPDGLEK-----VKEAAKELGPKDKIIVLDDKPDGVLSI---EDLLSPTLGEEDEDlppplkDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 220 LPKGVMLTHNNILASERAYCARL--NLTWQDVFMMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPDACLALLEQQRCT 297
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 298 CMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGI--KLLSVYGSTESSPHAVVNLDDPLsrFMHT 375
Cdd:cd05911 239 FLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPnaTIKQGYGMTETGGILTVNPDGDD--KPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 376 DGYAAAGVEIKVVDDA-RKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDI 454
Cdd:cd05911 317 VGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 455 IVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFFSrKRVAKYKypeH----I 530
Cdd:cd05911 397 IKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK-PGEKLTEKEVKDYVA-KKVASYK---QlrggV 471
|
490
....*....|....*
gi 1489134476 531 VVIEKLPRTTSGKIQ 545
Cdd:cd05911 472 VFVDEIPKSASGKIL 486
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-550 |
8.67e-93 |
|
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: 288.02 E-value: 8.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 213 FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLL-DIFTPDACLALL 291
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 292 EQQRCTCMLGaTPFVY-DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIK-LLSVYGSTESSPHAVVNL-DD 367
Cdd:cd05917 89 EKEKCTALHG-VPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVmNMKdVTIAYGMTETSPVSTQTRtDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 368 PLSRFMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIK 446
Cdd:cd05917 168 SIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 447 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFFSRKrVAKYKY 526
Cdd:cd05917 248 IVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK-EGAELTEEDIKAYCKGK-IAHYKV 325
|
330 340
....*....|....*....|....
gi 1489134476 527 PEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05917 326 PRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-550 |
5.00e-90 |
|
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: 283.41 E-value: 5.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMffapt 148
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 lfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqIIADntslttaitthgdeLAAVLFTSGTEGLPKGVMLTH 228
Cdd:cd05934 79 -----------------------------------------VVVD--------------PASILYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCM--LGAtpfv 306
Cdd:cd05934 104 ANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTnyLGA---- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 307 ydLLNVLEKQP--ADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSpHAVVNLDDPLSRFMHTdGYAAAGV 383
Cdd:cd05934 180 --MLSYLLAQPpsPDDRAHRLRAAYGAPNPPELHEEFEERfGVRLLEGYGMTETI-VGVIGPRDEPRRPGSI-GRPAPGY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 384 EIKVVDDARKTLPPGCEGE---EASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 460
Cdd:cd05934 256 EVRIVDDDGQELPAGEPGElviRGLRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 461 NISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTT 540
Cdd:cd05934 335 NISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFA-FCEGQLAYFKVPRYIRFVDDLPKTP 412
|
490
....*....|
gi 1489134476 541 SGKIQKFLLR 550
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
57-551 |
4.71e-89 |
|
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: 281.87 E-value: 4.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 57 DKIAVVDNHGaSYTYSALDHAASCLANWMLAKG-IESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd05941 1 DRIAIVDDGD-SITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAKMFFAPtlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgdelAAVLFTS 215
Cdd:cd05941 80 ITDSEPSLVLDP-------------------------------------------------------------ALILYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQR 295
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 296 CTcMLGATPFVYD-LLNVLEKQPAD--------LSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESsphaVVNL 365
Cdd:cd05941 179 IT-VFMGVPTIYTrLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTLEEWEAItGHTLLERYGMTEI----GMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 366 DDPL--SRFMHTDGYAAAGVEIKVVDDAR-KTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEA 442
Cdd:cd05941 254 SNPLdgERRPGTVGMPLPGVQARIVDEETgEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAfFSRKRV 521
Cdd:cd05941 334 GYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKE-WAKQRL 412
|
490 500 510
....*....|....*....|....*....|
gi 1489134476 522 AKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
41-552 |
3.53e-84 |
|
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: 271.03 E-value: 3.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDN-HGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:cd05904 4 DLPLDSVSFLFASAHPSRPALIDAaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFFA-PTLFKQTRPVDLilplqnqlpqlqQIVGVDKlAPATSSLSLSQIIADNTSLT 198
Cdd:cd05904 84 VTTANPLSTPAEIAKQVKDSGAKLAFTtAELAEKLASLAL------------PVVLLDS-AEFDSLSFSDLLFEADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 276
Cdd:cd05904 151 PVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGegSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 277 VLLDIFTPDACLALLEQQRCTCMlgatPFVYDLLNVLEKQPA----DLSALRFFLCGGTTIPKKVARECQQR--GIKLLS 350
Cdd:cd05904 231 VVMPRFDLEELLAAIERYKVTHL----PVVPPIVLALVKSPIvdkyDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 351 VYGSTESSPHAVVNLDDPLSRFMH-TDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEE 428
Cdd:cd05904 307 GYGMTESTGVVAMCFAPEKDRAKYgSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 429 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlKAPHHSLS 508
Cdd:cd05904 387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV-RKPGSSLT 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1489134476 509 LEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKD 552
Cdd:cd05904 466 EDEIMDFVA-KQVAPYKKVRKVAFVDAIPKSPSGKI----LRKE 504
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
27-558 |
1.92e-83 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 269.94 E-value: 1.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 27 EQRRAAYRQQGLWGDASLADYWqqTARAMPDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEF 106
Cdd:PRK10946 10 EEFARRYREKGYWQDLPLTDIL--TRHAASDAIAVICGE-RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 107 TVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAP---TLFKQTrpvDLILPLQNQLPQLQQIVgvdkLAPATS 183
Cdd:PRK10946 87 YITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADrqhALFSDD---DFLNTLVAEHSSLRVVL----LLNDDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 184 SLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH----- 258
Cdd:PRK10946 160 EHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypms 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 259 ATGFLhGVtapFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLE--KQPADLSALRFFLCGGTTIPKK 336
Cdd:PRK10946 240 SPGAL-GV---FLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAegGSRAQLASLKLLQVGGARLSET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 337 VAREC-QQRGIKLLSVYGSTEssphAVVN---LDDPLSRFMHTDGYAAAGV-EIKVVDDARKTLPPGCEGEEASRGPNVF 411
Cdd:PRK10946 316 LARRIpAELGCQLQQVFGMAE----GLVNytrLDDSDERIFTTQGRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 412 MGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLG 491
Cdd:PRK10946 392 RGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 492 ERSCAYVVLKAPHHSLSLEEvvafFSRKR-VAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLT 558
Cdd:PRK10946 472 EKSCAFLVVKEPLKAVQLRR----FLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
68-549 |
2.56e-82 |
|
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: 263.96 E-value: 2.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 68 SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffap 147
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 tlfkqtrpvdlilplqnqlpqlqqivgvdkLAPATSSLslsqiiadntslttaitthgDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05935 76 ------------------------------VAVVGSEL--------------------DDLALIPYTSGTTGLPKGCMHT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVY 307
Cdd:cd05935 106 HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 308 DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEIK 386
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTN--PPLRPKLQCLGIP*FGVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 387 VVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEG---WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENI 462
Cdd:cd05935 264 VIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 463 SSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSG 542
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
....*..
gi 1489134476 543 KIQKFLL 549
Cdd:cd05935 424 KILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
47-546 |
4.43e-82 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 265.19 E-value: 4.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 47 YW-QQTARAMPDKIAVVDNHgASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLl 124
Cdd:PRK06839 6 YWiEKRAYLHPDRIAIITEE-EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 125 pSWR--EAELVWVLNKCQAKMFFAPTLFKQTrpvdlilplqnqlpqLQQIVGVDKLAPATSSLSLSQIiaDNTSLTTAIT 202
Cdd:PRK06839 84 -NIRltENELIFQLKDSGTTVLFVEKTFQNM---------------ALSMQKVSYVQRVISITSLKEI--EDRKIDNFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 203 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF 282
Cdd:PRK06839 146 KNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAV 362
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 VNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEA 442
Cdd:PRK06839 306 MLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVA 522
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKK-SSSVLIEKDVIE-HCRLFLA 462
|
490 500
....*....|....*....|....
gi 1489134476 523 KYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQK 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
40-557 |
2.10e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 260.32 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPAL-DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFF-----APTLFKQTRPVDLilplqnqlpqlQQIVGVD-------------KL--- 178
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIvwdkvAPTVERLRRTTPL-----------ETIVSVNmiaampllqrlalRLpip 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 179 ----------APATSSLSLSQIIADNTSLTTAITTH----GDELAAVLFTSGTEGLPKGVMLTHNNILASeraycARLNL 244
Cdd:PRK05605 178 alrkaraaltGPAPGTVPWETLVDAAIGGDGSDVSHprptPDDVALILYTSGTTGKPKGAQLTHRNLFAN-----AAQGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 245 TW-------QDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcMLGATPFVYD-LLNVLEKQ 316
Cdd:PRK05605 253 AWvpglgdgPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPT-WLPGVPPLYEkIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 317 PADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNlddPLS--RFMHTDGYAAAGVEIKVVD--DA 391
Cdd:PRK05605 332 GVDLSGVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGN---PMSddRRPGYVGVPFPDTEVRIVDpeDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 392 RKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDIL 471
Cdd:PRK05605 409 DETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 472 LQHPKIHDACVVAMSDERLGERSCAYVVLkAPHHSLSlEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK05605 488 REHPGVEDAAVVGLPREDGSEEVVAAVVL-EPGAALD-PEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
....*.
gi 1489134476 552 DIMRRL 557
Cdd:PRK05605 566 ELLEKL 571
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
42-545 |
5.06e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 256.04 E-value: 5.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIV-FYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvDLilplqnqlpqlqqivgVDKLAPATSSLSLSQIIADN------ 194
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGS--------EL----------------APKVAPAVGNLRLRHVIVAQysdylp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 195 -------------------------TSLTTAI---------TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCA 240
Cdd:PRK08314 145 aepeiavpawlraepplqalapggvVAWKEALaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 241 RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADL 320
Cdd:PRK08314 225 WSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 321 SALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVN-LDDPLSRFMhtdGYAAAGVEIKVVD-DARKTLPP 397
Cdd:PRK08314 305 SSLRYIGGGGAAMPEAVAERLKELtGLDYVEGYGLTETMAQTHSNpPDRPKLQCL---GIPTFGVDARVIDpETLEELPP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 398 GCEGEEASRGPNVFMGYFDEPELTARA---LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH 474
Cdd:PRK08314 382 GEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489134476 475 PKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQ 545
Cdd:PRK08314 462 PAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-546 |
5.75e-77 |
|
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: 246.64 E-value: 5.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDA 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIK-LLSVYGSTESSPHAVVN 364
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 365 LDDPLSRFMHTDGYAAAGVEIKVVDDarktlppgceGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGY 444
Cdd:cd17638 161 PGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 445 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKY 524
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR-PGVTLTEEDVIA-WCRERLANY 308
|
330 340
....*....|....*....|..
gi 1489134476 525 KYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-551 |
5.83e-76 |
|
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: 249.85 E-value: 5.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNHGAS---YTYSALDHAASCLANWMLAKGIESGDRIAfqLPGW--CEFTVIYLACLKIGAVSVPLLPS 126
Cdd:cd12119 6 ARLHGDREIVSRTHEGEvhrYTYAEVAERARRLANALRRLGVKPGDRVA--TLAWntHRHLELYYAVPGMGAVLHTINPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 127 WREAELVWVLNKCQAK-MFFAPTLFKQTRPVDlilplQNQLPQLQQIVGVDKLAPATSS----LSLSQIIADNTslTTAI 201
Cdd:cd12119 84 LFPEQIAYIINHAEDRvVFVDRDFLPLLEAIA-----PRLPTVEHVVVMTDDAAMPEPAgvgvLAYEELLAAES--PEYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 TTHGDE--LAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR--LNLTWQDVFMMPAPLGHATGFlhGVT-APFLIGARS 276
Cdd:cd12119 157 WPDFDEntAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPMFHVNAW--GLPyAAAMVGAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 277 VLLDIF-TPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGST 355
Cdd:cd12119 235 VLPGPYlDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 356 ESSPHAVVNLDDP----LSRFMHTD-----GYAAAGVEIKVVDDARKTLP--PGCEGEEASRGPNVFMGYFDEPElTARA 424
Cdd:cd12119 315 ETSPLGTVARPPSehsnLSEDEQLAlrakqGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 425 LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPH 504
Cdd:cd12119 394 LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK-EG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1489134476 505 HSLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd12119 473 ATVTAEELLEFL-ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-550 |
1.50e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 245.10 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVD-NHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLlpSWR-- 128
Cdd:PRK09088 5 ARLQPQRLAAVDlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPL--NWRls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELVWVLNKCQakmffaPTLfkqtrpvdlilplqnqlpqlqqIVGVDKLAPA-TSSLSLSQIIADNTSLTTAITTHG-- 205
Cdd:PRK09088 83 ASELDALLQDAE------PRL----------------------LLGDDAVAAGrTDVEDLAAFIASADALEPADTPSIpp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPD 285
Cdd:PRK09088 135 ERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 286 ACLALLEQQRctcmLGATPF--VYDLLNVLEKQPA-DLSALRFF---LCGGTTIPKKVARECQQRGIKLLSVYGSTESSP 359
Cdd:PRK09088 215 RTLGRLGDPA----LGITHYfcVPQMAQAFRAQPGfDAAALRHLtalFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAVVNLDDPLSRF-MHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCR 438
Cdd:PRK09088 291 VFGMSVDCDVIRAkAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 439 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLkAPHHSLSLEEVVAFFSR 518
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVP-ADGAPLDLERIRSHLST 449
|
490 500 510
....*....|....*....|....*....|..
gi 1489134476 519 kRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK09088 450 -RLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
48-553 |
3.20e-74 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 244.10 E-value: 3.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 48 W-QQTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVplLPS 126
Cdd:PRK03640 7 WlKQRAFLTPDRTAIEFEEK-KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV--LLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 127 WR--EAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplqnqlpqlqqivgvDKLAPaTSSLSLSQIIADNTSLTTAITT- 203
Cdd:PRK03640 84 TRlsREELLWQLDDAEVKCLITDDDFE------------------------AKLIP-GISVKFAELMNGPKEEAEIQEEf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGF---LHGVtapfLIGARSVLLD 280
Cdd:PRK03640 139 DLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLsilMRSV----IYGMRVVLVE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADlSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPH 360
Cdd:PRK03640 215 KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 aVVNLDdplSRFMHTD----GYAAAGVEIKVVDDArKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDL 436
Cdd:PRK03640 294 -IVTLS---PEDALTKlgsaGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLkapHHSLSLEEVVAfF 516
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK---SGEVTEEELRH-F 443
|
490 500 510
....*....|....*....|....*....|....*..
gi 1489134476 517 SRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDI 553
Cdd:PRK03640 444 CEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
19-552 |
3.78e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 245.84 E-value: 3.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 19 MKVTLTFNEQRRAAYRQQglWgdaslADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAF 98
Cdd:PRK07786 1 TRALTLAQEQPYLARRQN--W-----VNQLARHALMQPDAPAL-RFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 99 QLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKqtrPVDLILPLQNQLPQLQQIVGVdkl 178
Cdd:PRK07786 73 LMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALA---PVATAVRDIVPLLSTVVVAGG--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 179 APATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNiLASERAYCARLN--LTWQDVFMMPAPL 256
Cdd:PRK07786 147 SSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNgaDINSDVGFVGVPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 257 GHATGFlhGVTAPFL-IGARSVL--LDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLsALRFFLCGGTTI 333
Cdd:PRK07786 226 FHIAGI--GSMLPGLlLGAPTVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 334 PKKVARECQQR--GIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVF 411
Cdd:PRK07786 303 SDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 412 MGYFDEPELTARALDEeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLG 491
Cdd:PRK07786 383 SGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489134476 492 ERSCAYVVLKAPHHSLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK07786 462 EVPVAVAAVRNDDAALTLEDLAEFLT-DRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
40-550 |
6.23e-74 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 244.59 E-value: 6.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVV--DNHG--ASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLK 115
Cdd:PRK08008 5 GGQHLRQMWDDLADVYGHKTALIfeSSGGvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 116 IGAVSVPLLPSWREAELVWVLNKCQAKMF-----FAPtLFKQTRPVDlilplqnqLPQLQQIVGVDKLAPATS-SLSLSQ 189
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLvtsaqFYP-MYRQIQQED--------ATPLRHICLTRVALPADDgVSSFTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 190 IIADN-TSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTA 268
Cdd:PRK08008 156 LKAQQpATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 269 PFLIGARSVLLDIFTPDACLALLEQQRCT---CMlgatPFVYDLLNVLEKQPAD----LSALRFFLcgGTTIPKKVAREc 341
Cdd:PRK08008 236 AFSAGATFVLLEKYSARAFWGQVCKYRATiteCI----PMMIRTLMVQPPSANDrqhcLREVMFYL--NLSDQEKDAFE- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 342 QQRGIKLLSVYGSTESsphaVVNL--DDPL-SRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGE---EASRGPNVFMGYF 415
Cdd:PRK08008 309 ERFGVRLLTSYGMTET----IVGIigDRPGdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEiciKGVPGKTIFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 416 DEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSC 495
Cdd:PRK08008 385 LDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 496 AYVVLkAPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK08008 465 AFVVL-NEGETLSEEEFFA-FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
51-550 |
7.00e-74 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 244.01 E-value: 7.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 51 TARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREA 130
Cdd:PRK07514 11 AAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 131 ELVWVLNKCQAKMFF-APTLFKQTRPVdlilplqnqlpqlQQIVGVDKLAP--ATSSLSLSQIIADNTSLTTAITTHGDE 207
Cdd:PRK07514 91 ELDYFIGDAEPALVVcDPANFAWLSKI-------------AAAAGAPHVETldADGTGSLLEAAAAAPDDFETVPRGADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 208 LAAVLFTSGTEGLPKGVMLTHNNILASERAycarLNLTW----QDVFMMPAPLGHATGF---LHGVtapFLIGARSVLLD 280
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGNLLSNALT----LVDYWrftpDDVLIHALPIFHTHGLfvaTNVA---LLAGASMIFLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDACLALLEqqRCTCMLGATPFVYDLLnvleKQPA---DLSA-LRFFLCGGTTIPKKVARECQQR-GIKLLSVYGST 355
Cdd:PRK07514 231 KFDPDAVLALMP--RATVMMGVPTFYTRLL----QEPRltrEAAAhMRLFISGSAPLLAETHREFQERtGHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 356 EssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYY 432
Cdd:PRK07514 305 E----TNMNTSNPYdgERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 433 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEV 512
Cdd:PRK07514 381 TGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPK-PGAALDEAAI 459
|
490 500 510
....*....|....*....|....*....|....*...
gi 1489134476 513 VAFFSRkRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK07514 460 LAALKG-RLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
68-551 |
3.00e-73 |
|
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: 239.56 E-value: 3.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 68 SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMffap 147
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 tlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05912 77 ----------------------------------------------------------DDIATIMYTSGTTGKPKGVQQT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVY 307
Cdd:cd05912 99 FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 308 DLLNVL-EKQPADLsalRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAV-VNLDDPLSRfMHTDGYAAAGVEI 385
Cdd:cd05912 178 RLLEILgEGYPNNL---RCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVtLSPEDALNK-IGSAGKPLFPVEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 386 KVVDDARktlPPGCEGEEASRGPNVFMGYFDEPELTaRALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSR 465
Cdd:cd05912 254 KIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDAT-EESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 466 EVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhsLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQ 545
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP---ISEEELIAYC-SEKLAKYKVPKKIYFVDELPRTASGKLL 405
|
....*.
gi 1489134476 546 KFLLRK 551
Cdd:cd05912 406 RHELKQ 411
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-550 |
1.12e-72 |
|
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: 240.73 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 37 GLWGDASLADywQQTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKI 116
Cdd:cd05959 1 EKYNAATLVD--LNLNEGRGDKTAFIDDAG-SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 117 GAVSVPLLPSWREAELVWVLNKCQAKMFFA-PTLFKQTRPVdlilpLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNT 195
Cdd:cd05959 78 GIVPVPVNTLLTPDDYAYYLEDSRARVVVVsGELAPVLAAA-----LTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 196 SLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYcAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIG 273
Cdd:cd05959 153 EQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELY-ARnvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 274 ARSVLLDIF-TPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSV 351
Cdd:cd05959 232 ATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARfGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 352 YGSTE-------SSPHAVvnlddplsRFmHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA 424
Cdd:cd05959 312 IGSTEmlhiflsNRPGRV--------RY-GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 425 LdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPH 504
Cdd:cd05959 383 F-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1489134476 505 H-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05959 462 EdSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
44-556 |
1.81e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 240.71 E-value: 1.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 44 LADYWQQTARAMPDKIAVVdnHGA-SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVP 122
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALV--WGDrSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 123 ----LLPswreAELVWVLNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGvdklapATSSLSLSQIIADN--TS 196
Cdd:PRK07470 87 tnfrQTP----DEVAYLAEASGARAMICHADFPEH--AAAVRAASPDLTHVVAIGG------ARAGLDYEALVARHlgAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 197 LTTAITTHgDELAAVLFTSGTEGLPKGVMLTH-------NNILASeraycarL--NLTWQDVFMMPAPLGHATGfLHGVT 267
Cdd:PRK07470 155 VANAAVDH-DDPCWFFFTSGTTGRPKAAVLTHgqmafviTNHLAD-------LmpGTTEQDASLVVAPLSHGAG-IHQLC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 268 ApFLIGARSVLL--DIFTPDACLALLEQQRCTCMLGatpfVYDLLNVLEKQPA----DLSALRFFLCGGTTIpkkvAREC 341
Cdd:PRK07470 226 Q-VARGAATVLLpsERFDPAEVWALVERHRVTNLFT----VPTILKMLVEHPAvdryDHSSLRYVIYAGAPM----YRAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 342 QQR-----GIKLLSVYGSTESS-------PHAVVNLDDPLSRFmHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPN 409
Cdd:PRK07470 297 QKRalaklGKVLVQYFGLGEVTgnitvlpPALHDAEDGPDARI-GTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 410 VFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDER 489
Cdd:PRK07470 376 VFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPV 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 490 LGERSCAYVVLKAPhHSLSLEEVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRR 556
Cdd:PRK07470 455 WGEVGVAVCVARDG-APVDEAELLAWLDGK-VARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
49-551 |
2.10e-71 |
|
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: 236.81 E-value: 2.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 49 QQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWR 128
Cdd:cd12118 11 ERAAAVYPDRTSIV-YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplqnqlpqlqqivGVDKLAPATSSLSLsQIIADNtslttaitthgDEL 208
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFE----------------------YEDLLAEGDPDFEW-IPPADE-----------WDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTWQ----DVFMMPAPLGHATG--FLHGVTApflIGARSVLLD 280
Cdd:cd12118 136 IALNYTSGTTGRPKGVVYHHRG------AYLNALAniLEWEmkqhPVYLWTLPMFHCNGwcFPWTVAA---VGGTNVCLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDACLALLEQQRCTCMLGAtPFVYDLL-NVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSP 359
Cdd:cd12118 207 KVDAKAIYDLIEKHKVTHFCGA-PTVLNMLaNAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAVVNLDDPLSRFMHTDGYAA----AGV------EIKVVD-DARKTLPPGCE--GEEASRGPNVFMGYFDEPELTARALd 426
Cdd:cd12118 286 PATVCAWKPEWDELPTEERARlkarQGVryvgleEVDVLDpETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 427 EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHS 506
Cdd:cd12118 365 RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELK-EGAK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1489134476 507 LSLEEVVAfFSRKRVAKYKYPEHIVVIEkLPRTTSGKIQKFLLRK 551
Cdd:cd12118 444 VTEEEIIA-FCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
34-546 |
1.10e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 234.55 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 34 RQQGLW------------GDASLADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLP 101
Cdd:PRK06178 13 LQQAAWpagiprepeyphGERPLTEYLRAWARERPQRPAI-IFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 102 GWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMF-----FAPTLfKQTRPvdlilplqNQLPQLQQIVGVD 176
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLlaldqLAPVV-EQVRA--------ETSLRHVIVTSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 177 KLAPATSSLSL-------SQIIADNTSLTTAITTHG----------DELAAVLFTSGTEGLPKGVMLTHNNILASERAYC 239
Cdd:PRK06178 163 DVLPAEPTLPLpdslrapRLAAAGAIDLLPALRACTapvplpppalDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 240 A-RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA 318
Cdd:PRK06178 243 AvAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 319 DLSALRFFLCggTTIPKKVARECQQR------GIKLLSVYGSTESsphavvNLDDPLSRFMHTD-----------GYAAA 381
Cdd:PRK06178 323 DLSSLRQVRV--VSFVKKLNPDYRQRwraltgSVLAEAAWGMTET------HTCDTFTAGFQDDdfdllsqpvfvGLPVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 382 GVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 460
Cdd:PRK06178 395 GTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 461 NISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEhIVVIEKLPRTT 540
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLK-PGADLTAAALQA-WCRENMAVYKVPE-IRIVDALPMTA 550
|
....*.
gi 1489134476 541 SGKIQK 546
Cdd:PRK06178 551 TGKVRK 556
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
70-546 |
2.15e-69 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 230.03 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 149
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 150 FKqtrpvdlilplqnqlpqlqqivgvdklAPATSSLSLSQIIADNTSLTTAITT-HGDELAAVLFTSGTEGLPKGVMLTH 228
Cdd:TIGR01923 81 LE---------------------------EKDFQADSLDRIEAAGRYETSLSASfNMDQIATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQDVFMMPAPLGHATGFlhGVTAPFLIGARSVLLdiftPDACLALLE---QQRCTcMLGATPf 305
Cdd:TIGR01923 134 RNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL--SILFRWLIEGATLRI----VDKFNQLLEmiaNERVT-HISLVP- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 306 vyDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHaVVNLDDPLSRFMHTDGYAAAGVEI 385
Cdd:TIGR01923 206 --TQLNRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQ-VTTATPEMLHARPDVGRPLAGREI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 386 KVVDDARKTlppgcEGEEASRGPNVFMGYFDEPELTArALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSR 465
Cdd:TIGR01923 283 KIKVDNKEG-----HGEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 466 EVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhsLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIQ 545
Cdd:TIGR01923 357 EIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD---ISQAKLIAYLT-EKLAKYKVPIAFEKLDELPYNASGKIL 432
|
.
gi 1489134476 546 K 546
Cdd:TIGR01923 433 R 433
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
68-484 |
2.25e-69 |
|
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: 230.56 E-value: 2.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 68 SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 147
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 TLfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05907 85 DP--------------------------------------------------------DDLATIIYTSGTTGRPKGVMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLL---DIFTPDaclalLEQQRCTCMLGAtP 304
Cdd:cd05907 109 HRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAssaETLLDD-----LSEVRPTVFLAV-P 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 305 FVYD---LLNVLEKQPADLSAL---------RFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPhaVVNLDDPLSRF 372
Cdd:cd05907 183 RVWEkvyAAIKVKAVPGLKRKLfdlavggrlRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSA--VVTLNPPGDNR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 373 MHTDGYAAAGVEIKVVDDarktlppgceGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK 452
Cdd:cd05907 261 IGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430
....*....|....*....|....*....|...
gi 1489134476 453 DIIV-RGGENISSREVEDILLQHPKIHDACVVA 484
Cdd:cd05907 331 DLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
43-553 |
1.64e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 229.77 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVP 122
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALV-YRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 123 LLPSWREAELVWVLNKCQAKMFFAPTLFKQtrPVDLILPlqnqlpqlqqIVGVDKLAPATSSlslsQIIADNTSLTTAIT 202
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEEFDA--IVALETP----------KIVIDAAAQADSR----RLAQGGLEIPPQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 203 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGF-LHGVTAPFLIGARSVLLDi 281
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHRE- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 FTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTES-S 358
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRvfTRARYIDAYGLTETcS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCR 438
Cdd:PRK06145 305 GDTLMEAGREIEKIGST-GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 439 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLkAPHHSLSLEEVVAfFSR 518
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVL-NPGATLTLEALDR-HCR 460
|
490 500 510
....*....|....*....|....*....|....*
gi 1489134476 519 KRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDI 553
Cdd:PRK06145 461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
56-544 |
1.65e-68 |
|
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: 228.18 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd05930 1 PDAVAVVDGDQ-SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAKmffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttAITTHGDELAAVLFTS 215
Cdd:cd05930 80 LEDSGAK---------------------------------------------------------LVLTDPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAtGFLHGVTAPFLIGARSVLLD---IFTPDACLALLE 292
Cdd:cd05930 103 GSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPeevRKDPEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTcMLGATPFVYDLLnVLEKQPADLSALRFFLCGGTTIPKKVARE--CQQRGIKLLSVYGSTESSPHA---VVNLDD 367
Cdd:cd05930 182 EEGIT-VLHLTPSLLRLL-LQELELAALPSLRLVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEATVDAtyyRVPPDD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 368 PLSRFMhTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA-----LDEEGWYY-SGDLCRMDE 441
Cdd:cd05930 260 EEDGRV-PIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 442 AGYIKITGRKKDII-VRG-----GenissrEVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHsLSLEEVVAF 515
Cdd:cd05930 339 DGNLEFLGRIDDQVkIRGyrielG------EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGE-LDEEELRAH 411
|
490 500
....*....|....*....|....*....
gi 1489134476 516 FsRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd05930 412 L-AERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
50-552 |
6.80e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 229.43 E-value: 6.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWRE 129
Cdd:PRK07788 57 HAARRAPDRAALIDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 130 AELVWVLNKCQAKMF-----FAPTLFKQTRPVDLILPLqnqlpqlqqIVGVDKLAPATSSL-SLSQIIADN-TSLTTAIT 202
Cdd:PRK07788 136 PQLAEVAAREGVKALvyddeFTDLLSALPPDLGRLRAW---------GGNPDDDEPSGSTDeTLDDLIAGSsTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 203 THGdelAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLiGARSVLLDIF 282
Cdd:PRK07788 207 KPG---GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMAL-GSTVVLRRRF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSP 359
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAkyDTSSLKIIFVSGSALSPELATRALEAfGPVLYNLYGSTEVAF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFD--EPELtaraldEEGWYYSGDLC 437
Cdd:PRK07788 363 ATIATPED-LAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgrDKQI------IDGLLSSGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 438 RMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlKAPHHSLSLEEVVAFFs 517
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV-KAPGAALDEDAIKDYV- 513
|
490 500 510
....*....|....*....|....*....|....*
gi 1489134476 518 RKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK07788 514 RDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
210-544 |
5.08e-67 |
|
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: 220.60 E-value: 5.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 210 AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPDACLA 289
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 290 LLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRffLCGGTTIPKKVARECQQRGIKLLSVYGSTESSphAVVNLddpl 369
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR--HVLGLDAPETIQRFEETTGATFWSLYGQTETS--GLVTL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 370 SRFMHTDGyaAAG-----VEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEeGWYYSGDLCRMDEAGY 444
Cdd:cd17637 155 SPYRERPG--SAGrpgplVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 445 IKITGRK--KDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFFSrKRVA 522
Cdd:cd17637 232 LWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK-PGATLTADELIEFVG-SRIA 309
|
330 340
....*....|....*....|..
gi 1489134476 523 KYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17637 310 RYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
43-550 |
2.47e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 225.47 E-value: 2.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAF-SNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMFFAPTLFKQ--------TRPVDLILPLQNQLPQLQ-------QIVGVDKLAPATS--- 183
Cdd:PRK12492 104 NTNPLYTAREMRHQFKDSGARALVYLNMFGKlvqevlpdTGIEYLIEAKMGDLLPAAkgwlvntVVDKVKKMVPAYHlpq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 184 SLSLSQIIADNTSLTTAITTHG-DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----------WQDVFMM 252
Cdd:PRK12492 184 AVPFKQALRQGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEVMIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 253 PAPLGHATGFLHGVTAPFLIGARSVLL----DI--FTPDaclalLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFF 326
Cdd:PRK12492 264 PLPLYHIYAFTANCMCMMVSGNHNVLItnprDIpgFIKE-----LGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 327 LCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDPLSRfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEAS 405
Cdd:PRK12492 339 NSGGTALVKATAERWEQlTGCTIVEGYGLTETSPVASTNPYGELAR-LGTVGIPVPGTALKVIDDDGNELPLGERGELCI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 406 RGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 485
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 486 SDERLGERSCAYVVLKAPhhSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK12492 498 PDERSGEAVKLFVVARDP--GLSVEELKA-YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
69-551 |
5.25e-66 |
|
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: 221.06 E-value: 5.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANwMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffap 147
Cdd:cd05972 1 WSFRELKRESAKAAN-VLAKlGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 tlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttAITTHGDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05972 75 ----------------------------------------------------AIVTDAEDPALIYFTSGTTGLPKGVLHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDACLALLEQQRCTCMLGAtPF 305
Cdd:cd05972 103 HSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGP-PT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 306 VYDLLNVLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSR-FMhtdGYAAAGV 383
Cdd:cd05972 182 AYRMLIKQDLSSYKFSHLRLVVSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPgSM---GRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 384 EIKVVDDARKTLPPGCEGEEASRGPNV--FMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGEN 461
Cdd:cd05972 259 DVAIIDDDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 462 ISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKA---PHHSLSLEevVAFFSRKRVAKYKYPEHIVVIEKLPR 538
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyePSEELAEE--LQGHVKKVLAPYKYPREIEFVEELPK 415
|
490
....*....|...
gi 1489134476 539 TTSGKIQKFLLRK 551
Cdd:cd05972 416 TISGKIRRVELRD 428
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
40-483 |
5.83e-66 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 225.36 E-value: 5.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVVDNHGA---SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKI 116
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 117 GAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLfKQtrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--LSLSQIIA-- 192
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQ-EQ---LDKLLEVRDELPSLRHIVVLDPRGLRDDPrlLSLDELLAlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 193 ----DNTSLTTAI-TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA---TGFLH 264
Cdd:COG1022 165 revaDPAELEARRaAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVferTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 265 GVTAPFLIG-ARSV--LLD---------IFTP--------------------------DACLALLEQQRCTCMLGATP-- 304
Cdd:COG1022 245 ALAAGATVAfAESPdtLAEdlrevkptfMLAVprvwekvyagiqakaeeagglkrklfRWALAVGRRYARARLAGKSPsl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 305 ------FVYDLLnVLEKqpadLSA-----LRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNlddPLSRF- 372
Cdd:COG1022 325 llrlkhALADKL-VFSK----LREalggrLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVN---RPGDNr 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 373 MHTDGYAAAGVEIKVVDDarktlppgceGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK 452
Cdd:COG1022 397 IGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKK 466
|
490 500 510
....*....|....*....|....*....|..
gi 1489134476 453 DIIV-RGGENISSREVEDILLQHPKIHDACVV 483
Cdd:COG1022 467 DLIVtSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
68-550 |
8.56e-65 |
|
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: 218.10 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 68 SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffap 147
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEAR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 tlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttAITTHGDELAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05919 85 ----------------------------------------------------LVVTSADDIAYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCAR-LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF-TPDACLALLEQQRCTCMLGATPF 305
Cdd:cd05919 113 HRDPLLFADAMAREaLGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 306 VYDLLNVLEKQPADLSALRFFLCGGTTIPKKVA-RECQQRGIKLLSVYGSTESSPHAVVNLDDPLSrfMHTDGYAAAGVE 384
Cdd:cd05919 193 YANLLDSCAGSPDALRSLRLCVSAGEALPRGLGeRWMEHFGGPILDGIGATEVGHIFLSNRPGAWR--LGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 385 IKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPElTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISS 464
Cdd:cd05919 271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 465 REVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPH-HSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAaPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
....*..
gi 1489134476 544 IQKFLLR 550
Cdd:cd05919 430 LQRFKLR 436
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
40-550 |
1.00e-62 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 215.39 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFG-GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFFA-PTLFKQTRPVDLilplQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLT 198
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVeAALLAALEAADP----GDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAITTHGDeLAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVL 278
Cdd:PRK06155 174 AAAVQPGD-TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFH-TNALNAFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 LDIFTPDACLALLEQQRCTC--MLGAtpfvydLLNVLEKQPADLS----ALRFFLCGGTtiPKKVARECQQR-GIKLLSV 351
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVtyLLGA------MVSILLSQPARESdrahRVRVALGPGV--PAALHAAFRERfGVDLLDG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 352 YGSTESSPHAVVNLDDPLSRFMhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRG--PNVFM-GYFDEPELTARALdEE 428
Cdd:PRK06155 324 YGSTETNFVIAVTHGSQRPGSM---GRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFAFAtGYFGMPEKTVEAW-RN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 429 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDErLGERSCAYVVLKAPHHSLS 508
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE-LGEDEVMAAVVLRDGTALE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1489134476 509 LEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK06155 479 PVALVR-HCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
46-551 |
6.28e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 213.27 E-value: 6.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTARAMPDKIAVVdnHGA-SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLL 124
Cdd:PRK08162 22 SFLERAAEVYPDRPAVI--HGDrRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 125 PSWREAELVWVLNKCQAKMFFAPTLFkqtrpVDLILPLQNQLPQLQQIV-----GVDKLAPATSSLSLSQIIADNTSlTT 199
Cdd:PRK08162 100 TRLDAASIAFMLRHGEAKVLIVDTEF-----AEVAREALALLPGPKPLVidvddPEYPGGRFIGALDYEAFLASGDP-DF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 200 AITTHGDELAAVL--FTSGTEGLPKGVMLTHNNilaserAYCARLN--LTWQ----DVFMMPAPLGHATGFLHgvtaPFL 271
Cdd:PRK08162 174 AWTLPADEWDAIAlnYTSGTTGNPKGVVYHHRG------AYLNALSniLAWGmpkhPVYLWTLPMFHCNGWCF----PWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 272 IGAR---SVLLDIFTPDACLALLEQQRCTCMLGAtPFVYDLL-NVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIK 347
Cdd:PRK08162 244 VAARagtNVCLRKVDPKLIFDLIREHGVTHYCGA-PIVLSALiNAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 348 LLSVYGSTESSPHAVVNLDDP----LSRFMHTDGYAAAGV------EIKVVDdaRKTLPP-----GCEGEEASRGpNVFM 412
Cdd:PRK08162 323 LTHVYGLTETYGPATVCAWQPewdaLPLDERAQLKARQGVryplqeGVTVLD--PDTMQPvpadgETIGEIMFRG-NIVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 413 -GYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLG 491
Cdd:PRK08162 400 kGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 492 ERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEkLPRTTSGKIQKFLLRK 551
Cdd:PRK08162 479 EVPCAFVELK-DGASATEEEIIA-HCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLRE 535
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
42-553 |
5.20e-61 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 211.03 E-value: 5.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFI-CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMF-----FAPTLFKQTRPVDL----ILPLQNQLPQLQQIVG-----VDKLAPATS---S 184
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAEAIvvlenFATTVQQVLAKTAVkhvvVASMGDLLGFKGHIVNfvvrrVKKMVPAWSlpgH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 185 LSLSQIIADNTSLT-TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS--------ERAYCARLNLTwQDVFMMPAP 255
Cdd:PRK07059 182 VRFNDALAEGARQTfKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqmeawlQPAFEKKPRPD-QLNFVCALP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 256 LGHatgfLHGVTAPFLIGARSVLLDIFTPD-----ACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGG 330
Cdd:PRK07059 261 LYH----IFALTVCGLLGMRTGGRNILIPNprdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 331 TTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPN 409
Cdd:PRK07059 337 MAVQRPVAERWLEMtGCPITEGYGLSETSPVATCNPVD-ATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 410 VFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDER 489
Cdd:PRK07059 416 VMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489134476 490 LGERSCAYVVLKAPhhSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKDI 553
Cdd:PRK07059 496 SGEAVKLFVVKKDP--ALTEEDVKA-FCKERLTNYKRPKFVEFRTELPKTNVGKI----LRREL 552
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
195-556 |
8.50e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 212.12 E-value: 8.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 195 TSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILAseRAYCARLNLTWQ--DVFMMPAPLGHATGFLHGVTAPFLI 272
Cdd:PRK07529 202 DRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA--NAWLGALLLGLGpgDTVFCGLPLFHVNALLVTGLAPLAR 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 273 GARSVLLdifTP-----DACLA----LLEQQRCTCMlGATPFVYdllNVLEKQP---ADLSALRFFLCGGTTIPKKVARE 340
Cdd:PRK07529 280 GAHVVLA---TPqgyrgPGVIAnfwkIVERYRINFL-SGVPTVY---AALLQVPvdgHDISSLRYALCGAAPLPVEVFRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 341 CQQR-GIKLLSVYGSTESSPHAVVN-LDDPLS------RFMHTDgyaaagVEIKVVDDARKTL---PPGCEGEEASRGPN 409
Cdd:PRK07529 353 FEAAtGVRIVEGYGLTEATCVSSVNpPDGERRigsvglRLPYQR------VRVVILDDAGRYLrdcAVDEVGVLCIAGPN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 410 VFMGYFdEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDER 489
Cdd:PRK07529 427 VFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAH 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 490 LGERSCAYVVLKaPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRR 556
Cdd:PRK07529 506 AGELPVAYVQLK-PGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALRRDAIRR 571
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
45-550 |
1.10e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 209.46 E-value: 1.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 45 ADYWQQTARAM---PDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCE-FTVIYLACLkIGAVS 120
Cdd:PRK06188 12 ATYGHLLVSALkryPDRPALVLG-DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQL-AGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMF-FAPTLFkQTRPVDLilplqnqlpqlqqivgvdklapATSSLSLSQIIA-----DN 194
Cdd:PRK06188 90 TALHPLGSLDDHAYVLEDAGISTLiVDPAPF-VERALAL----------------------LARVPSLKHVLTlgpvpDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 195 TSLTTAITTHG----------DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLh 264
Cdd:PRK06188 147 VDLLAAAAKFGpaplvaaalpPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 265 gVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlgATPFVYDLLNVLEKQP----ADLSALRFFLCGGTTI-PKKVAR 339
Cdd:PRK06188 226 -FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRIT----ATFLVPTMIYALLDHPdlrtRDLSSLETVYYGASPMsPVRLAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 340 ECQQRGIKLLSVYGSTESsPHAVVNL-------DDPlsRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFM 412
Cdd:PRK06188 301 AIERFGPIFAQYYGQTEA-PMVITYLrkrdhdpDDP--KRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 413 GYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGE 492
Cdd:PRK06188 378 GYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 493 RSCAYVVLKaPHHSLSLEEVVAFF-SRKRVAkyKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK06188 457 AVTAVVVLR-PGAAVDAAELQAHVkERKGSV--HAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
66-550 |
4.12e-60 |
|
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: 205.79 E-value: 4.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQakmf 144
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 145 faptlfkqtRPVDLIlplqnqlpqlqqivgVDKLapatsslslsqiiadntslttaitTHGDELAAVLFTSGTEGLPKGV 224
Cdd:cd05958 84 ---------ITVALC---------------AHAL------------------------TASDDICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 225 MLTHNNILASERAYCAR-LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGAT 303
Cdd:cd05958 116 MHFHRDPLASADRYAVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 304 PFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSpHAVVNLDDPLSRfMHTDGYAAAG 382
Cdd:cd05958 196 TAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEMF-HIFISARPGDAR-PGATGKPVPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 383 VEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEpelTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENI 462
Cdd:cd05958 274 YEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADK---RQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 463 SSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPH-HSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTS 541
Cdd:cd05958 351 APPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGViPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 1489134476 542 GKIQKFLLR 550
Cdd:cd05958 431 GKLQRFALR 439
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
43-557 |
1.56e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 207.31 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK05677 25 NIQAVLKQSCQRFADKPAF-SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSW--REAE----------LVWVLNKC-QAKMFFAPTLFKQ---TRPVDLILPLQNQLPQLQqIVGVDKLAPAtssL 185
Cdd:PRK05677 104 NTNPLYtaREMEhqfndsgakaLVCLANMAhLAEKVLPKTGVKHvivTEVADMLPPLKRLLINAV-VKHVKKMVPA---Y 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 186 SLSQIIADNTSLT-------TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASE---RAYCARLNLTWQDVFMMPAP 255
Cdd:PRK05677 180 HLPQAVKFNDALAkgagqpvTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcRALMGSNLNEGCEILIAPLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 256 LGHATGFLHGVTAPFLIGARSVLldIFTP---DACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTT 332
Cdd:PRK05677 260 LYHIYAFTFHCMAMMLIGNHNIL--ISNPrdlPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 333 IPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNlddPLSRF-MHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNV 410
Cdd:PRK05677 338 LQLATAERWKEvTGCAICEGYGMTETSPVVSVN---PSQAIqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 411 FMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERL 490
Cdd:PRK05677 415 MKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKS 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 491 GERSCAYVVLKaPHHSLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRL 557
Cdd:PRK05677 495 GEAIKVFVVVK-PGETLTKEQVMEHM-RANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
43-557 |
1.58e-58 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 204.06 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PLN02246 24 PLHDYCFERLSEFSDRPCLIDgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMffaptLFKQTRPVDLILPLQNQLPQLqqIVGVDklAPATSSLSLSQIIADNTSLTTAI 201
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKL-----IITQSCYVDKLKGLAEDDGVT--VVTID--DPPEGCLHFSELTQADENELPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASerayCAR--------LNLTWQDVFMMPAPLGH----ATGFLHGVTAp 269
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTS----VAQqvdgenpnLYFHSDDVILCVLPMFHiyslNSVLLCGLRV- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 270 fliGARSVLLDIFTPDACLALLEQQRCTcmlgATPFVYDLLNVLEKQPA----DLSALRFFLCGGTTIPKKVARECQQR- 344
Cdd:PLN02246 250 ---GAAILIMPKFEIGALLELIQRHKVT----IAPFVPPIVLAIAKSPVvekyDLSSIRMVLSGAAPLGKELEDAFRAKl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 -GIKLLSVYGSTESSPHAVVNL---DDPLSRFMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPE 419
Cdd:PLN02246 323 pNAVLGQGYGMTEAGPVLAMCLafaKEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 420 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVV 499
Cdd:PLN02246 403 ATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 500 lKAPHHSLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKDIMRRL 557
Cdd:PLN02246 483 -RSNGSEITEDEIKQFVA-KQVVFYKRIHKVFFVDSIPKAPSGKI----LRKDLRAKL 534
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
206-544 |
2.99e-58 |
|
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: 202.18 E-value: 2.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVlldiFTPD 285
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV----FHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 286 ACLA-----LLEQQRCTcMLGATP-FVYDLLNvlEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESS 358
Cdd:cd05909 223 PLDYkkipeLIYDKKAT-ILLGTPtFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PHAVVNLddPLSRFMH-TDGYAAAGVEIKVVDDARKT-LPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDL 436
Cdd:cd05909 300 PVISVNT--PQSPNKEgTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH-PKIHDACVVAMSDERLGERscayVVLKAPHHSLSLEEVVAF 515
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK----IVLLTTTTDTDPSSLNDI 452
|
330 340
....*....|....*....|....*....
gi 1489134476 516 FSRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd05909 453 LKNAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
66-549 |
1.42e-57 |
|
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: 199.59 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSAL-DHAAScLANWMLAKGIESGDRIAFQL---PGWCeftVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQA 141
Cdd:cd05914 5 GEPLTYKDLaDNIAK-FALLLKINGVGTGDRVALMGenrPEWG---IAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 142 KMFFaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaiTTHGDELAAVLFTSGTEGLP 221
Cdd:cd05914 81 KAIF--------------------------------------------------------VSDEDDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 222 KGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQrCTCMLG 301
Cdd:cd05914 105 KGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQ-VTPTLG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 302 AT-------PFVYDLLN---------VLEKQPADLS---------------ALRFFLCGGTTIPKKVARECQQRGIKLLS 350
Cdd:cd05914 184 VPvplviekIFKMDIIPkltlkkfkfKLAKKINNRKirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTIGFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 351 VYGSTESSPhaVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLppgcEGEEASRGPNVFMGYFDEPELTARALDEEGW 430
Cdd:cd05914 264 GYGMTETAP--IISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATG----EGEIIVRGPNVMKGYYKNPEATAEAFDKDGW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 YYSGDLCRMDEAGYIKITGRKKDIIVRG-GENISSREVEDILLQHPKIHDACVVaMSDERLGERSCAYV-VLKAPHHSLS 508
Cdd:cd05914 338 FHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV-VQEKKLVALAYIDPdFLDVKALKQR 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 509 ------LEEVVAFFSR-----KRVAKYKypehiVVIEKLPRTTSGKIQKFLL 549
Cdd:cd05914 417 niidaiKWEVRDKVNQkvpnyKKISKVK-----IVKEEFEKTPKGKIKRFLY 463
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
46-544 |
2.24e-57 |
|
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: 199.42 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLP 125
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDE-GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 126 SWREAELVWVLNKCQAKMFFaptlfkqTRPVDlilplqnqlpqlqqivgVDKLAPATSSLSLSQII-ADNTSLTTAITTH 204
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVL-------TTADL-----------------AARLPAGGDVALLGDEAlAAPPATPPLVPPR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 205 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLL----- 279
Cdd:cd17646 137 PDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVArpggh 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 -DiftPDACLALLEQQRCTCMlgatPFVYDLLNVLEKQPAD--LSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGST 355
Cdd:cd17646 216 rD---PAYLAALIREHGVTTC----HFVPSMLRVFLAEPAAgsCASLRRVFCSGEALPPELAARFLALpGAELHNLYGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 356 ESS---PHAVVNLDDPLSRFmhTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL------D 426
Cdd:cd17646 289 EAAidvTHWPVRGPAETPSV--PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfgP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 427 EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHS 506
Cdd:cd17646 367 GSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG 446
|
490 500 510
....*....|....*....|....*....|....*...
gi 1489134476 507 LSLEEVVAFFSRkRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17646 447 PDTAALRAHLAE-RLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-556 |
8.79e-57 |
|
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: 194.62 E-value: 8.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 205 GDELAAVLFTSGTEGLPKGVMLTHNNILASerAYCARLNLTWQ--DVFMMPAPLGHATGFLHGVTAPFLIGARSVLLdif 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDpdDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TP---------DACLALLEQQRCTCMLGaTPFVYdllNVLEKQP--ADLSALRFFLCGGTTIPKKVARECQQR-GIKLLS 350
Cdd:cd05944 76 GPagyrnpglfDNFWKLVERYRITSLST-VPTVY---AALLQVPvnADISSLRFAMSGAAPLPVELRARFEDAtGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 351 VYGSTE-SSPHAVVNLDDPLS------RFMHTDgyaaagVEIKVVD-DARKTLP--PGCEGEEASRGPNVFMGYFDEpEL 420
Cdd:cd05944 152 GYGLTEaTCLVAVNPPDGPKRpgsvglRLPYAR------VRIKVLDgVGRLLRDcaPDEVGEICVAGPGVFGGYLYT-EG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 421 TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVL 500
Cdd:cd05944 225 NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489134476 501 KaPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRR 556
Cdd:cd05944 305 K-PGAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
40-551 |
1.30e-56 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 198.14 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMP--DKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIG 117
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEGrgGKTAFIDDIS-SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 118 AVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtRPVDLILPLQNQLPQLQQIVGvdklAPATSSLSLSQIIADNTSL 197
Cdd:TIGR02262 80 IVPVALNTLLTADDYAYMLEDSRARVVFVSGAL---LPVIKAALGKSPHLEHRVVVG----RPEAGEVQLAELLATESEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 198 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR-LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 276
Cdd:TIGR02262 153 FKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNtLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 277 VLL-DIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGS 354
Cdd:TIGR02262 233 VLMgERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARfGVDIVDGIGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 355 TESSPHAVVNLDDPLSrfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSG 434
Cdd:TIGR02262 313 TEMLHIFLSNLPGDVR--YGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 435 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVA 514
Cdd:TIGR02262 390 DKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLR-PGQTALETELKE 468
|
490 500 510
....*....|....*....|....*....|....*..
gi 1489134476 515 FFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:TIGR02262 469 HV-KDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
59-550 |
1.61e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 197.82 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 59 IAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLlpSWR--EAELVWVL 136
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--NWHltAAEIAYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 137 NKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKlAPATSSLSLSQIIADNTSLTTAITTHGDELaavLFTSG 216
Cdd:PRK08276 80 DDSGAKVLIV-----SAALADTAAELAAELPAGVPLLLVVA-GPVPGFRSYEEALAAQPDTPIADETAGADM---LYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 217 TEGLPKGVM--LTHNNILASE----RAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPDACLAL 290
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPDEAPgmmlALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALAL-GGTVVVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 291 LEQQRCTCM-LGATPFVyDLLNVLEKQPA--DLSALRFFLCGGTTIPKKVarecQQRGIK-----LLSVYGSTESSPHAV 362
Cdd:PRK08276 230 IERYRVTHSqLVPTMFV-RMLKLPEEVRAryDVSSLRVAIHAAAPCPVEV----KRAMIDwwgpiIHEYYASSEGGGVTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 VNLDDPLSRfMHTDGYAAAGvEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEA 442
Cdd:PRK08276 305 ITSEDWLAH-PGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAyVVLKAPHHSLS---LEEVVAFFsRK 519
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPADGADAGdalAAELIAWL-RG 460
|
490 500 510
....*....|....*....|....*....|.
gi 1489134476 520 RVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK08276 461 RLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
42-552 |
3.65e-56 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 197.97 E-value: 3.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFI-NMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMF-----FAPTLFK-----QTRPVDLILPLQNQLPQLQQIVG-----VDKLAPATSsl 185
Cdd:PRK08974 102 VNVNPLYTPRELEHQLNDSGAKAIvivsnFAHTLEKvvfktPVKHVILTRMGDQLSTAKGTLVNfvvkyIKRLVPKYH-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 186 slsqiIADNTSLTTAITT-----------HGDELAAVLFTSGTEGLPKGVMLTHNNILAS----ERAYCARLNlTWQDVF 250
Cdd:PRK08974 180 -----LPDAISFRSALHKgrrmqyvkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqaKAAYGPLLH-PGKELV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 251 MMPAPLGHAtgFLHGVTAPFLI--GARSVLL----DIftpDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALR 324
Cdd:PRK08974 254 VTALPLYHI--FALTVNCLLFIelGGQNLLItnprDI---PGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 325 FFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEE 403
Cdd:PRK08974 329 LSVGGGMAVQQAVAERWVKlTGQYLLEGYGLTECSPLVSVNPYD-LDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 404 ASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 483
Cdd:PRK08974 408 WVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAV 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 484 AMSDERLGERSCAYVVLKAPhhSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK08974 487 GVPSEVSGEAVKIFVVKKDP--SLTEEELIT-HCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
49-546 |
3.22e-55 |
|
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: 193.57 E-value: 3.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 49 QQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWR 128
Cdd:cd12117 4 EEQAARTPDAVAVVYG-DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELVWVLNKCQAKMffaptLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSlslsqiiadntslttaittHGDEL 208
Cdd:cd12117 83 AERLAFMLADAGAKV-----LLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV-------------------SPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNNI--LASERAYcarLNLTWQDVFMMPAPLG-HATGFlhGVTAPFLIGARSVLLD---IF 282
Cdd:cd12117 139 AYVMYTSGSTGRPKGVAVTHRGVvrLVKNTNY---VTLGPDDRVLQTSPLAfDASTF--EIWGALLNGARLVLAPkgtLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTCMLGATPfvydLLNVL-EKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTE--- 356
Cdd:cd12117 214 DPDALGALIAEEGVTVLWLTAA----LFNQLaDEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEntt 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 -SSPHAVVNLDD-----PLsrfmhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR------A 424
Cdd:cd12117 290 fTTSHVVTELDEvagsiPI-------GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAErfvadpF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 425 LDEEGWYYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAP 503
Cdd:cd12117 363 GPGERLYRTGDLARWLPDGRLEFLGRIDDqVKIR-GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1489134476 504 hhsLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd12117 442 ---LDAAELRA-FLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
70-551 |
4.69e-55 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 194.58 E-value: 4.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKGIESGDRIAfqLPGWCefTVIYLAC----LKIGAVSVPLLPSWREAELVWVLNKCQAKMFF 145
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVA--TIAWN--TWRHLEAwygiMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 146 APTLFKqtrPVdlilplqnqlpqlqqivgVDKLAPATSSLSLSQIIAD-----NTSLTTAIT-------THGD------- 206
Cdd:PRK06018 117 TDLTFV---PI------------------LEKIADKLPSVERYVVLTDaahmpQTTLKNAVAyeewiaeADGDfawktfd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 --ELAAVLFTSGTEGLPKGVMLTH-NNILASERAYCA-RLNLTWQDVFMMPAPLGHATGFLHGVTAPfLIGARSVLldif 282
Cdd:PRK06018 176 enTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGdALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVM---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 tPDACL------ALLEQQRCTcMLGATPFVYD-LLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGST 355
Cdd:PRK06018 251 -PGAKLdgasvyELLDTEKVT-FTAGVPTVWLmLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 356 ESSPHAVVN-LDDPLSR--------FMHTDGYAAAGVEIKVVDDARKTLPPGCE--GEEASRGPNVFMGYFdepELTARA 424
Cdd:PRK06018 329 EMSPLGTLAaLKPPFSKlpgdarldVLQKQGYPPFGVEMKITDDAGKELPWDGKtfGRLKVRGPAVAAAYY---RVDGEI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 425 LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPH 504
Cdd:PRK06018 406 LDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLK-PG 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1489134476 505 HSLSLEEVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK06018 485 ETATREEILKYMDGK-IAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-544 |
7.33e-55 |
|
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: 192.27 E-value: 7.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 77 AASCLANWMLAKGIESGDRIAFQLPG-----WCEFTVIYLACLkIGAVSVPLLPSWREAELVWVLNKCQAKMFFA-PTLF 150
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNrftyiELSFAVAYAGGR-LGLVFVPLNPTLKESVLRYLVADAGGRIVLAdAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 151 KQTRPVdlilplqnqlpqlqQIVGVDklapATSSLSLSQIIADNTSLTTAITTHgDELAAVLFTSGTEGLPKGVMLTHNN 230
Cdd:cd05922 81 DRLRDA--------------LPASPD----PGTVLDADGIRAARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRLSHQN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 231 ILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFT-PDACLALLEQQRCTCMLGaTPFVYDL 309
Cdd:cd05922 142 LLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAG-VPSTYAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 310 LNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKV 387
Cdd:cd05922 220 LTRLGFDPAKLPSLRYLTQAGGRLPQETIARLREllPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 388 VDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREV 467
Cdd:cd05922 300 LDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 468 EDILLQHPKIHDACVVAMSDErLGERSCAYVVLKAphhSLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd05922 380 EAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPD---KIDPKDVLRSLA-ERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
44-556 |
8.29e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 194.48 E-value: 8.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 44 LADYWQQTARAMPDKIAVvdnH--GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK06710 26 LHKYVEQMASRYPEKKAL---HflGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNQLPQLQQI--VGVDKLA---PATSSLSLSQIIADNTS 196
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILC---------LDLVFPRVTNVQSATKIehVIVTRIAdflPFPKNLLYPFVQKKQSN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 197 LTTAI----TTH-------------------GDELAAVLFTSGTEGLPKGVMLTHNNILASeraycARLNLTW------- 246
Cdd:PRK06710 174 LVVKVseseTIHlwnsvekevntgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWlynckeg 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 247 QDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFF 326
Cdd:PRK06710 249 EEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRAC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 327 LCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDPlSRFMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEA 404
Cdd:PRK06710 329 ISGSAPLPVEVQEKFETvTGGKLVEGYGLTESSPVTHSNFLWE-KRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 405 SRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVA 484
Cdd:PRK06710 408 VKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 485 MSDERLGERSCAYVVLKapHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRR 556
Cdd:PRK06710 487 VPDPYRGETVKAFVVLK--EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRK 556
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-551 |
9.00e-55 |
|
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: 187.92 E-value: 9.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDiftpda 286
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 cLALLEQQRctcmLGATPFVY------DLLNVLEK--QPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESS 358
Cdd:cd17630 74 -RNQALAED----LAPPGVTHvslvptQLQRLLDSgqGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PHavVNLDDPLSRFMHTDGYAAAGVEIKVVDDarktlppgceGEEASRGPNVFMGYFDEPELtaRALDEEGWYYSGDLCR 438
Cdd:cd17630 149 SQ--VATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 439 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHhslSLEEVVAFFSR 518
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA---DPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|...
gi 1489134476 519 KrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd17630 292 K-LARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
52-544 |
4.47e-54 |
|
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: 189.77 E-value: 4.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSwreae 131
Cdd:cd05945 1 AAANPDRPAVVEG-GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 lvwvlnkcqakmffaptlfkqtRPVDLIlplqnqlpqlqqivgvdklapatsslslsQIIADNTSLTTAITThGDELAAV 211
Cdd:cd05945 75 ----------------------SPAERI-----------------------------REILDAAKPALLIAD-GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLghatGF---LHGVTAPFLIGARSVLLD---IFTPD 285
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF----SFdlsVMDLYPALASGATLVPVPrdaTADPK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 286 ACLALLEQQRCTCMLGaTPFVYDLLNVLEK-QPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESS---- 358
Cdd:cd05945 179 QLFRFLAEHGITVWVS-TPSFAAMCLLSPTfTPESLPSLRHFLFCGEVLPHKTARALQQRfpDARIYNTYGPTEATvavt 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 ----PHAVVNLDDPLSRfmhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL---DEEGWY 431
Cdd:cd05945 258 yievTPEVLDGYDRLPI-----GYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQRAY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 432 YSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEE 511
Cdd:cd05945 333 RTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK-PGAEAGLTK 411
|
490 500 510
....*....|....*....|....*....|...
gi 1489134476 512 VVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd05945 412 AIKAELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
70-482 |
9.72e-54 |
|
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: 187.86 E-value: 9.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLA-KGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffapt 148
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 lfkqtrpvdLILPLQNQLPQLQQIVGVDKLAPATSSLSLSqiiADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTH 228
Cdd:TIGR01733 75 ---------LLLTDSALASRLAGLVLPVILLDPLELAALD---DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVLL---DIFTPDACLALLEQQRCTCMLGATPF 305
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPDDRVLQFASLSF-DASVEEIFGALLAGATLVVPpedEERDDAALLAALIAEHPVTVLNLTPS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 306 VYDLLnvLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAVVNL--DDPLSRFMHTD-GYAA 380
Cdd:TIGR01733 222 LLALL--AAALPPALASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLvdPDDAPRESPVPiGRPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 381 AGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA--------RALDEEGWYYSGDLCRMDEAGYIKITGRKK 452
Cdd:TIGR01733 300 ANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRID 379
|
410 420 430
....*....|....*....|....*....|
gi 1489134476 453 DIIVRGGENISSREVEDILLQHPKIHDACV 482
Cdd:TIGR01733 380 DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
41-561 |
2.04e-53 |
|
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: 196.23 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLP-GWcEFTVIYLACLKIGAV 119
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVFG-DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErSL-EMVVALLAVLKAGAA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKmffaptlfkqtrpvdlilplqnqlpqlqQIVGVDKLAPATSSLSLSQIIADNTSLTT 199
Cdd:COG1020 553 YVPLDPAYPAERLAYMLEDAGAR----------------------------LVLTQSALAARLPELGVPVLALDALALAA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 200 A------ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLghatGF---LHGVTAPF 270
Cdd:COG1020 605 EpatnppVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASL----SFdasVWEIFGAL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 271 LIGARSVLLD---IFTPDACLALLEQQRCTCMLgATPFVYDLLnvLEKQPADLSALRFFLCGGTTIPKKVARECQQR--G 345
Cdd:COG1020 681 LSGATLVLAPpeaRRDPAALAELLARHRVTVLN-LTPSLLRAL--LDAAPEALPSLRLVLVGGEALPPELVRRWRARlpG 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 346 IKLLSVYGSTES---SPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA 422
Cdd:COG1020 758 ARLVNLYGPTETtvdSTYYEVTPPDADGGSVPI-GRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTA 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 423 RA-----LDEEG--WYYSGDLCRMDEAGYIKITGRK----KdiiVRG-----GenissrEVEDILLQHPKIHDACVVAMS 486
Cdd:COG1020 837 ERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG------EIEAALLQHPGVREAVVVARE 907
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 487 DERLGERSCAYVVlkAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDV 561
Cdd:COG1020 908 DAPGDKRLVAYVV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
40-561 |
2.41e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 189.95 E-value: 2.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVVDNHGASyTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK06164 8 RADTLASLLDAHARARPDAVALIDEDRPL-SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAK-MFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPAT-SSLSLSQIIADNTSL 197
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARwLVVWPGFKGIDFAAILAAVPPDALPPLRAIAVVDDAADATpAPAPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 198 TTAITTHG-----DELAAVLFT-SGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFlHGVTAPFL 271
Cdd:PRK06164 167 PAPPAAAGeraadPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 272 IGARSVLLDIFTPDACLALLEQQRCTCMLGATPFvYDLLNVLEKQPADLSALRffLCG-GTTIPK--KVARECQQRGIKL 348
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEM-LRRILDTAGERADFPSAR--LFGfASFAPAlgELAALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 349 LSVYGSTE-SSPHAVVNLDDPLSRFMHTDGY-AAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL 425
Cdd:PRK06164 323 TGLYGSSEvQALVALQPATDPVSVRIEGGGRpASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARAL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMsdERLGERSCAYVVLKAPHH 505
Cdd:PRK06164 403 TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPTDGA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 506 SLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSG---KIQKFLLRKDIMRRLTQDV 561
Cdd:PRK06164 481 SPDEAGLMAAC-REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAER 538
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
55-551 |
2.65e-53 |
|
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: 189.66 E-value: 2.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 55 MPDKIAVVDNH-GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELV 133
Cdd:cd17642 30 VPGTIAFTDAHtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 134 WVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNT-------SLTTAITTHGD 206
Cdd:cd17642 110 HSLNISKPTIVFC-----SKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLppgfneyDFKPPSFDRDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNIlaserayCARLNLTWQDVF---MMPA-------PLGHATGFLHGVTApFLIGARS 276
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNI-------VARFSHARDPIFgnqIIPDtailtviPFHHGFGMFTTLGY-LICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 277 VLLDIFTPDACLALLEQQRCTCMLgatpFVYDLLNVLEKQPA----DLSALRFFLCGGTTIPKKVARECQQRgIKLLSV- 351
Cdd:cd17642 257 VLMYKFEEELFLRSLQDYKVQSAL----LVPTLFAFFAKSTLvdkyDLSNLHEIASGGAPLSKEVGEAVAKR-FKLPGIr 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 352 --YGSTESSPHAVVN---LDDPLSRfmhtdGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL 425
Cdd:cd17642 332 qgYGLTETTSAILITpegDDKPGAV-----GKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKApHH 505
Cdd:cd17642 407 DKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEA-GK 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1489134476 506 SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd17642 486 TMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
69-550 |
8.26e-53 |
|
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: 186.17 E-value: 8.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFA-P 147
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 148 TLFKQTRPVDLilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgdelAAVLFTSGTEGLPKGVMLT 227
Cdd:cd05969 81 ELYERTDPEDP--------------------------------------------------TLLHYTSGTTGTPKGVLHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI-FTPDACLALLEQQRCTCMLGAtPFV 306
Cdd:cd05969 111 HDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGrFDAESWYGIIERVKVTVWYTA-PTA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 307 YDLLNVLEKQPA---DLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSPHAVVN-LDDPLSrfMHTDGYAAA 381
Cdd:cd05969 190 IRMLMKEGDELArkyDLSSLRFIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETGSIMIANyPCMPIK--PGSMGKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 382 GVEIKVVDDARKTLPPGCEGEEASRG--PNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGG 459
Cdd:cd05969 268 GVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 460 ENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHH-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPR 538
Cdd:cd05969 347 HRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEpSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|..
gi 1489134476 539 TTSGKIQKFLLR 550
Cdd:cd05969 427 TRSGKIMRRVLK 438
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
41-543 |
1.49e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 187.78 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVdnHGA-SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK07798 2 AWNIADLFEAVADAVPDRVALV--CGDrRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKmffapTLFKQTRPVDLILPLQNQLPQLQQIVGVD---KLAPATSSLSLSQIIADNTS 196
Cdd:PRK07798 80 PVNVNYRYVEDELRYLLDDSDAV-----ALVYEREFAPRVAEVLPRLPKLRTLVVVEdgsGNDLLPGAVDYEDALAAGSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 197 LTTAITTHGDELAaVLFTSGTEGLPKGVMLTHNNI---------------LASERAYCARLNLTWQDVFMMPAPLGHATG 261
Cdd:PRK07798 155 ERDFGERSPDDLY-LLYTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 262 FLHGVTApFLIGARSVLLDI--FTPDACLALLEQQRCTCMlgatPFVYD-----LLNVLE-KQPADLSALRFFLCGGTTI 333
Cdd:PRK07798 234 QWAAFAA-LFSGQTVVLLPDvrFDADEVWRTIEREKVNVI----TIVGDamarpLLDALEaRGPYDLSSLFAIASGGALF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 334 PKKVARECQQR--GIKLLSVYGSTES---SPHAVVnlddplSRFMHTDG-YAAAGVEIKVVDDARKTLPPGcEGEE--AS 405
Cdd:PRK07798 309 SPSVKEALLELlpNVVLTDSIGSSETgfgGSGTVA------KGAVHTGGpRFTIGPRTVVLDEDGNPVEPG-SGEIgwIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 406 RGPNVFMGYFDEPELTA---RALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV 482
Cdd:PRK07798 382 RRGHIPLGYYKDPEKTAetfPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489134476 483 VAMSDERLGERSCAyVVLKAPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:PRK07798 462 VGVPDERWGQEVVA-VVQLREGARPDLAELRA-HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
56-544 |
2.85e-51 |
|
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: 182.49 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd12116 1 PDATAVRDDDR-SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNkcqakmffaptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSslslsqiiADNTSLTTaiTTHGDELAAVLFTS 215
Cdd:cd12116 80 LE--------------DAEPALVLTDDALPDRLPAGLPVLLLALAAAA--------AAPAAPRT--PVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTaPFLIGARSVLL---DIFTPDACLALLE 292
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLL-PLLAGARVVIApreTQRDPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTcMLGATPFVYDLLnvLEKQPADLSALRfFLCGGTTIPKKVARECQQRGIKLLSVYGSTE----SSPHAVVNLDDP 368
Cdd:cd12116 215 AHSIT-VMQATPATWRML--LDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVGSLWNLYGPTEttiwSTAARVTAAAGP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 369 LsrfmhTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL-----DEEG--WYYSGDLCRMDE 441
Cdd:cd12116 291 I-----PIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfAGPGsrLYRTGDLVRRRA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 442 AGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDAcVVAMSDERLGERSCAYVVLKAPhHSLSLEEVVAFFsRKR 520
Cdd:cd12116 366 DGRLEYLGRADGqVKIR-GHRIELGEIEAALAAHPGVAQA-AVVVREDGGDRRLVAYVVLKAG-AAPDAAALRAHL-RAT 441
|
490 500
....*....|....*....|....
gi 1489134476 521 VAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKL 465
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
52-549 |
5.74e-51 |
|
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: 182.32 E-value: 5.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVD-NHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREA 130
Cdd:cd05923 11 ASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 131 ELVWVLNKCQAKmffAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQiiadntslttaitTHGDELAA 210
Cdd:cd05923 91 ELAELIERGEMT---AAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPP-------------REPEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNilASER----AYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDA 286
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQRA--AESRvlfmSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTCMLgATPFVYD-LLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTEssphAVVN 364
Cdd:cd05923 233 ALKLIEQERVTSLF-ATPTHLDaLAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhLPGEKVNIYGTTE----AMNS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 365 LDDPLSRfMHTDGYAAAGVEIKVV---DDARKTLPPGCEGE--EASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRM 439
Cdd:cd05923 308 LYMRDAR-TGTEMRPGFFSEVRIVrigGSPDEALANGEEGEliVAAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 440 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhSLSLEEVVAFFSRK 519
Cdd:cd05923 386 DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--TLSADELDQFCRAS 463
|
490 500 510
....*....|....*....|....*....|
gi 1489134476 520 RVAKYKYPEHIVVIEKLPRTTSGKIQKFLL 549
Cdd:cd05923 464 ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-551 |
1.21e-50 |
|
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: 180.02 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSwreaelvwvlnkcqakmfFAPT 148
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTA------------------FGPK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 LFKQtrpvdlilplqnqlpqlqqivgvdKLAPATSSLSLSQiiADNTSLTTaitthgDELAAVLFTSGTEGLPKGVMLTH 228
Cdd:cd05973 63 AIEH------------------------RLRTSGARLVVTD--AANRHKLD------SDPFVMMFTSGTTGLPKGVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD-IFTPDACLALLEQQRCTCMLGAtPFVY 307
Cdd:cd05973 111 RALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVIERLGVTNLAGS-PTAY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 308 DLLNV--LEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSphAVVNLDDPLSRFMH--TDGYAAAG 382
Cdd:cd05973 190 RLLMAagAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELG--MVLANHHALEHPVHagSAGRAMPG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 383 VEIKVVDDARKTLPPGCEGE---EASRGPNV-FMGYFDEPELTARAldeeGWYYSGDLCRMDEAGYIKITGRKKDIIVRG 458
Cdd:cd05973 268 WRVAVLDDDGDELGPGEPGRlaiDIANSPLMwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 459 GENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHH-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLP 537
Cdd:cd05973 344 GYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEgTPALADELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|....
gi 1489134476 538 RTTSGKIQKFLLRK 551
Cdd:cd05973 424 KTPSGKIQRFLLRR 437
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
77-550 |
1.21e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 181.82 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 77 AASCLANWmlakGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT-LFKQTRP 155
Cdd:PRK12406 24 AAGGLAAL----GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAdLLHGLAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 156 -----VDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITThgdELAAVLFTSGTEGLPKGVML---T 227
Cdd:PRK12406 100 alpagVTVLSVPTPPEIAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGPPVP---QPQSMIYTSGTTGHPKGVRRaapT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 228 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTApFLIGARSVLLDIFTPDACLALLEQQRCTCM-LGATPFV 306
Cdd:PRK12406 177 PEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQLIERHRITHMhMVPTMFI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 307 yDLLNVLEKQPA--DLSALRFFLCGGTTIPKKVARE-CQQRGIKLLSVYGSTESSPHAVVNLDDPLSRfMHTDGYAAAGV 383
Cdd:PRK12406 256 -RLLKLPEEVRAkyDVSSLRHVIHAAAPCPADVKRAmIEWWGPVIYEYYGSTESGAVTFATSEDALSH-PGTVGKAAPGA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 384 EIKVVDDARKTLPPGCEGEEASRGP-NVFMGYFDEPElTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENI 462
Cdd:PRK12406 334 ELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPE-KRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 463 SSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSG 542
Cdd:PRK12406 413 YPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQ-PGATLDEADIRAQL-KARLAGYKVPKHIEIMAELPREDSG 490
|
....*...
gi 1489134476 543 KIQKFLLR 550
Cdd:PRK12406 491 KIFKRRLR 498
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
50-544 |
1.53e-50 |
|
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: 181.39 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWRE 129
Cdd:cd17651 3 RQAARTPDAPALVAE-GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 130 AELVWVLNKCQakmffaPTLfkqtrpvdlilplqnqlpqlqqIVGVDKLAPATSSLSLSQIIADNTSLTTAIT------T 203
Cdd:cd17651 82 ERLAFMLADAG------PVL----------------------VLTHPALAGELAVELVAVTLLDQPGAAAGADaepdpaL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNIlaseraycarLNLT-WQDVFmMPAPLGHAT------GF---LHGVTAPFLIG 273
Cdd:cd17651 134 DADDLAYVIYTSGSTGRPKGVVMPHRSL----------ANLVaWQARA-SSLGPGARTlqfaglGFdvsVQEIFSTLCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 274 ARSVLL--DI-FTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGG--TTIPKKVAREC-QQRGIK 347
Cdd:cd17651 203 ATLVLPpeEVrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGeqLVLTEDLREFCaGLPGLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 348 LLSVYGSTESspHAVVNLDDPLSRFMHTD----GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR 423
Cdd:cd17651 283 LHNHYGPTET--HVVTALSLPGDPAAWPApppiGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 424 ALDEEGW------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAY 497
Cdd:cd17651 361 RFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAY 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1489134476 498 VVLkAPHHSLSLEEVVAFFSRkRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17651 441 VVG-DPEAPVDAAELRAALAT-HLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
206-552 |
1.82e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 180.57 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPD 285
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 286 ACLALLeQQRCTCMLGaTPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKV-ARECQQRGIKLLSVYGSTESSPHAVVN 364
Cdd:PRK07787 208 AYAQAL-SEGGTLYFG-VPTVWSRIAADPEAARALRGARLLVSGSAALPVPVfDRLAALTGHRPVERYGMTETLITLSTR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 365 LDDPlsRFMHTDGYAAAGVEIKVVDDARKTLPPGCE--GEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEA 442
Cdd:PRK07787 286 ADGE--RRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlkaPHHSLSLEEVVAFFSRkRV 521
Cdd:PRK07787 364 GMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV---GADDVAADELIDFVAQ-QL 439
|
330 340 350
....*....|....*....|....*....|.
gi 1489134476 522 AKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK07787 440 SVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
42-552 |
3.99e-50 |
|
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: 180.94 E-value: 3.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDK-IAVVDNHGASY--TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGA 118
Cdd:cd05906 10 RTLLELLLRAAERGPTKgITYIDADGSEEfqSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 119 VSVPL--LPSWREAelvwvlNKCQAKMFFAPTLFKQtrPVDLilplqNQLPQLQQIVGVDKLAPATSSLSLSQIIADNT- 195
Cdd:cd05906 90 VPAPLtvPPTYDEP------NARLRKLRHIWQLLGS--PVVL-----TDAELVAEFAGLETLSGLPGIRVLSIEELLDTa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 196 SLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgvtapflIGAR 275
Cdd:cd05906 157 ADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVE-------LHLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 276 SVLLDIFT----PDACLA-------LLEQQRCTCMLgATPFVYDLLN-VLEK---QPADLSALRFFLCGGTTIPKKVAR- 339
Cdd:cd05906 230 AVYLGCQQvhvpTEEILAdplrwldLIDRYRVTITW-APNFAFALLNdLLEEiedGTWDLSSLRYLVNAGEAVVAKTIRr 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 340 ------ECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAA-----AGVEIKVVDDARKTLPPGCEGEEASRGP 408
Cdd:cd05906 309 llrllePYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSlgrpiPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 409 NVFMGYFDEPELTARALDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENISSREVEdillqhpkihdACVvamsdE 488
Cdd:cd05906 389 VVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIE-----------AAV-----E 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 489 RLGERSCAYVVlKAPHHSL--SLEEVVAFFS----------------RKRVAKYK--YPEHIVVIEK--LPRTTSGKIQK 546
Cdd:cd05906 452 EVPGVEPSFTA-AFAVRDPgaETEELAIFFVpeydlqdalsetlraiRSVVSREVgvSPAYLIPLPKeeIPKTSLGKIQR 530
|
....*.
gi 1489134476 547 FLLRKD 552
Cdd:cd05906 531 SKLKAA 536
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
31-556 |
5.58e-50 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 180.72 E-value: 5.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 31 AAYRQQGLWGDASLAdywqQTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIY 110
Cdd:PRK13382 36 AAMRREGMGPTSGFA----IAAQRCPDRPGLIDELG-TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 111 LACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLilplqnqlpqlqqivgvDKLAPATSSLSLSQI 190
Cdd:PRK13382 111 LAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRAL-----------------ADCPQATRIVAWTDE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 191 IADNTSLTTaITTHGDELA--------AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGF 262
Cdd:PRK13382 174 DHDLTVEVL-IAAHAGQRPeptgrkgrVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 263 LHGVTApFLIGARSVLLDIFTPDACLALLEQQRCTCmLGATPFVYD-LLNVLEK--QPADLSALRFFLCGGTTIPKKVAR 339
Cdd:PRK13382 253 SQLVLA-ASLACTIVTRRRFDPEATLDLIDRHRATG-LAVVPVMFDrIMDLPAEvrNRYSGRSLRFAAASGSRMRPDVVI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 340 ECQQR-GIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYfdep 418
Cdd:PRK13382 331 AFMDQfGDVIYNNYNATEAGMIATATPAD-LRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 elTARALDE--EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCA 496
Cdd:PRK13382 406 --TSGSTKDfhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 497 YVVLKAphHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKDIMRR 556
Cdd:PRK13382 484 FVVLKP--GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKI----LRRELQAR 537
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-550 |
1.19e-49 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 177.62 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLlpswreaelvwvlnkcqakmffaPT 148
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL-----------------------FA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 LFkqtrpvdlilplqnqlpqlqqivGVDKLAPATSSLSLSQIIADNTslttaitthgDELAAVLFTSGTEGLPKGVMLTH 228
Cdd:cd05971 64 LF-----------------------GPEALEYRLSNSGASALVTDGS----------DDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQ--DVFMMPAPLGHATGFLhGVTAPFLIGARSVL---LDIFTPDACLALLEQQRCTcMLGAT 303
Cdd:cd05971 111 RVLLGHLPGVQFPFNLFPRdgDLYWTPADWAWIGGLL-DVLLPSLYFGVPVLahrMTKFDPKAALDLMSRYGVT-TAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 304 PFVYDLLNVLEKQ--PADLSaLRFFLCGGTTIPKKV---AREcqQRGIKLLSVYGSTES----SPHAVVNLDDPLSRfmh 374
Cdd:cd05971 189 PTALKMMRQQGEQlkHAQVK-LRAIATGGESLGEELlgwARE--QFGVEVNEFYGQTECnlviGNCSALFPIKPGSM--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 375 tdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPN--VFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKK 452
Cdd:cd05971 263 --GKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 453 DIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHH-SLSLEEVVAFFSRKRVAKYKYPEHIV 531
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETpSDALAREIQELVKTRLAAHEYPREIE 419
|
490
....*....|....*....
gi 1489134476 532 VIEKLPRTTSGKIQKFLLR 550
Cdd:cd05971 420 FVNELPRTATGKIRRRELR 438
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
64-550 |
1.40e-49 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 180.07 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 64 NHGASYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAEL---------- 132
Cdd:PRK08751 46 SFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELkhqlidsgas 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 133 --VWVLNKCQA-KMFFAPTLFKQTRPVDL--ILPLQNQLPQLQQIVGVDKLAP---ATSSLSLSQIIADNTSLT-TAITT 203
Cdd:PRK08751 126 vlVVIDNFGTTvQQVIADTPVKQVITTGLgdMLGFPKAALVNFVVKYVKKLVPeyrINGAIRFREALALGRKHSmPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ-----DVFMMPAPLGHatgfLHGVTAPFLI-----G 273
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYH----IFALTANGLVfmkigG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 274 ARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ-RGIKLLSVY 352
Cdd:PRK08751 282 CNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQvTGLTLVEAY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 353 GSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYY 432
Cdd:PRK08751 362 GLTETSPAACINPLT-LKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLH 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 433 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhSLSLEEV 512
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDP--ALTAEDV 518
|
490 500 510
....*....|....*....|....*....|....*...
gi 1489134476 513 VAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK08751 519 KA-HARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
81-557 |
5.55e-49 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 178.45 E-value: 5.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 81 LANWMLAKGIESGDRIAFqlpgwCEF-TVIYLACLK----IGAVSVPLlpSWReaelvWVLNKCQAKMffaptlfKQTRP 155
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAI-----AALnSDLYLEWLLavacAGGIVAPL--NYR-----WSFEEAKSAM-------LLVRP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 156 VDLILPLQNQLPQLQqiVGVDKLAPA-----TSSLSLSQIIADNTSLTT------AITTHGDELA-----AVL--FTSGT 217
Cdd:PLN02860 106 VMLVTDETCSSWYEE--LQNDRLPSLmwqvfLESPSSSVFIFLNSFLTTemlkqrALGTTELDYAwapddAVLicFTSGT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 218 EGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCT 297
Cdd:PLN02860 184 TGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGG-LSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 298 CMLGATPFVYDLLNV--LEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTES-SPHAVVNLDDP-LSR 371
Cdd:PLN02860 263 SMITVPAMMADLISLtrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTEAcSSLTFMTLHDPtLES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 372 FMHTD-------------------GYAAAGVEIKVVDDARKTlppgcEGEEASRGPNVFMGYFDEPELTARALDEEGWYY 432
Cdd:PLN02860 343 PKQTLqtvnqtksssvhqpqgvcvGKPAPHVELKIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLD 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 433 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLK---------AP 503
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRdgwiwsdneKE 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 504 HHS----LSLEEVVAFFSRKRVAKYKYPEHIVVIEK-LPRTTSGKIQKFLLRKDIMRRL 557
Cdd:PLN02860 498 NAKknltLSSETLRHHCREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREVLSHL 556
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
43-546 |
1.18e-48 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 177.00 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIA-VVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK05852 17 RIADLVEVAATRLPEAPAlVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMffapTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSqIIADNTSLTTAI 201
Cdd:PRK05852 97 PLDPALPIAEQRVRSQAAGARV----VLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLD-AATEPTPATSTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPfLIGARSVLL-- 279
Cdd:PRK05852 172 EGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAT-LASGGAVLLpa 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 -----------DIFTPDAClalleqqrctcMLGATPFVYDLLNVL---EKQPADLSALRFFLCGGTTIPKKVARECQQR- 344
Cdd:PRK05852 251 rgrfsahtfwdDIKAVGAT-----------WYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQTEf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 GIKLLSVYGSTESSpHAVVNLDDPLSRFMHTDGYA------AAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEP 418
Cdd:PRK05852 320 AAPVVCAFGMTEAT-HQVTTTQIEGIGQTENPVVStglvgrSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PRK05852 399 TITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVI 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1489134476 499 VLKAPHHSlSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK05852 478 VPRESAPP-TAEELVQ-FCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
43-544 |
2.41e-48 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 181.28 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANwMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVP 122
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 123 LLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQ-------LQQIVGVDKL-APATSSLSLSQIIAdn 194
Cdd:PRK08633 695 LNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKviyledlKAKISKVDKLtALLAARLLPARLLK-- 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 195 TSLTTAITThgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLhgVTA--PFLI 272
Cdd:PRK08633 773 RLYGPTFKP--DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLT--VTLwlPLLE 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 273 GARSVlldiFTPD-----ACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GI 346
Cdd:PRK08633 849 GIKVV----YHPDptdalGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKfGI 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 347 KLLSVYGSTESSPHAVVNLDDPLSR--FMHTD------GYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDE 417
Cdd:PRK08633 925 RILEGYGATETSPVASVNLPDVLAAdfKRQTGskegsvGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 418 PELTARAL---DEEGWYYSGDLCRMDEAGYIKITGRkkdiIVR----GGENISSREVEDILLQhpKIHDA----CVVAMS 486
Cdd:PRK08633 1005 PEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR----YSRfakiGGEMVPLGAVEEELAK--ALGGEevvfAVTAVP 1078
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 487 DERLGERscayVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:PRK08633 1079 DEKKGEK----LVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
56-544 |
4.24e-48 |
|
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: 174.38 E-value: 4.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDnHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLP-GWcEFTVIYLACLKIGAVSVPLLPSWREAELVW 134
Cdd:cd12114 1 PDATAVIC-GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPkGP-EQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 135 VLNKCQAKMFFaptlfkqtrpVDLILPLQNQLPQLQQIVGVDKLAPAtsslslsqiiADNTSLTTAItthgDELAAVLFT 214
Cdd:cd12114 79 ILADAGARLVL----------TDGPDAQLDVAVFDVLILDLDALAAP----------APPPPVDVAP----DDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 215 SGTEGLPKGVMLTH----NNILASERaycaRLNLTWQDVFMMPAPLGH--ATGFLHGVTApflIGARSVLLD---IFTPD 285
Cdd:cd12114 135 SGSTGTPKGVMISHraalNTILDINR----RFAVGPDDRVLALSSLSFdlSVYDIFGALS---AGATLVLPDearRRDPA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 286 ACLALLEQQRCTcMLGATPFVYD-LLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAV 362
Cdd:cd12114 208 HWAELIERHGVT-LWNSVPALLEmLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 V-NLDDPlsrfmHTD------GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL----DEEGWY 431
Cdd:cd12114 287 YhPIDEV-----PPDwrsipyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 432 YSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMsDERLGERSCAYVVLKAPHHSLSLEE 511
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDA 440
|
490 500 510
....*....|....*....|....*....|...
gi 1489134476 512 VVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd12114 441 LRAFLA-QTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
46-550 |
6.72e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 174.49 E-value: 6.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTARAMPDKIAVV-DNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLl 124
Cdd:PRK13391 1 MYPGIHAQTTPDKPAVImASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 125 pSWR--EAELVWVLNKCQAKMFF--------APTLFKQTRPVDLILPLQNQLPQLqqivGVDKLAPATSSLSLSQIiaDN 194
Cdd:PRK13391 80 -NSHltPAEAAYIVDDSGARALItsaakldvARALLKQCPGVRHRLVLDGDGELE----GFVGYAEAVAGLPATPI--AD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 195 TSLTTAItthgdelaavLFTSGTEGLPKGVM--LTHNNIlASERAYCARLNLTWQ----DVFMMPAPLGH-ATGFLHGVT 267
Cdd:PRK13391 153 ESLGTDM----------LYSSGTTGRPKGIKrpLPEQPP-DTPLPLTAFLQRLWGfrsdMVYLSPAPLYHsAPQRAVMLV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 268 APFliGARSVLLDIFTPDACLALLEQQRCT-CMLGATPFVYDLlnvleKQPA------DLSALRFFLCGGTTIPKKVARE 340
Cdd:PRK13391 222 IRL--GGTVIVMEHFDAEQYLALIEEYGVThTQLVPTMFSRML-----KLPEevrdkyDLSSLEVAIHAAAPCPPQVKEQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 341 -CQQRGIKLLSVYGSTESSPHAVVNLDDPLSRfMHTDGYAAAGVeIKVVDDARKTLPPGCEGEEASRGPNVFMgYFDEPE 419
Cdd:PRK13391 295 mIDWWGPIIHEYYAATEGLGFTACDSEEWLAH-PGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 420 LTARALDEEG-WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PRK13391 372 KTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 499 VLK---APHHSLSlEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK13391 452 QPVdgvDPGPALA-AELIAFC-RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
211-542 |
7.49e-48 |
|
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: 169.79 E-value: 7.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVLLDIFTPDACLAL 290
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 291 LEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCG---GTTIPKKVARECQQRGikllsVYGSTESSPHAVVN-LD 366
Cdd:cd17636 84 IEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewNDMATVDTSPWGRKPG-----GYGQTEVMGLATFAaLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 367 DPLSRFMhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIK 446
Cdd:cd17636 159 GGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 447 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKY 526
Cdd:cd17636 235 FVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLK-PGASVTEAELIE-HCRARIASYKK 312
|
330
....*....|....*.
gi 1489134476 527 PEHIVVIEKLPRTTSG 542
Cdd:cd17636 313 PKSVEFADALPRTAGG 328
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
206-550 |
1.73e-47 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 173.99 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAY---CARLNLTWQDV--FMMPAPLGHatgfLHGVTAPFLIGARS-VLL 279
Cdd:TIGR03205 192 DDVALLQYTGGTTGLPKGAMLTHGNLTSAVSIYdvwGKPSRATRGDVerVICVLPLFH----IYALTVILLRSLRRgDLI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 DI---FTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGST 355
Cdd:TIGR03205 268 SLhqrFDVAAVFRDIEEKRATVFPGVPTMWIALANDPSLEKRDLSSLATIGSGGAPLPVEVANFFERKtGLKLKSGWGMT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 356 ES-SP---HAVVNLDDPLSRfmhtdGYAAAGVEIKVV--DDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEG 429
Cdd:TIGR03205 348 ETcSPgtgHPPEGPDKPGSI-----GLMLPGIELDVVslDDPTKVLPPGEVGELRIRGPNVTRGYWNRPEESAEAF-VGD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 430 WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSL 509
Cdd:TIGR03205 422 RFLTGDIGYMDTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQEVIVIGIPDQYRGEAAKAFVKLRPGAKPFSL 501
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1489134476 510 EEVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:TIGR03205 502 DELRAFLAGK-LGKHELPVAVEFVDELPRTPVGKLSRHELR 541
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
187-491 |
4.33e-47 |
|
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: 171.39 E-value: 4.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 187 LSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA------- 259
Cdd:cd17640 69 LLYILNHSESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSyersaey 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 260 TGFLHGVTAPFlIGARSVLLDI--FTPDaclalleqqrctcMLGATPFVYD-LLNVLEKQPADLSA-------------- 322
Cdd:cd17640 149 FIFACGCSQAY-TSIRTLKDDLkrVKPH-------------YIVSVPRLWEsLYSGIQKQVSKSSPikqflflfflsggi 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 LRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVN-LDDPLsrfMHTDGYAAAGVEIKVVD-DARKTLPPGCE 400
Cdd:cd17640 215 FKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARrLKCNV---RGSVGRPLPGTEIKIVDpEGNVVLPPGEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 401 GEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIV-RGGENISSREVEDILLQHPKIHD 479
Cdd:cd17640 292 GIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQ 371
|
330
....*....|..
gi 1489134476 480 ACVVAMSDERLG 491
Cdd:cd17640 372 IMVVGQDQKRLG 383
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
212-550 |
6.31e-47 |
|
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: 171.02 E-value: 6.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVM--LTHNNILASERAYCArLNLTWQ--DVFMMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPDAC 287
Cdd:cd05929 131 LYSGGTTGRPKGIKrgLPGGPPDNDTLMAAA-LGFGPGadSVYLSPAPLYHAAPFRWSMTALFM-GGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 288 LALLEQQRCTCM-LGATPFVyDLLNVLEKQPA--DLSALRFFLCGGTTIPKKVarecQQRGI-----KLLSVYGSTESSP 359
Cdd:cd05929 209 LRLIERYRVTFAqFVPTMFV-RLLKLPEAVRNayDLSSLKRVIHAAAPCPPWV----KEQWIdwggpIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 360 HAVVNLDDPLSrfmH--TDGYAAAGvEIKVVDDARKTLPPGCEGEEASRGPNVFMgYFDEPELTARALDEEGWYYSGDLC 437
Cdd:cd05929 284 LTIINGEEWLT---HpgSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 438 RMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV--VLKAPHHSLSLEEVVAF 515
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpAPGADAGTALAEELIAF 438
|
330 340 350
....*....|....*....|....*....|....*
gi 1489134476 516 FsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05929 439 L-RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
50-551 |
7.06e-47 |
|
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: 172.42 E-value: 7.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVV-----DNHGASYTYSALDHAASCLANWMLAKGiESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLL 124
Cdd:cd05931 1 RRAAARPDRPAYTflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 125 PSWREAELVWVLNkcqakmffaptLFKQTRPVDLILPLQNqlpqlqqIVGVDKLAPATSSLSLSQIIADNTSLTTAITT- 203
Cdd:cd05931 80 PPTPGRHAERLAA-----------ILADAGPRVVLTTAAA-------LAAVRAFAASRPAAGTPRLLVVDLLPDTSAADw 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 -----HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 278
Cdd:cd05931 142 pppspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 LdifTPDACLA-------LLEQQRCTCMlGATPFVYDL----LNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--- 344
Cdd:cd05931 222 M---SPAAFLRrplrwlrLISRYRATIS-AAPNFAYDLcvrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfap 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 -GIK---LLSVYGSTESS---------PHAVVNLDDPLSRFMHTD---------------GYAAAGVEIKVVDDA-RKTL 395
Cdd:cd05931 298 fGFRpeaFRPSYGLAEATlfvsggppgTGPVVLRVDRDALAGRAVavaaddpaarelvscGRPLPDQEVRIVDPEtGREL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 396 PPGCEGEEASRGPNVFMGYFDEPELTAR------ALDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENISSREVED 469
Cdd:cd05931 378 PDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 470 ILLQ-HPKIHDACVVAMS-DERLGERSCAYVVLKAPHHSLSLEEVVAFFsRKRVAKykypEH------IVVIE--KLPRT 539
Cdd:cd05931 457 TAEEaHPALRPGCVAAFSvPDDGEERLVVVAEVERGADPADLAAIAAAI-RAAVAR----EHgvapadVVLVRpgSIPRT 531
|
570
....*....|..
gi 1489134476 540 TSGKIQKFLLRK 551
Cdd:cd05931 532 SSGKIQRRACRA 543
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
52-550 |
4.82e-46 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 169.98 E-value: 4.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVV--DNHGAS--YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSW 127
Cdd:cd05970 27 AKEYPDKLALVwcDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 128 REAELVWVLNKCQAKMFFA------PTLFKQTRP---VDLILPLQNQLPQLQQI---VGVDKLAPatsslslsqiiaDNT 195
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAiaedniPEEIEKAAPecpSKPKLVWVGDPVPEGWIdfrKLIKNASP------------DFE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 196 SLTTAITTHGDELAAVLFTSGTEGLPKgvMLTHNNILASERAYCARLnltWQDV-----FMMPAPLGHATGFLHGVTAPF 270
Cdd:cd05970 175 RPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKY---WQNVregglHLTVADTGWGKAVWGKIYGQW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 271 LIGARSVLLDI--FTPDACLALLEQQRCTCmLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIK 347
Cdd:cd05970 250 IAGAAVFVYDYdkFDPKALLEKLSKYGVTT-FCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALnPEVFNTFKEKTGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 348 LLSVYGSTESSPH-AVVNLDDPLSRFMhtdGYAAAGVEIKVVDDARKTLPPGCEGE---EASRGPNV--FMGYFDEPELT 421
Cdd:cd05970 329 LMEGFGQTETTLTiATFPWMEPKPGSM---GKPAPGYEIDLIDREGRSCEAGEEGEiviRTSKGKPVglFGGYYKDAEKT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 422 ARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLK 501
Cdd:cd05970 406 AEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 502 APHH-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05970 485 KGYEpSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
57-557 |
5.81e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 170.08 E-value: 5.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 57 DKIAV--VDNHGA-SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELV 133
Cdd:PRK04319 59 DKVALryLDASRKeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 134 WVLNKCQAKMFF-APTLFKQtRPVDLILPLQNQLpqlqqIVG-VDKLAPATssLSLSQIIADNTSLTTAITTHGDELAAV 211
Cdd:PRK04319 139 DRLEDSEAKVLItTPALLER-KPADDLPSLKHVL-----LVGeDVEEGPGT--LDFNALMEQASDEFDIEWTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNNILAseRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI-FTPDACL 288
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHNAMLQ--HYQTGKyvLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGrFSPERWY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 289 ALLEQQRCTC---------ML-GATPfvydllNVLEKQpaDLSALRFFLCGGTTIPKKVARECQQrgikllsVYG----- 353
Cdd:PRK04319 289 RILEDYKVTVwytaptairMLmGAGD------DLVKKY--DLSSLRHILSVGEPLNPEVVRWGMK-------VFGlpihd 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 ---STESSPHAVVN---LD-DPLSrfMhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRG--PNVFMGYFDEPELTARA 424
Cdd:PRK04319 354 nwwMTETGGIMIANypaMDiKPGS--M---GKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 425 LdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPH 504
Cdd:PRK04319 429 F-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1489134476 505 H-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKiqkfllrkdIMRRL 557
Cdd:PRK04319 508 EpSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK---------IMRRV 552
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
69-550 |
7.92e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 169.12 E-value: 7.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIA-FQLPGWCEFTvIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAK--MF- 144
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGtLAWNGYRHLE-AYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRyvLFd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 145 --FAPTlfkqtrpVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVL-FTSGTEGLP 221
Cdd:PRK07008 119 ltFLPL-------VDALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLcYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 222 KGVMLTHNNILAseRAYCARL----NLTWQDVFMMPAPLGH--ATGFLHGVTapfLIGARSVL----LDiftPDACLALL 291
Cdd:PRK07008 192 KGALYSHRSTVL--HAYGAALpdamGLSARDAVLPVVPMFHvnAWGLPYSAP---LTGAKLVLpgpdLD---GKSLYELI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 292 EQQRCTCMLGaTPFVY-DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVV------ 363
Cdd:PRK07008 264 EAERVTFSAG-VPTVWlGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDeYGVEVIHAWGMTEMSPLGTLcklkwk 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 364 NLDDPLSRFMHT---DGYAAAGVEIKVVDDARKTLP--PGCEGEEASRGPNVFMGYF--DEPELTaraldeEGWYYSGDL 436
Cdd:PRK07008 343 HSQLPLDEQRKLlekQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVRGPWVIDRYFrgDASPLV------DGWFPTGDV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAFF 516
Cdd:PRK07008 417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR-PGAEVTREELLAFY 495
|
490 500 510
....*....|....*....|....*....|....
gi 1489134476 517 SRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK07008 496 EGK-VAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
56-550 |
1.03e-45 |
|
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: 167.16 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd17649 1 PDAVALVFG-DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LnkcqakmffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiaDNTSLTTAITTHGDELAAVLFTS 215
Cdd:cd17649 80 L--------------------------------------------------------EDSGAGLLLTHHPRQLAYVIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGhATGFLHGVTAPFLIGARSVLLD---IFTPDACLALLE 292
Cdd:cd17649 104 GSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGACVVLRPdelWASADELAEMVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTCMLGATPFVYDLLNVLEKQPADL-SALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTEssphAVVN--LDDPL 369
Cdd:cd17649 183 ELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTE----ATVTplVWKCE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 370 SRFmhTDGYAA-------AGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA-----RALDEEG--WYYSGD 435
Cdd:cd17649 259 AGA--ARAGASmpigrplGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAerfvpDPFGAPGsrLYRTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 436 LCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDErLGERSCAYVVLKAPHHSLSLEEVVAF 515
Cdd:cd17649 337 LARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPELRAQLRT 415
|
490 500 510
....*....|....*....|....*....|....*
gi 1489134476 516 FSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd17649 416 ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
56-565 |
5.48e-45 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 167.33 E-value: 5.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDN-HGASYTYSAL----DHAASCLANWMlakGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREA 130
Cdd:PLN02574 53 NGDTALIDSsTGFSISYSELqplvKSMAAGLYHVM---GVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 131 ELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSlsQIIADNTSLTTAITTHGDELAA 210
Cdd:PLN02574 130 EIKKRVVDCSVGLAFT-----SPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFY--ELIKEDFDFVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNIL----------ASERAYCARLNltwqdVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD 280
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIamvelfvrfeASQYEYPGSDN-----VYLAALPMFHIYGLSLFVVGLLSLGSTIVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDACLALLEQQRCTCMlgatPFVYDLLNVLEKQPAD-----LSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYG 353
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHF----PVVPPILMALTKKAKGvcgevLKSLKQVSCGAAPLSGKFIQDFVQTlpHVDFIQGYG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 STESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYY 432
Cdd:PLN02574 354 MTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 433 SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlKAPHHSLSLEEV 512
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-RRQGSTLSQEAV 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 513 VAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKDIMRRLTQDVCEEI 565
Cdd:PLN02574 513 INYVA-KQVAPYKKVRKVVFVQSIPKSPAGKI----LRRELKRSLTNSVSSRL 560
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
56-546 |
2.99e-44 |
|
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: 162.86 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd17643 1 PEAVAVVDED-RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaITTHGDELAAVLFTS 215
Cdd:cd17643 80 LADSGPSL---------------------------------------------------------LLTDPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMpaplGHATGF------LHGvtaPFLIGARSVLLDIFT---PDA 286
Cdd:cd17643 103 GSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTL----FHSYAFdfsvweIWG---ALLHGGRLVVVPYEVarsPED 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTcMLGATP--FvYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR----GIKLLSVYGSTESSPH 360
Cdd:cd17643 176 FARLLRDEGVT-VLNQTPsaF-YQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRfgldRPQLVNMYGITETTVH 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 AVVNLDDPLSRFMHTD---GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR-----ALDEEG--W 430
Cdd:cd17643 254 VTFRPLDAADLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanPFGGPGsrM 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLE 510
Cdd:cd17643 334 YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAE 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 1489134476 511 evVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17643 414 --LRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
89-551 |
3.93e-44 |
|
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: 164.56 E-value: 3.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 89 GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffaptlfkqtrpvdlilplqnqlpq 168
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK-------------------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 169 lqQIVGVDKLAPATS-------SLSLSQIIADNTS---------LTTAITTH------GDELAAVLFTSGTEGLPKGVML 226
Cdd:cd05928 117 --CIVTSDELAPEVDsvasecpSLKTKLLVSEKSRdgwlnfkelLNEASTEHhcvetgSQEPMAIYFTSGTTGSPKMAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 227 THNNILASERAyCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLALLEQQRCTCMLGA 302
Cdd:cd05928 195 SHSSLGLGLKV-NGRywLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFvhHLPRFDPLVILKTLSSYPITTFCGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 303 tPFVYDLLnVLEkqpaDLS-----ALRFFLCGGTTIPKKVARECQ-QRGIKLLSVYGSTESSPHAVVNLDDPL-SRFMht 375
Cdd:cd05928 274 -PTVYRML-VQQ----DLSsykfpSLQHCVTGGEPLNPEVLEKWKaQTGLDIYEGYGQTETGLICANFKGMKIkPGSM-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 376 dGYAAAGVEIKVVDDARKTLPPGCEGEEASR-GPN----VFMGYFDEPELTArALDEEGWYYSGDLCRMDEAGYIKITGR 450
Cdd:cd05928 346 -GKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTA-ATIRGDFYLTGDRGIMDEDGYFWFMGR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 451 KKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFS---RKRVAKYKYP 527
Cdd:cd05928 424 ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQqhvKSVTAPYKYP 503
|
490 500
....*....|....*....|....
gi 1489134476 528 EHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd05928 504 RKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
41-554 |
3.49e-43 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 162.07 E-value: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDN-HGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PLN02330 27 KLTLPDFVLQDAELYADKVAFVEAvTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 120 SVPLLPSWREAELVWVLNKCQAKMFFAPTL-FKQTRPVDLilplqnqlpqLQQIVGVDKLAPATSSLSLSQIiADNTSLT 198
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDTnYGKVKGLGL----------PVIVLGEEKIEGAVNWKELLEA-ADRAGDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAI-TTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS--ERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 275
Cdd:PLN02330 176 SDNeEILQTDLCALPFSSGTTGISKGVMLTHRNLVANlcSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 276 SVLLDIFTPDACL-ALLEQQrctcmLGATPFVYDLLNVLEKQPA----DLSALRFFLCGGTTIPKK----VARECQQRGI 346
Cdd:PLN02330 256 VVVMSRFELRTFLnALITQE-----VSFAPIVPPIILNLVKNPIveefDLSKLKLQAIMTAAAPLApellTAFEAKFPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 347 KLLSVYGSTEsspHAVVNLD--DP-----LSRfMHTDGYAAAGVEIKVVD-DARKTLPPGCEGEEASRGPNVFMGYFDEP 418
Cdd:PLN02330 331 QVQEAYGLTE---HSCITLThgDPekghgIAK-KNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PLN02330 407 EETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489134476 499 VLKaPHHSLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIM 554
Cdd:PLN02330 487 VIN-PKAKESEEDILNFVA-ANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKML 540
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
209-546 |
1.05e-42 |
|
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: 155.88 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDAC 287
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 288 LALLEQQRCTcMLGATPFVYD-LLNVLEKQPADLSALRFFLCGGT-TIPKKVARECQQRGIKLLSVYGSTESSPHAVVNL 365
Cdd:cd17635 84 FKILTTNAVT-TTCLVPTLLSkLVSELKSANATVPSLRLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSETGTALCLPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 366 DDPLSRfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYI 445
Cdd:cd17635 163 DDDSIE-INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 446 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLkaphhSLSLEEVVA----FFSRKRV 521
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA-----SAELDENAIralkHTIRREL 315
|
330 340
....*....|....*....|....*
gi 1489134476 522 AKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
56-544 |
1.39e-42 |
|
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: 158.18 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd17652 1 PDAPAVVFG-DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAkmffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntsltTAITTHGDELAAVLFTS 215
Cdd:cd17652 80 LADARP---------------------------------------------------------ALLLTTPDNLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARSVLLD---IFTPDACLALLE 292
Cdd:cd17652 103 GSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATLVLAPaeeLLPGEPLADLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTCMLgATPFVydlLNVLEkqPADLSALRFFLCGGTTIPKKVAREcQQRGIKLLSVYGSTESSPHAVVNLDDPLSRf 372
Cdd:cd17652 182 EHRITHVT-LPPAA---LAALP--PDDLPDLRTLVVAGEACPAELVDR-WAPGRRMINAYGPTETTVCATMAGPLPGGG- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 373 MHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR-------ALDEEGWYYSGDLCRMDEAGYI 445
Cdd:cd17652 254 VPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfvadpfGAPGSRMYRTGDLARWRADGQL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 446 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlKAPHHSLSLEEVVAfFSRKRVAKYK 525
Cdd:cd17652 334 EFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV-PAPGAAPTAAELRA-HLAERLPGYM 411
|
490
....*....|....*....
gi 1489134476 526 YPEHIVVIEKLPRTTSGKI 544
Cdd:cd17652 412 VPAAFVVLDALPLTPNGKL 430
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
210-550 |
2.19e-42 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 160.01 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 210 AVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTWQ----DVFMMPAPLGHATGFLHGVTAPFLIGArSVLLDIFT 283
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRG------AYLMALSnaLIWGmnegAVYLWTLPMFHCNGWCFTWTLAALCGT-NICLRQVT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 284 PDACLALLEQQRCTCMLGAtPFVydlLNVLEKQPADLSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTES- 357
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAA-PVV---LNTIVNAPKSETILPLprvvhVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETy 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 358 SPHAVVNL--------DDPLSRFMHTDGYAAAGVE-IKVVDDarKTLPP-----GCEGEEASRGPNVFMGYFDEPELTAR 423
Cdd:PLN02479 348 GPSTVCAWkpewdslpPEEQARLNARQGVRYIGLEgLDVVDT--KTMKPvpadgKTMGEIVMRGNMVMKGYLKNPKANEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 424 ALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKA- 502
Cdd:PLN02479 426 AF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPg 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 503 --PHHSLSLEEVVAFFSRKRVAKYKYPEHiVVIEKLPRTTSGKIQKFLLR 550
Cdd:PLN02479 505 vdKSDEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVLR 553
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
69-483 |
4.51e-42 |
|
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: 158.02 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT 148
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 L--FKQTRPVdlilplqnqLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVML 226
Cdd:cd05932 87 LddWKAMAPG---------VPEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 227 THNNILASERAYCARLNLTWQDVFMMPAPLGHAT--------GFLHGVTAPFligARSvlLDIFTPDaclalLEQQRCTC 298
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTervfveggSLYGGVLVAF---AES--LDTFVED-----VQRARPTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 299 MLGA----TPF---VYD-----LLNVLEKQPA-------------DLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYG 353
Cdd:cd05932 228 FFSVprlwTKFqqgVQDkipqqKLNLLLKIPVvnslvkrkvlkglGLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 STESSPHAVVNLddPLSRFMHTDGYAAAGVEIKVVDDarktlppgceGEEASRGPNVFMGYFDEPELTARALDEEGWYYS 433
Cdd:cd05932 308 MTENFAYSHLNY--PGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLRT 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1489134476 434 GDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVV 483
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-544 |
6.91e-41 |
|
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: 150.63 E-value: 6.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 213 FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVLLDIFTPDACLALLE 292
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTCMLGATPFVYDLLNVLEKQpadlSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTESSpHAVVNLDDPlS 370
Cdd:cd17633 86 QYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNifPKANLIEFYGTSELS-FITYNFNQE-S 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 371 RFMHTDGYAAAGVEIKVVDDARktlppGCEGEEASRGPNVFMGYFDEPELTaraldEEGWYYSGDLCRMDEAGYIKITGR 450
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN-----PDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 451 KKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCA-YVVLKAPHHSLSLeevvafFSRKRVAKYKYPEH 529
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAlYSGDKLTYKQLKR------FLKQKLSRYEIPKK 303
|
330
....*....|....*
gi 1489134476 530 IVVIEKLPRTTSGKI 544
Cdd:cd17633 304 IIFVDSLPYTSSGKI 318
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-544 |
7.19e-41 |
|
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: 156.20 E-value: 7.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 53 RAMPDKIAVV---DNHGASYTYSALD-HAASC-LANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSW 127
Cdd:cd17634 64 RENGDRTAIIyegDDTSQSRTISYRElHREVCrFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 128 REAELVWVLNKCQAKMFF-APTLFKQTRPVDLILPLQNQLPQLQQIV---------GVDKLAPATSSLSLSQIIADNTSL 197
Cdd:cd17634 144 APEAVAGRIIDSSSRLLItADGGVRAGRSVPLKKNVDDALNPNVTSVehvivlkrtGSDIDWQEGRDLWWRDLIAKASPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 198 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNI---LASERAYCarLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGA 274
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYlvyAATTMKYV--FDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 275 RSVLLDIF----TPDACLALLEQQRCTcMLGATPFVYDLL-----NVLEKQpaDLSALRFFLCGGTTI-PKKVA---REC 341
Cdd:cd17634 302 TTLLYEGVpnwpTPARMWQVVDKHGVN-ILYTAPTAIRALmaagdDAIEGT--DRSSLRILGSVGEPInPEAYEwywKKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 342 QQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGE---EASRGPNVFMGYFDEP 418
Cdd:cd17634 379 GKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlviTDPWPGQTRTLFGDHE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTARALDE-EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAY 497
Cdd:cd17634 459 RFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAY 538
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 498 VVLKA---PHHSLSlEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17634 539 VVLNHgvePSPELY-AELRNWV-RKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
49-549 |
1.85e-40 |
|
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: 153.25 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 49 QQTARAMPDKIAVVdNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWR 128
Cdd:cd17655 4 EEQAEKTPDHTAVV-FEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELVWVLNKCQAKMFFAPTLFKQtrPVDLILPLQNQLPQLQQIVGVDKLAPATSSlslsqiiadntslttaitthgDEL 208
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQP--PIAFIGLIDLLDEDTIYHEESENLEPVSKS---------------------DDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTH----NNILASERAYcarlNLTWQDVFMMPAPLgHATGFLHGVTAPFLIGARSVLL---DI 281
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHrgvvNLVEWANKVI----YQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVrkeTV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 FTPDACLALLEQQRCTCMLGaTPFVYDLLNVLEKQPAdlSALRFFLCGGTTIPKKVAR---ECQQRGIKLLSVYGSTESS 358
Cdd:cd17655 215 LDGQALTQYIRQNRITIIDL-TPAHLKLLDAADDSEG--LSLKHLIVGGEALSTELAKkiiELFGTNPTITNAYGPTETT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PHAVVNLDDPLSRFMHTD--GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDE------EGW 430
Cdd:cd17655 292 VDASIYQYEPETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfvpgERM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhsLSLE 510
Cdd:cd17655 372 YRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE---LPVA 448
|
490 500 510
....*....|....*....|....*....|....*....
gi 1489134476 511 EVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLL 549
Cdd:cd17655 449 QLREFLARE-LPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
44-557 |
1.02e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 151.09 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 44 LADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESgDRIAFQLPGWCEFTVIYLACLKIGAVSVPL 123
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKEND-RVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 124 LPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvdlilplqnqlpqlqQIVGVDklAPATSSLSLSQIIADNTSLTTAITT 203
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIVTERYKLN------------------DLPDEE--GRVIEIDEWKRMIEKYLPTYAPIEN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATgFLHGVTAPFLIGARSVLLDIFT 283
Cdd:PRK07638 141 VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 284 PDACLALLEQQRCTCMLGatpfVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSphA 361
Cdd:PRK07638 220 PNQVLDKLETENISVMYT----VPTMLESLYKENRVIENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASELS--F 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 362 VVNLDDPLS-RFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELtARALDEEGWYYSGDLCRMD 440
Cdd:PRK07638 294 VTALVDEESeRRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL-ARELNADGWMTVRDVGYED 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 441 EAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVvlKAPHHSLSLEEvvafFSRKR 520
Cdd:PRK07638 373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKS----FCLQR 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 1489134476 521 VAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRL 557
Cdd:PRK07638 447 LSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-543 |
1.32e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 148.30 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNI---------------LASERAYCARLNLTwqDVFMMPA-PLGHATGFLHGVTApFLIGA 274
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgefTPSEDAHKAAAAAA--GTVMFPApPLMHGTGSWTAFGG-LLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 275 RSVLLDI-FTPDACLALLEQQRCTCMlgatPFVYD-----LLNVLEKQ-PADLSALRFFLCGGTTIPKKVARECQQR--G 345
Cdd:cd05924 85 TVVLPDDrFDPEEVWRTIEKHKVTSM----TIVGDamarpLIDALRDAgPYDLSSLFAISSGGALLSPEVKQGLLELvpN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 346 IKLLSVYGSTESS--PHAVVNLDDPLSRFmhtdgYAAAGVEIKVVDDARKTLPPGCEGEE--ASRGpNVFMGYFDEPELT 421
Cdd:cd05924 161 ITLVDAFGSSETGftGSGHSAGSGPETGP-----FTRANPDTVVLDDDGRVVPPGSGGVGwiARRG-HIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 422 ARALDEEG---WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:cd05924 235 AETFPEVDgvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1489134476 499 VLkAPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:cd05924 315 QL-REGAGVDLEELRE-HCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-559 |
1.25e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 152.42 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAE 131
Cdd:PRK12316 2013 AARAPEAIAVVFG-DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 LVWVLNKCQAKMFFAPTLFKQTRPVDlilplqnqlpqlqqiVGVDKLApatssLSLSQIIADNTSLTTAITTHGDELAAV 211
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQRHLLERLPLP---------------AGVARLP-----LDRDAEWADYPDTAPAVQLAGENLAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDV---FMMPAPLGHATGFLHgvtaPFLIGARSVLLD--IFTPDA 286
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCelqFMSFSFDGAHEQWFH----PLLNGARVLIRDdeLWDPEQ 2227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTcmLGATPFVY-DLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTEssphAVV 363
Cdd:PRK12316 2228 LYDEMERHGVT--ILDFPPVYlQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTE----AVV 2301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 364 nldDPLS-RFMHTDGYAAAGVEIKVVDDARKT---------LPPGCEGEEASRGPNVFMGYFDEPELTA-RALDE----- 427
Cdd:PRK12316 2302 ---TPLLwKCRPQDPCGAAYVPIGRALGNRRAyildadlnlLAPGMAGELYLGGEGLARGYLNRPGLTAeRFVPDpfsas 2378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 428 -EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMsDERLGERSCAYVVLKAPHHS 506
Cdd:PRK12316 2379 gERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAED 2457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 507 LSLEevVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQ 559
Cdd:PRK12316 2458 LLAE--LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ 2508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-546 |
1.57e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 152.42 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAE 131
Cdd:PRK12316 4561 ARMTPDAVAVVFD-EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 LVWVLNKCQAKMFFAPTLFKQTRPVdlilplqnqlpqlqqivgvdklAPATSSLSLSQI--IADNTSLTTAITTHGDELA 209
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPI----------------------PDGLASLALDRDedWEGFPAHDPAVRLHPDNLA 4697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 210 AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVLLD--IFTPDAC 287
Cdd:PRK12316 4698 YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF-DGSHEGLYHPLINGASVVIRDdsLWDPERL 4776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 288 LALLEQQRCTCMLGATPFVYDLLNVLEKQpADLSALRFFLCGGTTIPKKVAREC--QQRGIKLLSVYGSTE----SSPHA 361
Cdd:PRK12316 4777 YAEIHEHRVTVLVFPPVYLQQLAEHAERD-GEPPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTEttvtVLLWK 4855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 362 VVNLDDPLSRFMHTdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR-----ALDEEG--WYYSG 434
Cdd:PRK12316 4856 ARDGDACGAAYMPI-GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTG 4934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 435 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMsDERLGERSCAYVVLKAPHHSLSLEEVVA 514
Cdd:PRK12316 4935 DLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVVPQDPALADADEAQAE 5013
|
490 500 510
....*....|....*....|....*....|....*...
gi 1489134476 515 FFS------RKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK12316 5014 LRDelkaalRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
46-544 |
1.89e-38 |
|
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: 147.30 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLP 125
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 126 SWREAELVWVLNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttAITTHG 205
Cdd:cd05918 82 SHPLQRLQEILQDTGAKV--------------------------------------------------------VLTSSP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLnltwqdvfmmpaPLGHATGFLH------GVTapfligarsvLL 279
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRAL------------GLTSESRVLQfasytfDVS----------IL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 DIFTP---DACLALLEQQRC-----TCM-------LGATPFVYDLLnvlekQPADLSALRFFLCGGTTIPKKVARECQQR 344
Cdd:cd05918 164 EIFTTlaaGGCLCIPSEEDRlndlaGFInrlrvtwAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWADR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 gIKLLSVYGSTESSPHAVVNLDDPLSRFmHTDGYAAAGVeIKVVD--DARKTLPPGCEGEEASRGPNVFMGYFDEPELTA 422
Cdd:cd05918 239 -VRLINAYGPAECTIAATVSPVVPSTDP-RNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 423 RA-LDEEGW------------YYSGDLCRMDEAGYIKITGRKKDII-VRGgenisSR----EVEDILLQH-PKIHDACV- 482
Cdd:cd05918 316 AAfIEDPAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVkIRG-----QRvelgEIEHHLRQSlPGAKEVVVe 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 483 -VAMSDERLGERSCAYVVLKAPH------HSLSLEEVVAFFS---------RKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd05918 391 vVKPKDGSSSPQLVAFVVLDGSSsgsgdgDSLFLEPSDEFRAlvaelrsklRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
49-544 |
2.82e-38 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 146.81 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 49 QQTARAmPDKIAVVDnHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWR 128
Cdd:cd17644 8 EQVERT-PDAVAVVF-EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELVWVLNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaITTHGDEL 208
Cdd:cd17644 86 QERLTYILEDAQISV---------------------------------------------------------LLTQPENL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNNIlaseraycarLNLTW--QDVFMMPAPL--GHATGFLHGVTAP-----FLIGARSVL- 278
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSL----------VNLSHglIKEYGITSSDrvLQFASIAFDVAAEeiyvtLLSGATLVLr 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 --LDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADL-SALRFFLCGGTTI-PKKVA--RECQQRGIKLLSVY 352
Cdd:cd17644 179 peEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVqPELVRqwQKNVGNFIQLINVY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 353 GSTESSPHAVV-NLDDPLSRFMH--TDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL---- 425
Cdd:cd17644 259 GPTEATIAATVcRLTQLTERNITsvPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishp 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 ----DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLK 501
Cdd:cd17644 339 fnssESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPH 418
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1489134476 502 APhHSLSLEEVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17644 419 YE-ESPSTVELRQFLKAK-LPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
48-546 |
2.72e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 148.39 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 48 WQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSW 127
Cdd:PRK12467 518 IEAQARQHPERPALVFG-EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 128 REAELVWVLNKCQAKMFFA-PTLFKQT-RPVDLilplqnqlpqlqQIVGVDKLAPatsslSLSQIIADNTSLTTAitthG 205
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLLTqSHLLAQLpVPAGL------------RSLCLDEPAD-----LLCGYSGHNPEVALD----P 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGhATGFLHGVTAPFLIGARSVLLD---IF 282
Cdd:PRK12467 656 DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA-FDLGVTELFGALASGATLHLLPpdcAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTcMLGATPFVYDLLnVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPH 360
Cdd:PRK12467 735 DAEAFAALMADQGVT-VLKIVPSHLQAL-LQASRVALPRPQRALVCGGEALQVDLLARVRALgpGARLINHYGPTETTVG 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 AVVN--LDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR-------ALDEEGWY 431
Cdd:PRK12467 813 VSTYelSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAErfvpdpfGADGGRLY 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 432 YSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERlGERSCAYVVLKAP----HHSL 507
Cdd:PRK12467 893 RTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAVadgaEHQA 971
|
490 500 510
....*....|....*....|....*....|....*....
gi 1489134476 508 SLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK12467 972 TRDELKAQL-RQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
52-550 |
2.89e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.38 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAV-VDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREA 130
Cdd:PRK13390 7 AQIAPDRPAViVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 131 ELVWVLNKCQAKMFFAPTLFKQtrpvdlilplqnqlpqlqqiVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDEL-- 208
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDG--------------------LAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLte 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 ----AAVLFTSGTEGLPKGVM---------LTHNNILASERAYcarLNLTWQDVFMMPAPLGHAT-----GFLHGvtapf 270
Cdd:PRK13390 147 qpcgAVMLYSSGTTGFPKGIQpdlpgrdvdAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHA----- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 271 lIGARSVLLDIFTPDACLALLEQQRCTC-MLGATPFVYDL-LNVLEKQPADLSALRFFLCGGTTIPKKVARE-CQQRGIK 347
Cdd:PRK13390 219 -LGGTVVLAKRFDAQATLGHVERYRITVtQMVPTMFVRLLkLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAmIDWLGPI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 348 LLSVYGSTESspHAVVNLDDPlsRFMHTDGYAAAGV--EIKVVDDARKTLPPGCEGE---EASRGPnvfMGYFDEPELTA 422
Cdd:PRK13390 298 VYEYYSSTEA--HGMTFIDSP--DWLAHPGSVGRSVlgDLHICDDDGNELPAGRIGTvyfERDRLP---FRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 423 RALDEEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVL 500
Cdd:PRK13390 371 AAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 501 KA---PHHSLSLEEVVafFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK13390 451 VEgirGSDELARELID--YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
42-527 |
6.15e-37 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 142.70 E-value: 6.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADY-WQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAfqLPGWCEFTVI--YLACLKIGA 118
Cdd:PRK09029 2 MIFSDWpWRHWAQVRPQAIALRLN-DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVA--LRGKNSPETLlaYLALLQCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 119 VSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvdlilplqnqlpqlqqivgvdklAPATSSLSLSQIIAdntslT 198
Cdd:PRK09029 79 RVLPLNPQLPQPLLEELLPSLTLDFALVLEGENT--------------------------FSALTSLHLQLVEG-----A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGflHGVTAPFLI-GARSV 277
Cdd:PRK09029 128 HAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG--QGIVWRWLYaGATLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 278 LLDIFTPDACLalleqQRCT-CMLGATPfvydlLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTE 356
Cdd:PRK09029 206 VRDKQPLEQAL-----AGCThASLVPTQ-----LWRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 --SSPHAVVNldDPLSrfmhTDGYAAAGVEIKVVDDarktlppgcegEEASRGPNVFMGYFDEPELTArALDEEGWYYSG 434
Cdd:PRK09029 276 maSTVCAKRA--DGLA----GVGSPLPGREVKLVDG-----------EIWLRGASLALGYWRQGQLVP-LVNDEGWFATR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 435 DLCRMDEaGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLkaphHSLSLEEVVA 514
Cdd:PRK09029 338 DRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES----DSEAAVVNLA 412
|
490
....*....|...
gi 1489134476 515 FFSRKRVAKYKYP 527
Cdd:PRK09029 413 EWLQDKLARFQQP 425
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
52-549 |
3.30e-36 |
|
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: 140.53 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNHGaSYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAE 131
Cdd:cd12115 9 AARTPDAIALVCGDE-SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 LVWVLNKCQAKmffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttAITTHGDELAAV 211
Cdd:cd12115 88 LRFILEDAQAR---------------------------------------------------------LVLTDPDDLAYV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNN-------------------ILASErAYCARLNltwqdVFMMPAPLghATG----FLHGVTA 268
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNaaaflqwaaaafsaeelagVLAST-SICFDLS-----VFELFGPL--ATGgkvvLADNVLA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 269 PFLIGARSVLLDIFT-PDACLALLEQqrctcmlgatpfvydllnvlEKQPADLSALRFflcGGTTIPKKVARECQQR--G 345
Cdd:cd12115 183 LPDLPAAAEVTLINTvPSAAAELLRH--------------------DALPASVRVVNL---AGEPLPRDLVQRLYARlqV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 346 IKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA--- 422
Cdd:cd12115 240 ERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAerf 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 423 ---RALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVV 499
Cdd:cd12115 320 lpdPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 500 LKAPHHSLsLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLL 549
Cdd:cd12115 400 AEPGAAGL-VEDLRRHL-GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-551 |
9.23e-36 |
|
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: 140.26 E-value: 9.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 96 IAFQLPGWCEftvIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvdlilplqnqlpqlqqivgv 175
Cdd:cd05915 55 LGFNHFRHLE---AYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNL------------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 176 dkLAPATSSLSLSQIIADNTSLTTAITTHGDELA------------------AVLFTSGTEGLPKGVMLTHNNILASERA 237
Cdd:cd05915 107 --LPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEealgeeadpvrvperaacGMAYTTGTTGLPKGVVYSHRALVLHSLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 238 YCARLNLTWQD--VFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEK 315
Cdd:cd05915 185 ASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 316 QPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNL---------DDPLSRFMHTDGYAAAGVEIK 386
Cdd:cd05915 265 TGHRLKTLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQNFvkshleslsEEEKLTLKAKTGLPIPLVRLR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 387 VVDDARKTLPPgcEGEE----ASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENI 462
Cdd:cd05915 345 VADEEGRPVPK--DGKAlgevQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 463 SSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHhsLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSG 542
Cdd:cd05915 423 SSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEK--PTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAG 500
|
....*....
gi 1489134476 543 KIQKFLLRK 551
Cdd:cd05915 501 KFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-546 |
1.06e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 143.56 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDKIAVVdnHGA-SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK12316 511 RGVHRLFEEQVERTPEAPALA--FGEeTLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDlilplqnqlpqlqqiVGVDKLAPATSSLSLSQIIADNTSltta 200
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLA---------------AGVQVLDLDRPAAWLEGYSEENPG---- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 201 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAP----LGHATGFLhgvtaPFLIGARS 276
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPfsfdVSVWEFFW-----PLMSGARL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 277 VLL---DIFTPDACLALLEQQRCTCMlgatPFVYDLLNVL--EKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLL 349
Cdd:PRK12316 725 VVAapgDHRDPAKLVELINREGVDTL----HFVPSMLQAFlqDEDVASCTSLRRIVCSGEALPADAQEQVFAKlpQAGLY 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 350 SVYGSTEssphAVVNLDDPLSRFMHTD----GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL 425
Cdd:PRK12316 801 NLYGPTE----AAIDVTHWTCVEEGGDsvpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 ------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLgersCAYVV 499
Cdd:PRK12316 877 vpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL----VGYVV 952
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1489134476 500 LKAPhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK12316 953 LESE--GGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-553 |
2.03e-35 |
|
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: 139.16 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL----LDI 281
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmptrLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 FTPDACLALLEQQRCT---CMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARE----CQQRGIK---LLSV 351
Cdd:cd05908 186 RRPILWLKKASEHKATivsSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEfldhMSKYGLKrnaILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 352 YGSTESS-----------------PHAVVNLDDPLSRFMHTD---------GYAAAGVEIKVVDDARKTLPPGCEGEEAS 405
Cdd:cd05908 266 YGLAEASvgaslpkaqspfktitlGRRHVTHGEPEPEVDKKDsecltfvevGKPIDETDIRICDEDNKILPDGYIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 406 RGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 485
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAC 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 486 ---SDERLGERSCAYVVlkaphHSLSLEEVVAFfsRKRVAKYKYP------EHIVVIEKLPRTTSGKIQKFLLRKDI 553
Cdd:cd05908 425 gvnNSNTRNEEIFCFIE-----HRKSEDDFYPL--GKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
213-557 |
3.24e-35 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 139.77 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 213 FTSGTEGLPKGVMLTHNNilaserAYCARLNLT--WQ----DVFMMPAPLGHATGFLH--GVTAPfliGARSVLLDIFTP 284
Cdd:PLN03102 193 YTSGTTADPKGVVISHRG------AYLSTLSAIigWEmgtcPVYLWTLPMFHCNGWTFtwGTAAR---GGTSVCMRHVTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 DACLALLEQQRCTCMlGATPFVYDLLnvLEKQPADLSALR---FFLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PH 360
Cdd:PLN03102 264 PEIYKNIEMHNVTHM-CCVPTVFNIL--LKGNSLDLSPRSgpvHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 AVVNLDDPLSRF---MHTDGYAAAGVEIKVVDD-------ARKTLPPGCE--GEEASRGPNVFMGYFDEPELTARALdEE 428
Cdd:PLN03102 341 LFCEWQDEWNRLpenQQMELKARQGVSILGLADvdvknkeTQESVPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAF-KH 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 429 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLS 508
Cdd:PLN03102 420 GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKE 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 509 LEEV--------VAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRkDIMRRL 557
Cdd:PLN03102 500 DRVDklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR-DIAKGL 555
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
52-544 |
2.88e-34 |
|
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: 134.74 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAE 131
Cdd:cd17653 7 AAAHPDAVAVESL-GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 132 LVWVLNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqIIADNTslttaitthGDELAAV 211
Cdd:cd17653 86 IQAILRTSGATL----------------------------------------------LLTTDS---------PDDLAYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-------------WQDVFMMPAPLGH-ATGFLHGVTAPFLIGARSV 277
Cdd:cd17653 111 IFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGpgsrvaqvlsiafDACIGEIFSTLCNgGTLVLADPSDPFAHVARTV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 278 llDIFTpdaclalleqqrctcmlgATPfvyDLLNVLEkqPADLSALRFFLCGGTTIPKKVARECQQrGIKLLSVYGSTE- 356
Cdd:cd17653 191 --DALM------------------STP---SILSTLS--PQDFPNLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTEc 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 --SSPHAVVNLDDPLsrfmhTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL----DEEGW 430
Cdd:cd17653 245 tiSSTMTELLPGQPV-----TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 --YYSGDLCRMDEAGYIKITGRKKDII-VRG-----GEnissrEVEDILLQHPKIHDACVVaMSDERLgersCAYVvlkA 502
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVkVRGfrinlEE-----IEEVVLQSQPEVTQAAAI-VVNGRL----VAFV---T 386
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1489134476 503 PhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17653 387 P--ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
46-551 |
4.03e-34 |
|
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: 136.68 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTARamPDKIAV-----VDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:cd05967 57 DRHVEAGR--GDQIALiydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMFFA--------------PTLFK-----QTRPVDLILPLQNQLPQLQQIVGVDklapa 181
Cdd:cd05967 135 SVVFGGFAAKELASRIDDAKPKLIVTascgiepgkvvpykPLLDKalelsGHKPHHVLVLNRPQVPADLTKPGRD----- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 182 tssLSLSQIIADNTSLTTAITTHGDELAaVLFTSGTEGLPKGVMLTHNnilaserAYCARLNLTWQ--------DVFMMP 253
Cdd:cd05967 210 ---LDWSELLAKAEPVDCVPVAATDPLY-ILYTSGTTGKPKGVVRDNG-------GHAVALNWSMRniygikpgDVWWAA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 254 APLGHATGFLHGVTAPFLIGARSVLLD---IFTPD--ACLALLEQQRCTCMLGA-TPFvydllNVLEKQPA--------D 319
Cdd:cd05967 279 SDVGWVVGHSYIVYGPLLHGATTVLYEgkpVGTPDpgAFWRVIEKYQVNALFTApTAI-----RAIRKEDPdgkyikkyD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 320 LSALR-FFLCGGTTIPKKVARECQQRGIKLLSVYGSTES------SPHAVVNLDDPLSrfmhTDGYAAAGVEIKVVDDAR 392
Cdd:cd05967 354 LSSLRtLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgwpitaNPVGLEPLPIKAG----SPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 393 KTLPPGCEGEEASRGP---NVFMGYFDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREV 467
Cdd:cd05967 430 EPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 468 EDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLE----EVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:cd05967 510 EESVLSHPAVAECAVVGVRDELKGQVPLGLVVLK-EGVKITAEelekELVALV-REQIGPVAAFRLVIFVKRLPKTRSGK 587
|
....*...
gi 1489134476 544 IQKFLLRK 551
Cdd:cd05967 588 ILRRTLRK 595
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
206-559 |
5.00e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 132.48 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAplGHATGF---LHGVTApfliGARSVLLDI- 281
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLALPA--HHIAGLqvlVRSVIA----GSEPVELDVs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 --FTPDA---CLALLEQQRCTCMLGATpfvyDLLNVLEkQPADLSALRFF---LCGGTTIPKKVARECQQRGIKLLSVYG 353
Cdd:PRK07824 109 agFDPTAlprAVAELGGGRRYTSLVPM----QLAKALD-DPAATAALAELdavLVGGGPAPAPVLDAAAAAGINVVRTYG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 STESSPHAVVnlddplsrfmhtDGYAAAGVEIKVvDDARKTLPpgcegeeasrGPNVFMGYFDEPELTARAldEEGWYYS 433
Cdd:PRK07824 184 MSETSGGCVY------------DGVPLDGVRVRV-EDGRIALG----------GPTLAKGYRNPVDPDPFA--EPGWFRT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 434 GDLCRMDEaGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAyVVLKAPHHSLSLEEVV 513
Cdd:PRK07824 239 DDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA-AVVGDGGPAPTLEALR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1489134476 514 AFFSRkRVAKYKYPEHIVVIEKLPRTTSGKIQkfllRKDIMRRLTQ 559
Cdd:PRK07824 317 AHVAR-TLDRTAAPRELHVVDELPRRGIGKVD----RRALVRRFAG 357
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
11-544 |
5.34e-34 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 137.79 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 11 DVLFRESNMKVTLtFNEQRRAAYRQQglwgdasladywqqtaramPDKIAVVDNHGASYTYSALDHAASCLANwMLAKGI 90
Cdd:PRK06814 621 DMMFETSDYDRTL-FEALIEAAKIHG-------------------FKKLAVEDPVNGPLTYRKLLTGAFVLGR-KLKKNT 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 91 ESGDRIAFQLPGWCEFTVIYLACLKIGavSVPLLPSWrEAELVWVLNKCQA---KMFFAPTLF-KQTRPVDLILPLQNQL 166
Cdd:PRK06814 680 PPGENVGVMLPNANGAAVTFFALQSAG--RVPAMINF-SAGIANILSACKAaqvKTVLTSRAFiEKARLGPLIEALEFGI 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 167 PqlqqIVGVDKL-APATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT 245
Cdd:PRK06814 757 R----IIYLEDVrAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFS 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 246 WQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL----LDI-FTPDaclaLLEQQRCTCMLGATPFvydlLNVLEK--QPA 318
Cdd:PRK06814 833 PEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLypspLHYrIIPE----LIYDTNATILFGTDTF----LNGYARyaHPY 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 319 DLSALRFFLCGGttipKKVARECQQR-----GIKLLSVYGSTESSPhaVVNLDDPlsrfMH----TDGYAAAGVEIKVVD 389
Cdd:PRK06814 905 DFRSLRYVFAGA----EKVKEETRQTwmekfGIRILEGYGVTETAP--VIALNTP----MHnkagTVGRLLPGIEYRLEP 974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 390 darktlPPGCE--GEEASRGPNVFMGYFD-------EPEltaraldEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 460
Cdd:PRK06814 975 ------VPGIDegGRLFVRGPNVMLGYLRaenpgvlEPP-------ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGE 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 461 NISSREVEDILLQHPKIHDACVVAMSDERLGERscayVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTT 540
Cdd:PRK06814 1042 MISLAAVEELAAELWPDALHAAVSIPDARKGER----IILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLG 1117
|
....
gi 1489134476 541 SGKI 544
Cdd:PRK06814 1118 TGKI 1121
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
41-546 |
3.67e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.06 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFG-DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAY 3172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVdlilplqnqlPQLQQIVGVDKLAPATSSLSlsqiiadntslTTA 200
Cdd:PRK12467 3173 VPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPA----------PAGDTALTLDRLDLNGYSEN-----------NPS 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 201 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGARSVLLD 280
Cdd:PRK12467 3232 TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSF-DGAQERFLWTLICGGCLVVRD 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 --IFTPDACLALLEQQRCTCMLGATPFVYDLLNvlEKQPADLSALRFFLCGGTTIP----KKVARECQQRGikLLSVYGS 354
Cdd:PRK12467 3311 ndLWDPEELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASLDIYVFGGEAVPpaafEQVKRKLKPRG--LTNGYGP 3386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 355 TESSphavvnlDDPLSRFMHTD----------GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA-R 423
Cdd:PRK12467 3387 TEAV-------VTVTLWKCGGDavceapyapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAeR 3459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 424 ALDE------EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMsDERLGERSCA 496
Cdd:PRK12467 3460 FVADpfsgsgGRLYRTGDLARYRADGVIEYLGRiDHQVKIRGFR-IELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVA 3537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 497 YVVLKAPhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK12467 3538 YVVPADP--QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
182-550 |
4.94e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 132.84 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 182 TSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATG 261
Cdd:PRK13388 126 VDTPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 262 FLHGVtAPFLI-GARSVLLDIFTPDACLAllEQQRctcmLGATPFVY------DLLNVLEK-QPADLSALRFFlcGGTTI 333
Cdd:PRK13388 206 VMAGW-APAVAsGAAVALPAKFSASGFLD--DVRR----YGATYFNYvgkplaYILATPERpDDADNPLRVAF--GNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 334 PKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFmhtdGYAAAGVEIkvVD-DARKTLPPG--------CEGEEA 404
Cdd:PRK13388 277 PRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSI----GRGAPGVAI--YNpETLTECAVArfdahgalLNADEA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 405 ------SRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH 478
Cdd:PRK13388 351 igelvnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAIN 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 479 DACVVAMSDERLGERSCAYVVLKAPhHSLSLEEVVAFFSRKRVAKYK-YPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK13388 430 RVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLAAQPDLGTKaWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-552 |
1.10e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 134.31 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 31 AAYRQQGL--WGDASlADY---------WQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQ 99
Cdd:PRK12316 3036 AEERGQLLeaWNATA-AEYplergvhrlFEEQVERTPDAVALAFG-EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVA 3113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 100 LPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTrpvdlilplqnqlpqlqqivgvdkLA 179
Cdd:PRK12316 3114 VERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLP------------------------LA 3169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 180 PATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHa 259
Cdd:PRK12316 3170 QGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSF- 3248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 260 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcMLGATPFVYDLLNVL--EKQPADLSALRFFLCGGTTIPKKV 337
Cdd:PRK12316 3249 DVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSE-GVDVLHAYPSMLQAFleEEDAHRCTSLKRIVCGGEALPADL 3327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 338 ARECQQrGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDE 417
Cdd:PRK12316 3328 QQQVFA-GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNR 3406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 418 PELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLg 491
Cdd:PRK12316 3407 PGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQL- 3485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 492 ersCAYVVLKAPhhSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI-QKFLLRKD 552
Cdd:PRK12316 3486 ---VAYVVPEDE--AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLdRKALPRPD 3542
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
206-546 |
2.54e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 130.89 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ-DVFMMPAPLGHATGFLHGVTAPFLIGARSVLLdifTP 284
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV---TP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 DACLA-------LLEQQRCTcMLGATPFVYDLL-NVLEKQPA----DLSALRFFLCGGTTI-PKKVARECQQ------RG 345
Cdd:PRK07768 229 MDFLRdpllwaeLISKYRGT-MTAAPNFAYALLaRRLRRQAKpgafDLSSLRFALNGAEPIdPADVEDLLDAgarfglRP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 346 IKLLSVYGSTES------SP------------------HAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEG 401
Cdd:PRK07768 308 EAILPAYGMAEAtlavsfSPcgaglvvdevdadllaalRRAVPATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 402 EEASRGPNVFMGYfDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAC 481
Cdd:PRK07768 388 VIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGN 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 482 VVAMSDERLGERSCAYVVLKAPHHSlSLEEVVAFfsRKRVAKYKY------PEHIVVIEK--LPRTTSGKIQK 546
Cdd:PRK07768 467 AVAVRLDAGHSREGFAVAVESNAFE-DPAEVRRI--RHQVAHEVVaevgvrPRNVVVLGPgsIPKTPSGKLRR 536
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
56-544 |
2.86e-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: 129.12 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd17650 1 PDAIAVSDAT-RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaITTHGDELAAVLFTS 215
Cdd:cd17650 80 LEDSGAKL---------------------------------------------------------LLTQPEDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 216 GTEGLPKGVMLTHNNIlaseraycARLNLTWQDVFMMPAplghatgflhgvTAPFLIGARSVLLDIFTPDACLALL---- 291
Cdd:cd17650 103 GTTGKPKGVMVEHRNV--------AHAAHAWRREYELDS------------FPVRLLQMASFSFDVFAGDFARSLLnggt 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 292 ----------EQQRCT--------CMLGATP-FVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR---GIKLL 349
Cdd:cd17650 163 lvicpdevklDPAALYdlilksriTLMESTPaLIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARfgqGMRII 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 350 SVYGSTESSPHAVV--NLDDPLSRFMHTD-GYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALD 426
Cdd:cd17650 243 NSYGVTEATIDSTYyeEGRDPLGDSANVPiGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 427 E------EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVl 500
Cdd:cd17650 323 EnpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV- 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1489134476 501 kaPHHSLSLEEVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17650 402 --AAATLNTAELRAFLA-KELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
43-550 |
2.91e-32 |
|
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: 131.46 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTAramPDKIAVV----DNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGA 118
Cdd:cd05968 65 QLLDKWLADT---RTRPALRwegeDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 119 VSVPLLPSWREAELVWVLNKCQAKMFFAPTLF-KQTRPVDLILPLQNQLPQLQqivGVDKLA---------PATSSLSLS 188
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFtRRGREVNLKEEADKACAQCP---TVEKVVvvrhlgndfTPAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 189 QIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNI---LASERAYCarLNLTWQDVFMMPAPLGHATGflhg 265
Cdd:cd05968 219 YDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQ--FDLKPGDLLTWFTDLGWMMG---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 266 vtaPFLI------GARSVLLDIF----TPDACLALLEQQRCTcMLGATPFVYDLLNVLEKQPA---DLSALRFFLCGGTT 332
Cdd:cd05968 293 ---PWLIfgglilGATMVLYDGApdhpKADRLWRMVEDHEIT-HLGLSPTLIRALKPRGDAPVnahDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 333 IPKKVAREC-QQRGIK---LLSVYGSTESSPHAVVNLddpLSRFMHTDGYAAA--GVEIKVVDDARKTLPPGcEGEEASR 406
Cdd:cd05968 369 WNPEPWNWLfETVGKGrnpIINYSGGTEISGGILGNV---LIKPIKPSSFNGPvpGMKADVLDESGKPARPE-VGELVLL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 407 GPNVFM--GYFDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHD 479
Cdd:cd05968 445 APWPGMtrGFWRDED---RYLETywsrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 480 ACVVAMSDERLGERSCAYVVLKaPHHSLS--LEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLK-PGVTPTeaLAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
206-551 |
3.14e-32 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 131.76 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR-----SVLLD 280
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEvflypSPLHY 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 281 IFTPDaclaLLEQQRCTCMLGATPFvydLLNVLE-KQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESS 358
Cdd:PRK08043 445 RIVPE----LVYDRNCTVLFGTSTF---LGNYARfANPYDFARLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGVTECA 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PhaVVNLDDPLSRFMHTDGYAAAGVeikvvdDARKTLPPGCE--GEEASRGPNVFMGYF--DEP-ELTARALD------E 427
Cdd:PRK08043 518 P--VVSINVPMAAKPGTVGRILPGM------DARLLSVPGIEqgGRLQLKGPNIMNGYLrvEKPgVLEVPTAEnargemE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 428 EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQ--HPKIHDAcvVAMSDERLGERscayVVLKAPHH 505
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvsPDKQHAT--AIKSDASKGEA----LVLFTTDS 663
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1489134476 506 SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK08043 664 ELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
41-478 |
3.46e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 130.40 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNHG------ASY---TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYL 111
Cdd:PRK09274 5 MANIARHLPRAAQERPDQLAVAVPGGrgadgkLAYdelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 112 ACLKIGAVSVPLLPSWReaelVWVLNKCqakmffaptlFKQTRP-----------VDLILPLQNQLPQLQQIVGVDKLAP 180
Cdd:PRK09274 85 ALFKAGAVPVLVDPGMG----IKNLKQC----------LAEAQPdafigipkahlARRLFGWGKPSVRRLVTVGGRLLWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 181 ATSslsLSQIIAD--NTSLTTAITTHgDELAAVLFTSGTEGLPKGVMLTHNNILASERAycarlnltwqdvfmmpapLGH 258
Cdd:PRK09274 151 GTT---LATLLRDgaAAPFPMADLAP-DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA------------------LRE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 259 ATGFLHG----VTAPFL------IGARSVLLDI-FT------PDACLALLEQQRCTCMLGAtPfvyDLLNVL----EKQP 317
Cdd:PRK09274 209 DYGIEPGeidlPTFPLFalfgpaLGMTSVIPDMdPTrpatvdPAKLFAAIERYGVTNLFGS-P---ALLERLgrygEANG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 318 ADLSALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTESSPHAVVNLDDPLSRFM-HTD-------GYAAAGVEIK 386
Cdd:PRK09274 285 IKLPSLRRVISAGAPVPIAVIERFRAmlpPDAEILTPYGATEALPISSIESREILFATRaATDngagicvGRPVDGVEVR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 387 VV----------DDARKtLPPGCEGEEASRGPNVFMGYFDEPELTARA--LDEEG--WYYSGDLCRMDEAGYIKITGRKK 452
Cdd:PRK09274 365 IIaisdapipewDDALR-LATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKA 443
|
490 500
....*....|....*....|....*.
gi 1489134476 453 DIIVRGGENISSREVEDILLQHPKIH 478
Cdd:PRK09274 444 HRVETAGGTLYTIPCERIFNTHPGVK 469
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
48-546 |
1.29e-31 |
|
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: 127.29 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 48 WQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSW 127
Cdd:cd17645 4 FEEQVERTPDHVAVVDR-GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 128 REAELVWVLNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaITTHGDE 207
Cdd:cd17645 83 PGERIAYMLADSSAKI---------------------------------------------------------LLTNPDD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 208 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHaTGFLHGVTAPFLIGA------RSVLLDI 281
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAalhvvpSERRLDL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 ftpDACLALLEQQRCTCMLGATPFVYDLLNVlekqpaDLSALRFFLCGGTTIPKKVarecqQRGIKLLSVYGSTESSPHA 361
Cdd:cd17645 185 ---DALNDYFNQEGITISFLPTGAAEQFMQL------DNQSLRVLLTGGDKLKKIE-----RKGYKLVNNYGPTENTVVA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 362 VVNLDDPLSRFMHTdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA------LDEEGWYYSGD 435
Cdd:cd17645 251 TSFEIDKPYANIPI-GKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 436 LCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlkaPHHSLSLEEVVAF 515
Cdd:cd17645 330 LAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT---APEEIPHEELREW 406
|
490 500 510
....*....|....*....|....*....|.
gi 1489134476 516 FsRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17645 407 L-KNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
20-560 |
1.41e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.05 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 20 KVTLTFNEQRRAAYRQqglWgDASLADY---------WQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGI 90
Cdd:PRK12467 1547 ELDLLDEAERRQILEG---W-NATHTGYplarlvhqlIEDQAAATPEAVALVFG-EQELTYGELNRRANRLAHRLIALGV 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 91 ESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVdlilplqnqlpqlq 170
Cdd:PRK12467 1622 GPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPL-------------- 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 171 qivgVDKLapatSSLSLSQIIA--DNTSLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ 247
Cdd:PRK12467 1688 ----PDGL----RSLVLDQEDDwlEGYSDSNpAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA 1759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 248 DVFMMPAPL---GHATGFLHgvtaPFLIGARSVLLDIFT---PDACLALLEQQRCTcMLGATPFVYDLLNVLEKQPADLS 321
Cdd:PRK12467 1760 DVVLQFTSFafdVSVWELFW----PLINGARLVIAPPGAhrdPEQLIQLIERQQVT-TLHFVPSMLQQLLQMDEQVEHPL 1834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 322 ALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAV---VNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLP 396
Cdd:PRK12467 1835 SLRRVVCGGEALEVEALRPWLERlpDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVP 1914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 397 PGCEGEEASRGPNVFMGYFDEPELTAR-------ALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVED 469
Cdd:PRK12467 1915 IGVAGELYLGGVGLARGYLNRPALTAErfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA 1994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 470 ILLQHPKIHDACVVAMsDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVA------KYKYPEHIVVIEKLPRTTSGK 543
Cdd:PRK12467 1995 RLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQVALRAILKNHlkaslpEYMVPAHLVFLARMPLTPNGK 2073
|
570
....*....|....*..
gi 1489134476 544 IQKFLLRKDIMRRLTQD 560
Cdd:PRK12467 2074 LDRKALPAPDASELQQA 2090
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
43-552 |
2.03e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 128.84 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVP 122
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFE-DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 123 LLPSWREAELVWVLNKCQAKMF-----FAPTlFKQTRPVDLILPLQNQLPQLQQI--VGVDKLAPATSSLSlsqiiADNT 195
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLivgeeLVEA-FEEARADLARPPRLWVAGGDTLDdpEGYEDLAAAAAGAP-----TTNP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 196 SLTTAITthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 275
Cdd:PRK08279 191 ASRSGVT--AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGAT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 276 SVLLDIFT-----PDAclallEQQRCTCmlgatpFVY--DLLNVLEKQPADLS----ALRffLCGGTTIPKKVARECQQR 344
Cdd:PRK08279 269 LALRRKFSasrfwDDV-----RRYRATA------FQYigELCRYLLNQPPKPTdrdhRLR--LMIGNGLRPDIWDEFQQR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 345 -GI-KLLSVYGSTES----------------------SPHAVVNLD----DPLsRfmHTDGYAaagveIKVvddarktlP 396
Cdd:PRK08279 336 fGIpRILEFYAASEGnvgfinvfnfdgtvgrvplwlaHPYAIVKYDvdtgEPV-R--DADGRC-----IKV--------K 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 397 PG----CEGEEASRGPnvFMGYFDePELTARAL--D--EEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSRE 466
Cdd:PRK08279 400 PGevglLIGRITDRGP--FDGYTD-PEASEKKIlrDvfKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 467 VEDILLQHPKIHDACV----VAMSDERLGersCAYVVLkAPHHSLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSG 542
Cdd:PRK08279 477 VENALSGFPGVEEAVVygveVPGTDGRAG---MAAIVL-ADGAEFDLAALAAHL-YERLPAYAVPLFVRLVPELETTGTF 551
|
570
....*....|
gi 1489134476 543 KIQKFLLRKD 552
Cdd:PRK08279 552 KYRKVDLRKE 561
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
199-552 |
7.47e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 126.33 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 278
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIAL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 LDIFTPDACLALLEQqrctcmLGATPFVY---DLLNVL--EKQPADLS-ALRFfLCGGTTIPKKVARECQQRGIKLLSVY 352
Cdd:PRK07867 225 RRKFSASGFLPDVRR------YGATYANYvgkPLSYVLatPERPDDADnPLRI-VYGNEGAPGDIARFARRFGCVVVDGF 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 353 GSTESSPhAVVNLDDPLSRFMhtdGYAAAGVEIkvVD-DARKTLPPG-------CEGEEA------SRGPNVFMGYFDEP 418
Cdd:PRK07867 298 GSTEGGV-AITRTPDTPPGAL---GPLPPGVAI--VDpDTGTECPPAedadgrlLNADEAigelvnTAGPGGFEGYYNDP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PRK07867 372 EADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAAL 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 499 VLkAPHHSLSLEEVVAFF-SRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:PRK07867 451 VL-APGAKFDPDAFAEFLaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
56-544 |
9.17e-31 |
|
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: 124.82 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHgASYTYSALDHAASCLANWMLAKG-IESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVW 134
Cdd:cd17648 1 PDRVAVVYGD-KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 135 VLNKCQAKMffaptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqIIADNTslttaitthgdELAAVLFT 214
Cdd:cd17648 80 ILEDTGARV----------------------------------------------VITNST-----------DLAYAIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 215 SGTEGLPKGVMLTHNNILASERAYCARlnltwqdvFMMPAPLGHATGFLHG-VTAPF-------LIGARSVLL----DIF 282
Cdd:cd17648 103 SGTTGKPKGVLVEHGSVVNLRTSLSER--------YFGRDNGDEAVLFFSNyVFDFFveqmtlaLLNGQKLVVppdeMRF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTcMLGATPFV---YDLlnvlekqpADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESS 358
Cdd:cd17648 175 DPDRFYAYINREKVT-YLSGTPSVlqqYDL--------ARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 359 PHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTA-------------RAL 425
Cdd:cd17648 246 VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAerflpnpfqteqeRAR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 DEEG-WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDE-RLGERSCAYVV---L 500
Cdd:cd17648 326 GRNArLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLVgyyL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1489134476 501 KAPHHsLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:cd17648 406 PEPGH-VPESDLLSFL-RAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
206-474 |
1.54e-30 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 125.70 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL-LDIFTP 284
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFaYNPLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 DACLALLEQQRCTcMLGATPFVYD-LLNVLEKQPADLSALRFFLCGGTTIPKKVARECQ--QRGIKLLSVYGSTESSPHA 361
Cdd:PRK06334 263 KKIVEMIDEAKVT-FLGSTPVFFDyILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALktFPHIQLRQGYGTTECSPVI 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 362 VVNLDDPlSRFMHTDGYAAAGVEIKVVDDARKT-LPPGCEGEEASRGPNVFMGYFDE-PELTARALDEEGWYYSGDLCRM 439
Cdd:PRK06334 342 TINTVNS-PKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWYVTGDLGYV 420
|
250 260 270
....*....|....*....|....*....|....*
gi 1489134476 440 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQH 474
Cdd:PRK06334 421 DRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
31-546 |
1.72e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 127.59 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 31 AAYRQQGLWGDAS-------LADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGW 103
Cdd:PRK05691 1113 AERAQLAQWGQAPcapaqawLPELLNEQARQTPERIALVWD-GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERS 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 104 CEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMffaptLFKQTRPVDLILPlqnqlpqlqqivgvdklAPATS 183
Cdd:PRK05691 1192 PQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVEL-----LLTQSHLLERLPQ-----------------AEGVS 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 184 SLSLSQIIADN-TSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATG- 261
Cdd:PRK05691 1250 AIALDSLHLDSwPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSv 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 262 ---FLhgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCMlgatPFVYDLLNVLEKQP--ADLSALRFFLCGGTTI 333
Cdd:PRK05691 1330 wecFW-----PLITGCRLVLAgpgEHRDPQRIAELVQQYGVTTL----HFVPPLLQLFIDEPlaAACTSLRRLFSGGEAL 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 334 PKKVARECQQR--GIKLLSVYGSTESS---PHAVVNLDD----PLSRFMhtdgyaaAGVEIKVVDDARKTLPPGCEGEEA 404
Cdd:PRK05691 1401 PAELRNRVLQRlpQVQLHNRYGPTETAinvTHWQCQAEDgersPIGRPL-------GNVLCRVLDAELNLLPPGVAGELC 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 405 SRGPNVFMGYFDEPELTAR-----ALDEEG--WYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPK 476
Cdd:PRK05691 1474 IGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRlDQQVKLRGFR-VEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 477 IHDAcVVAMSDERLGERSCAYVVLKAPH--HSLSLEEVVAffsrKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK05691 1553 VAQA-AVLVREGAAGAQLVGYYTGEAGQeaEAERLKAALA----AELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
199-488 |
2.77e-30 |
|
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: 124.25 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 199 TAITTHG--DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN--LTWQDVFMMPAPLGH-------ATGFLHGVT 267
Cdd:cd17639 79 SAIFTDGkpDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHifelaaeNVCLYRGGT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 268 apflIGARSVLldIFTPDA---CLALLEQQRCTCMLGaTPFVYDLL--NVLEKQP---------------ADLSA----- 322
Cdd:cd17639 159 ----IGYGSPR--TLTDKSkrgCKGDLTEFKPTLMVG-VPAIWDTIrkGVLAKLNpmgglkrtlfwtayqSKLKAlkegp 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 --------------------LRFFLCGGTTIpkkvARECQqrgiKLLSV--------YGSTESSPHAVVNLDDPLSrfmh 374
Cdd:cd17639 232 gtplldelvfkkvraalggrLRYMLSGGAPL----SADTQ----EFLNIvlcpviqgYGLTETCAGGTVQDPGDLE---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 375 tdgYAAAG-----VEIKVVD--DAR-KTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIK 446
Cdd:cd17639 300 ---TGRVGpplpcCEIKLVDweEGGySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLK 376
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1489134476 447 ITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVVAMSDE 488
Cdd:cd17639 377 IIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDK 419
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
42-550 |
9.08e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 124.37 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 42 ASLADYWQQTARAMPDKIavvdnhgasyTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSV 121
Cdd:PRK06060 14 ASEAGWYDRPAFYAADVV----------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 122 PLLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvdlilplqnqlpqlqqivgvDKLAPATSsLSLSQIIADNTSLTTAI 201
Cdd:PRK06060 84 LANPELHRDDHALAARNTEPALVVTSDALR------------------------DRFQPSRV-AEAAELMSEAARVAPGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 --TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR-LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 278
Cdd:PRK06060 139 yePMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 279 LDIFTPDACLALLEQQRCTCMLGATPFVYDLLnVLEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTE 356
Cdd:PRK06060 219 NSAPVTPEAAAILSARFGPSVLYGVPNFFARV-IDSCSPDSFRSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 SSPHAVVNLDDPLSrfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPEltaRALDEEGWYYSGDL 436
Cdd:PRK06060 298 VGQTFVSNRVDEWR--LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSdERLGERSCAYVVLKAPHHSLSlEEVVAFF 516
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR-ESTGASTLQAFLVATSGATID-GSVMRDL 450
|
490 500 510
....*....|....*....|....*....|....*..
gi 1489134476 517 SRK---RVAKYKYPEHIVVIEKLPRTTSGKIQKFLLR 550
Cdd:PRK06060 451 HRGllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
30-553 |
1.32e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 122.41 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 30 RAAYRqqglwGDASLADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVI 109
Cdd:PRK13383 28 REASR-----GGTNPYTLLAVTAARWPGRTAIIDDDGA-LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 110 YLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvdlilplqnqlpqlqqivgVDKLAPATSSLSL-- 187
Cdd:PRK13383 102 VFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEF------------------------AERIAGADDAVAVid 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 188 -SQIIADNTSLTTAITTHGdelAAVLFTSGTEGLPKGVMLTH--NNILASERAYCARLNLTWQDVFMMPAPLGHATGFlH 264
Cdd:PRK13383 158 pATAGAEESGGRPAVAAPG---RIVLLTSGTTGKPKGVPRAPqlRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGL-G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 265 GVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCmLGATPFVydLLNVLEKQPA-----DLSALRFFLCGGTTIPKKVAR 339
Cdd:PRK13383 234 MLMLTIALGGTVLTHRHFDAEAALAQASLHRADA-FTAVPVV--LARILELPPRvrarnPLPQLRVVMSSGDRLDPTLGQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 340 E-CQQRGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEp 418
Cdd:PRK13383 311 RfMDTYGDILYNGYGSTEVGIGALATPAD-LRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 elTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PRK13383 389 --GGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 499 VLKaPHHSLSLEEVVAFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIqkflLRKDI 553
Cdd:PRK13383 466 VLH-PGSGVDAAQLRDYL-KDRVSRFEQPRDINIVSSIPRNPTGKV----LRKEL 514
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
69-551 |
2.32e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 122.42 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPL-LPSW---REA---ELVWVLNKCQA 141
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLpLPMGfggRESyiaQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 142 KMFFAPTLFkqtrpVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADntslttaitthgdELAAVLFTSGTEGLP 221
Cdd:PRK09192 130 AAIITPDEL-----LPWVNEATHGNPLLHVLSHAWFKALPEADVALPRPTPD-------------DIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 222 KGVMLTHNNILASERAY-CARLNLTWQDVFMMPAPLGHATGFLHGVTAPFligARSVLLDIFT-------PDACLALLEQ 293
Cdd:PRK09192 192 RGVIITHRALMANLRAIsHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPV---ATQLSVDYLPtrdfarrPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 294 QRCTcMLGATPFVYDL----LNVLEKQPADLSALRFFLCGGTTIPKKVAR---EC------------------------- 341
Cdd:PRK09192 269 NRGT-ISYSPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHqfaEAfapagfddkafmpsyglaeatlavs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 342 ---QQRGIKLLSVYGSTESSPHAVVNLDDPLSRF--MHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFD 416
Cdd:PRK09192 348 fspLGSGIVVEEVDRDRLEYQGKAVAPGAETRRVrtFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 417 EPElTARALDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH--DACVVAMSDErlGERS 494
Cdd:PRK09192 428 DEE-SQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE--NGEK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489134476 495 CAYVVlkapHHSLSLEEVVAFFsRKRVAKYKYPEHIV--VIE-----KLPRTTSGKIQKFLLRK 551
Cdd:PRK09192 504 IVLLV----QCRISDEERRGQL-IHALAALVRSEFGVeaAVElvpphSLPRTSSGKLSRAKAKK 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
207-469 |
2.09e-28 |
|
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: 119.77 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTW----QDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDif 282
Cdd:cd05933 151 QCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPatvgQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQ-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 tPDA----CLALLEQQRCTCMLGaTPFVYD-LLNVLEKQPADLSALR--------------------------------- 324
Cdd:cd05933 229 -PDAlkgtLVKTLREVRPTAFMG-VPRVWEkIQEKMKAVGAKSGTLKrkiaswakgvgletnlklmggespsplfyrlak 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 325 -----------------FFLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVVNLDdplSRFMHTDGYAAAGVEIK 386
Cdd:cd05933 307 klvfkkvrkalgldrcqKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSgPHTISNPQ---AYRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 387 VVDdarktlpPGCE--GEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENIS 463
Cdd:cd05933 384 IHN-------PDADgiGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVP 456
|
....*.
gi 1489134476 464 SREVED 469
Cdd:cd05933 457 PVPIED 462
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
69-551 |
5.25e-28 |
|
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: 116.51 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 69 YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPllpswreaelvwvlnkcqakmffAPT 148
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-----------------------ATT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 LFKqtrPVDLilplqnqlpqlqqivgVDKLAPATSSLSlsqiIADNTslttaitTHGDELAAVLFTSGTEGLPKGVMLTH 228
Cdd:cd05974 58 LLT---PDDL----------------RDRVDRGGAVYA----AVDEN-------THADDPMLLYFTSGTTSKPKLVEHTH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 229 NNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI--FTPDACLALLEQQRCTcMLGATPFV 306
Cdd:cd05974 108 RSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYarFDAKRVLAALVRYGVT-TLCAPPTV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 307 YDLLnVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLDDPLSrfMHTDGYAAAGVEI 385
Cdd:cd05974 187 WRML-IQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQPVK--AGSMGRPLPGYRV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 386 KVVDDARKtlpPGCEGE-----EASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGE 460
Cdd:cd05974 264 ALLDPDGA---PATEGEvaldlGDTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 461 NISSREVEDILLQHPKIHDACVVAMSD-ERLGERScAYVVLKA-----PHHSLSLEEvvafFSRKRVAKYKYPEHIVVIE 534
Cdd:cd05974 340 RISPFELESVLIEHPAVAEAAVVPSPDpVRLSVPK-AFIVLRAgyepsPETALEIFR----FSRERLAPYKRIRRLEFAE 414
|
490
....*....|....*..
gi 1489134476 535 kLPRTTSGKIQKFLLRK 551
Cdd:cd05974 415 -LPKTISGKIRRVELRR 430
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-551 |
7.57e-28 |
|
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: 118.05 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVV-----DNHGASYTYSALdHAASC-LANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV-SVpLL 124
Cdd:cd05966 63 LKERGDKVAIIwegdePDQSRTITYREL-LREVCrFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhSV-VF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 125 PSWREAELVWVLNKCQAKMFF-APTLFKQTRPVDLILPlqnqlpqlqqivgVDKLAPATSSLSlSQIIADNTSLTTAITT 203
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVItADGGYRGGKVIPLKEI-------------VDEALEKCPSVE-KVLVVKRTGGEVPMTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGD----ELAA------------------VLFTSGTEGLPKGVMLTHNNILAseraYCAR-----LNLTWQDVFMMPAPL 256
Cdd:cd05966 207 GRDlwwhDLMAkqspecepewmdsedplfILYTSGSTGKPKGVVHTTGGYLL----YAATtfkyvFDYHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 257 GHATGFLHGVTAPFLIGARSVLL----DIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA--DLSALRffLCG- 329
Cdd:cd05966 283 GWITGHSYIVYGPLANGATTVMFegtpTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKkhDLSSLR--VLGs 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 330 -GTTI-P-------KKVARE-CQqrgikLLSVYGSTESSPHAVVNLddPLSRFMHTdGYAAA---GVEIKVVDDARKTLP 396
Cdd:cd05966 361 vGEPInPeawmwyyEVIGKErCP-----IVDTWWQTETGGIMITPL--PGATPLKP-GSATRpffGIEPAILDEEGNEVE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 397 PGCEGEEASRG--PNVFMGYFDEPEltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVED 469
Cdd:cd05966 433 GEVEGYLVIKRpwPGMARTIYGDHE---RYEDTyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVES 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 470 ILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHH-SLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFL 548
Cdd:cd05966 510 ALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEpSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRI 589
|
...
gi 1489134476 549 LRK 551
Cdd:cd05966 590 LRK 592
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
56-546 |
5.42e-27 |
|
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: 114.11 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWV 135
Cdd:cd17656 2 PDAVAVVFEN-QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 136 LNKCQAKMFFA----PTLFKQTRPVDLILPLqnqlpqlqqivgvdklapatsslSLSQIIADNTSLTTAitthGDELAAV 211
Cdd:cd17656 81 MLDSGVRVVLTqrhlKSKLSFNKSTILLEDP-----------------------SISQEDTSNIDYINN----SDDLLYI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 LFTSGTEGLPKGVMLTHNNI---LASERAYCarLNLTWQDVFMMPAPlghatGF---LHGVTAPFLIGARSVLLDIFTP- 284
Cdd:cd17656 134 IYTSGTTGKPKGVQLEHKNMvnlLHFEREKT--NINFSDKVLQFATC-----SFdvcYQEIFSTLLSGGTLYIIREETKr 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 --DACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGT--TIPKKVARECQQRGIKLLSVYGSTESspH 360
Cdd:cd17656 207 dvEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEqlVITNEFKEMLHEHNVHLHNHYGPSET--H 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 AV----VNLDDPLSRfMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL------DEEGW 430
Cdd:cd17656 285 VVttytINPEAEIPE-LPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNERM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 431 YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVlkaPHHSLSLE 510
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---MEQELNIS 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 1489134476 511 EVVAFFSrKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17656 441 QLREYLA-KQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
206-482 |
7.84e-27 |
|
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: 114.62 E-value: 7.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASerayCARLNLTW--------QDVFMMPAPLGH-------ATGFLHGVTAPF 270
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSN----VAGVFKILeilnkinpTDVYISYLPLAHifervveALFLYHGAKIGF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 271 LIGARSVLLD-----------------------IFTPDACLALLEQ-------QRCTCML-----GATPFVYDLlnVLEK 315
Cdd:cd05927 190 YSGDIRLLLDdikalkptvfpgvprvlnriydkIFNKVQAKGPLKRklfnfalNYKLAELrsgvvRASPFWDKL--VFNK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 316 QPADL-SALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD---- 389
Cdd:cd05927 268 IKQALgGNVRLMLTGSAPLSPEVLEFLRVAlGCPVLEGYGQTECT--AGATLTLPGDTSVGHVGGPLPCAEVKLVDvpem 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 390 --DARKTLPpgcEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSRE 466
Cdd:cd05927 346 nyDAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEK 422
|
330
....*....|....*.
gi 1489134476 467 VEDILLQHPKIHDACV 482
Cdd:cd05927 423 IENIYARSPFVAQIFV 438
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
70-551 |
9.72e-27 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 114.49 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANwMLAK--GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFA- 146
Cdd:PRK05620 40 TFAAIGARAAALAH-ALHDelGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 147 PTLFKQTRPVdlilPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGD-------ELAAVLFTSGTEG 219
Cdd:PRK05620 119 PRLAEQLGEI----LKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDwpeldetTAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 220 LPKGVMLTHNNIlaseraYCARLNLTWQDVFMMPaplgHATGFLHGV-----------TAPFLIGARSVLLDiftPDACL 288
Cdd:PRK05620 195 APKGVVYSHRSL------YLQSLSLRTTDSLAVT----HGESFLCCVpiyhvlswgvpLAAFMSGTPLVFPG---PDLSA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 289 ALLEQQRCTCM----LGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVV 363
Cdd:PRK05620 262 PTLAKIIATAMprvaHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETSPVGTV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 364 NldDPLS--------RFMHTDGYAAAGVEIKVVDDARKTLPPG-CEGEEASRGPNVFMGYFDEP---------------- 418
Cdd:PRK05620 342 A--RPPSgvsgearwAYRVSQGRFPASLEYRIVNDGQVMESTDrNEGEIQVRGNWVTASYYHSPteegggaastfrgedv 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV 498
Cdd:PRK05620 420 EDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 499 VLkAPHHSLSLE--EVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK05620 500 VL-APGIEPTREtaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
41-544 |
5.10e-25 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 110.13 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK10252 457 ETTLSALVAQQAAKTPDAPALADAR-YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLNKCQAKMFFApTLFKQTRPVDLILPLQNQLPQLQqivgvdkLAPATSSLSLSQiiadntsltta 200
Cdd:PRK10252 536 LPLDTGYPDDRLKMMLEDARPSLLIT-TADQLPRFADVPDLTSLCYNAPL-------APQGAAPLQLSQ----------- 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 201 itthGDELAAVLFTSGTEGLPKGVMLTHnnilaseRAYCARL-------NLTWQDVFMMPAPLGHATG----FLhgvtaP 269
Cdd:PRK10252 597 ----PHHTAYIIFTSGSTGRPKGVMVGQ-------TAIVNRLlwmqnhyPLTADDVVLQKTPCSFDVSvwefFW-----P 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 270 FLIGARSVLL------DiftPDACLALLEQQRCTC------MLGAtpFVYDLLNvlEKQPADLSALRFFLCGGTTIPKKV 337
Cdd:PRK10252 661 FIAGAKLVMAepeahrD---PLAMQQFFAEYGVTTthfvpsMLAA--FVASLTP--EGARQSCASLRQVFCSGEALPADL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 338 ARECQQR-GIKLLSVYGSTE---------SSPHAVVNLDD---PLsrfmhtdGYAAAGVEIKVVDDARKTLPPGCEGEEA 404
Cdd:PRK10252 734 CREWQQLtGAPLHNLYGPTEaavdvswypAFGEELAAVRGssvPI-------GYPVWNTGLRILDARMRPVPPGVAGDLY 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 405 SRGPNVFMGYFDEPELTA-RALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH 478
Cdd:PRK10252 807 LTGIQLAQGYLGRPDLTAsRFIADpfapgERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 479 ----DACVVAMSDERLGE--RSCAYVVlkaPHHSLSLE-EVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI 544
Cdd:PRK10252 887 qavtHACVINQAAATGGDarQLVGYLV---SQSGLPLDtSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
67-557 |
3.45e-24 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 106.91 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 67 ASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFA 146
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 147 PTLFKQ-TRPVDLilplqnqlpqlQQIVGVDKLAPATSSLSLSQIIA-DNTSLTTAITTHGDELAAV------------- 211
Cdd:PLN02654 199 CNAVKRgPKTINL-----------KDIVDAALDESAKNGVSVGICLTyENQLAMKREDTKWQEGRDVwwqdvvpnyptkc 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 -------------LFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV 277
Cdd:PLN02654 268 evewvdaedplflLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 278 LLDIFT--PDA--CLALLEQQRCTCMLGATPFVYDL---------------LNVLEK--QPADLSALRFF--LCGGTTIP 334
Cdd:PLN02654 348 VFEGAPnyPDSgrCWDIVDKYKVTIFYTAPTLVRSLmrdgdeyvtrhsrksLRVLGSvgEPINPSAWRWFfnVVGDSRCP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 335 kkvarecqqrgikLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRG--PNVFM 412
Cdd:PLN02654 428 -------------ISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKswPGAFR 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 413 GYFDEPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERL 490
Cdd:PLN02654 495 TLYGDHERyeTTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 491 GERSCAYVVL-KAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRL 557
Cdd:PLN02654 575 GQGIYAFVTLvEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 642
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
206-560 |
4.61e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPfLIGARSVLL--DI-F 282
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAP-LFGARVEIVpnAIaH 3947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACLALLEQQRCTcMLGATPFVydLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSph 360
Cdd:PRK05691 3948 DPQGLLAHVQAQGIT-VLESVPSL--IQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRypQIGLVNAYGPAECS-- 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 361 avvnlDDplSRFMHTDGYAAAGV-----------EIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARAL---- 425
Cdd:PRK05691 4023 -----DD--VAFFRVDLASTRGSylpigsptdnnRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphp 4095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 ---DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAcVVAMSDERLGERSCAYVV-LK 501
Cdd:PRK05691 4096 fgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVpHQ 4174
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 502 APHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKI-QKFLLRKDIMRRLTQD 560
Cdd:PRK05691 4175 TVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLdRKALPALDIGQLQSQA 4234
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
66-551 |
1.33e-23 |
|
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: 104.05 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDHAASCLANWML-AKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmf 144
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 145 faptlfkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsQIIADNtslttaitthgDELAAVLFTSGTEGLPKGV 224
Cdd:cd05937 81 --------------------------------------------FVIVDP-----------DDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 225 MLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGvTAPFLIGARSVLL------DIFTPDACLAlleqqrctc 298
Cdd:cd05937 106 AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLG-ACNCLMSGGTLALsrkfsaSQFWKDVRDS--------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 299 mlGATPFVY--DLLNVLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GIKLL-SVYGSTE----SSPHAV------ 362
Cdd:cd05937 176 --GATIIQYvgELCRYLLSTPPspYDRDHKVRVAWGNGLRPDIWERFRERfNVPEIgEFYAATEgvfaLTNHNVgdfgag 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 -VNLDDPLSRFMHTDGYAAAGVEIKVVDDAR--KT-----LPPGCEGEEASRGPNV----FMGYFDEPELTA----RALD 426
Cdd:cd05937 254 aIGHHGLIRRWKFENQVVLVKMDPETDDPIRdpKTgfcvrAPVGEPGEMLGRVPFKnreaFQGYLHNEDATEsklvRDVF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 427 EEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMS----DERLGersCAYVVL 500
Cdd:cd05937 334 RKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAG---CAAITL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1489134476 501 KAPHHSLSLE--EVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:cd05937 411 EESSAVPTEFtkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
81-490 |
2.27e-23 |
|
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: 104.04 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 81 LANWMLAKGIESGDRIAF---QLPGWCEFTviyLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfKQTRPVD 157
Cdd:cd17641 24 FALGLLALGVGRGDVVAIlgdNRPEWVWAE---LAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA----EDEEQVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 158 LILPLQNQLPQLQQIVGVD----------KLAPATSSLSLSQIIA--DNTSLTTAIT-THGDELAAVLFTSGTEGLPKGV 224
Cdd:cd17641 97 KLLEIADRIPSVRYVIYCDprgmrkyddpRLISFEDVVALGRALDrrDPGLYEREVAaGKGEDVAVLCTTSGTTGKPKLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 225 MLTHNNILASERAYCAR------------LNLTWQDVFMMPAPLGHATGF-LHGVTAPFL-------IGARSVLLdifTP 284
Cdd:cd17641 177 MLSHGNFLGHCAAYLAAdplgpgdeyvsvLPLPWIGEQMYSVGQALVCGFiVNFPEEPETmmedlreIGPTFVLL---PP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 DACLALLEQQRCTcMLGATPF---VYDLLNVLEKQPAD--------------------------------LSALRFFLCG 329
Cdd:cd17641 254 RVWEGIAADVRAR-MMDATPFkrfMFELGMKLGLRALDrgkrgrpvslwlrlaswladallfrplrdrlgFSRLRSAATG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 330 GTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLsRFmHTDGYAAAGVEIKVVDdarktlppgcEGEEASRGPN 409
Cdd:cd17641 333 GAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDV-DP-DTVGVPFPGTEVRIDE----------VGEILVRSPG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 410 VFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRG-GENISSREVEDILLQHPKIHDACVVAMSDE 488
Cdd:cd17641 401 VFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
..
gi 1489134476 489 RL 490
Cdd:cd17641 481 YL 482
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
67-549 |
3.90e-23 |
|
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: 102.55 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 67 ASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCqakmffa 146
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 147 ptlfkqtrpvdlilplqnqlpqlqqivGVDKLAPATSSLSLSQIIADNTSLTTAITTHGdeLAAVLFTSGTEGLPKGVML 226
Cdd:cd17654 88 ---------------------------HVSYLLQNKELDNAPLSFTPEHRHFNIRTDEC--LAYVIHTSGTTGTPKIVAV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 227 THNNILASERAYCARLNLTWQDVFMMPAPLgHATGFLHGVTAPFLIGArsVLldIFTPD------ACLA--LLEQQRCTc 298
Cdd:cd17654 139 PHKCILPNIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGA--TL--LIVPTsvkvlpSKLAdiLFKRHRIT- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 299 MLGATPFVYDLLNVLEKQPADLSA---LRFFLCGGTTIPKKVAREC---QQRGIKLLSVYGSTE----SSPHAVVNLDDP 368
Cdd:cd17654 213 VLQATPTLFRRFGSQSIKSTVLSAtssLRVLALGGEPFPSLVILSSwrgKGNRTRIFNIYGITEvscwALAYKVPEEDSP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 369 LSRfmhtdGYAAAGVEIKVVDDARKTLPPGCEGEEASRGpnvfmGYFDEPELTARALdeegWYYSGDLCRMDEaGYIKIT 448
Cdd:cd17654 293 VQL-----GSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV-----CILDDEVTVPKGT----MRATGDFVTVKD-GELFFL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 449 GRKKDIIVRGGENISSREVEDILLQHPKIhDACVVAMSDErlgERSCAYVV---LKAP-HHSLSLEEvvaffsrkrVAKY 524
Cdd:cd17654 358 GRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVgesSSSRiHKELQLTL---------LSSH 424
|
490 500
....*....|....*....|....*
gi 1489134476 525 KYPEHIVVIEKLPRTTSGKIQKFLL 549
Cdd:cd17654 425 AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
50-546 |
4.64e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.78 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 50 QTARAMPDKIAVVDNHGAS-YTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWR 128
Cdd:PRK05857 22 EQARQQPEAIALRRCDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 129 EAELvwvlnkcqakmffapTLFKQ-TRPVDLILPLQNqlpqlqqivGVDKLAPATSSLSLSQIIADNTSLTTAITTHG-- 205
Cdd:PRK05857 102 IAAI---------------ERFCQiTDPAAALVAPGS---------KMASSAVPEALHSIPVIAVDIAAVTRESEHSLda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 -----------DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARlNLTWQD-----VFMMPAPLGHA-------TGF 262
Cdd:PRK05857 158 aslagnadqgsEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKE-GLNWVTwvvgeTTYSPLPATHIgglwwilTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 263 LHGvtAPFLIGA------RSVLLDIFTPDACL--ALLEQqrctcmlgatpfvydLLNVLEKQPADLSALRFFLCGGTTIP 334
Cdd:PRK05857 237 MHG--GLCVTGGenttslLEILTTNAVATTCLvpTLLSK---------------LVSELKSANATVPSLRLVGYGGSRAI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 335 KKVARECQQRGIKLLSVYGSTESSPHAVV--NLDDPLSRFMH-TDGYAAAGVEIKVVDD--ARKTLPPGceGEEASRG-- 407
Cdd:PRK05857 300 AADVRFIEATGVRTAQVYGLSETGCTALClpTDDGSIVKIEAgAVGRPYPGVDVYLAATdgIGPTAPGA--GPSASFGtl 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 408 ----PNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 483
Cdd:PRK05857 378 wiksPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1489134476 484 AMSDERLGERSCAYVVLKAP---HHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK05857 457 EIPDEEFGALVGLAVVASAEldeSAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
66-552 |
4.94e-23 |
|
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: 102.05 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFF 145
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 146 APTLFkqtrpvdlilplqnqlpqlqqivgvdklapatsslslsqiiadntslttaitthgdelaaVLFTSGTEGLPKGVM 225
Cdd:cd05940 81 VDAAL------------------------------------------------------------YIYTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 226 LTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCmlgatpF 305
Cdd:cd05940 101 ISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATI------F 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 306 VY--DLLNVLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GI-KLLSVYGSTE----------------------- 356
Cdd:cd05940 175 QYigELCRYLLNQPPkpTERKHKVRMIFGNGLRPDIWEEFKERfGVpRIAEFYAATEgnsgfinffgkpgaigrnpsllr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 357 -SSPHAVVNLD----DPLSrfmhtdgyAAAGVEIKVvddarktlPPGCEGEEASR--GPNVFMGYFDEPELTARAL---- 425
Cdd:cd05940 255 kVAPLALVKYDlesgEPIR--------DAEGRCIKV--------PRGEPGLLISRinPLEPFDGYTDPAATEKKILrdvf 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 426 -DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERS-CAYVVLKAP 503
Cdd:cd05940 319 kKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPN 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 504 HhslslEEVVAFFSR---KRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:cd05940 399 E-----EFDLSALAAhleKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
40-438 |
8.15e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 102.43 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 40 GDASLADYWQQTARAMPDKIAVVD---NHGA--SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACL 114
Cdd:PRK12582 47 YPRSIPHLLAKWAAEAPDRPWLAQrepGHGQwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 115 KIGAVSVPLLPSWR-----EAELVWVLNKCQAKMFFA---PTLFKQTRPVDLILPLqnqlpqlqqIVGVDKLAPATSSLS 186
Cdd:PRK12582 127 QAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFAqsgAPFARALAALDLLDVT---------VVHVTGPGEGIASIA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 187 LSQIIAdnTSLTTAI-----TTHGDELAAVLFTSGTEGLPKGVMLTHNnILASERAYCARL-----------NLTWQdvf 250
Cdd:PRK12582 198 FADLAA--TPPTAAVaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQR-MMCANIAMQEQLrprepdppppvSLDWM--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 251 mmpaPLGHATGFLHGVTaPFLIGARSVLLDIFTP-----DACLALLEQQRCTCMlGATPFVYDLL-NVLEKQPADLSA-- 322
Cdd:PRK12582 272 ----PWNHTMGGNANFN-GLLWGGGTLYIDDGKPlpgmfEETIRNLREISPTVY-GNVPAGYAMLaEAMEKDDALRRSff 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 --LRFFLCGGTTIPKKVARECQQ-------RGIKLLSVYGSTESSPHAVVNLDDPlsRFMHTDGYAAAGVEIKVVddark 393
Cdd:PRK12582 346 knLRLMAYGGATLSDDLYERMQAlavrttgHRIPFYTGYGATETAPTTTGTHWDT--ERVGLIGLPLPGVELKLA----- 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1489134476 394 tlPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCR 438
Cdd:PRK12582 419 --PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAAR 461
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
46-554 |
1.45e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 101.13 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 46 DYWQQTAramPDKIAVvDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAfqLPGWCEFTVI--YLACLKIGAVSVPL 123
Cdd:PRK04813 9 EEFAQTQ---PDFPAY-DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPII--VFGHMSPEMLatFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 124 ---LPSWReaeLVWVLNKCQAKMFFAPTLFkqtrPVDLILplqnqlpqlqqivgvdklapaTSSLSLSQIIADNTSLTTA 200
Cdd:PRK04813 83 dvsSPAER---IEMIIEVAKPSLIIATEEL----PLEILG---------------------IPVITLDELKDIFATGNPY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 201 ITTH---GDELAAVLFTSGTEGLPKGVMLTHNNILAseraycarlnLT-WqdvfMMPA-PLGHATGFLHgvTAPF---Li 272
Cdd:PRK04813 135 DFDHavkGDDNYYIIFTSGTTGKPKGVQISHDNLVS----------FTnW----MLEDfALPEGPQFLN--QAPYsfdL- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 273 garSVLlDIFtPdaCLALleqqrctcmlGATPFVYD---------LLNVLEKQP----------ADLSAL---------- 323
Cdd:PRK04813 198 ---SVM-DLY-P--TLAS----------GGTLVALPkdmtanfkqLFETLPQLPinvwvstpsfADMCLLdpsfneehlp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 324 ---RFFLCGgTTIPKKVARECQQR--GIKLLSVYGSTEssphAVVNL------DDPLSRFmhtD----GYAAAGVEIKVV 388
Cdd:PRK04813 261 nltHFLFCG-EELPHKTAKKLLERfpSATIYNTYGPTE----ATVAVtsieitDEMLDQY---KrlpiGYAKPDSPLLII 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 389 DDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA---LDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENISSR 465
Cdd:PRK04813 333 DEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 466 EVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFS--RKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:PRK04813 412 EIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKelKERLMEYMIPRKFIYRDSLPLTPNGK 491
|
570
....*....|.
gi 1489134476 544 IQkfllRKDIM 554
Cdd:PRK04813 492 ID----RKALI 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
70-552 |
8.34e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 98.30 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVwvlnKCQAKMffAPTL 149
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLK----QCLQEA--EPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 150 FkqtrpvdlilplqnqlpqlqqiVGVDKlapatsslslsqiiadntslttaitthGDELAAVLFTSGTEGLPKGVMLTHN 229
Cdd:cd05910 78 F----------------------IGIPK---------------------------ADEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 230 NILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVT--APFLIGARSVLLDiftPDACLALLEQQRCTCMLGaTPFVY 307
Cdd:cd05910 109 TFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTsvIPDMDPTRPARAD---PQKLVGAIRQYGVSIVFG-SPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 308 DLLNVL-EKQPADLSALRFFLCGGTTIPKKVA---RECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMH-TD------ 376
Cdd:cd05910 185 ERVARYcAQHGITLPSLRRVLSAGAPVPIALAarlRKMLSDEAEILTPYGATEALPVSSIGSRELLATTTAaTSggagtc 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 377 -GYAAAGVEIKVVD---------DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA----LDEEGWYYSGDLCRMDEA 442
Cdd:cd05910 265 vGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAkiddNSEGFWHRMGDLGYLDDE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 443 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIhdacvvamsderlgeRSCAYVVLKAPHHSLSLEEVVAFFSRKRVA 522
Cdd:cd05910 345 GRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV---------------RRSALVGVGKPGCQLPVLCVEPLPGTITPR 409
|
490 500 510
....*....|....*....|....*....|
gi 1489134476 523 KYKYPEHIVVIEKLPRTTSgkIQKFLLRKD 552
Cdd:cd05910 410 ARLEQELRALAKDYPHTQR--IGRFLIHPS 437
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
70-470 |
1.03e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 99.40 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQ-AKMFFAPt 148
Cdd:PLN02736 80 TYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvAAIFCVP- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 149 lfkQTRPVDLILPLQNQLPQLQQIV-GVDKLAPATSS------LSLSQIIAD-NTSLTTAITTHGDELAAVLFTSGTEGL 220
Cdd:PLN02736 159 ---QTLNTLLSCLSEIPSVRLIVVVgGADEPLPSLPSgtgveiVTYSKLLAQgRSSPQPFRPPKPEDVATICYTSGTTGT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 221 PKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSVLLD--------IF--T 283
Cdd:PLN02736 236 PKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyervnqIVMLHYGVAVGFYQGDNLKLMDdlaalrptIFcsV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 284 P-------DACLALLEQ---------------QRCTCMLGATPF-VYDLLnVLEKQPADLSA-LRFFLCGGTTIPKKVA- 338
Cdd:PLN02736 316 PrlynriyDGITNAVKEsgglkerlfnaaynaKKQALENGKNPSpMWDRL-VFNKIKAKLGGrVRFMSSGASPLSPDVMe 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 339 --RECqqRGIKLLSVYGSTESS-PHAVVNLDDPLSRfmHTdGYAAAGVEIKVVDdarktLP---------PGCEGEEASR 406
Cdd:PLN02736 395 flRIC--FGGRVLEGYGMTETScVISGMDEGDNLSG--HV-GSPNPACEVKLVD-----VPemnytsedqPYPRGEICVR 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489134476 407 GPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 470
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
382-551 |
1.25e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 99.06 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 382 GVEIKVVDDARKTLPPGCEGEEASRGP------NVFmG--------YFDEpeltaraldEEGWYYSGDLCRMDEAGYIKI 447
Cdd:PRK00174 432 GIQPAVVDEEGNPLEGGEGGNLVIKDPwpgmmrTIY-GdherfvktYFST---------FKGMYFTGDGARRDEDGYYWI 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 448 TGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKA---PHHSLSlEEVVAFFSRK--RVA 522
Cdd:PRK00174 502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGgeePSDELR-KELRNWVRKEigPIA 580
|
170 180
....*....|....*....|....*....
gi 1489134476 523 KykyPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK00174 581 K---PDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
255-551 |
1.65e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 97.37 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 255 PLGHATGFLHGVTApFLIGARSVLLD-----------IFTPDACLALLEQQrctcmlgatpfvydLLNVLEKQPADLSAL 323
Cdd:PRK07445 168 PLYHVSGLMQFMRS-FLTGGKLVILPykrlksgqelpPNPSDFFLSLVPTQ--------------LQRLLQLRPQWLAQF 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 324 RFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHaVVNL--DDPLsrfmhtDGYAAAGveiKVVDDARKTLPPGCEG 401
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQ-IATLkpDDFL------AGNNSSG---QVLPHAQITIPANQTG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 402 EEASRGPNVFMGYFdePELtaraLDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAC 481
Cdd:PRK07445 303 NITIQAQSLALGYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVC 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 482 VVAMSDERLGERSCAYVVLKAPhhSLSLEEVVAFFSRKrVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK 551
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYVPKDP--SISLEELKTAIKDQ-LSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
38-442 |
3.01e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 94.56 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 38 LWGDASLADYWQQT-------ARAMPDKIAVVDNHGA----SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEF 106
Cdd:PRK08180 28 LRSAEPLGDYPRRLtdrlvhwAQEAPDRVFLAERGADggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 107 TVIYLACLKIGAVSVPL-----LPSWREAELVWVLNKCQAKMFFA--PTLFkqTRPVDLILPLQNQlpqlqqIVGVDKLA 179
Cdd:PRK08180 108 ALLALAAMYAGVPYAPVspaysLVSQDFGKLRHVLELLTPGLVFAddGAAF--ARALAAVVPADVE------VVAVRGAV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 180 PATSSLSLSQIIAdnTSLTTAI-----TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAycarLNLTWqdvfmmpa 254
Cdd:PRK08180 180 PGRAATPFAALLA--TPPTAAVdaahaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQM----LAQTF-------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 255 plghatgflhgvtaPFLIGARSVLLD------------IFTpdacLAL-------LEQQRCT-CMLGAT--------PFV 306
Cdd:PRK08180 246 --------------PFLAEEPPVLVDwlpwnhtfggnhNLG----IVLynggtlyIDDGKPTpGGFDETlrnlreisPTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 307 Y--------DLLNVLEKQPA----DLSALRFFLCGGTTIPKKV--------ARECQQRgIKLLSVYGSTESSPhAVVNLD 366
Cdd:PRK08180 308 YfnvpkgweMLVPALERDAAlrrrFFSRLKLLFYAGAALSQDVwdrldrvaEATCGER-IRMMTGLGMTETAP-SATFTT 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 367 DPLSRFMHTdGYAAAGVEIKVVDDARKTlppgcegEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRM-DEA 442
Cdd:PRK08180 386 GPLSRAGNI-GLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPA 454
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
52-435 |
4.04e-20 |
|
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: 94.04 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 52 ARAMPDKIAVVDNHGA----SYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLP-- 125
Cdd:cd05921 5 ARQAPDRTWLAEREGNggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 126 ---SWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQlpqlqqIVGVDKLAPATSSLSLSQIIAdnTSLTTAI- 201
Cdd:cd05921 85 slmSQDLAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTP------LVVSRNAVAGRGAISFAELAA--TPPTAAVd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 202 ----TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASEraycARLNLTWQD------VFMMPAPLGHATGFLHGVtAPFL 271
Cdd:cd05921 157 aafaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQ----AMLEQTYPFfgeeppVLVDWLPWNHTFGGNHNF-NLVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 272 IGARSVLLDIFTPDA-----CLALLEQQRCTCMLGAtPFVYD-LLNVLEKQPAdLSA-----LRFFLCGGTTIPKKV--- 337
Cdd:cd05921 232 YNGGTLYIDDGKPMPggfeeTLRNLREISPTVYFNV-PAGWEmLVAALEKDEA-LRRrffkrLKLMFYAGAGLSQDVwdr 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 338 -----ARECQQRgIKLLSVYGSTESSPHAVvNLDDPLSRFMHTdGYAAAGVEIKVVddarktlPPGCEGEEASRGPNVFM 412
Cdd:cd05921 310 lqalaVATVGER-IPMMAGLGATETAPTAT-FTHWPTERSGLI-GLPAPGTELKLV-------PSGGKYEVRVKGPNVTP 379
|
410 420
....*....|....*....|...
gi 1489134476 413 GYFDEPELTARALDEEGWYYSGD 435
Cdd:cd05921 380 GYWRQPELTAQAFDEEGFYCLGD 402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-546 |
7.28e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.46 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 41 DASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS 120
Cdd:PRK05691 2187 DQTLHGLFAAQAARTPQAPALTFA-GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 121 VPLLPSWREAELVWVLnkcqakmffaptlfKQTRPVDLILPLQNQLPQLQQIVGVDKL-----APATSSLSLSQIiaDNT 195
Cdd:PRK05691 2266 VPLDPEYPLERLHYMI--------------EDSGIGLLLSDRALFEALGELPAGVARWcleddAAALAAYSDAPL--PFL 2329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 196 SLTtaitthgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD--VFMMPAPLGHATGFLhgvTAPFLIG 273
Cdd:PRK05691 2330 SLP-------QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDceLHFYSINFDAASERL---LVPLLCG 2399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 274 ARSVLLDIFTPDA---ClALLEQQRCTcMLGATP-FVYDLLNVLEKQPADLSaLRFFLCGGTTIPKKVARECQQ--RGIK 347
Cdd:PRK05691 2400 ARVVLRAQGQWGAeeiC-QLIREQQVS-ILGFTPsYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQafAPQL 2476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 348 LLSVYGSTESsphAVVNLDDPLSRFMHTDgyaAAGVEI-KVV--------DDARKTLPPGCEGEEASRGPNVFMGYFDEP 418
Cdd:PRK05691 2477 FFNAYGPTET---VVMPLACLAPEQLEEG---AASVPIgRVVgarvayilDADLALVPQGATGELYVGGAGLAQGYHDRP 2550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 419 ELTAR-------ALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMsDERLG 491
Cdd:PRK05691 2551 GLTAErfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSG 2629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489134476 492 ERSCAYVVLKAPHHS----LSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:PRK05691 2630 KQLAGYLVSAVAGQDdeaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
211-563 |
9.61e-20 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 93.09 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLT---HNNILAS--ERAYCARLNltwqDVFMMPAPLGHATGFLHGVTAPFLIGARSVL---LDIf 282
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDtggYAVALATsmDTIFGGKAG----ETFFCASDIGWVVGHSYIVYAPLLAGMATIMyegLPT- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 283 TPDACL--ALLEQQRCTCMLGATPFVydllNVLEKQPA------DLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYG 353
Cdd:PRK10524 313 RPDAGIwwRIVEKYKVNRMFSAPTAI----RVLKKQDPallrkhDLSSLRALFLAGEPLDEPTASWISEAlGVPVIDNYW 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 STESS-P-HAVVN-LDDPLSRFmHTDGYAAAGVEIKVVDDA---------------RKTLPPGCE----GEEAsRGPNVF 411
Cdd:PRK10524 389 QTETGwPiLAIARgVEDRPTRL-GSPGVPMYGYNVKLLNEVtgepcgpnekgvlviEGPLPPGCMqtvwGDDD-RFVKTY 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 412 MGYFDEPEltaraldeegwYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLG 491
Cdd:PRK10524 467 WSLFGRQV-----------YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKG 535
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 492 ERSCAYVVLK------APHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKiqkfllrkdIMRRLTQDVCE 563
Cdd:PRK10524 536 QVAVAFVVPKdsdslaDREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGK---------LLRRAIQAIAE 604
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
466-543 |
1.15e-19 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 83.36 E-value: 1.15e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 466 EVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKaPHHSLSLEEVVAfFSRKRVAKYKYPEHIVVIEKLPRTTSGK 543
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLK-PGVELLEEELVA-HVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
43-546 |
1.20e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 43 SLADYWQQTARAMPDKIAV-----VDNHGASYTYSALDHAASCLANWMLAKGiESGDRIAFQLPGWCEFTVIYLACLKIG 117
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALrfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 118 AVSVPLLP--SWRE---AELVWVLNKCQAKMFFAPTLFKQTrpvdLILPLQNQLPQLQQIVGVDKLAPAtsslslsqiIA 192
Cdd:PRK05691 89 VIAVPAYPpeSARRhhqERLLSIIADAEPRLLLTVADLRDS----LLQMEELAAANAPELLCVDTLDPA---------LA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 193 DNTSlttAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASE----RAYcaRLNLTWQDVFMMPAPLGHATGFLHGVTA 268
Cdd:PRK05691 156 EAWQ---EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEqlirHGF--GIDLNPDDVIVSWLPLYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 269 PFLIGARSVLLD----IFTPDACLALLEQQRCTcMLGATPFVYDLLNVLEKQPA----DLS------------------- 321
Cdd:PRK05691 231 PIFSGVPCVLMSpayfLERPLRWLEAISEYGGT-ISGGPDFAYRLCSERVSESAlerlDLSrwrvaysgsepirqdsler 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 322 -ALRFFLCGGTtiPKK-------------VARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSrfmhTDGYAAAGVEIKV 387
Cdd:PRK05691 310 fAEKFAACGFD--PDSffasyglaeatlfVSGGRRGQGIPALELDAEALARNRAEPGTGSVLM----SCGRSQPGHAVLI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 388 VDDAR-KTLPPGCEGEEASRGPNVFMGYFDEPELTARA---LDEEGWYYSGDLCRMDEaGYIKITGRKKDIIVRGGENIS 463
Cdd:PRK05691 384 VDPQSlEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 464 SREVEDILLQH-PKIHDACVVAMSDERLGERS--CAYVVLKAPHHSLSLEEVVAFFsRKRVAK--YKYPEHIVVIE--KL 536
Cdd:PRK05691 463 PQDIEKTVEREvEVVRKGRVAAFAVNHQGEEGigIAAEISRSVQKILPPQALIKSI-RQAVAEacQEAPSVVLLLNpgAL 541
|
570
....*....|
gi 1489134476 537 PRTTSGKIQK 546
Cdd:PRK05691 542 PKTSSGKLQR 551
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
213-549 |
1.58e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 85.09 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 213 FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLE 292
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 293 QQRCTCMLGATPFVYDLLNVLekqPADLsalRFF--LCGGTTIPKKVARECQQRGIKLLSVYGSTESsphAVVNLDDPLS 370
Cdd:PRK08308 188 NTPQHILYAVPLMLHILGRLL---PGTF---QFHavMTSGTPLPEAWFYKLRERTTYMMQQYGCSEA---GCVSICPDMK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 371 RfmHTD-GYAAAGVEIKVvddarktlppGcEGEEASRgpnvfmgyfdepELTARALDEEgwYYSGDLCRMDEAGYIKITG 449
Cdd:PRK08308 259 S--HLDlGNPLPHVSVSA----------G-SDENAPE------------EIVVKMGDKE--IFTKDLGYKSERGTLHFMG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 450 RKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEvvafFSRKRVAKYKYPEH 529
Cdd:PRK08308 312 RMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLRE----WCIQHLAPYQVPHE 387
|
330 340
....*....|....*....|
gi 1489134476 530 IVVIEKLPRTTSGKIQKFLL 549
Cdd:PRK08308 388 IESVTEIPKNANGKVSRKLL 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
176-553 |
1.60e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 85.59 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 176 DKLAPATSSLS---LSQIIADNTSLTTAITTHGDelAAVL-FTSGTEGLPKGVMLTHNNILASERAYCARLNLTW-QDVF 250
Cdd:PRK05851 120 ERLRAVDSSVTvhdLATAAHTNRSASLTPPDSGG--PAVLqGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 251 MMPAPLGHATGFLHGVTApFLIGARSVLLDI--FT--PDACLALLEQQRCTcMLGATPFVYDLLNVLEKQ--PADLSALR 324
Cdd:PRK05851 198 CSWLPLYHDMGLAFLLTA-ALAGAPLWLAPTtaFSasPFRWLSWLSDSRAT-LTAAPNFAYNLIGKYARRvsDVDLGALR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 325 FFLCGGTTIP----KKVARECQQRGIK---LLSVYGSTESS-------PHAVVNLDD---PLSRFMHTD---GYAAAGVE 384
Cdd:PRK05851 276 VALNGGEPVDcdgfERFATAMAPFGFDagaAAPSYGLAESTcavtvpvPGIGLRVDEvttDDGSGARRHavlGNPIPGME 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 385 IKVV--DDARKTLPPGCeGEEASRGPNVFMGYFDEPeltarALDEEGWYYSGDLCRMDEAGYIkITGRKKDIIVRGGENI 462
Cdd:PRK05851 356 VRISpgDGAAGVAGREI-GEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 463 SSREVEDILLQHPKIHDACVVAM-SDERlGERSCAYVVL--KAPHHSLSLEEVVaffsrKRVAKY--KYPEHIVVIE--K 535
Cdd:PRK05851 429 FPTEIERVAAQVRGVREGAVVAVgTGEG-SARPGLVIAAefRGPDEAGARSEVV-----QRVASEcgVVPSDVVFVApgS 502
|
410
....*....|....*...
gi 1489134476 536 LPRTTSGKIQKFLLRKDI 553
Cdd:PRK05851 503 LPRTSSGKLRRLAVKRSL 520
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
66-552 |
5.53e-17 |
|
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: 83.88 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDhAASCLANWMLAK--GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAK- 142
Cdd:cd05938 3 GETYTYRDVD-RRSNQAARALLAhaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 143 MFFAPTLFKqtrpvdlilplqnqlpqlqqivGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAV----------- 211
Cdd:cd05938 82 LVVAPELQE----------------------AVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAAsdepvpaslra 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 ----------LFTSGTEGLPKGVMLTHNNILASERAYCARlNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI 281
Cdd:cd05938 140 hvtikspalyIYTSGTTGLPKAARISHLRVLQCSGFLSLC-GVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 282 FTP----DACLalleQQRCTCMLgatpFVYDLLNVLEKQPADLS--ALRFFLCGGTTIPKKVARECQQR--GIKLLSVYG 353
Cdd:cd05938 219 FSAsqfwDDCR----KHNVTVIQ----YIGELLRYLCNQPQSPNdrDHKVRLAIGNGLRADVWREFLRRfgPIRIREFYG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 354 STESSphavvnlddpLSRFMHTDGYAAAGveikVVDDARKTLPP------GCEGEEASRGP------------------- 408
Cdd:cd05938 291 STEGN----------IGFFNYTGKIGAVG----RVSYLYKLLFPfelikfDVEKEEPVRDAqgfcipvakgepgllvaki 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 409 ---NVFMGYFDEPELTARAL--D--EEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHD 479
Cdd:cd05938 357 tqqSPFLGYAGDKEQTEKKLlrDvfKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 480 ACV----VAMSDERLGersCAYVVLKaPHHSLSLEEVVAFFSRKRVAkYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:cd05938 437 VNVygvtVPGHEGRIG---MAAVKLK-PGHEFDGKKLYQHVREYLPA-YARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
200-528 |
8.64e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 80.79 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 200 AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN-----LTWQDVFMMPAPLGHATGFlhGVTAPFLigA 274
Cdd:PTZ00216 258 NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNdligpPEEDETYCSYLPLAHIMEF--GVTNIFL--A 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 275 RSVLLDIFTPDACLAL-------LEQQRCTcMLGATPFVYDLL--NVLEKQP---------------ADLSAL------- 323
Cdd:PTZ00216 334 RGALIGFGSPRTLTDTfarphgdLTEFRPV-FLIGVPRIFDTIkkAVEAKLPpvgslkrrvfdhayqSRLRALkegkdtp 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 324 ------------------RFFLCGGTTIPKKVarecQQrgikLLSV--------YGSTESsphaVVNLDDPLSRFMHTD- 376
Cdd:PTZ00216 413 ywnekvfsapravlggrvRAMLSGGGPLSAAT----QE----FVNVvfgmviqgWGLTET----VCCGGIQRTGDLEPNa 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 377 -GYAAAGVEIKVVD--DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKD 453
Cdd:PTZ00216 481 vGQLLKGVEMKLLDteEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKA 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 454 IIVRG-GENISSREVEDILLQHPKIHDACVVAMSDERlgeRS--CAYVvlkaphhsLSLEEVVAFFSRKRVAKYKYPE 528
Cdd:PTZ00216 561 LAKNClGEYIALEALEALYGQNELVVPNGVCVLVHPA---RSyiCALV--------LTDEAKAMAFAKEHGIEGEYPA 627
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
211-563 |
2.00e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 79.40 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHN-NILASERAYCARLNLTWQDVFMMPAPLGHAT--GFLHGVTA---PFLIGARSVLLDIFTP 284
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGpHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSfhGFLYGSLSlgnTFVMFEGGIIKNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 285 DACLALLEQQRCTCMLgATPFVYDLLNVLE------KQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTES 357
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTL-TLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGYGQTEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 358 SPHAVVNLDDPLSRFmHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASR--GPNVFMGYFDEPELTARALDEE--GWYYS 433
Cdd:PTZ00237 418 GITYLYCYGHINIPY-NATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpMPPSFATTFYKNDEKFKQLFSKfpGYYNS 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 434 GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAP--HHSLSLEE 511
Cdd:PTZ00237 497 GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDqsNQSIDLNK 576
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 512 V---VAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRK---DIMRRLTQDVCE 563
Cdd:PTZ00237 577 LkneINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKflnDSNYQLPDNVND 634
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
56-546 |
2.46e-15 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 78.71 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 56 PDKIAVV------DNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV-SV--PLLPS 126
Cdd:cd17647 2 PERTCVVetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATfSVidPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 127 WREAELVWVlnkcqakmffaptlfkqTRPVDLILPLQNQLpqlqqIVGVDklapatSSLSLSqiiadntslttaitthgd 206
Cdd:cd17647 82 ARQNIYLGV-----------------AKPRGLIVIRAAGV-----VVGPD------SNPTLS------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 elaavlFTSGTEGLPKGVMLTHNNIlaserAY-----CARLNLTWQDVFMMPAPLGHATgFLHGVTAPFLIGARsvLL-- 279
Cdd:cd17647 116 ------FTSGSEGIPKGVLGRHFSL-----AYyfpwmAKRFNLSENDKFTMLSGIAHDP-IQRDMFTPLFLGAQ--LLvp 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 ---DIFTPDACLALLEQQRCTcMLGATPFVYDLLNVLEKQPADLSALRFFLcgGTTIPKKVARECQ--QRGIKLLSVYGS 354
Cdd:cd17647 182 tqdDIGTPGRLAEWMAKYGAT-VTHLTPAMGQLLTAQATTPFPKLHHAFFV--GDILTKRDCLRLQtlAENVRIVNMYGT 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 355 TE--------------SSPHAVVNLDD--PLSRFMHTdgyaaagVEIKVVD--DARKTLPPGCEGEEASRGPNVFMGYFD 416
Cdd:cd17647 259 TEtqravsyfevpsrsSDPTFLKNLKDvmPAGRGMLN-------VQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 417 EPELTARA------LDEEGW----------------------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVE 468
Cdd:cd17647 332 LPELNKEKfvnnwfVEPDHWnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 469 DILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAF-------------------------FSRKRVAK 523
Cdd:cd17647 412 THISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQEDVpkevstdpivkgligyrklikdireFLKKRLAS 491
|
570 580
....*....|....*....|...
gi 1489134476 524 YKYPEHIVVIEKLPRTTSGKIQK 546
Cdd:cd17647 492 YAIPSLIVVLDKLPLNPNGKVDK 514
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
66-552 |
2.00e-14 |
|
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: 75.92 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 66 GASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLN--KCQAKM 143
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITvsKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 144 FfaptlfkqtrpvDLilplqnqlpqlqqivgVDKLAPATSSLSLSQIIADNTSLTTAItthgdelaavlFTSGTEGLPKG 223
Cdd:cd05939 81 F------------NL----------------LDPLLTQSSTEPPSQDDVNFRDKLFYI-----------YTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 224 VMLTHNNIL--ASERAYCARLNLtwQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlg 301
Cdd:cd05939 122 AVIVHSRYYriAAGAYYAFGMRP--EDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCT---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 302 ATPFVYDLLNVLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GIKLLS-VYGSTESSPhAVVNLDDPLSR--FMHT 375
Cdd:cd05939 196 IVQYIGEICRYLLAQPPseEEQKHNVRLAVGNGLRPQIWEQFVRRfGIPQIGeFYGATEGNS-SLVNIDNHVGAcgFNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 376 DGYAAAGVEIKVVDDARKTL-----------PPGCEGE-----EASRGPNVFMGYFDEPELT---ARALDEEG--WYYSG 434
Cdd:cd05939 275 ILPSVYPIRLIKVDEDTGELirdsdglcipcQPGEPGLlvgkiIQNDPLRRFDGYVNEGATNkkiARDVFKKGdsAFLSG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 435 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMS-DERLGERSCAYVVlkAPHHSLSLEEVV 513
Cdd:cd05939 355 DVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvPGVEGRAGMAAIV--DPERKVDLDRFS 432
|
490 500 510
....*....|....*....|....*....|....*....
gi 1489134476 514 AFFsRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKD 552
Cdd:cd05939 433 AVL-AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
206-482 |
2.04e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 76.31 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 206 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGH-----ATGFLHGVTAPFLIGARSVLL 279
Cdd:PLN02387 250 NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHilelaAESVMAAVGAAIGYGSPLTLT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 DI--------------FTPD---ACLALLEQQR--------------------------------CTCMLGATPFVYDLL 310
Cdd:PLN02387 330 DTsnkikkgtkgdasaLKPTlmtAVPAILDRVRdgvrkkvdakgglakklfdiaykrrlaaiegsWFGAWGLEKLLWDAL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 311 nVLEKQPADLSA-LRFFLCGGTTIPKKVarecqQR------GIKLLSVYGSTESSPHAVV-NLDDPlsrfmhTDGYAAAG 382
Cdd:PLN02387 410 -VFKKIRAVLGGrIRFMLSGGAPLSGDT-----QRfiniclGAPIGQGYGLTETCAGATFsEWDDT------SVGRVGPP 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 383 VE---IKVVD----DARKTLPPGCEGEEASRGPNVFMGYFDEPELTARA--LDEEG--WYYSGDLCRMDEAGYIKITGRK 451
Cdd:PLN02387 478 LPccyVKLVSweegGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRK 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1489134476 452 KDII-VRGGENIS----------SREVEDILLQHPKIHDACV 482
Cdd:PLN02387 558 KDIVkLQHGEYVSlgkveaalsvSPYVDNIMVHADPFHSYCV 599
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
211-482 |
6.09e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 74.85 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNILASERAYCARLN-----LTWQDVFMMPAPLGH---------------ATGFLHG----- 265
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHildrmieeyffrkgaSVGYYHGdlnal 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 266 ------VTAPFLIGARSVLLDIFtpDACLALLEQQRctcmlgatPFVYDLLNVLEKQP----------------ADLSA- 322
Cdd:PLN02430 305 rddlmeLKPTLLAGVPRVFERIH--EGIQKALQELN--------PRRRLIFNALYKYKlawmnrgyshkkaspmADFLAf 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 ----------LRFFLCGGTTIPKKVArecqqrgiKLLSV---------YGSTESSPHAVVNLDDPLSrFMHTDGYAAAGV 383
Cdd:PLN02430 375 rkvkaklggrLRLLISGGAPLSTEIE--------EFLRVtscafvvqgYGLTETLGPTTLGFPDEMC-MLGTVGAPAVYN 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 384 EIKVVDDARKTLPPGCE---GEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGG 459
Cdd:PLN02430 446 ELRLEEVPEMGYDPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQG 524
|
330 340
....*....|....*....|...
gi 1489134476 460 ENISSREVEDILLQHPKIHDACV 482
Cdd:PLN02430 525 EYVALEYLENVYGQNPIVEDIWV 547
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
70-443 |
1.36e-13 |
|
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: 73.64 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKG-IESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMF---- 144
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLavsa 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 145 -------------FAPT---LFKQTRPVDLILPLQNQLPqlqqivgvDKLAPATSSLSLSQIIAD-----NTSLTTAITT 203
Cdd:cd17632 149 ehldlaveavlegGTPPrlvVFDHRPEVDAHRAALESAR--------ERLAAVGIPVTTLTLIAVrgrdlPPAPLFRPEP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNIlaserAYCARLNLTWQDVFMMPA------PLGHATG-------FLHGVTAPF 270
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLV-----ATFWLKVSSIQDIRPPASitlnfmPMSHIAGrislygtLARGGTAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 271 LigARSVLLDIFTPdacLALLeqqRCTcMLGATPFVYDLL-----------NVLEKQPADLSA-----LRFFLCGGTTI- 333
Cdd:cd17632 296 A--AASDMSTLFDD---LALV---RPT-ELFLVPRVCDMLfqryqaeldrrSVAGADAETLAErvkaeLRERVLGGRLLa 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 334 ----PKKVARECQQ-----RGIKLLSVYGSTESsphAVVNLDDPLSRFMHTDgYaaagveiKVVDDAR----KTLPPGCE 400
Cdd:cd17632 367 avcgSAPLSAEMKAfmeslLDLDLHDGYGSTEA---GAVILDGVIVRPPVLD-Y-------KLVDVPElgyfRTDRPHPR 435
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1489134476 401 GEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLcrMDEAG 443
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV--MAELG 476
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
70-559 |
1.29e-10 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 64.33 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 70 TYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKmffapTL 149
Cdd:PLN03052 210 TLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAK-----AI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 150 FKQtrpvDLILPLQNQLPQLQQIVGVDK----LAPATSSLSLSQIIADNTS----LTTAITT-HGDELAAV--------- 211
Cdd:PLN03052 285 FTQ----DVIVRGGKSIPLYSRVVEAKApkaiVLPADGKSVRVKLREGDMSwddfLARANGLrRPDEYKAVeqpveaftn 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 212 -LFTSGTEGLPKGVMLTHNN-ILASERAYCaRLNLTWQDVFMMPAPLGHATGflhgvtaPFLIGARsvlldiFTPDACLA 289
Cdd:PLN03052 361 iLFSSGTTGEPKAIPWTQLTpLRAAADAWA-HLDIRKGDIVCWPTNLGWMMG-------PWLVYAS------LLNGATLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 290 LLE------------QQRCTCMLGATPFV---YDLLNVLEKqpADLSALRFFLCGGTTIP-------------KKVAREC 341
Cdd:PLN03052 427 LYNgsplgrgfakfvQDAKVTMLGTVPSIvktWKNTNCMAG--LDWSSIRCFGSTGEASSvddylwlmsragyKPIIEYC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 342 qqrgikllsvyGSTE-SSPHAVVNLDDP--LSRFmhtdGYAAAGVEIKVVDDARKTLPP--GCEGEEAsRGPNVFMG--- 413
Cdd:PLN03052 505 -----------GGTElGGGFVTGSLLQPqaFAAF----STPAMGCKLFILDDSGNPYPDdaPCTGELA-LFPLMFGAsst 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 414 ---------YFD-EPELTARALDEEgwyysGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQ-HPKIHDACV 482
Cdd:PLN03052 569 llnadhykvYFKgMPVFNGKILRRH-----GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 483 VAMSDERLG-ERSCAYVVLKAPHHS-LSLEEVVAFFSRKRVAK----YKYpEHIVVIEKLPRTTSGKIQKFLLRKDIMRR 556
Cdd:PLN03052 644 IGVPPPGGGpEQLVIAAVLKDPPGSnPDLNELKKIFNSAIQKKlnplFKV-SAVVIVPSFPRTASNKVMRRVLRQQLAQE 722
|
...
gi 1489134476 557 LTQ 559
Cdd:PLN03052 723 LSR 725
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
211-554 |
3.18e-10 |
|
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: 62.67 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 211 VLFTSGTEGLPKGVMLTHNNILA---SERAYCArlNLTWQDVF--------MMpaplghatgfLHGVTAPFLIGARSVLL 279
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGGTLLqhlKEHILHC--DLRPGDRLfyyttcgwMM----------WNWLVSGLAVGATIVLY 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 D----IFTPDACLALLEQQRCTcMLGATPFVYDLLNVLEKQPA---DLSALRFFLCGGTTIPKKVAR---ECQQRGIKLL 349
Cdd:cd05943 322 DgspfYPDTNALWDLADEEGIT-VFGTSAKYLDALEKAGLKPAethDLSSLRTILSTGSPLKPESFDyvyDHIKPDVLLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 350 SVYGSTessphavvnldDPLSRFMHTD-------GYAAA---GVEIKVVDDARKTLPpGCEGEEASRGPNVFM------- 412
Cdd:cd05943 401 SISGGT-----------DIISCFVGGNpllpvyrGEIQCrglGMAVEAFDEEGKPVW-GEKGELVCTKPFPSMpvgfwnd 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 413 --------GYFDEpeltaraldEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVA 484
Cdd:cd05943 469 pdgsryraAYFAK---------YPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVG 539
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489134476 485 MSDERLGERSCAYVVLkAPHHSLSLEEVVAFFSRKRVA--KYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIM 554
Cdd:cd05943 540 QEWKDGDERVILFVKL-REGVELDDELRKRIRSTIRSAlsPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIA 610
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
323-483 |
8.74e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 61.66 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 LRFFLCGGTTIPKKVARE-CQQRGIKLLSVYGSTESS-PHAVVNLDDplSRFMHTDGYAAAGVEIKVVD----DARKTLP 396
Cdd:PTZ00342 463 LEVILNGGGKLSPKIAEElSVLLNVNYYQGYGLTETTgPIFVQHADD--NNTESIGGPISPNTKYKVRTwetyKATDTLP 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 397 pgcEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHP 475
Cdd:PTZ00342 541 ---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIETDMLNNLYSQIS 617
|
....*...
gi 1489134476 476 KIHDaCVV 483
Cdd:PTZ00342 618 FINF-CVV 624
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
214-477 |
1.93e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 59.78 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 214 TSGTEGLPKGVMLTHN--NILAS--ERAYCArLNLTWQDVFMMPAPLGHATGFL---HGVTApflIGARSVLLDIFTPDA 286
Cdd:COG1541 91 SSGTTGKPTVVGYTRKdlDRWAElfARSLRA-AGVRPGDRVQNAFGYGLFTGGLglhYGAER---LGATVIPAGGGNTER 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 287 CLALLEQQRCTCMLGATPFVYDLLNVLEKQ---PADLSaLRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPhaV 362
Cdd:COG1541 167 QLRLMQDFGPTVLVGTPSYLLYLAEVAEEEgidPRDLS-LKKGIFGGEPWSEEMRKEIEERwGIKAYDIYGLTEVGP--G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 363 VNLDDPLSRFMH--TDGYAaagVEIkvVD-DARKTLPPGCEGeeasrgpnvfmgyfdepELTARALDEEGW----YYSGD 435
Cdd:COG1541 244 VAYECEAQDGLHiwEDHFL---VEI--IDpETGEPVPEGEEG-----------------ELVVTTLTKEAMplirYRTGD 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489134476 436 LC--------------RMDeagyiKITGRKKD-IIVRGGeNISSREVEDILLQHPKI 477
Cdd:COG1541 302 LTrllpepcpcgrthpRIG-----RILGRADDmLIIRGV-NVFPSQIEEVLLRIPEV 352
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
207-470 |
2.01e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 60.42 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 207 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYC-----ARLNLTWQDVFMMPAPLGH---------------ATGFLHGV 266
Cdd:PLN02614 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLSYLPLAHifdrvieecfiqhgaAIGFWRGD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 267 TA----------PFLIGARSVLLD-------------------IFTPDACLALLEQQRCTCMLGATPFVYDLlnVLEKQP 317
Cdd:PLN02614 304 VKlliedlgelkPTIFCAVPRVLDrvysglqkklsdggflkkfVFDSAFSYKFGNMKKGQSHVEASPLCDKL--VFNKVK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 318 ADLSA-LRFFLCGGTTIPKKVarECQQRGI---KLLSVYGSTESSPHAVVNLDDPLSrFMHTDGYAAAGVEIKVVD---- 389
Cdd:PLN02614 382 QGLGGnVRIILSGAAPLASHV--ESFLRVVaccHVLQGYGLTESCAGTFVSLPDELD-MLGTVGPPVPNVDIRLESvpem 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 390 --DARKTLPpgcEGEEASRGPNVFMGYFDEPELTARALDEeGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSRE 466
Cdd:PLN02614 459 eyDALASTP---RGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVEN 534
|
....
gi 1489134476 467 VEDI 470
Cdd:PLN02614 535 IENI 538
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
204-477 |
3.73e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 59.47 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 204 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-----WQDVFMMPAPLGH---------------ATGFL 263
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHvydqvietyciskgaSIGFW 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 264 HG-----------VTAPFLIGARSVLLDIFTpdaclALLEQQRCTCMLGATPFV----YDLLNVLEKQPADLSA------ 322
Cdd:PLN02861 298 QGdirylmedvqaLKPTIFCGVPRVYDRIYT-----GIMQKISSGGMLRKKLFDfaynYKLGNLRKGLKQEEASprldrl 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 323 ------------LRFFLCGGTTIPKKVARECQQRGIKLLSV-YGSTESSPHAVVNLDDPLSrFMHTDGYAAAGVEIKVVD 389
Cdd:PLN02861 373 vfdkikeglggrVRLLLSGAAPLPRHVEEFLRVTSCSVLSQgYGLTESCGGCFTSIANVFS-MVGTVGVPMTTIEARLES 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 390 ------DARKTLPpgcEGEEASRGPNVFMGYFDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENI 462
Cdd:PLN02861 452 vpemgyDALSDVP---RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYV 527
|
330
....*....|....*
gi 1489134476 463 SSREVEDILLQHPKI 477
Cdd:PLN02861 528 AVENLENTYSRCPLI 542
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
213-544 |
1.22e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 57.64 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 213 FTSGTEGLPKGVMLTHNNILA----SERAY------CARLNLT---WqdvfmmpAPLGHATGFLHGVTAPFLIGARSVLL 279
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIAnfeqLMSDYfgdtggVPPPDTTvvsW-------LPFYHDMGLVLGVCAPILGGCPAVLT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 280 difTPDACL--------ALLEQQRCtcmLGATP-FVYDL---------LNVLekqpaDLSALRFFLCGGTTI-PKKVARE 340
Cdd:PRK05850 240 ---SPVAFLqrparwmqLLASNPHA---FSAAPnFAFELavrktsdddMAGL-----DLGGVLGIISGSERVhPATLKRF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 341 CQQ------RGIKLLSVYG----------STESSPHAVVNLD-DPLSrfmhtDGYAA-----AGVE-----------IKV 387
Cdd:PRK05850 309 ADRfapfnlRETAIRPSYGlaeatvyvatREPGQPPESVRFDyEKLS-----AGHAKrcetgGGTPlvsygsprsptVRI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 388 VD-DARKTLPPGCEGEEASRGPNVFMGYFDEPELTAR----ALDE------EG-WYYSGDLCRMDEaGYIKITGRKKDII 455
Cdd:PRK05850 384 VDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERtfgaTLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 456 VRGGENISSrevEDILLQHPKIHDACVVAMS-DERLGERSCAYVVLKAPHHS-------LSL--EEVVAFFSRK---RVA 522
Cdd:PRK05850 463 IVDGRNHYP---DDIEATIQEITGGRVAAISvPDDGTEKLVAIIELKKRGDSdeeamdrLRTvkREVTSAISKShglSVA 539
|
410 420
....*....|....*....|....*
gi 1489134476 523 KykypehiVVI---EKLPRTTSGKI 544
Cdd:PRK05850 540 D-------LVLvapGSIPITTSGKI 557
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
61-324 |
6.58e-06 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 48.88 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 61 VVDNHGA---SYTYSALDHAASCLANWMLAK-GIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVL 136
Cdd:cd05905 4 LLDSKGKeatTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 137 NKCQAKMFFA--------PTLFKQTRPVDLIlPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNtslttaitthgDEL 208
Cdd:cd05905 84 GTCKVRVALTveaclkglPKKLLKSKTAAEI-AKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRD-----------GDT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 209 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD--IFTPD- 285
Cdd:cd05905 152 AYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPpeLMKTNp 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1489134476 286 -ACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA-------DLSALR 324
Cdd:cd05905 232 lLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLAslknrdvNLSSLR 278
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
448-559 |
3.01e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 43.21 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 448 TGRK-KDIIVRGGENISSRE------------VEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPhhslSLEEVVa 514
Cdd:PRK09188 213 TGKKvYNFITRGLFSWSDGEgtgdridneapaIQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELP----ADEKSL- 287
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1489134476 515 ffsRKRVAKY---KYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQ 559
Cdd:PRK09188 288 ---RARLAGAkppKPPEHIQPVAALPRDADGTVRDDILRLIAMNQIDE 332
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
214-475 |
3.95e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 43.00 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 214 TSGTEGLPKGVMLTHNNI--LASERAYCARL-NLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLAL 290
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLdvWAELVARCLDAaGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 291 LEQQRCTcMLGATP-FVYDLLNVLEKQPADL--SALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSpHAVVNLD 366
Cdd:cd05913 166 IKDFGPT-VLCCTPsYALYLAEEAEEEGIDPreLSLKVGIFGAEPWTEEMRKRIERRlGIKAYDIYGLTEII-GPGVAFE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134476 367 DPLSRFMH--TDGYAaagVEIkvVDDarKTLPPGCEGEEAsrgpnvfmgyfdepELTARALDEEGW----YYSGDL---- 436
Cdd:cd05913 244 CEEKDGLHiwEDHFI---PEI--IDP--ETGEPVPPGEVG--------------ELVFTTLTKEAMplirYRTRDItrll 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1489134476 437 -----C-----RMDeagyiKITGRKKD-IIVRgGENISSREVEDILLQHP 475
Cdd:cd05913 303 pgpcpCgrthrRID-----RITGRSDDmLIIR-GVNVFPSQIEDVLLKIP 346
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
56-119 |
4.54e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 39.78 E-value: 4.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489134476 56 PDKIAVV----DNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAV 119
Cdd:PRK03584 98 DDRPAIIfrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI 165
|
|
| |
