|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-546 |
0e+00 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 1089.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 2 SVTLTFDAARRKTYRESGYWGDASLGDYWRQTARAVPDKIAVVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQ 81
Cdd:PRK06087 1 KVTLTFNEQRRAAYRQQGYWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 82 LPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQNQLRHLTHIVGVDKLA 161
Cdd:PRK06087 81 LPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 162 PATTALALSQIIDRSEPLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHA 241
Cdd:PRK06087 161 PATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 242 TGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVAR 321
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 322 DCQQRGIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPE 401
Cdd:PRK06087 321 ECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 402 LTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVV 481
Cdd:PRK06087 401 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 482 LKPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTAV 546
Cdd:PRK06087 481 LKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEE 545
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
52-533 |
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: 635.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTV 131
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FKQNRPVDLilplqnqlrhlthivgvdklapattalalsqiidrseplqsdinihGDELAAVLFTSGTEGMPKGVMLTHN 211
Cdd:cd05903 83 FRQFDPAAM----------------------------------------------PDAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDL 291
Cdd:cd05903 117 TLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 292 LCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGI-KLLSIYGSTEsSPHSMVNLGDSTS-RMMNTDGYAATGVEIKI 369
Cdd:cd05903 197 LNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGaKVCSAYGSTE-CPGAVTSITPAPEdRRLYTDGRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 370 VDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDnEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREV 449
Cdd:cd05903 276 VDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 450 EDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKF 529
Cdd:cd05903 355 EDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGA-LLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKF 433
|
....
gi 604198150 530 LLRQ 533
Cdd:cd05903 434 RLRE 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
7-542 |
5.60e-179 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 515.37 E-value: 5.60e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 7 FDAARRKTYRESGYWGDASLGDYWRQTARAVPDKIAVVD---NHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQ 81
Cdd:PRK13295 7 LLPPRRAASIAAGHWHDRTINDDLDACVASCPDKTAVTAvrlGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 82 LPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQNQLRHLTHIVGVDK-- 159
Cdd:PRK13295 87 LPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELPALRHVVVVGGdg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 160 --------LAPA-TTALALSQIIDRSEPlqsdiniHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQD 230
Cdd:PRK13295 167 adsfeallITPAwEQEPDAPAILARLRP-------GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 231 VFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLC 310
Cdd:PRK13295 240 VILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 311 GGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRG 389
Cdd:PRK13295 320 AGAPIPGALVERARAAlGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 390 PNVFMGYLDEPELTarALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPD 469
Cdd:PRK13295 400 CSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 604198150 470 ERLGERSCAYVVLKPPHlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRqdiiERLRQE 542
Cdd:PRK13295 478 ERLGERACAFVVPRPGQ-SLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLR----EMLRGE 545
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
26-542 |
1.71e-176 |
|
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: 505.50 E-value: 1.71e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 26 LGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL 105
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 106 LPAWREAELVWVLNKCQAKIFFAptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsdini 185
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 186 hgdelAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 265
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSM 344
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDnEGWYYSGDLCRMDED 424
Cdd:COG0318 258 VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDED 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 425 GYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFFsRKRVA 504
Cdd:COG0318 337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA-ELDAEELRAFL-RERLA 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 604198150 505 KYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQE 542
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
8-537 |
1.68e-151 |
|
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: 444.59 E-value: 1.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 8 DAARRktYRESGYWGDASLGDYWRQTARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCE 87
Cdd:COG1021 11 EFAAR--YREAGYWRGETLGDLLRRRAERHPDRIAVVDGER-RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 88 FTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQNQLRHLTHIVGVDKLAPATtal 167
Cdd:COG1021 88 FVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGDAGEFT--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 168 ALSQIIDRSEPLqSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGH-ATGFLH 246
Cdd:COG1021 165 SLDALLAAPADL-SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnFPLSSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 247 GVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTcMSGATPFIYDL-LCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQ 325
Cdd:COG1021 244 GVLGVLYAGGTVVLAPDPSPDTAFPLIERERVT-VTALVPPLALLwLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 326 R-GIKLLSIYGSTESsphsMVN---LGDSTSRMMNTDGYA-ATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEP 400
Cdd:COG1021 323 AlGCTLQQVFGMAEG----LVNytrLDDPEEVILTTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 401 ELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYV 480
Cdd:COG1021 399 EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 481 VLKPPhlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIE 537
Cdd:COG1021 479 VPRGE--PLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-537 |
5.37e-139 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 412.27 E-value: 5.37e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVVDNHGAsWTYAALDYAASRLANWLLSQGIQPGDRVAfqLPGW--CEFTLIYLACLKTGAVS 102
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR-TTYAELDERVNRLANALRALGVKKGDRVA--VFDWnsHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLlpAWR--EAELVWVLNKCQAKIFFAPTVFkqnrpVDLILPLQNQLRHLTHIVGV---DKLAPATTALALSQIIDRSE 177
Cdd:PRK06187 84 HPI--NIRlkPEEIAYILNDAEDRVVLVDSEF-----VPLLAAILPQLPTVRTVIVEgdgPAAPLAPEVGEYEELLAAAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 178 PLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHAtgflHGVTAP---FLI 254
Cdd:PRK06187 157 DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHV----HAWGLPylaLMA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 GARSVLLDIFTPEACLTLLAQQRCTcMSGATPFIY-DLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLS 332
Cdd:PRK06187 233 GAKQVIPRRFDPENLLDLIETERVT-FFFAVPTIWqMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKfGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 333 IYGSTESSPHSMVNL----GDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHE--GEEASRGPNVFMGYLDEPELTARA 406
Cdd:PRK06187 312 GYGMTETSPVVSVLPpedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 407 LDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPH 486
Cdd:PRK06187 392 IDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 604198150 487 lSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIE 537
Cdd:PRK06187 471 -TLDAKELRA-FLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-532 |
1.11e-131 |
|
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: 391.54 E-value: 1.11e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 26 LGDYWRQTARAVPDKIAVVdNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL 105
Cdd:cd05936 1 LADLLEEAARRFPDKTALI-FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 106 LPAWREAELVWVLNKCQAKIFFAPTVFKqnrpvdlilplqnqlrhlthivgvDKLAPAttalalsqiidrsEPLQSDINI 185
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT------------------------DLLAAG-------------APLGERVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 186 HGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLN--LTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDI 263
Cdd:cd05936 123 TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMSGAtPFIYDLLC-AVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSP 341
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGV-PTMYIALLnAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNLGDsTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRM 421
Cdd:cd05936 282 VVAVNPLD-GPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 422 DEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRK 501
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGA-SLTEEEIIA-FCRE 437
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 502 RVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05936 438 QLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
31-533 |
5.13e-131 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 391.57 E-value: 5.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:PRK07656 12 ARAARRFGDKEAYVFG-DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFFAPTVF-KQNRPVDLILPlqnQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDE 189
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFlGVDYSATTRLP---ALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 190 LAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEAC 269
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTLLAQQRCTCMSGAtPFIYD-LLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIK-LLSIYGSTESSP-HSMV 345
Cdd:PRK07656 248 FRLIETERITVLPGP-PTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESElGVDiVLTGYGLSEASGvTTFN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 346 NLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDG 425
Cdd:PRK07656 327 RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 426 YIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAK 505
Cdd:PRK07656 407 YLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGA-ELTEEELIA-YCREHLAK 484
|
490 500
....*....|....*....|....*...
gi 604198150 506 YKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK07656 485 YKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
31-528 |
1.35e-127 |
|
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: 380.03 E-value: 1.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:cd17631 2 RRRARRHPDRTALVFG-GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFFaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsdinihgDEL 190
Cdd:cd17631 81 PPEVAYILADSGAKVLF------------------------------------------------------------DDL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACL 270
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 271 TLLAQQRCTCMSGAtPFIYDLLCAVEQ-QPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNLGD 349
Cdd:cd17631 181 DLIERHRVTSFFLV-PTMIQALLQHPRfATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 350 STSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKI 429
Cdd:cd17631 260 DHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 430 TGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYP 509
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA-ELDEDELIA-HCRERLARYKIP 416
|
490
....*....|....*....
gi 604198150 510 ERIVIVEKLPRTASGKVQK 528
Cdd:cd17631 417 KSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-440 |
2.22e-125 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 373.57 E-value: 2.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 30 WRQTARAVPDKIAVVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFFAPTVFKqnrpVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDE 189
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK----LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 190 LAAVLFTSGTEGMPKGVMLTHNNILASERAYC----ARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 265
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 ---PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSP 341
Cdd:pfam00501 237 aldPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNLGDSTS-RMMNTDGYAATGVEIKIVDEDR-NTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLC 419
Cdd:pfam00501 317 VVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLG 396
|
410 420
....*....|....*....|.
gi 604198150 420 RMDEDGYIKITGRKKDIIIRG 440
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-540 |
1.59e-119 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 363.75 E-value: 1.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDNH-GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDqGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLI---LP-LQNQLR---------HLTHIV-----------GV 157
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLyelAPeLATCEPgqlqsarlpELRRVIflgdekhpgmlNF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 158 DKLAPATTALALSQIIDRSEPLQSD--INIHgdelaavlFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMP 235
Cdd:PRK08315 175 DELLALGRAVDDAELAARQATLDPDdpINIQ--------YTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 236 APLGHATGFLHGVTAPFLIGARSVL-LDIFTPEACLTLLAQQRCTCMSGA-TPFIydllcAVEQQPA----DLSSLRFFL 309
Cdd:PRK08315 247 VPLYHCFGMVLGNLACVTHGATMVYpGEGFDPLATLAAVEEERCTALYGVpTMFI-----AELDHPDfarfDLSSLRTGI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 310 CGGTIIPKKVARDCQQR-GIKLLSI-YGSTESSPHS-MVNLGDSTSRMMNTDGYAATGVEIKIVDEDRN-TLPAGHEGEE 385
Cdd:PRK08315 322 MAGSPCPIEVMKRVIDKmHMSEVTIaYGMTETSPVStQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGeTVPRGEQGEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 386 ASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVV 465
Cdd:PRK08315 402 CTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 466 AMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLR 540
Cdd:PRK08315 482 GVPDEKYGEEVCAWIILRPGA-TLTEEDVRD-FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELG 554
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-527 |
4.27e-116 |
|
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: 346.97 E-value: 4.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 ELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLhGVTAPFLIGARSVLLDIFTPEA 268
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSGaTPFIYDLLC-AVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVN 346
Cdd:cd04433 80 ALELIEREKVTILLG-VPTLLARLLkAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 347 LGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTArALDNEGWYYSGDLCRMDEDGY 426
Cdd:cd04433 159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 427 IKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKY 506
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAEELRA-HVRERLAPY 315
|
330 340
....*....|....*....|.
gi 604198150 507 KYPERIVIVEKLPRTASGKVQ 527
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
8-528 |
3.17e-115 |
|
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: 350.09 E-value: 3.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 8 DAARRktYRESGYWGDASLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCE 87
Cdd:cd05920 1 EFARR--YRAAGYWQDEPLGDLLARSAARHPDRIAVVDG-DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 88 FTLIYLACLKTGAVSVPLLPAWREAELVWVLnkcqakiffaptvfKQNRPVDLILPLQNQlrhlthivGVDKLAPATTal 167
Cdd:cd05920 78 FVVLFFALLRLGAVPVLALPSHRRSELSAFC--------------AHAEAVAYIVPDRHA--------GFDHRALARE-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 168 alsqiidrsepLQSDINihgdELAAVLFTSGTEGMPKGVMLTHNNILASERAyCARL-NLTWQDVFLMPAPLGHatGFLH 246
Cdd:cd05920 134 -----------LAESIP----EVALFLLSGGTTGTPKLIPRTHNDYAYNVRA-SAEVcGLDQDTVYLAVLPAAH--NFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 247 ---GVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDC 323
Cdd:cd05920 196 acpGVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 324 QQR-GIKLLSIYGSTESsphsMVN---LGDSTSRMMNTDGYAAT-GVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLD 398
Cdd:cd05920 276 PPVlGCTLQQVFGMAEG----LLNytrLDDPDEVIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 399 EPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCA 478
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 604198150 479 YVVLKPPhlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd05920 432 FVVLRDP--PPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
23-539 |
4.55e-111 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 341.75 E-value: 4.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDNH-GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPL--------QNQLRH--LTHIVGVDKLAPATTA--LAL 169
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELlpglaegqPGALACerLPELRGVVSLAPAPPPgfLAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 170 SQIIDRSEPL------QSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATG 243
Cdd:PRK12583 177 HELQARGETVsrealaERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 244 FLHGVTAPFLIGARSVL-LDIFTPEACLTLLAQQRCTCMSGA-TPFIYDLlcaveQQPA----DLSSLRFFLCGGTIIPK 317
Cdd:PRK12583 257 MVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVpTMFIAEL-----DHPQrgnfDLSSLRTGIMAGAPCPI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 318 KVARDC--QQRGIKLLSIYGSTESSPHSMVN-LGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFM 394
Cdd:PRK12583 332 EVMRRVmdEMHMAEVQIAYGMTETSPVSLQTtAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 395 GYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGE 474
Cdd:PRK12583 412 GYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 475 RSCAYVVLKPPHlSLTLEEvIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERL 539
Cdd:PRK12583 492 EIVAWVRLHPGH-AASEEE-LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEEL 554
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-537 |
2.87e-110 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 338.45 E-value: 2.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVP 104
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGD-RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 105 LLPAWREAELVWVLNKCQAKIFF--------APTVFKQNRPVDLILPLQnqlrhlthIVGVDKLAPATTALALSQIIDRS 176
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLvdpalaptAEAALALLPVDTLILSLV--------LGGREAPGGWLDFADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 177 EPlqsDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAP-FLIG 255
Cdd:PRK08316 163 EP---DVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQ-LDVFLGPyLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 256 ARSVLLDIFTPEACLTLLAQQRCTcMSGATPFIY-DLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLS 332
Cdd:PRK08316 239 ATNVILDAPDPELILRTIEAERIT-SFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERlpGLRFYN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 333 IYGSTESSPHSMVnLG-DSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeG 411
Cdd:PRK08316 318 CYGQTEIAPLATV-LGpEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG-G 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTL 491
Cdd:PRK08316 396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA-TVTE 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 492 EEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIE 537
Cdd:PRK08316 475 DELIA-HCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-533 |
5.59e-104 |
|
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: 321.18 E-value: 5.59e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIA-VVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVW 116
Cdd:cd05926 1 PDAPAlVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 117 VLNKCQAKIFFAPTVfkQNRPVDLILP-LQNQLRHLTHIVGVDKLAPatTALALSQIIDRSEPLQSDINIHGDELAAVLF 195
Cdd:cd05926 81 YLADLGSKLVLTPKG--ELGPASRAASkLGLAILELALDVGVLIRAP--SAESLSNLLADKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQ 275
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 276 QRCTCMSgATPFIYDLLCAVEQQPAD--LSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTS 352
Cdd:cd05926 237 YNATWYT-AVPTIHQILLNRPEPNPEspPPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 353 RMMNTDGyAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGR 432
Cdd:cd05926 316 RKPGSVG-KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 433 KKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFFsRKRVAKYKYPERI 512
Cdd:cd05926 395 IKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-SVTEEELRAFC-RKHLAAFKVPKKV 472
|
490 500
....*....|....*....|.
gi 604198150 513 VIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05926 473 YFVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
34-533 |
5.93e-104 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 323.60 E-value: 5.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVV----DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:COG0365 19 AEGRGDKVALIwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFF-APTVFKQNRPVDL---ILPLQNQLRHLTHIVGVDKLAPATT---ALALSQIIDRSEPLQSD 182
Cdd:COG0365 99 GAEALADRIEDAEAKVLItADGGLRGGKVIDLkekVDEALEELPSLEHVIVVGRTGADVPmegDLDWDELLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 INIHGDELAAVLFTSGTEGMPKGVMLTHNNILAsERAYCAR--LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL 260
Cdd:COG0365 179 EPTDADDPLFILYTSGTTGKPKGVVHTHGGYLV-HAATTAKyvLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 261 LD---IF-TPEACLTLLAQQRCTCMsGATPFIYDLLCAVEQQPA---DLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLS 332
Cdd:COG0365 258 YEgrpDFpDPGRLWELIEKYGVTVF-FTAPTAIRALMKAGDEPLkkyDLSSLRLLGSAGEPLNPEVWEWWYEAvGVPIVD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 333 IYGSTESSpHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRG--PNVFMGYLDEPELTARAL--D 408
Cdd:COG0365 337 GWGQTETG-GIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 409 NEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPH-L 487
Cdd:COG0365 416 FPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVeP 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 488 SLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:COG0365 496 SDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
48-527 |
4.51e-100 |
|
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: 311.07 E-value: 4.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFF 127
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 A-----PTV---FKQNRPVDLILPLQNQLRHLTHIVGVDklapatTALALSQIIDRSEPLqsdiNIHGDELAAVLFTSGT 199
Cdd:cd05911 88 TdpdglEKVkeaAKELGPKDKIIVLDDKPDGVLSIEDLL------SPTLGEEDEDLPPPL----KDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 200 EGMPKGVMLTHNNILASERAYCARL--NLTWQDVFLMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPEACLTLLAQQR 277
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 278 CTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGI--KLLSIYGSTESSPHSMVNLGdsTSRMM 355
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPnaTIKQGYGMTETGGILTVNPD--GDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 356 NTDGYAATGVEIKIVDED-RNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKK 434
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 435 DIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIAFFSrKRVAKYKYPE-RIV 513
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK-PGEKLTEKEVKDYVA-KKVASYKQLRgGVV 472
|
490
....*....|....
gi 604198150 514 IVEKLPRTASGKVQ 527
Cdd:cd05911 473 FVDEIPKSASGKIL 486
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-532 |
3.09e-97 |
|
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: 299.19 E-value: 3.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLL-DIFTPEACLTLL 273
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 274 AQQRCTCMSGA-TPFIyDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSI-YGSTESSPHS-MVNLGD 349
Cdd:cd05917 89 EKEKCTALHGVpTMFI-AELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVmNMKDVTIaYGMTETSPVStQTRTDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 350 STSRMMNTDGYAATGVEIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIK 428
Cdd:cd05917 168 SIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 429 ITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIAFFSRKrVAKYKY 508
Cdd:cd05917 248 IVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK-EGAELTEEDIKAYCKGK-IAHYKV 325
|
330 340
....*....|....*....|....
gi 604198150 509 PERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05917 326 PRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-532 |
6.47e-96 |
|
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: 298.05 E-value: 6.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFfapt 130
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 131 vfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqIIDrseplqsdinihgdeLAAVLFTSGTEGMPKGVMLTH 210
Cdd:cd05934 80 -----------------------------------------VVD---------------PASILYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 211 NNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSgATPFIYD 290
Cdd:cd05934 104 ANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTN-YLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 291 LLCAVEQQPADlSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSpHSMVNLGDSTSRMMnTDGYAATGVEIKI 369
Cdd:cd05934 183 YLLAQPPSPDD-RAHRLRAAYGAPNPPELHEEFEERfGVRLLEGYGMTETI-VGVIGPRDEPRRPG-SIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 370 VDEDRNTLPAGHEGE---EASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISS 446
Cdd:cd05934 260 VDDDGQELPAGEPGElviRGLRGWGFFKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 447 REVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd05934 339 AEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGE-TLDPEELFA-FCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
....*.
gi 604198150 527 QKFLLR 532
Cdd:cd05934 417 AKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
39-533 |
2.88e-94 |
|
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: 294.58 E-value: 2.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 39 DKIAVVDNHGaSWTYAALDYAASRLANWLLSQG-IQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd05941 1 DRIAIVDDGD-SITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIffaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqIIDRseplqsdinihgdelAAVLFTS 197
Cdd:cd05941 80 ITDSEPSL----------------------------------------------VLDP---------------ALILYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQR 277
Cdd:cd05941 99 GTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 278 CTcMSGATPFIYD-LLCAVEQQPAD--------LSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESsphsmvnl 347
Cdd:cd05941 179 IT-VFMGVPTIYTrLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTLEEWEAItGHTLLERYGMTEI-------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 348 GDSTS------RMMNTDGYAATGVEIKIVDEDRN-TLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCR 420
Cdd:cd05941 250 GMALSnpldgeRRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 421 MDEDGYIKITGRKK-DIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEVIAfFS 499
Cdd:cd05941 330 VDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKE-WA 408
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 500 RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05941 409 KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
8-539 |
2.70e-93 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 294.98 E-value: 2.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 8 DAARRktYRESGYWGDASLGDYWrqTARAVPDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCE 87
Cdd:PRK10946 11 EFARR--YREKGYWQDLPLTDIL--TRHAASDAIAVICGE-RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 88 FTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAP---TVFKQNrpvDLILPLQNQLRHLTHIVgvdkLAPAT 164
Cdd:PRK10946 86 FYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADrqhALFSDD---DFLNTLVAEHSSLRVVL----LLNDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 165 TALALSQIIDRSEPLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGH---- 240
Cdd:PRK10946 159 GEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypm 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 241 -ATGFLhGVtapFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVE--QQPADLSSLRFFLCGGTIIPK 317
Cdd:PRK10946 239 sSPGAL-GV---FLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAegGSRAQLASLKLLQVGGARLSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 318 KVARDC-QQRGIKLLSIYGSTESsphsMVN---LGDSTSRMMNTDGYAATGV-EIKIVDEDRNTLPAGHEGEEASRGPNV 392
Cdd:PRK10946 315 TLARRIpAELGCQLQQVFGMAEG----LVNytrLDDSDERIFTTQGRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 393 FMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERL 472
Cdd:PRK10946 391 FRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELM 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 473 GERSCAYVVLKPPHLSLTLEEviafFSRKR-VAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERL 539
Cdd:PRK10946 471 GEKSCAFLVVKEPLKAVQLRR----FLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-527 |
1.53e-90 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 288.01 E-value: 1.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDKIAVVdNHGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVS 102
Cdd:PRK08314 10 TSLFHNLEVSARRYPDKTAIV-FYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLLPAWREAELVWVLNKCQAKIFFAPTVFkqnrpVDLILPLQN--QLRHLthIVG--VDKLaPATTALALSQIIDRSEP 178
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSEL-----APKVAPAVGnlRLRHV--IVAqySDYL-PAEPEIAVPAWLRAEPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 179 LQSDI--------------------NIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPL 238
Cdd:PRK08314 161 LQALApggvvawkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 239 GHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKK 318
Cdd:PRK08314 241 FHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 319 VARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTSRmmNTDGYAATGVEIKIVDEDRNT-LPAGHEGEEASRGPNVFMGY 396
Cdd:PRK08314 321 VAERLKELtGLDYVEGYGLTETMAQTHSNPPDRPKL--QCLGIPTFGVDARVIDPETLEeLPPGEVGEIVVHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 397 LDEPELTARA---LDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLG 473
Cdd:PRK08314 399 WNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 604198150 474 ERSCAYVVLKPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQ 527
Cdd:PRK08314 479 ETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
23-534 |
5.50e-90 |
|
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: 285.67 E-value: 5.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDN-HGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:cd05904 4 DLPLDSVSFLFASAHPSRPALIDAaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIffaptVFKQNRPVDLILPLqnqlrHLTHIVGVDKLAPATTALALSQIIDRSEPLQS 181
Cdd:cd05904 84 VTTANPLSTPAEIAKQVKDSGAKL-----AFTTAELAEKLASL-----ALPVVLLDSAEFDSLSFSDLLFEADEAEPPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 182 DIniHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCAR--LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSV 259
Cdd:cd05904 154 VI--KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGegSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 260 LLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGST 337
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 338 ESSPHSMVNLGDSTSRM-MNTDGYAATGVEIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYS 415
Cdd:cd05904 312 ESTGVVAMCFAPEKDRAkYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 416 GDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVI 495
Cdd:cd05904 392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGS-SLTEDEIM 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 604198150 496 AFFSrKRVAKYKYPERIVIVEKLPRTASGKVqkflLRQD 534
Cdd:cd05904 471 DFVA-KQVAPYKKVRKVAFVDAIPKSPSGKI----LRKE 504
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
22-539 |
3.14e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 285.74 E-value: 3.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPAL-DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFFAptvfkQNRPVDLILPLQNQLRhLTHIVGVD-------------KL-------- 160
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIV-----WDKVAPTVERLRRTTP-LETIVSVNmiaampllqrlalRLpipalrka 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 161 -----APATTALALSQIIDRSEPLQSDINIH----GDELAAVLFTSGTEGMPKGVMLTHNNILASeraycARLNLTW--- 228
Cdd:PRK05605 183 raaltGPAPGTVPWETLVDAAIGGDGSDVSHprptPDDVALILYTSGTTGKPKGAQLTHRNLFAN-----AAQGKAWvpg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 229 ----QDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGaTPFIYD-LLCAVEQQPADLS 303
Cdd:PRK05605 258 lgdgPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPG-VPPLYEkIAEAAEERGVDLS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 304 SLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPhsmVNLGD--STSRMMNTDGYAATGVEIKIVDEDR--NTLP 378
Cdd:PRK05605 337 GVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSP---IIVGNpmSDDRRPGYVGVPFPDTEVRIVDPEDpdETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 379 AGHEGEEASRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPR 458
Cdd:PRK05605 414 DGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 459 IHDACVVAMPDERLGERSCAYVVLKPphlSLTL-EEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIE 537
Cdd:PRK05605 493 VEDAAVVGLPREDGSEEVVAAVVLEP---GAALdPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLE 569
|
..
gi 604198150 538 RL 539
Cdd:PRK05605 570 KL 571
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
50-531 |
5.93e-87 |
|
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: 275.13 E-value: 5.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 50 SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKcqakiffap 129
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILND--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 tvfkqnrpvdlilplqnqlrhlthivgvdklAPATTALALSQIidrseplqsdinihgDELAAVLFTSGTEGMPKGVMLT 209
Cdd:cd05935 72 -------------------------------SGAKVAVVGSEL---------------DDLALIPYTSGTTGLPKGCMHT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 210 HNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIY 289
Cdd:cd05935 106 HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 290 DLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTSRmmNTDGYAATGVEIK 368
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKL--QCLGIP*FGVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 369 IVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARA---LDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENI 444
Cdd:cd05935 264 VIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 445 SSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASG 524
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
....*..
gi 604198150 525 KVQKFLL 531
Cdd:cd05935 424 KILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
29-528 |
3.49e-86 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 275.20 E-value: 3.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 29 YW-RQTARAVPDKIAVVDNHgASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLl 106
Cdd:PRK06839 6 YWiEKRAYLHPDRIAIITEE-EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 107 pAWR--EAELVWVLNKCQAKIFFAPTVFkqnrpvdlilplQNQLRHLTHIVGVdklAPATTALALSQIIDRSEPLQSDIN 184
Cdd:PRK06839 84 -NIRltENELIFQLKDSGTTVLFVEKTF------------QNMALSMQKVSYV---QRVISITSLKEIEDRKIDNFVEKN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 185 ihGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIF 264
Cdd:PRK06839 148 --ESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 265 TPEACLTLLAQQRCTCMSGaTPFIYD-LLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHS 343
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMG-VPTIHQaLINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 344 MVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDE 423
Cdd:PRK06839 305 FMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 424 DGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRV 503
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS-VLIEKDVIE-HCRLFL 461
|
490 500
....*....|....*....|....*
gi 604198150 504 AKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQK 486
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-533 |
3.45e-85 |
|
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: 273.35 E-value: 3.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAfqlpgwcefTL---------IYLACLKTGAVSVPLLPAWREAELVWVLNKCQ 122
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVA---------TLawnthrhleLYYAVPGMGAVLHTINPRLFPEQIAYIINHAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 123 AKIFFAPTVFkqnrpVDLILPLQNQLRHLTHIV----GVDKLAPAT-TALALSQIIDRSEPLQSDINIHGDELAAVLFTS 197
Cdd:cd12119 98 DRVVFVDRDF-----LPLLEAIAPRLPTVEHVVvmtdDAAMPEPAGvGVLAYEELLAAESPEYDWPDFDENTAAAICYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCAR--LNLTWQDVFLMPAPLGHATGFlhGVT-APFLIGARSVLLDIF-TPEACLTLL 273
Cdd:cd12119 173 GTTGNPKGVVYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPMFHVNAW--GLPyAAAMVGAKLVLPGPYlDPASLAELI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 274 AQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNLgdSTSR 353
Cdd:cd12119 251 EREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVAR--PPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 MMNTD-----------GYAATGVEIKIVDEDRNTLPagHEGEEAS----RGPNVFMGYLDEPElTARALDNEGWYYSGDL 418
Cdd:cd12119 329 HSNLSedeqlalrakqGRPVPGVELRIVDDDGRELP--WDGKAVGelqvRGPWVTKSYYKNDE-ESEALTEDGWLRTGDV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 419 CRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFF 498
Cdd:cd12119 406 ATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGA-TVTAEELLEFL 484
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 499 sRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd12119 485 -ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
34-534 |
4.76e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 271.27 E-value: 4.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK07786 27 ALMQPDAPAL-RFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKIFFAPTVfkqnrpvdlILPLQNQLRHLT---HIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDEL 190
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA---------LAPVATAVRDIVpllSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNiLASERAYCARLN--LTWQDVFLMPAPLGHATGFlhGVTAPFL-IGARSVL--LDIFT 265
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNgaDINSDVGFVGVPLFHIAGI--GSMLPGLlLGAPTVIypLGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSgATPFIYDLLCAVEQ-QPADLSsLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPH 342
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIF-LVPAQWQAVCAEQQaRPRDLA-LRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMD 422
Cdd:PRK07786 332 TCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 423 EDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEVIAFFSrKR 502
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLT-DR 489
|
490 500 510
....*....|....*....|....*....|..
gi 604198150 503 VAKYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
30-537 |
1.28e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 268.37 E-value: 1.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 30 W-RQTARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPA 108
Cdd:PRK03640 7 WlKQRAFLTPDRTAIEFEEK-KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 109 WREAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQnqlrhlthivgvdklapattalALSQIIDRSEPLQSDIniHGD 188
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFA----------------------ELMNGPKEEAEIQEEF--DLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 ELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGF---LHGVtapfLIGARSVLLDIFT 265
Cdd:PRK03640 142 EVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLsilMRSV----IYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADlSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTES------ 339
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETasqivt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 -SPHSMVN-LGDStsrmmntdGYAATGVEIKIVDeDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGD 417
Cdd:PRK03640 297 lSPEDALTkLGSA--------GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 418 LCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLkppHLSLTLEEVIAf 497
Cdd:PRK03640 367 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK---SGEVTEEELRH- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 604198150 498 FSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIE 537
Cdd:PRK03640 443 FCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-532 |
1.02e-81 |
|
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: 263.39 E-value: 1.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVdnHGASW-TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:cd12118 11 ERAAAVYPDRTSIV--YGDRRyTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFFAPTVFKQNrpvdlilplqnqlrhlthivgvDKLAPATTALALSQIIDRSEPLqsdinihgde 189
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREFEYE----------------------DLLAEGDPDFEWIPPADEWDPI---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 190 laAVLFTSGTEGMPKGVMLTHNNilaserAYCARLN--LTWQ----DVFLMPAPLGHATG--FLHGVTApflIGARSVLL 261
Cdd:cd12118 137 --ALNYTSGTTGRPKGVVYHHRG------AYLNALAniLEWEmkqhPVYLWTLPMFHCNGwcFPWTVAA---VGGTNVCL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 262 DIFTPEACLTLLAQQRCTCMSGAtPFIYDLLCavEQQPADLSSLR---FFLCGGTIIPKKVARDCQQRGIKLLSIYGSTE 338
Cdd:cd12118 206 RKVDAKAIYDLIEKHKVTHFCGA-PTVLNMLA--NAPPSDARPLPhrvHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 SSPHSMV--------NLGDSTSRMMNtdgyAATGVEIKIVDE----DRNTL-PAGHEGEE----ASRGPNVFMGYLDEPE 401
Cdd:cd12118 283 TYGPATVcawkpewdELPTEERARLK----ARQGVRYVGLEEvdvlDPETMkPVPRDGKTigeiVFRGNIVMKGYLKNPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 402 LTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVV 481
Cdd:cd12118 359 ATAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 604198150 482 LKPPHlSLTLEEVIAfFSRKRVAKYKYPeRIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd12118 438 LKEGA-KVTEEEIIA-FCREHLAGFMVP-KTVVFGELPKTSTGKIQKFVLR 485
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
22-542 |
2.52e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 264.60 E-value: 2.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PRK06178 31 GERPLTEYLRAWARERPQRPAI-IFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIF-----FAPTVfKQNRPvdlilplQNQLRHLTHIVGVDKLAPATT----------A 166
Cdd:PRK06178 110 HVPVSPLFREHELSYELNDAGAEVLlaldqLAPVV-EQVRA-------ETSLRHVIVTSLADVLPAEPTlplpdslrapR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 167 LALSQIID-----RSEPLQSDINIHG-DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCA-RLNLTWQDVFLMPAPLG 239
Cdd:PRK06178 182 LAAAGAIDllpalRACTAPVPLPPPAlDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAvAVVGGEDSVFLSFLPEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 240 HATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGatpfIYDLLCAVEQQPA----DLSSLRFFLCGGTIi 315
Cdd:PRK06178 262 WIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVM----LVDNAVELMDHPRfaeyDLSSLRQVRVVSFV- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 316 pKKVARDCQQR------GIKLLSIYGSTESsphsmvNLGDSTSRMMNTD-----------GYAATGVEIKIVDEDRN-TL 377
Cdd:PRK06178 337 -KKLNPDYRQRwraltgSVLAEAAWGMTET------HTCDTFTAGFQDDdfdllsqpvfvGLPVPGTEFKICDFETGeLL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 378 PAGHEGEEASRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHP 457
Cdd:PRK06178 410 PLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 458 RIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPErIVIVEKLPRTASGKVQKfllrQDIIE 537
Cdd:PRK06178 489 AVLGSAVVGRPDPDKGQVPVAFVQLKPGA-DLTAAALQA-WCRENMAVYKVPE-IRIVDALPMTATGKVRK----QDLQA 561
|
....*
gi 604198150 538 RLRQE 542
Cdd:PRK06178 562 LAEEL 566
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-533 |
3.92e-81 |
|
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: 259.59 E-value: 3.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 50 SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWvlnkcqakiffap 129
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAF------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 tvfkqnrpvdlilplqnQLRhlthivgvdklapattalalsqiidrseplqsDINIHGDELAAVLFTSGTEGMPKGVMLT 209
Cdd:cd05912 68 -----------------QLK--------------------------------DSDVKLDDIATIMYTSGTTGKPKGVQQT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 210 HNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIY 289
Cdd:cd05912 99 FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 290 DLLcavEQQPADLS-SLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSM-VNLGDSTSRMmNTDGYAATGVEI 367
Cdd:cd05912 178 RLL---EILGEGYPnNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVtLSPEDALNKI-GSAGKPLFPVEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 368 KIVDEDRNtlPAGHeGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSR 447
Cdd:cd05912 254 KIEDDGQP--PYEV-GEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 448 EVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlsLTLEEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQ 527
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP---ISEEELIAYC-SEKLAKYKVPKKIYFVDELPRTASGKLL 405
|
....*.
gi 604198150 528 KFLLRQ 533
Cdd:cd05912 406 RHELKQ 411
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
26-538 |
4.95e-81 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 262.67 E-value: 4.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 26 LGDYWRQTARAVPDKIAVVdnHGA-SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVP 104
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALV--WGDrSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 105 ----LLPAwreaELVWVLNKCQAKIFFAPTVFKQNrpVDLILPLQNQLRHLTHIvGVDKLAPATTALALSQIIDRSEPLQ 180
Cdd:PRK07470 87 tnfrQTPD----EVAYLAEASGARAMICHADFPEH--AAAVRAASPDLTHVVAI-GGARAGLDYEALVARHLGARVANAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 181 SDinihGDELAAVLFTSGTEGMPKGVMLTH-------NNILASeraycarL--NLTWQDVFLMPAPLGHATGfLHGVTAp 251
Cdd:PRK07470 160 VD----HDDPCWFFFTSGTTGRPKAAVLTHgqmafviTNHLAD-------LmpGTTEQDASLVVAPLSHGAG-IHQLCQ- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 252 FLIGARSVLL--DIFTPEACLTLLAQQRCTCMSgATPFIYDLLC---AVEQqpADLSSLRFFLCGGTIIpkkvARDCQQR 326
Cdd:PRK07470 227 VARGAATVLLpsERFDPAEVWALVERHRVTNLF-TVPTILKMLVehpAVDR--YDHSSLRYVIYAGAPM----YRADQKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 -----GIKLLSIYGSTESS------PHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMG 395
Cdd:PRK07470 300 alaklGKVLVQYFGLGEVTgnitvlPPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 396 YLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGER 475
Cdd:PRK07470 380 YYNNPEANAKAFRD-GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEV 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 604198150 476 SCAYVVLKPPHlSLTLEEVIAFFSRKrVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIER 538
Cdd:PRK07470 459 GVAVCVARDGA-PVDEAELLAWLDGK-VARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
33-533 |
5.95e-81 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 261.73 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 33 TARAVPDKIAVVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREA 112
Cdd:PRK07514 11 AAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 113 ELVWVLNKCQAKIFF-APTVFKQNRPVdlilplqNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDinihGDELA 191
Cdd:PRK07514 91 ELDYFIGDAEPALVVcDPANFAWLSKI-------AAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVPRG----ADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNILASERAycarLNLTW----QDVFLMPAPLGHATGF---LHGVtapFLIGARSVLLDIF 264
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALT----LVDYWrftpDDVLIHALPIFHTHGLfvaTNVA---LLAGASMIFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 265 TPEACLTLLAqqRCTCMSGATPFIYDLLcaveQQPA---DL-SSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTE- 338
Cdd:PRK07514 233 DPDAVLALMP--RATVMMGVPTFYTRLL----QEPRltrEAaAHMRLFISGSAPLLAETHREFQERtGHAILERYGMTEt 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 ----SSPHSmvnlGDstsRMMNTDGYAATGVEIKIVDEDRN-TLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWY 413
Cdd:PRK07514 307 nmntSNPYD----GE---RRAGTVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 414 YSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEE 493
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA-ALDEAA 458
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 604198150 494 VIAFFSRkRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK07514 459 ILAALKG-RLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
189-528 |
7.77e-81 |
|
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: 255.89 E-value: 7.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 ELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEA 268
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSGAtPFIYDLLCAVEQQP-ADLSSLRFFLCGGTIIPKKVARDCQQR-GIK-LLSIYGSTESSPHSMV 345
Cdd:cd17638 81 ILEAIERERITVLPGP-PTLFQSLLDHPGRKkFDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 346 NLGDSTSRMMNTDGYAATGVEIKIVDEdrntlpagheGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDG 425
Cdd:cd17638 160 RPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 426 YIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhLSLTLEEVIAfFSRKRVAK 505
Cdd:cd17638 230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTEEDVIA-WCRERLAN 307
|
330 340
....*....|....*....|...
gi 604198150 506 YKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17638 308 YKVPRFVRFLDELPRNASGKVMK 330
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
28-532 |
2.03e-80 |
|
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: 260.76 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 28 DYWRQTARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLP 107
Cdd:cd05959 8 LVDLNLNEGRGDKTAFIDDAG-SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 108 AWREAELVWVLNKCQAKIFFAPTVFKQNrpvdLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHG 187
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPV----LAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYcAR--LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIF- 264
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVHLHADIYWTAELY-ARnvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 265 TPEACLTLLAQQRCTCMSGAtPFIYDLLCAVEQQPA-DLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPH 342
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGV-PTLYAAMLAAPNLPSrDLSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SMVNLGDSTSrmMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEgWYYSGDLCRMD 422
Cdd:cd05959 321 FLSNRPGRVR--YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGDKYVRD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 423 EDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLT-LEEVIAFFSRK 501
Cdd:cd05959 398 DDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaLEEELKEFVKD 477
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 502 RVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05959 478 RLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
22-532 |
8.42e-80 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 259.23 E-value: 8.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVV--DNHG--ASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLK 97
Cdd:PRK08008 5 GGQHLRQMWDDLADVYGHKTALIfeSSGGvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 98 TGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFkqnrpvdliLPLQNQLRH-----LTHIVGVDKLAPATT-ALALSQ 171
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQF---------YPMYRQIQQedatpLRHICLTRVALPADDgVSSFTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 172 IIDRSEP-LQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTA 250
Cdd:PRK08008 156 LKAQQPAtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 251 PFLIGARSVLLDIFTPEACLTLLAQQRCT---CMsgatPFIYDLLCAVEQQPAD----LSSLRFFLCggtiIPKKVARDC 323
Cdd:PRK08008 236 AFSAGATFVLLEKYSARAFWGQVCKYRATiteCI----PMMIRTLMVQPPSANDrqhcLREVMFYLN----LSDQEKDAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 324 QQR-GIKLLSIYGSTESsphsMVNL-GDSTS--RMMNTDGYAATGVEIKIVDEDRNTLPAGHEGE---EASRGPNVFMGY 396
Cdd:PRK08008 308 EERfGVRLLTSYGMTET----IVGIiGDRPGdkRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEiciKGVPGKTIFKEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 397 LDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERS 476
Cdd:PRK08008 384 YLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 477 CAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK08008 464 KAFVVLNEGE-TLSEEEFFA-FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-532 |
2.17e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 254.73 E-value: 2.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVD-NHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLlpAWR-- 110
Cdd:PRK09088 5 ARLQPQRLAAVDlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPL--NWRls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPlqnqlrhlTHIVGVDKLAPATTALalsqiIDRSEPlqsdinihgdel 190
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDDAVAAGRTDVEDLA--------AFIASADALEPADTPS-----IPPERV------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACL 270
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 271 TLLAQQRCtcmsGATPF--IYDLLCAVEQQP----ADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTES-SPHS 343
Cdd:PRK09088 218 GRLGDPAL----GITHYfcVPQMAQAFRAQPgfdaAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 344 MVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDE 423
Cdd:PRK09088 294 MSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 424 DGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIAFFSRkRV 503
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPA-DGAPLDLERIRSHLST-RL 451
|
490 500
....*....|....*....|....*....
gi 604198150 504 AKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK09088 452 AKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-532 |
1.82e-75 |
|
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: 245.32 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIffapt 130
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 131 vfkqnrpvdlilplqnqlrhlthIVgvdklapaTTAlalsqiidrseplqsdinihgDELAAVLFTSGTEGMPKGVMLTH 210
Cdd:cd05972 76 -----------------------IV--------TDA---------------------EDPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 211 NNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPEACLTLLAQQRCTCMSGAtPFI 288
Cdd:cd05972 104 SYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGP-PTA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 289 YDLLCAVEQQPADLSSLRFFLCGG-TIIPKKVARDCQQRGIKLLSIYGSTESSphsmVNLGDSTSRMMN--TDGYAATGV 365
Cdd:cd05972 183 YRMLIKQDLSSYKFSHLRLVVSAGePLNPEVIEWWRAATGLPIRDGYGQTETG----LTVGNFPDMPVKpgSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 366 EIKIVDEDRNTLPAGHEGEEASRGPNV--FMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGEN 443
Cdd:cd05972 259 DVAIIDDDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 444 ISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLK---PPHLSLTLEevIAFFSRKRVAKYKYPERIVIVEKLPR 520
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTsgyEPSEELAEE--LQGHVKKVLAPYKYPREIEFVEELPK 415
|
490
....*....|..
gi 604198150 521 TASGKVQKFLLR 532
Cdd:cd05972 416 TISGKIRRVELR 427
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
192-526 |
2.43e-74 |
|
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: 239.09 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPEACLT 271
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 272 LLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRffLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSphSMVNLGDST 351
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR--HVLGLDAPETIQRFEETTGATFWSLYGQTETS--GLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 352 SRMmNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITG 431
Cdd:cd17637 159 ERP-GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 432 RK--KDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFFSrKRVAKYKYP 509
Cdd:cd17637 237 RKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA-TLTADELIEFVG-SRIARYKKP 314
|
330
....*....|....*..
gi 604198150 510 ERIVIVEKLPRTASGKV 526
Cdd:cd17637 315 RYVVFVEALPKTADGSI 331
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
31-538 |
3.86e-74 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 247.56 E-value: 3.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAV-----VDNHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK07529 32 SRAAARHPDAPALsflldADPLDRPetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 --PLLPAWREAELvwvLNKCQAKIFFAPTVFKQNRPVDLILPLQNQLRHLTHIVGVD--KLAPATTALALS--------Q 171
Cdd:PRK07529 112 inPLLEPEQIAEL---LRAAGAKVLVTLGPFPGTDIWQKVAEVLAALPELRTVVEVDlaRYLPGPKRLAVPlirrkahaR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 172 IID-----RSEP---LQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILAseRAYCARLNLTWQ--DVFLMPAPLGHA 241
Cdd:PRK07529 189 ILDfdaelARQPgdrLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA--NAWLGALLLGLGpgDTVFCGLPLFHV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 242 TGFLHGVTAPFLIGARSVLLdifTP-----EACL----TLLAQQRCTCMSGaTPFIYDLLCAVEQQPADLSSLRFFLCGG 312
Cdd:PRK07529 267 NALLVTGLAPLARGAHVVLA---TPqgyrgPGVIanfwKIVERYRINFLSG-VPTVYAALLQVPVDGHDISSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 313 TIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVN-------LGDSTSRMMNTDgyaatgVEIKIVDEDRNTL---PAGH 381
Cdd:PRK07529 343 APLPVEVFRRFEAAtGVRIVEGYGLTEATCVSSVNppdgerrIGSVGLRLPYQR------VRVVILDDAGRYLrdcAVDE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 382 EGEEASRGPNVFMGYLdEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHD 461
Cdd:PRK07529 417 VGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVAL 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 462 ACVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIER 538
Cdd:PRK07529 496 AAAVGRPDAHAGELPVAYVQLK-PGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALRRDAIRR 571
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
22-465 |
3.92e-74 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 246.55 E-value: 3.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVVDNHGASW---TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKT 98
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIWqslTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 99 GAVSVPLLPAWREAELVWVLNKCQAKIFFAptvfkQNRP-VDLILPLQNQLRHLTHIVGVDKLAPA--TTALALSQIIDR 175
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFV-----EDQEqLDKLLEVRDELPSLRHIVVLDPRGLRddPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 176 SEPLQSDI-------NIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHA------- 241
Cdd:COG1022 164 GREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVfertvsy 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 242 TGFLHGVTAPFLIGARSVLLDI--FTPeaclTLL-------------AQQRctcMSGATPF---IYDLLCAV--EQQPAD 301
Cdd:COG1022 244 YALAAGATVAFAESPDTLAEDLreVKP----TFMlavprvwekvyagIQAK---AEEAGGLkrkLFRWALAVgrRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 302 LSS-----------------------------LRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNLGDSts 352
Cdd:COG1022 317 LAGkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGD-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 353 RMMNTDGYAATGVEIKIvDEDrntlpagheGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGR 432
Cdd:COG1022 395 NRIGTVGPPLPGVEVKI-AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGR 464
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 433 KKDIII-RGGENISSREVEDILLQHPRIHDACVV 465
Cdd:COG1022 465 KKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
38-526 |
6.89e-73 |
|
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: 238.97 E-value: 6.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd05930 1 PDAVAVVDGDQ-SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIffaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqIIDrseplqsdiniHGDELAAVLFTS 197
Cdd:cd05930 80 LEDSGAKL----------------------------------------------VLT-----------DPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHAtGFLHGVTAPFLIGARSVLLD---IFTPEACLTLLA 274
Cdd:cd05930 103 GSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPeevRKDPEALADLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSgATPFIYDLLcAVEQQPADLSSLRFFLCGGTIIPKKVARD--CQQRGIKLLSIYGSTESSphsmvnlGDSTS 352
Cdd:cd05930 182 EEGITVLH-LTPSLLRLL-LQELELAALPSLRLVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEAT-------VDATY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 353 ---RMMNTD------GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR---ALDNEGW---YYSGD 417
Cdd:cd05930 253 yrvPPDDEEdgrvpiGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAErfvPNPFGPGermYRTGD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 418 LCRMDEDGYIKITGRKKDII-IRG-----GenissrEVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTL 491
Cdd:cd05930 333 LVRWLPDGNLEFLGRIDDQVkIRGyrielG------EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG-ELDE 405
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 492 EEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd05930 406 EELRAHL-AERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-532 |
1.09e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 240.66 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PRK06188 10 SGATYGHLLVSALKRYPDRPALVLG-DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFfaptVFKQNRPVDLILPLQNQLRHLTHIVGvdkLAPATTALALSQIIDRSEPLQS 181
Cdd:PRK06188 89 RTALHPLGSLDDHAYVLEDAGISTL----IVDPAPFVERALALLARVPSLKHVLT---LGPVPDGVDLLAAAAKFGPAPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 182 DINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLhgVTAPFLIGARSVLL 261
Cdd:PRK06188 162 VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPTLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 262 DIFTPEACLTLLAQQRCTcmsgATPF----IYDLLCAVEQQPADLSSLRFFLCGGT-IIPKKVARDCQQRGIKLLSIYGS 336
Cdd:PRK06188 240 AKFDPAEVLRAIEEQRIT----ATFLvptmIYALLDHPDLRTRDLSSLETVYYGASpMSPVRLAEAIERFGPIFAQYYGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 337 TES-SPHSMVNLGD---STSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGW 412
Cdd:PRK06188 316 TEApMVITYLRKRDhdpDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 413 YYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLE 492
Cdd:PRK06188 395 LHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGA-AVDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 604198150 493 EVIAFF-SRKRVAkyKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK06188 474 ELQAHVkERKGSV--HAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
50-531 |
1.99e-72 |
|
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: 237.88 E-value: 1.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 50 SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAP 129
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 TvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsdinihGDELAAVLFTSGTEGMPKGVMLT 209
Cdd:cd05907 85 D--------------------------------------------------------PDDLATIIYTSGTTGRPKGVMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 210 HNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLdiFTPEACLTLLAQQRCTCMSGAtPFIY 289
Cdd:cd05907 109 HRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFA--SSAETLLDDLSEVRPTVFLAV-PRVW 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 290 DLLCA---VEQQP---------ADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNLGDSTSrmMNT 357
Cdd:cd05907 186 EKVYAaikVKAVPglkrklfdlAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNR--IGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 358 DGYAATGVEIKIVDEdrntlpagheGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDII 437
Cdd:cd05907 264 VGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 438 I-RGGENISSREVEDILLQHPRIHDACVVA----------MPDERLGERSCAYVVLKPPHLS--LTLEEVIAFFsRKRVA 504
Cdd:cd05907 334 ItSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEALEAWAEEHGIAYTDVAelAANPAVRAEI-EAAVE 412
|
490 500
....*....|....*....|....*..
gi 604198150 505 KykyperivIVEKLPRTASgkVQKFLL 531
Cdd:cd05907 413 A--------ANARLSRYEQ--IKKFLL 429
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
28-533 |
2.77e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 240.23 E-value: 2.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 28 DYWRQTARAVPDKIAVVdnHGA---SW--TYAAldyaASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVS 102
Cdd:PRK08162 22 SFLERAAEVYPDRPAVI--HGDrrrTWaeTYAR----CRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPL---LPAwreAELVWVLNKCQAKIFFAPTVFkqnrpVDLILPLQNQLRHLTHIVgVDKLAPATTALALSQIIDRSEPL 179
Cdd:PRK08162 96 NTLntrLDA---ASIAFMLRHGEAKVLIVDTEF-----AEVAREALALLPGPKPLV-IDVDDPEYPGGRFIGALDYEAFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QS-----DINIHGDELAAVL--FTSGTEGMPKGVMLTHNNilaserAYCARLN--LTWQ----DVFLMPAPLGHATGFLH 246
Cdd:PRK08162 167 ASgdpdfAWTLPADEWDAIAlnYTSGTTGNPKGVVYHHRG------AYLNALSniLAWGmpkhPVYLWTLPMFHCNGWCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 247 gvtaPFLIGAR---SVLLDIFTPEACLTLLAQQRCTCMSGAtPFIYDLLC-AVEQQPADLSSLRFFLCGGTIIPKKVARD 322
Cdd:PRK08162 241 ----PWTVAARagtNVCLRKVDPKLIFDLIREHGVTHYCGA-PIVLSALInAPAEWRAGIDHPVHAMVAGAAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 323 CQQRGIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAA----TGVEIKIVDE----DRNTL---PAGHE--GEEASRG 389
Cdd:PRK08162 316 MEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQlkarQGVRYPLQEGvtvlDPDTMqpvPADGEtiGEIMFRG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 390 pNVFM-GYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMP 468
Cdd:PRK08162 396 -NIVMkGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKP 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 469 DERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEkLPRTASGKVQKFLLRQ 533
Cdd:PRK08162 474 DPKWGEVPCAFVELKDGA-SATEEEIIA-HCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLRE 535
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
52-528 |
9.25e-72 |
|
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: 235.81 E-value: 9.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTV 131
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FKqnrpvdlilplqnqlrhlthivgvdklAPATTALALSQIidrSEPLQSDINIH----GDELAAVLFTSGTEGMPKGVM 207
Cdd:TIGR01923 81 LE---------------------------EKDFQADSLDRI---EAAGRYETSLSasfnMDQIATLMFTSGTTGKPKAVP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 208 LTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTpeACLTLLAQQRCTCMSGATPF 287
Cdd:TIGR01923 131 HTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 288 IYDLLcaveQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSphsmvnlgdSTSRMMNTDGYAAT---- 363
Cdd:TIGR01923 208 LNRLL----DEGGHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETC---------SQVTTATPEMLHARpdvg 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 364 ----GVEIKIvdedRNTLPAGHeGEEASRGPNVFMGYLDEPELTArALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIR 439
Cdd:TIGR01923 275 rplaGREIKI----KVDNKEGH-GEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 440 GGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlsLTLEEVIAFFSrKRVAKYKYPERIVIVEKLP 519
Cdd:TIGR01923 349 GGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD---ISQAKLIAYLT-EKLAKYKVPIAFEKLDELP 424
|
....*....
gi 604198150 520 RTASGKVQK 528
Cdd:TIGR01923 425 YNASGKILR 433
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
31-534 |
9.07e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 236.36 E-value: 9.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:PRK07788 56 AHAARRAPDRAALIDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFFAPTVFkqnrpVDLILPLQNQL-RHLTHIVGVDKLAPAT-TALALSQIIDR--SEPLQSdINIH 186
Cdd:PRK07788 135 GPQLAEVAAREGVKALVYDDEF-----TDLLSALPPDLgRLRAWGGNPDDDEPSGsTDETLDDLIAGssTAPLPK-PPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 187 GdelAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTP 266
Cdd:PRK07788 209 G---GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMAL-GSTVVLRRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLTLLAQQRCTCMSgATPF----IYDLLCAVEQQPaDLSSLRF-FLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSP 341
Cdd:PRK07788 285 EATLEDIAKHKATALV-VVPVmlsrILDLGPEVLAKY-DTSSLKIiFVSGSALSPELATRALEAFGPVLYNLYGSTEVAF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNLGDsTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLD--EPELTaraldnEGWYYSGDLC 419
Cdd:PRK07788 363 ATIATPED-LAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgrDKQII------DGLLSSGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 420 RMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAFFs 499
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGA-ALDEDAIKDYV- 513
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 500 RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:PRK07788 514 RDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
34-535 |
9.26e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 235.17 E-value: 9.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVdNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK06145 12 ARRTPDRAALV-YRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKIFFAPTVFKQnrPVDLILPlqnqlrhlthIVGVDKLAPATTalalSQIIDRSEPLQSDINIHGDELAAV 193
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDA--IVALETP----------KIVIDAAAQADS----RRLAQGGLEIPPQAAVAPTDLVRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGF-LHGVTAPFLIGARSVLLDiFTPEACLTL 272
Cdd:PRK06145 155 MYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHRE-FDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 273 LAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQ--RGIKLLSIYGSTES-SPHSMVNLGD 349
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRvfTRARYIDAYGLTETcSGDTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 350 STSRMMNTdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKI 429
Cdd:PRK06145 314 EIEKIGST-GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 430 TGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEvIAFFSRKRVAKYKYP 509
Cdd:PRK06145 392 TDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA-TLTLEA-LDRHCRQRLASFKVP 469
|
490 500
....*....|....*....|....*.
gi 604198150 510 ERIVIVEKLPRTASGKVQKFLLRQDI 535
Cdd:PRK06145 470 RQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
50-532 |
3.89e-70 |
|
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: 231.58 E-value: 3.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 50 SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFap 129
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 tvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsdinIHGDELAAVLFTSGTEGMPKGVMLT 209
Cdd:cd05919 88 -------------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 210 HNNILASERAYCAR-LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIF-TPEACLTLLAQQRCTCMSGATPF 287
Cdd:cd05919 113 HRDPLLFADAMAREaLGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 288 IYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVA-RDCQQRGIKLLSIYGSTESSPHSMVNLGDSTSrmMNTDGYAATGVE 366
Cdd:cd05919 193 YANLLDSCAGSPDALRSLRLCVSAGEALPRGLGeRWMEHFGGPILDGIGATEVGHIFLSNRPGAWR--LGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 367 IKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPElTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISS 446
Cdd:cd05919 271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 447 REVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHL-SLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGK 525
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
....*..
gi 604198150 526 VQKFLLR 532
Cdd:cd05919 430 LQRFKLR 436
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
31-533 |
1.13e-69 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 233.50 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAvPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:PRK06155 29 RQAERY-PDRPLLVFG-GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFFAPTVFkqnrpVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIidrsEPLQSD-----INI 185
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAAL-----LAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTA----PLPPLDapapaAAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 186 HGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLDIFT 265
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFH-TNALNAFFQALLAGATYVLEPRFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTC--MSGAtpfIYDLLCAVEQQPAD-LSSLRFFLCGGTiiPKKVARDCQQR-GIKLLSIYGSTESSp 341
Cdd:PRK06155 257 ASGFWPAVRRHGATVtyLLGA---MVSILLSQPARESDrAHRVRVALGPGV--PAALHAAFRERfGVDLLDGYGSTETN- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 hsMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRG--PNVFM-GYLDEPELTARALDNEgWYYSGDL 418
Cdd:PRK06155 331 --FVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFAFAtGYFGMPEKTVEAWRNL-WFHTGDR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 419 CRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDErLGERSCAYVVLKPPHLSLTLEEVIAfF 498
Cdd:PRK06155 408 VVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE-LGEDEVMAAVVLRDGTALEPVALVR-H 485
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 499 SRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK06155 486 CEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
48-532 |
1.50e-68 |
|
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: 227.36 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQakif 126
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 127 faptvfkqnrpvdlilplqnqlrhLTHIVGVDKLApattalalsqiidrseplqsdiniHGDELAAVLFTSGTEGMPKGV 206
Cdd:cd05958 84 ------------------------ITVALCAHALT------------------------ASDDICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 207 MLTHNNILASERAYCAR-LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCT-CMSGA 284
Cdd:cd05958 116 MHFHRDPLASADRYAVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTvLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 285 TPFIYDLLCAVEQQPaDLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSpHSMVNLGDSTSRMMNTdGYAAT 363
Cdd:cd05958 196 TAYRAMLAHPDAAGP-DLSSLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEMF-HIFISARPGDARPGAT-GKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 364 GVEIKIVDEDRNTLPAGHEGEEASRGPNVFMgYLDEPelTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGEN 443
Cdd:cd05958 273 GYEAKVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADK--RQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 444 ISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHL-SLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTA 522
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
490
....*....|
gi 604198150 523 SGKVQKFLLR 532
Cdd:cd05958 430 TGKLQRFALR 439
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
41-532 |
1.38e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 224.01 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 41 IAVVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLlpAWR--EAELVWVL 118
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--NWHltAAEIAYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 119 NKCQAKIFFA-PTVFKQNRPVDLILPLQNQLRHLTH--IVGVDKLAPATTALALSQIIDRSEplqsdinihGDELaavLF 195
Cdd:PRK08276 80 DDSGAKVLIVsAALADTAAELAAELPAGVPLLLVVAgpVPGFRSYEEALAAQPDTPIADETA---------GADM---LY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVM--LTHNNILASE----RAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPEAC 269
Cdd:PRK08276 148 SSGTTGRPKGIKrpLPGLDPDEAPgmmlALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALAL-GGTVVVMEKFDAEEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTLLAQQRCTCMSGA-TPFIyDLLCAVEQQPA--DLSSLRFFLCGGTIIPKKVardcQQRGIK-----LLSIYGSTESSP 341
Cdd:PRK08276 227 LALIERYRVTHSQLVpTMFV-RMLKLPEEVRAryDVSSLRVAIHAAAPCPVEV----KRAMIDwwgpiIHEYYASSEGGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNLGDSTSRMmNTDGYAATGvEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRM 421
Cdd:PRK08276 302 VTVITSEDWLAHP-GSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 422 DEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLS---LTlEEVIAFF 498
Cdd:PRK08276 380 DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAgdaLA-AELIAWL 458
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 499 sRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK08276 459 -RGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-532 |
2.95e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 224.70 E-value: 2.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAF-SNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKIFFAPTVFKQNrpVDLILPlQNQLRHLTHI---------------VGVDKLAPATTALA 168
Cdd:PRK12492 104 NTNPLYTAREMRHQFKDSGARALVYLNMFGKL--VQEVLP-DTGIEYLIEAkmgdllpaakgwlvnTVVDKVKKMVPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 169 LSQIIDRSEPLQ-------SDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLT----------WQDV 231
Cdd:PRK12492 181 LPQAVPFKQALRqgrglslKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 232 FLMPAPLGHATGFLHGVTAPFLIGARSVLL----DI--FTPEacltlLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSL 305
Cdd:PRK12492 261 MIAPLPLYHIYAFTANCMCMMVSGNHNVLItnprDIpgFIKE-----LGKWRFSALLGLNTLFVALMDHPGFKDLDFSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 306 RFFLCGGTIIPKKVARDCQQ-RGIKLLSIYGSTESSPHSMVNLGDSTSRMmNTDGYAATGVEIKIVDEDRNTLPAGHEGE 384
Cdd:PRK12492 336 KLTNSGGTALVKATAERWEQlTGCTIVEGYGLTETSPVASTNPYGELARL-GTVGIPVPGTALKVIDDDGNELPLGERGE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 385 EASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV 464
Cdd:PRK12492 415 LCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 465 VAMPDERLGERSCAYVVLKPPhlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK12492 495 IGVPDERSGEAVKLFVVARDP--GLSVEELKA-YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
25-539 |
6.02e-65 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 220.62 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVVD-NHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PLN02246 24 PLHDYCFERLSEFSDRPCLIDgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKIffaptVFKQNRPVDLILPLQNQlRHLThIVGVDklAPATTALALSQIIDRSEPLQSDI 183
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKL-----IITQSCYVDKLKGLAED-DGVT-VVTID--DPPEGCLHFSELTQADENELPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 184 NIHGDELAAVLFTSGTEGMPKGVMLTHNNILASerayCAR--------LNLTWQDVFLMPAPLGH----ATGFLHGVTAp 251
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTS----VAQqvdgenpnLYFHSDDVILCVLPMFHiyslNSVLLCGLRV- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 252 fliGARSVLLDIFTPEACLTLLAQQRCTcmsgATPFIYDLLCAVEQQPA----DLSSLRFFLCGGTIIPKKVARDCQQR- 326
Cdd:PLN02246 250 ---GAAILIMPKFEIGALLELIQRHKVT----IAPFVPPIVLAIAKSPVvekyDLSSIRMVLSGAAPLGKELEDAFRAKl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 -GIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAATGV---EIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPE 401
Cdd:PLN02246 323 pNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSGSCGTVVrnaELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 402 LTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVV 481
Cdd:PLN02246 403 ATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 482 lKPPHLSLTLEEVIAFFSrKRVAKYKYPERIVIVEKLPRTASGKVqkflLRQDIIERL 539
Cdd:PLN02246 483 -RSNGSEITEDEIKQFVA-KQVVFYKRIHKVFFVDSIPKAPSGKI----LRKDLRAKL 534
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
25-525 |
6.54e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 220.53 E-value: 6.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVVdnHGA-SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALV--CGDrRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKiffapTVFKQNRPVDLILPLQNQLRHLTHIVGVD---KLAPATTALALSQIIDRSEPLQ 180
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAV-----ALVYEREFAPRVAEVLPRLPKLRTLVVVEdgsGNDLLPGAVDYEDALAAGSPER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 181 SDINIHGDELAaVLFTSGTEGMPKGVMLTHNNI---------------LASERAYCARLNLTWQDVFLMPAPLGHATGFL 245
Cdd:PRK07798 157 DFGERSPDDLY-LLYTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 246 HGVTApFLIGARSVLLDI--FTPEACLTLLAQQRCTCMS--G---ATPFIYDLLCAveqQPADLSSLRFFLCGGTIIPKK 318
Cdd:PRK07798 236 AAFAA-LFSGQTVVLLPDvrFDADEVWRTIEREKVNVITivGdamARPLLDALEAR---GPYDLSSLFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 319 VardcQQR------GIKLLSIYGSTESSphsmvNLGDSTSrmmnTDGYAATG---VEI----KIVDEDRNTLPAGHEGE- 384
Cdd:PRK07798 312 V----KEAllellpNVVLTDSIGSSETG-----FGGSGTV----AKGAVHTGgprFTIgprtVVLDEDGNPVEPGSGEIg 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 385 EASRGPNVFMGYLDEPELTA---RALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHD 461
Cdd:PRK07798 379 WIARRGHIPLGYYKDPEKTAetfPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 604198150 462 ACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGK 525
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLREGA-RPDLAELRA-HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
31-531 |
1.26e-63 |
|
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: 215.84 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVD-NHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:cd05923 8 RRAASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKiffapTVFKQN--RPVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQiidrSEPLQSdinihg 187
Cdd:cd05923 88 KAAELAELIERGEMT-----AAVIAVdaQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPP----REPEQP------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 delAAVLFTSGTEGMPKGVMLTHNNilASER----AYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDI 263
Cdd:cd05923 153 ---AFVFYTSGTTGLPKGAVIPQRA--AESRvlfmSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMSgATPFIYD-LLCAVEQQPADLSSLRFFLCGGTIIPKKV-ARDCQQRGIKLLSIYGSTESsp 341
Cdd:cd05923 228 FDPADALKLIEQERVTSLF-ATPTHLDaLAAAAEFAGLKLSSLRHVTFAGATMPDAVlERVNQHLPGEKVNIYGTTEA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 hsMVNLGDSTSRMmNTDGYAATGVEIKIV---DEDRNTLPAGHEGE--EASRGPNVFMGYLDEPELTARALdNEGWYYSG 416
Cdd:cd05923 305 --MNSLYMRDART-GTEMRPGFFSEVRIVrigGSPDEALANGEEGEliVAAAADAAFTGYLNQPEATAKKL-QDGWYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 417 DLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlSLTLEEVIA 496
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--TLSADELDQ 458
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 497 FFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLL 531
Cdd:cd05923 459 FCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
31-528 |
3.87e-63 |
|
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: 214.37 E-value: 3.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:cd12117 4 EEQAARTPDAVAVVYG-DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDEL 190
Cdd:cd12117 83 AERLAFMLADAGAKVL------------------------LTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNI--LASERAYcarLNLTWQDVFLMPAPLG-HATGFlhGVTAPFLIGARSVLLD---IF 264
Cdd:cd12117 139 AYVMYTSGSTGRPKGVAVTHRGVvrLVKNTNY---VTLGPDDRVLQTSPLAfDASTF--EIWGALLNGARLVLAPkgtLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 265 TPEACLTLLAQQRCTCMSGATPFIYDLlcaVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTE---- 338
Cdd:cd12117 214 DPDALGALIAEEGVTVLWLTAALFNQL---ADEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEnttf 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 SSPHSMVNLGDSTSRM------MNTDGYaatgveikIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR------A 406
Cdd:cd12117 291 TTSHVVTELDEVAGSIpigrpiANTRVY--------VLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAErfvadpF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 407 LDNEGWYYSGDLCRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPP 485
Cdd:cd12117 363 GPGERLYRTGDLARWLPDGRLEFLGRIDDqVKIR-GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 604198150 486 hlsLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd12117 442 ---LDAAELRA-FLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
31-539 |
9.30e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 215.40 E-value: 9.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:PRK05677 31 KQSCQRFADKPAF-SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAK--IFFAPTVFKQNRPV--------------DLILPLQNQL-----RHLTHIVGVDKLAPA---TT 165
Cdd:PRK05677 110 TAREMEHQFNDSGAKalVCLANMAHLAEKVLpktgvkhvivtevaDMLPPLKRLLinavvKHVKKMVPAYHLPQAvkfND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 166 ALALSqiidRSEPLQsDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASE---RAYCARLNLTWQDVFLMPAPLGHAT 242
Cdd:PRK05677 190 ALAKG----AGQPVT-EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcRALMGSNLNEGCEILIAPLPLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 243 GFLHGVTAPFLIGARSVLldIFTP---EACLTLLAQQRCTCMSGA-TPFIydLLCAVEQ-QPADLSSLRFFLCGGTIIPK 317
Cdd:PRK05677 265 AFTFHCMAMMLIGNHNIL--ISNPrdlPAMVKELGKWKFSGFVGLnTLFV--ALCNNEAfRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 318 KVARDCQQ-RGIKLLSIYGSTESSPHSMVNLGDSTSrmMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGY 396
Cdd:PRK05677 341 ATAERWKEvTGCAICEGYGMTETSPVVSVNPSQAIQ--VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 397 LDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERS 476
Cdd:PRK05677 419 WQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAI 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 604198150 477 CAYVVLKpPHLSLTLEEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERL 539
Cdd:PRK05677 499 KVFVVVK-PGETLTKEQVMEHM-RANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
24-542 |
1.12e-62 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 214.88 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDKIAVVdNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFI-CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAK-IF----FAPTVFKqnrpvdlILPlQNQLRHLT------------HIVG-----VDKLA 161
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAEaIVvlenFATTVQQ-------VLA-KTAVKHVVvasmgdllgfkgHIVNfvvrrVKKMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 162 PA---------TTALALSqiidRSEPLQSdINIHGDELAAVLFTSGTEGMPKGVMLTHNNILAS--------ERAYCARL 224
Cdd:PRK07059 174 PAwslpghvrfNDALAEG----ARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqmeawlQPAFEKKP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 225 NLTwQDVFLMPAPLGHatgfLHGVTAPFLI----GARSVLL----DI--FTPEacltlLAQQRCTCMSGATPFIYDLLCA 294
Cdd:PRK07059 249 RPD-QLNFVCALPLYH----IFALTVCGLLgmrtGGRNILIpnprDIpgFIKE-----LKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 295 VEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTSrMMNTDGYAATGVEIKIVDED 373
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMtGCPITEGYGLSETSPVATCNPVDATE-FSGTIGLPLPSTEVSIRDDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 374 RNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDIL 453
Cdd:PRK07059 398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 454 LQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVqkflLRQ 533
Cdd:PRK07059 478 ASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDP--ALTEEDVKA-FCKERLTNYKRPKFVEFRTELPKTNVGKI----LRR 550
|
....*....
gi 604198150 534 DiierLRQE 542
Cdd:PRK07059 551 E----LRDG 555
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
51-532 |
1.52e-62 |
|
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: 211.59 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAwreaelvwvlnkcqakifFAPT 130
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSA------------------FGPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 131 VFKQNrpvdlilpLQNqlrhlthivgvdklAPATTALALSQIIDRSEPlqsdinihgDELAAVLFTSGTEGMPKGVMLTH 210
Cdd:cd05969 63 AIRDR--------LEN--------------SEAKVLITTEELYERTDP---------EDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 211 NNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDI-FTPEACLTLLAQQRCTCMSGAtPFIY 289
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGrFDAESWYGIIERVKVTVWYTA-PTAI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 290 DLLCAVEQQPA---DLSSLRFFLCGGTII-PKKVARDCQQRGIKLLSIYGSTESSPHSMVNL--GDSTSRMMntdGYAAT 363
Cdd:cd05969 191 RMLMKEGDELArkyDLSSLRFIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYpcMPIKPGSM---GKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 364 GVEIKIVDEDRNTLPAGHEGEEASRG--PNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGG 441
Cdd:cd05969 268 GVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 442 ENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPH-LSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPR 520
Cdd:cd05969 347 HRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFePSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|..
gi 604198150 521 TASGKVQKFLLR 532
Cdd:cd05969 427 TRSGKIMRRVLK 438
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-526 |
1.67e-62 |
|
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: 211.92 E-value: 1.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 59 AASRLANWLLSQGIQPGDRVAFQLPG-----WCEFTLIYLACLKtGAVSVPLLPAWREAELVWVLNKCQAKIffaptVFK 133
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNrftyiELSFAVAYAGGRL-GLVFVPLNPTLKESVLRYLVADAGGRI-----VLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 134 QNRPVDLILPLQNQLRHLTHIVGVDKLApattalalsqiiDRSEPLQSDINIHgDELAAVLFTSGTEGMPKGVMLTHNNI 213
Cdd:cd05922 76 DAGAADRLRDALPASPDPGTVLDADGIR------------AARASAPAHEVSH-EDLALLLYTSGSTGSPKLVRLSHQNL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 214 LASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFT-PEACLTLLAQQRCTCMSGaTPFIYDLL 292
Cdd:cd05922 143 LANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAG-VPSTYAML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 293 CAVEQQPADLSSLRFFL-CGGTIIPKKVARDCQQ-RGIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAATGVEIKIV 370
Cdd:cd05922 221 TRLGFDPAKLPSLRYLTqAGGRLPQETIARLRELlPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 371 DEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVE 450
Cdd:cd05922 301 DDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 451 DILLQHPRIHDACVVAMPDErLGERSCAYVVLKPphlSLTLEEVIAFFSrKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd05922 381 AAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPD---KIDPKDVLRSLA-ERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
27-526 |
1.95e-62 |
|
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: 212.52 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 27 GDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLL 106
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDE-GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 107 PAWREAELVWVLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHIVGVDKLAPATTALALSQIIDRSEP-LQSDINI 185
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVV------------------------LTTADLAARLPAGGDVALLGDEALAAPPaTPPLVPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 186 HGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLL---- 261
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVArpgg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 262 --DiftPEACLTLLAQQRCTCMSgatpFIYDLLCAVEQQPAD--LSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGS 336
Cdd:cd17646 215 hrD---PAYLAALIREHGVTTCH----FVPSMLRVFLAEPAAgsCASLRRVFCSGEALPPELAARFLALpGAELHNLYGP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 337 TESS---PHSMVNLGDSTSRMmnTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA-RALDN--- 409
Cdd:cd17646 288 TEAAidvTHWPVRGPAETPSV--PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAeRFVPDpfg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 410 --EGWYYSGDLCRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPH 486
Cdd:cd17646 366 pgSRMYRTGDLARWRPDGALEFLGRSDDqVKIR-GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA 444
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 604198150 487 LSLTLEEVIAFFSRkRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17646 445 AGPDTAALRAHLAE-RLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-464 |
3.49e-61 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 207.12 E-value: 3.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKiffapt 130
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 131 vfkqnrpvdLILpLQNQLRHLTHIVGVDKLAPATTALALSQiiDRSEPLQSDINIHGDELAAVLFTSGTEGMPKGVMLTH 210
Cdd:TIGR01733 75 ---------LLL-TDSALASRLAGLVLPVILLDPLELAALD--DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 211 NNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLD----IFTPEACLTLLAQQRCTCMSgATP 286
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPDDRVLQFASLSF-DASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLN-LTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 287 FIYDLLcaVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPHSMVNlgdSTSRMMNTD------ 358
Cdd:TIGR01733 221 SLLALL--AAALPPALASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTAT---LVDPDDAPRespvpi 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 359 GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA--------RALDNEGWYYSGDLCRMDEDGYIKIT 430
Cdd:TIGR01733 296 GRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 604198150 431 GRKKDII-IRG-----GenissrEVEDILLQHPRIHDACV 464
Cdd:TIGR01733 376 GRIDDQVkIRGyrielG------EIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
34-526 |
4.17e-61 |
|
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: 207.87 E-value: 4.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLlpawreae 113
Cdd:cd05945 1 AAANPDRPAVVEG-GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 lvwvlnkcqakiffaptvfkqnrpvdlilplqnqlrhlthivgvdklAPATTALALSQIIDRSEPlqsDINIH-GDELAA 192
Cdd:cd05945 72 -----------------------------------------------DASSPAERIREILDAAKP---ALLIAdGDDNAY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 193 VLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGhatgF---LHGVTAPFLIGARSVLLD---IFTP 266
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS----FdlsVMDLYPALASGATLVPVPrdaTADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLTLLAQQRCTCMSGaTPFIYDLlCAVEQQ--PADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESsph 342
Cdd:cd05945 178 KQLFRFLAEHGITVWVS-TPSFAAM-CLLSPTftPESLPSLRHFLFCGEVLPHKTARALQQRfpDARIYNTYGPTEA--- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 smvNLGDSTSRMMNTD---------GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL---DNE 410
Cdd:cd05945 253 ---TVAVTYIEVTPEVldgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 411 GWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLT 490
Cdd:cd05945 330 RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK-PGAEAG 408
|
490 500 510
....*....|....*....|....*....|....*.
gi 604198150 491 LEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd05945 409 LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-538 |
6.08e-61 |
|
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: 205.02 E-value: 6.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 187 GDELAAVLFTSGTEGMPKGVMLTHNNILASerAYCARLNLTWQ--DVFLMPAPLGHATGFLHGVTAPFLIGARSVLLdif 264
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDpdDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 265 TPEA---------CLTLLAQQRCTCMSGaTPFIYDLLCAVEQQpADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIY 334
Cdd:cd05944 76 GPAGyrnpglfdnFWKLVERYRITSLST-VPTVYAALLQVPVN-ADISSLRFAMSGAAPLPVELRARFEDAtGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 335 GSTESSPHSMVNLGDSTSRMmNTDGYAA--TGVEIKIVDEDRNTLP--AGHE-GEEASRGPNVFMGYLDEpELTARALDN 409
Cdd:cd05944 154 GLTEATCLVAVNPPDGPKRP-GSVGLRLpyARVRIKVLDGVGRLLRdcAPDEvGEICVAGPGVFGGYLYT-EGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 410 EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSL 489
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK-PGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 604198150 490 TLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIER 538
Cdd:cd05944 311 EEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
52-531 |
6.53e-61 |
|
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: 208.07 E-value: 6.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQL---PGWCeftLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFA 128
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGenrPEWG---IAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 129 ptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrSEPlqsdinihgDELAAVLFTSGTEGMPKGVML 208
Cdd:cd05914 86 -----------------------------------------------SDE---------DDVALINYTSGTTGNSKGVML 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 209 THNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIfTPEACLTLLAQQRCTCMSGAT-PF 287
Cdd:cd05914 110 TYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDK-IPSAKIIALAFAQVTPTLGVPvPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 288 IYDLLCAVEQQPADLSS------------------------------LRFFLCGGTIIPKKVARDCQQRGIKLLSIYGST 337
Cdd:cd05914 189 VIEKIFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggnIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 338 ESSPhsMVNLGDSTSRMMNTDGYAATGVEIKIVDEDrntlPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGD 417
Cdd:cd05914 269 ETAP--IISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 418 LCRMDEDGYIKITGRKKDIIIRG-GENISSREVEDILLQHPRIHDACVVaMPDERLGERSCAYV-VLKPPHLSLT----- 490
Cdd:cd05914 343 LGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV-VQEKKLVALAYIDPdFLDVKALKQRniida 421
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 604198150 491 -LEEVIAFFSRKrVAKYKYPERIVIV-EKLPRTASGKVQKFLL 531
Cdd:cd05914 422 iKWEVRDKVNQK-VPNYKKISKVKIVkEEFEKTPKGKIKRFLY 463
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
48-534 |
8.17e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 207.92 E-value: 8.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLAnwllsQGIQPGDRVAFqlpgWCEFT----LIYLACLKTGAVSVPLLPAWREAELVWVLnkcqa 123
Cdd:PRK07787 23 GRVLSRSDLAGAATAVA-----ERVAGARRVAV----LATPTlatvLAVVGALIAGVPVVPVPPDSGVAERRHIL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 124 kiffaptvfKQNRPVDLILPLQNQLRHLTHiVGVDKLAPATTALAlsqiidrsEPlqsdiniHGDELAAVLFTSGTEGMP 203
Cdd:PRK07787 89 ---------ADSGAQAWLGPAPDDPAGLPH-VPVRLHARSWHRYP--------EP-------DPDAPALIVYTSGTTGPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 204 KGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEAcltlLAQQrctCMSG 283
Cdd:PRK07787 144 KGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEA----YAQA---LSEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 284 AT-----PFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKV-ARDCQQRGIKLLSIYGSTESsphsMVNLGDSTS--RMM 355
Cdd:PRK07787 217 GTlyfgvPTVWSRIAADPEAARALRGARLLVSGSAALPVPVfDRLAALTGHRPVERYGMTET----LITLSTRADgeRRP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 356 NTDGYAATGVEIKIVDEDRNTLPAGHE--GEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRK 433
Cdd:PRK07787 293 GWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 434 K-DIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlkpPHLSLTLEEVIAFFSRkRVAKYKYPERI 512
Cdd:PRK07787 373 StDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV---GADDVAADELIDFVAQ-QLSVHKRPREV 448
|
490 500
....*....|....*....|..
gi 604198150 513 VIVEKLPRTASGKVQKFLLRQD 534
Cdd:PRK07787 449 RFVDALPRNAMGKVLKKQLLSE 470
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
45-526 |
8.85e-60 |
|
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: 205.64 E-value: 8.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 45 DNHGASWTYAALDYAASRLANwLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAK 124
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 125 IFFAPTVFKQNRPVDLILPLQNQLRHL------THIVGVDKLAPATTALALSQIIDRSEPLqsdINIHGDELAAVLFTSG 198
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVyledlrAKISKADKCKAFLAGKFPPKWLLRIFGV---APVQPDDPAVILFTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 199 TEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL----LDiftPEACLTLLA 274
Cdd:cd05909 158 SEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFhpnpLD---YKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMsGATPFIYDLLcAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGDSTSR 353
Cdd:cd05909 235 DKKATIL-LGTPTFLRGY-ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSPNK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 mMNTDGYAATGVEIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGR 432
Cdd:cd05909 313 -EGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 433 KKDIIIRGGENISSREVEDILLQH-PRIHDACVVAMPDERLGERscayVVLKPPHLSLTLEEVIAFFSRKRVAKYKYPER 511
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK----IVLLTTTTDTDPSSLNDILKNAGISNLAKPSY 466
|
490
....*....|....*
gi 604198150 512 IVIVEKLPRTASGKV 526
Cdd:cd05909 467 IHQVEEIPLLGTGKP 481
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
52-533 |
4.82e-59 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 204.99 E-value: 4.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAfqLPGWCefTLIYLAC----LKTGAVSVPLLPAWREAELVWVLNKCQAKIFF 127
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVA--TIAWN--TWRHLEAwygiMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 APTVFkqnrpVDLILPLQNQLRHL-THIVGVDK-LAPATT---ALALSQIIDRSeplqsdiniHGD---------ELAAV 193
Cdd:PRK06018 117 TDLTF-----VPILEKIADKLPSVeRYVVLTDAaHMPQTTlknAVAYEEWIAEA---------DGDfawktfdenTAAGM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTH-NNILASERAYCA-RLNLTWQDVFLMPAPLGHATGFLHGVTAPfLIGARSVLldiftPEACL- 270
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVLHALMANNGdALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVM-----PGAKLd 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 271 -----TLLAQQRCTcMSGATPFIYD-LLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSM 344
Cdd:PRK06018 257 gasvyELLDTEKVT-FTAGVPTVWLmLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 V--------NL-GDSTSRMMNTDGYAATGVEIKIVDEDRNTLPagHEGEEAS----RGPNVFMGYLdepELTARALDNEG 411
Cdd:PRK06018 336 LaalkppfsKLpGDARLDVLQKQGYPPFGVEMKITDDAGKELP--WDGKTFGrlkvRGPAVAAAYY---RVDGEILDDDG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTL 491
Cdd:PRK06018 411 FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGE-TATR 489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 604198150 492 EEVIAFFSRKrVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK06018 490 EEILKYMDGK-IAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
26-542 |
6.58e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 205.27 E-value: 6.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 26 LGDYWRQTARAVPDKIAVvdnH--GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK06710 26 LHKYVEQMASRYPEKKAL---HflGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKIFFAptvfkqnrpVDLILPLQNQLRHLTHI--VGVDKLA-----PAT------------ 164
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILC---------LDLVFPRVTNVQSATKIehVIVTRIAdflpfPKNllypfvqkkqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 165 --TALALSQIIDRSEPLQSDINIHGD-------ELAAVLFTSGTEGMPKGVMLTHNNILASeraycARLNLTW------- 228
Cdd:PRK06710 174 lvVKVSESETIHLWNSVEKEVNTGVEvpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWlynckeg 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 229 QDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFF 308
Cdd:PRK06710 249 EEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRAC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 309 LCGGTIIPKKVARDCQQ-RGIKLLSIYGSTESSPHSMVNLgDSTSRMMNTDGYAATGVEIKIVD-EDRNTLPAGHEGEEA 386
Cdd:PRK06710 329 ISGSAPLPVEVQEKFETvTGGKLVEGYGLTESSPVTHSNF-LWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 387 SRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVA 466
Cdd:PRK06710 408 VKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 467 MPDERLGERSCAYVVLKPPhlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVqkflLRQDIIERLRQE 542
Cdd:PRK06710 487 VPDPYRGETVKAFVVLKEG--TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEKRK 556
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
24-541 |
7.59e-59 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 204.90 E-value: 7.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDKIAVVdNHGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVS 102
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFI-NMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLLPAWREAELVWVLNKCQAKIF-----FAPTVFK--QNRPVD-LILP-LQNQL----RHLTHIV--GVDKLAP----- 162
Cdd:PRK08974 102 VNVNPLYTPRELEHQLNDSGAKAIvivsnFAHTLEKvvFKTPVKhVILTrMGDQLstakGTLVNFVvkYIKRLVPkyhlp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 163 -ATTALALSQIIDRSEPLQSDINihGDELAAVLFTSGTEGMPKGVMLTHNNILAS----ERAYCARLNlTWQDVFLMPAP 237
Cdd:PRK08974 182 dAISFRSALHKGRRMQYVKPELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqaKAAYGPLLH-PGKELVVTALP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 238 LGHAtgFLHGVTAPFLI--GARSVLL----DI--FTPEacltlLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFL 309
Cdd:PRK08974 259 LYHI--FALTVNCLLFIelGGQNLLItnprDIpgFVKE-----LKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 310 CGGTIIPKKVARDCQQ-RGIKLLSIYGSTESSPHSMVNLGDSTsRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASR 388
Cdd:PRK08974 332 GGGMAVQQAVAERWVKlTGQYLLEGYGLTECSPLVSVNPYDLD-YYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 389 GPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMP 468
Cdd:PRK08974 411 GPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVP 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 604198150 469 DERLGERSCAYVVLKPPhlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQ 541
Cdd:PRK08974 490 SEVSGEAVKIFVVKKDP--SLTEEELIT-HCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
189-533 |
9.75e-59 |
|
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: 197.94 E-value: 9.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 ELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPEA 268
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 clTLLAQQRCTCMSGATPFIYDLLcAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSphSMVNLG 348
Cdd:cd17630 80 --EDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETA--SQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 349 DSTSRMMNTDGYAATGVEIKIVDEdrntlpagheGEEASRGPNVFMGYLDEPELtaRALDNEGWYYSGDLCRMDEDGYIK 428
Cdd:cd17630 155 RPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 429 ITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlslTLEEVIAFFSRKrVAKYKY 508
Cdd:cd17630 223 VLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA---DPAELRAWLKDK-LARFKL 298
|
330 340
....*....|....*....|....*
gi 604198150 509 PERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd17630 299 PKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
34-545 |
1.37e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 203.82 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNHGASwTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK06164 20 ARARPDAVALIDEDRPL-SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKIFFAPTVFKQnrpVDLILPLQ----NQLRHLTHIVGVDKLAPATTA------LALSQIIDRSEPLQSDI 183
Cdd:PRK06164 99 VAHILGRGRARWLVVWPGFKG---IDFAAILAavppDALPPLRAIAVVDDAADATPApapgarVQLFALPDPAPPAAAGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 184 NIHGDELAAVLFT-SGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFlHGVTAPFLIGARSVLLD 262
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 IFTPEACLTLLAQQRCTCMSGATPFiYDLLCAVEQQPADLSSLRffLCG-GTIIPK--KVARDCQQRGIKLLSIYGSTES 339
Cdd:PRK06164 255 VFDAARTARALRRHRVTHTFGNDEM-LRRILDTAGERADFPSAR--LFGfASFAPAlgELAALARARGVPLTGLYGSSEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 spHSMVNLGDST---SRMMNTDGY-AATGVEIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYY 414
Cdd:PRK06164 332 --QALVALQPATdpvSVRIEGGGRpASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 415 SGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMpdERLGERSCAYVVLKPPHLSLTLEEV 494
Cdd:PRK06164 410 TGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPTDGASPDEAGL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 604198150 495 IAFFsRKRVAKYKYPERIVIVEKLPRTASG---KVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK06164 488 MAAC-REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAERAA 540
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-546 |
2.08e-57 |
|
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: 207.79 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLP-GWcEFTLIYLACLKTGAV 101
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVFG-DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErSL-EMVVALLAVLKAGAA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQNRPvdlilplqnqlRHLTHIVGVDKLAPATTAlalsqiidrSEPLQS 181
Cdd:COG1020 553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLP-----------ELGVPVLALDALALAAEP---------ATNPPV 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 182 DIniHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLghatGF---LHGVTAPFLIGARS 258
Cdd:COG1020 613 PV--TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASL----SFdasVWEIFGALLSGATL 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 259 VLLD---IFTPEACLTLLAQQRCTCMSgATPFIYDLLcaVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSI 333
Cdd:COG1020 687 VLAPpeaRRDPAALAELLARHRVTVLN-LTPSLLRAL--LDAAPEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 334 YGSTESSPHSM---VNLGDSTSRMMNTdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARA---- 406
Cdd:COG1020 764 YGPTETTVDSTyyeVTPPDADGGSVPI-GRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvad 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 407 ---LDNEGWYYSGDLCRMDEDGYIKITGRK----KdiiIRG-----GenissrEVEDILLQHPRIHDACVVAMPDERLGE 474
Cdd:COG1020 843 pfgFPGARLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG------EIEAALLQHPGVREAVVVAREDAPGDK 913
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 475 RSCAYVVlkPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTAV 546
Cdd:COG1020 914 RLVAYVV--PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPP 983
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
5-526 |
3.45e-57 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 206.70 E-value: 3.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 5 LTFDA-ARRKTYRESgywgdasLGDYWRQTARAVPDKIAVVDNHGASWTYAALDYAASRLANwLLSQGIQPGDRVAFQLP 83
Cdd:PRK08633 602 LSFDSwKSRKEALPP-------LAEAWIDTAKRNWSRLAVADSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLP 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 84 GWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQ---NRPVDLILPLQNQLRHL----THIVG 156
Cdd:PRK08633 674 PSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEklkNKGFDLELPENVKVIYLedlkAKISK 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 157 VDKL-APATTALALSQIIDRSeplqSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMP 235
Cdd:PRK08633 754 VDKLtALLAARLLPARLLKRL----YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSS 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 236 APLGHATGFLhgVTA--PFLIGARSVL----LDIFTPEAcltLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFL 309
Cdd:PRK08633 830 LPFFHSFGLT--VTLwlPLLEGIKVVYhpdpTDALGIAK---LVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVV 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 310 CGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNL-----GDSTSRMMN---TDGYAATGVEIKIVDEDR-NTLPA 379
Cdd:PRK08633 905 AGAEKLKPEVADAFEEKfGIRILEGYGATETSPVASVNLpdvlaADFKRQTGSkegSVGMPLPGVAVRIVDPETfEELPP 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 380 GHEGEEASRGPNVFMGYLDEPELTARAL---DNEGWYYSGDLCRMDEDGYIKITGRkkdiIIR----GGENISSREVEDI 452
Cdd:PRK08633 985 GEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR----YSRfakiGGEMVPLGAVEEE 1060
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 453 LLQhpRIHDA----CVVAMPDERLGERscayVVLKPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:PRK08633 1061 LAK--ALGGEevvfAVTAVPDEKKGEK----LVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
34-533 |
2.14e-56 |
|
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: 197.72 E-value: 2.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVV--DNHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:cd05970 27 AKEYPDKLALVwcDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFFA------PTVFKQNRPVDLILPLQNQlrhlthiVGVDKLapaTTALALSQIIDRS----EPL 179
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAiaedniPEEIEKAAPECPSKPKLVW-------VGDPVP---EGWIDFRKLIKNAspdfERP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QSDINIHGDELAAVLFTSGTEGMPKgvMLTHNNILASERAYCARLnltWQDV-----FLMPAPLGHATGFLHGVTAPFLI 254
Cdd:cd05970 177 TANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKY---WQNVregglHLTVADTGWGKAVWGKIYGQWIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 GARSVLLDI--FTPEACLTLLAQQRCTCMSgATPFIYDLLCAVEQQPADLSSLRFFLCGGTII-PKKVARDCQQRGIKLL 331
Cdd:cd05970 252 GAAVFVYDYdkFDPKALLEKLSKYGVTTFC-APPTIYRFLIREDLSRYDLSSLRYCTTAGEALnPEVFNTFKEKTGIKLM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 332 SIYGSTESS------------PHSMvnlgdstsrmmntdGYAATGVEIKIVDEDRNTLPAGHEGE---EASRGPNV--FM 394
Cdd:cd05970 331 EGFGQTETTltiatfpwmepkPGSM--------------GKPAPGYEIDLIDREGRSCEAGEEGEiviRTSKGKPVglFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 395 GYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGE 474
Cdd:cd05970 397 GYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQ 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 475 RSCAYVVL-KPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05970 476 VVKATIVLaKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
28-532 |
9.64e-56 |
|
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: 195.76 E-value: 9.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 28 DYWRQTARA--VPDKIAV--VDNHGAS--WTYAALDYAASRLANwLLSQ--GIQPGDRVAFQLPGWCEFTLIYLACLKTG 99
Cdd:cd05928 13 DQWADKEKAgkRPPNPALwwVNGKGDEvkWSFRELGSLSRKAAN-VLSGacGLQRGDRVAVILPRVPEWWLVNVACIRTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 100 AVSVPLLPAWREAELVWVLNKCQAKIffaptvfkqnrpvdlilplqnqlrhlthIVGVDKLAPATTALALSQIIDRSEPL 179
Cdd:cd05928 92 LVFIPGTIQLTAKDILYRLQASKAKC----------------------------IVTSDELAPEVDSVASECPSLKTKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QSDINIHG----------------------DELAAVLFTSGTEGMPKGVMLTHNNILASERAyCAR--LNLTWQDVFLMP 235
Cdd:cd05928 144 VSEKSRDGwlnfkellneastehhcvetgsQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKV-NGRywLDLTASDIMWNT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 236 APLGHATGFLHGVTAPFLIGARSV--LLDIFTPEACLTLLAQQRCTCMSGAtPFIYDLLcaVEQqpaDLSSLRF-----F 308
Cdd:cd05928 223 SDTGWIKSAWSSLFEPWIQGACVFvhHLPRFDPLVILKTLSSYPITTFCGA-PTVYRML--VQQ---DLSSYKFpslqhC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 309 LCGG-TIIPKKVARDCQQRGIKLLSIYGSTEssphsmVNLGDSTSRMMNTD----GYAATGVEIKIVDEDRNTLPAGHEG 383
Cdd:cd05928 297 VTGGePLNPEVLEKWKAQTGLDIYEGYGQTE------TGLICANFKGMKIKpgsmGKASPPYDVQIIDDNGNVLPPGTEG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 384 EEASR-GPN----VFMGYLDEPELTARALDNEgWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPR 458
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPA 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 459 IHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEVIAFFS---RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05928 450 VVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQqhvKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-533 |
1.02e-55 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 195.30 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 53 YAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTvf 132
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 133 kqnrpvDLILPLQNQL-RHLT--------HIVGVDKLAPATTAlALSQIIDRSEPLQSDINIHGDELAA---VLFTSGTE 200
Cdd:PRK12406 92 ------DLLHGLASALpAGVTvlsvptppEIAAAYRISPALLT-PPAGAIDWEGWLAQQEPYDGPPVPQpqsMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 201 GMPKGVML---THNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTApFLIGARSVLLDIFTPEACLTLLAQQR 277
Cdd:PRK12406 165 GHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQPRFDPEELLQLIERHR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 278 CTCMSGA-TPFI--YDLLCAVEQQpADLSSLRFFLCGGTIIPKKVARD-CQQRGIKLLSIYGSTESSPHSMVNLGDSTSR 353
Cdd:PRK12406 244 ITHMHMVpTMFIrlLKLPEEVRAK-YDVSSLRHVIHAAAPCPADVKRAmIEWWGPVIYEYYGSTESGAVTFATSEDALSH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 MmNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGP-NVFMGYLDEPElTARALDNEGWYYSGDLCRMDEDGYIKITGR 432
Cdd:PRK12406 323 P-GTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPE-KRAEIDRGGFITSGDVGYLDADGYLFLCDR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 433 KKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVvlkPPHLSLTL-EEVIAFFSRKRVAKYKYPER 511
Cdd:PRK12406 401 KRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV---EPQPGATLdEADIRAQLKARLAGYKVPKH 477
|
490 500
....*....|....*....|..
gi 604198150 512 IVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK12406 478 IEIMAELPREDSGKIFKRRLRD 499
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-533 |
1.48e-55 |
|
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: 193.12 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAwreaelvwvlnkcqakifFAPTV 131
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTA------------------FGPKA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FKQnrpvdlilplqnqlrhlthivgvdKLAPATTALALSQIIDRSEpLQSDINIHgdelaavLFTSGTEGMPKGVMLTHN 211
Cdd:cd05973 64 IEH------------------------RLRTSGARLVVTDAANRHK-LDSDPFVM-------MFTSGTTGLPKGVPVPLR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLD-IFTPEACLTLLAQQRCTCMSGAtPFIYD 290
Cdd:cd05973 112 ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVIERLGVTNLAGS-PTAYR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 291 LLCA--VEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTEsspHSMV---NLGDSTSRMMNTDGYAATG 364
Cdd:cd05973 191 LLMAagAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTE---LGMVlanHHALEHPVHAGSAGRAMPG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 365 VEIKIVDEDRNTLPAGHEGE---EASRGPNV-FMGYLDEPELTARAldneGWYYSGDLCRMDEDGYIKITGRKKDIIIRG 440
Cdd:cd05973 268 WRVAVLDDDGDELGPGEPGRlaiDIANSPLMwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 441 GENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPH-LSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLP 519
Cdd:cd05973 344 GYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHeGTPALADELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|....
gi 604198150 520 RTASGKVQKFLLRQ 533
Cdd:cd05973 424 KTPSGKIQRFLLRR 437
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-526 |
2.41e-55 |
|
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: 193.28 E-value: 2.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd12116 1 PDATAVRDDDR-SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDELAAVLFTS 197
Cdd:cd12116 80 LEDAEPALV------------------------LTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTaPFLIGARSVLL---DIFTPEACLTLLA 274
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLL-PLLAGARVVIApreTQRDPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSgATPFIYDLLCAVEQQPADlsSLRfFLCGGTIIPKKVARDCQQRGIKLLSIYGSTES---SPHSMVNLGDST 351
Cdd:cd12116 215 AHSITVMQ-ATPATWRMLLDAGWQGRA--GLT-ALCGGEALPPDLAARLLSRVGSLWNLYGPTETtiwSTAARVTAAAGP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 352 SrmmnTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL-------DNEGWYYSGDLCRMDED 424
Cdd:cd12116 291 I----PIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRAD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 425 GYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDeRLGERSCAYVVLKPPhLSLTLEEVIAFFsRKRV 503
Cdd:cd12116 367 GRLEYLGRADGqVKIR-GHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAG-AAPDAAALRAHL-RATL 442
|
490 500
....*....|....*....|...
gi 604198150 504 AKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKL 465
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
193-526 |
3.25e-55 |
|
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: 189.05 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 193 VLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLDIFTPEACLTL 272
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 273 LAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCG---GTIIPKKVARDCQQRGIkllsiYGSTE-SSPHSMVNLG 348
Cdd:cd17636 84 IEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAApewNDMATVDTSPWGRKPGG-----YGQTEvMGLATFAALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 349 DSTsrmMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIK 428
Cdd:cd17636 159 GGA---IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 429 ITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKY 508
Cdd:cd17636 235 FVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA-SVTEAELIE-HCRARIASYKK 312
|
330
....*....|....*...
gi 604198150 509 PERIVIVEKLPRTASGKV 526
Cdd:cd17636 313 PKSVEFADALPRTAGGAD 330
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
24-532 |
3.34e-55 |
|
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: 194.42 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDK-IAVVDNHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGA 100
Cdd:cd05906 10 RTLLELLLRAAERGPTKgITYIDADGSEefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 101 VSVPL--LPAWREAElvwvlnkcqakiffaptvfKQNRPVDLILPLQNQLRHLTHIVGVDKLAPATT-----ALALSQII 173
Cdd:cd05906 90 VPAPLtvPPTYDEPN-------------------ARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETlsglpGIRVLSIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 174 DRSEPLqSDINIH---GDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHgvta 250
Cdd:cd05906 151 ELLDTA-ADHDLPqsrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVE---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 251 pflIGARSVLLDIFT-----------PEACLTLLAQQRCTcMSGATPFIY----DLLCAVEQQPADLSSLRFFLCGGTII 315
Cdd:cd05906 226 ---LHLRAVYLGCQQvhvpteeiladPLRWLDLIDRYRVT-ITWAPNFAFallnDLLEEIEDGTWDLSSLRYLVNAGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 316 PKKVARDCQQrgikLLSIY-----------GSTESSPHSMVNLGDSTSRMMNTDGYAAT-----GVEIKIVDEDRNTLPA 379
Cdd:cd05906 302 VAKTIRRLLR----LLEPYglppdairpafGMTETCSGVIYSRSFPTYDHSQALEFVSLgrpipGVSMRIVDDEGQLLPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 380 GHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDeDGYIKITGRKKDIIIRGGENISSREVEDILLQHP-- 457
Cdd:cd05906 378 GEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPgv 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 458 RIHDACVVAMPDERLGERSCAYVVL----KPPHLSLTLEEVIAFFSRKRVAKykyPERIVIVEK--LPRTASGKVQKFLL 531
Cdd:cd05906 457 EPSFTAAFAVRDPGAETEELAIFFVpeydLQDALSETLRAIRSVVSREVGVS---PAYLIPLPKeeIPKTSLGKIQRSKL 533
|
.
gi 604198150 532 R 532
Cdd:cd05906 534 K 534
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
22-533 |
3.99e-55 |
|
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: 194.28 E-value: 3.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDA-SLGDYWRQTARAVPDKIAVVDNH-GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTG 99
Cdd:cd17642 14 GTAgEQLHKAMKRYASVPGTIAFTDAHtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 100 AVSVPLLPAWREAELVWVLNKCQAKIffaptVFKQNRPVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPL 179
Cdd:cd17642 94 VGVAPTNDIYNERELDHSLNISKPTI-----VFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QSDINI-------HGDELAAVLFTSGTEGMPKGVMLTHNNIlaserayCARLNLTWQDVF---LMPA-------PLGHAT 242
Cdd:cd17642 169 GFNEYDfkppsfdRDEQVALIMNSSGSTGLPKGVQLTHKNI-------VARFSHARDPIFgnqIIPDtailtviPFHHGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 243 GFLHGVTApFLIGARSVLLDIFTPEACLTLLAQQRCTcMSGATPFIYDLLCAVE-QQPADLSSLRFFLCGGTIIPKKVAR 321
Cdd:cd17642 242 GMFTTLGY-LICGFRVVLMYKFEEELFLRSLQDYKVQ-SALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 322 DCQQRgIKLLSI---YGSTESSphSMVNLGDSTSRMMNTDGYAATGVEIKIVDED-RNTLPAGHEGEEASRGPNVFMGYL 397
Cdd:cd17642 320 AVAKR-FKLPGIrqgYGLTETT--SAILITPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 398 DEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSC 477
Cdd:cd17642 397 NNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 478 AYVVLKpPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd17642 477 AVVVLE-AGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
31-532 |
4.47e-55 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 194.73 E-value: 4.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAV--VDNHGA-SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLP 107
Cdd:PRK04319 51 RHADGGRKDKVALryLDASRKeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 108 AWREAELVWVLNKCQAKIFFAPTVFKQNRPVDlilplqnQLRHLTHIVGVD---KLAPATTAL--ALSQIIDRSEPLQSD 182
Cdd:PRK04319 131 AFMEEAVRDRLEDSEAKVLITTPALLERKPAD-------DLPSLKHVLLVGedvEEGPGTLDFnaLMEQASDEFDIEWTD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 InihgDELAAVLFTSGTEGMPKGVMLTHNNILAseRAYCAR--LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL 260
Cdd:PRK04319 204 R----EDGAILHYTSGSTGKPKGVLHVHNAMLQ--HYQTGKyvLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 261 LDI-FTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPA--DLSSLRFFLCGGTIIPKKVARDCQQ------------ 325
Cdd:PRK04319 278 DGGrFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKkyDLSSLRHILSVGEPLNPEVVRWGMKvfglpihdnwwm 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 326 --RGIKLLSIYGSTESSPHSMvnlgdstsrmmntdGYAATGVEIKIVDEDRNTLPAGHEGEEASRG--PNVFMGYLDEPE 401
Cdd:PRK04319 358 teTGGIMIANYPAMDIKPGSM--------------GKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 402 LTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVV 481
Cdd:PRK04319 424 KYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 604198150 482 LKPPHL-SLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK04319 503 LRPGYEpSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-532 |
1.13e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 192.60 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 28 DYWRQTARAVPDKIAVV-DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTG----AVS 102
Cdd:PRK13391 1 MYPGIHAQTTPDKPAVImASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyytCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLLPAwreaELVWVLNKCQAKIFFAPTvfkqnRPVDLILPLQNQLRHLTHIVGVDK---------LAPATTALALSQII 173
Cdd:PRK13391 81 SHLTPA----EAAYIVDDSGARALITSA-----AKLDVARALLKQCPGVRHRLVLDGdgelegfvgYAEAVAGLPATPIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 174 DRSEplqsdinihGDELaavLFTSGTEGMPKGVM--LTHNNIlASERAYCARLNLTWQ----DVFLMPAPLGH-ATGFLH 246
Cdd:PRK13391 152 DESL---------GTDM---LYSSGTTGRPKGIKrpLPEQPP-DTPLPLTAFLQRLWGfrsdMVYLSPAPLYHsAPQRAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 247 GVTAPFliGARSVLLDIFTPEACLTLLAQQRCT-CMSGATPFIYDLLCAVEQQPA-DLSSLRFFLCGGTIIPKKVARD-C 323
Cdd:PRK13391 219 MLVIRL--GGTVIVMEHFDAEQYLALIEEYGVThTQLVPTMFSRMLKLPEEVRDKyDLSSLEVAIHAAAPCPPQVKEQmI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 324 QQRGIKLLSIYGSTESSPHSMVNLGDSTSRMmNTDGYAATGVeIKIVDEDRNTLPAGHEGEEASRGPNVFMgYLDEPELT 403
Cdd:PRK13391 297 DWWGPIIHEYYAATEGLGFTACDSEEWLAHP-GTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 404 ARALDNEG-WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVL 482
Cdd:PRK13391 374 AEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 483 KP-----PHLSltlEEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK13391 454 VDgvdpgPALA---AELIAFC-RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-532 |
1.51e-54 |
|
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: 190.66 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd17649 1 PDAVALVFG-DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHivgvdklapattalalsqiidrseplqsdiniHGDELAAVLFTS 197
Cdd:cd17649 80 LEDSGAGLL------------------------LTH--------------------------------HPRQLAYVIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGhATGFLHGVTAPFLIGARSVLLD---IFTPEACLTLLA 274
Cdd:cd17649 104 GSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGACVVLRPdelWASADELAEMVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSGATPFIYDLLC-AVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNLGdstsR 353
Cdd:cd17649 183 ELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKC----E 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 MMNTDGYAAT-------GVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA-----RALDNEG--WYYSGDLC 419
Cdd:cd17649 259 AGAARAGASMpigrplgGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAerfvpDPFGAPGsrLYRTGDLA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 420 RMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDErLGERSCAYVVLKPPHLSLTLEEVIAFFS 499
Cdd:cd17649 339 RWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPELRAQLRTAL 417
|
490 500 510
....*....|....*....|....*....|...
gi 604198150 500 RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd17649 418 RASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
31-526 |
8.90e-54 |
|
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: 189.48 E-value: 8.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:cd17651 2 ERQAARTPDAPALVAE-GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLNKCQAKiffaptvfkqnrpvdLILPLQnqlrHLTHIVGVDKLAPATTALALSQIIDRSEPlqsDINIHGDEL 190
Cdd:cd17651 81 AERLAFMLADAGPV---------------LVLTHP----ALAGELAVELVAVTLLDQPGAAAGADAEP---DPALDADDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFlHGVTAPFLIGARSVLL--DI-FTPE 267
Cdd:cd17651 139 AYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLPpeEVrTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 ACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGG--TIIPKKVARDC-QQRGIKLLSIYGSTESSPHSM 344
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGeqLVLTEDLREFCaGLPGLRLHNHYGPTETHVVTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDSTSRMMNTD--GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR------ALDNEGWYYSG 416
Cdd:cd17651 298 LSLPGDPAAWPAPPpiGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAErfvpdpFVPGARMYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 417 DLCRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVI 495
Cdd:cd17651 378 DLARWLPDGELEFLGRADDqVKIR-GFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEA-PVDAAELR 455
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 496 AFFSRkRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17651 456 AALAT-HLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
51-533 |
1.13e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 190.30 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAfqlpgwcefTL---------IYLACLKTGAVSVPLLPAWREAELVWVLNKC 121
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVG---------TLawngyrhleAYYGVSGSGAVCHTINPRLFPEQIAYIVNHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 122 QAKIFFAPTVFKqnrP-VDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDELAAVL-FTSGT 199
Cdd:PRK07008 111 EDRYVLFDLTFL---PlVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLcYTSGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 200 EGMPKGVMLTHNNILAseRAYCARL----NLTWQDVFLMPAPLGH--ATGFLHGVTapfLIGARSVL----LDiftPEAC 269
Cdd:PRK07008 188 TGNPKGALYSHRSTVL--HAYGAALpdamGLSARDAVLPVVPMFHvnAWGLPYSAP---LTGAKLVLpgpdLD---GKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQ-RGIKLLSIYGSTESSP------- 341
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDeYGVEVIHAWGMTEMSPlgtlckl 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 ---HSMVNLgDSTSRMMNTDGYAATGVEIKIVDEDRNTLP--AGHEGEEASRGPNVFMGYL--DEPELTaraldnEGWYY 414
Cdd:PRK07008 340 kwkHSQLPL-DEQRKLLEKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVRGPWVIDRYFrgDASPLV------DGWFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 415 SGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEV 494
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR-PGAEVTREEL 491
|
490 500 510
....*....|....*....|....*....|....*....
gi 604198150 495 IAFFSRKrVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK07008 492 LAFYEGK-VAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-533 |
1.23e-53 |
|
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: 188.02 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFfapt 130
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 131 vfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqIIDRSeplqsdinihgDELAAVLFTSGTEGMPKGVMLTH 210
Cdd:cd05971 83 -----------------------------------------VTDGS-----------DDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 211 NNILASERAYCARLNLTWQ--DVFLMPAPLGHATGFLhGVTAPFLIGARSVL---LDIFTPEACLTLLAQQRCTcMSGAT 285
Cdd:cd05971 111 RVLLGHLPGVQFPFNLFPRdgDLYWTPADWAWIGGLL-DVLLPSLYFGVPVLahrMTKFDPKAALDLMSRYGVT-TAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 286 PFIYDLLCAVEQQ--PADLSsLRFFLCGGTIIPKKV---ARDcqQRGIKLLSIYGSTESSphsMVnLGDSTSRMMNTD-- 358
Cdd:cd05971 189 PTALKMMRQQGEQlkHAQVK-LRAIATGGESLGEELlgwARE--QFGVEVNEFYGQTECN---LV-IGNCSALFPIKPgs 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 359 -GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPN--VFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGRKKD 435
Cdd:cd05971 262 mGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAG-DWLLTGDLGRKDSDGYFWYVGRDDD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 436 IIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHL-SLTLEEVIAFFSRKRVAKYKYPERIVI 514
Cdd:cd05971 341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETpSDALAREIQELVKTRLAAHEYPREIEF 420
|
490
....*....|....*....
gi 604198150 515 VEKLPRTASGKVQKFLLRQ 533
Cdd:cd05971 421 VNELPRTATGKIRRRELRA 439
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-526 |
1.30e-53 |
|
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: 188.63 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDnHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLP-GWcEFTLIYLACLKTGAVSVPLLPAWREAELVW 116
Cdd:cd12114 1 PDATAVIC-GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPkGP-EQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 117 VLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIHGDELAAVLFT 196
Cdd:cd12114 79 ILADAGARLV------------------------LTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 197 SGTEGMPKGVMLTH----NNILASERaycaRLNLTWQDVFLMPAPLGH--ATGFLHGVTApflIGARSVLLD---IFTPE 267
Cdd:cd12114 135 SGSTGTPKGVMISHraalNTILDINR----RFAVGPDDRVLALSSLSFdlSVYDIFGALS---AGATLVLPDearRRDPA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 ACLTLLAQQRCTcMSGATPFIYDLLCAV-EQQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPHSM 344
Cdd:cd12114 208 HWAELIERHGVT-LWNSVPALLEMLLDVlEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDSTsrmmNTD------GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL----DNEGWYY 414
Cdd:cd12114 287 YHPIDEV----PPDwrsipyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 415 SGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMpDERLGERSCAYVVLKPPHLSLTLEEV 494
Cdd:cd12114 363 TGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDAL 441
|
490 500 510
....*....|....*....|....*....|..
gi 604198150 495 IAFFSrKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd12114 442 RAFLA-QTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-528 |
1.83e-52 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 187.02 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIA-VVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK05852 17 RIADLVEVAATRLPEAPAlVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKIffapTVFKQNRPVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDI 183
Cdd:PRK05852 97 PLDPALPIAEQRVRSQAAGARV----VLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 184 NIHGDElAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPfLIGARSVLLDI 263
Cdd:PRK05852 173 GLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAT-LASGGAVLLPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMS--GATPFIYDLL---CAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGST 337
Cdd:PRK05852 251 RGRFSAHTFWDDIKAVGATwyTAVPTIHQILlerAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEfAAPVVCAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 338 ESSpHSMVNLG------DSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALdNEG 411
Cdd:PRK05852 331 EAT-HQVTTTQiegigqTENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhLSLTL 491
Cdd:PRK05852 409 WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES-APPTA 487
|
490 500 510
....*....|....*....|....*....|....*..
gi 604198150 492 EEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK05852 488 EELVQ-FCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
46-532 |
2.73e-52 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 187.01 E-value: 2.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 46 NHGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAEL---------- 114
Cdd:PRK08751 46 SFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELkhqlidsgas 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 115 --VWVLNKCQA-KIFFAPTVFKQNRPVDLILPLQNQLRHLTHIV--GVDKLAPATT---------ALALSqiidrSEPLQ 180
Cdd:PRK08751 126 vlVVIDNFGTTvQQVIADTPVKQVITTGLGDMLGFPKAALVNFVvkYVKKLVPEYRingairfreALALG-----RKHSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 181 SDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQ-----DVFLMPAPLGHatgfLHGVTAPFLI- 254
Cdd:PRK08751 201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYH----IFALTANGLVf 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 ----GARSVLLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQ-RGIK 329
Cdd:PRK08751 277 mkigGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQvTGLT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 330 LLSIYGSTESSPHSMVNlgdstsrMMNTDGY-AATGVEIK-----IVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELT 403
Cdd:PRK08751 357 LVEAYGLTETSPAACIN-------PLTLKEYnGSIGLPIPstdacIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEET 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 404 ARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLK 483
Cdd:PRK08751 430 AKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 604198150 484 PPhlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK08751 510 DP--ALTAEDVKA-HARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-540 |
6.66e-52 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 185.57 E-value: 6.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDN-HGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV 101
Cdd:PLN02330 27 KLTLPDFVLQDAELYADKVAFVEAvTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 102 SVPLLPAWREAELVWVLNKCQAKIFFAPTVfKQNRPVDLILPLQnqlrhlthIVGVDKLAPATTALALSQIIDRSEPLQS 181
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDT-NYGKVKGLGLPVI--------VLGEEKIEGAVNWKELLEAADRAGDTSD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 182 DINIHGDELAAVLFTSGTEGMPKGVMLTHNNILAS--ERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSV 259
Cdd:PLN02330 178 NEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANlcSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 260 LLDIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRF---FLCGGTIIPKKV-ARDCQQRGIKLLSIYG 335
Cdd:PLN02330 258 VMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaiMTAAAPLAPELLtAFEAKFPGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 336 STEsspHSMVNL--GDSTS----RMMNTDGYAATGVEIKIVDEDRN-TLPAGHEGEEASRGPNVFMGYLDEPELTARALD 408
Cdd:PLN02330 338 LTE---HSCITLthGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 409 NEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlS 488
Cdd:PLN02330 415 EDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPK--A 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 604198150 489 LTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLR 540
Cdd:PLN02330 493 KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINK 544
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
32-533 |
1.03e-50 |
|
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: 182.44 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 32 QTARAVPDKIAVV-----DNHGASWTYAALDYAASRLANWLLSQGiQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLL 106
Cdd:cd05931 1 RRAAARPDRPAYTflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 107 PAWREAELVWVLNkcqakiffaptVFKQNRPVdLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLQSDINIH 186
Cdd:cd05931 80 PPTPGRHAERLAA-----------ILADAGPR-VVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 187 GDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLdifTP 266
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM---SP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLT-------LLAQQRCTCmSGATPFIYDLLC--AVEQQPA--DLSSLRFFLCGGTIIPKKVARDCQQR----GIK-- 329
Cdd:cd05931 225 AAFLRrplrwlrLISRYRATI-SAAPNFAYDLCVrrVRDEDLEglDLSSWRVALNGAEPVRPATLRRFAEAfapfGFRpe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 330 -LLSIYGSTESS------------------------PHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNT-LPAGHEG 383
Cdd:cd05931 304 aFRPSYGLAEATlfvsggppgtgpvvlrvdrdalagRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGReLPDGEVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 384 EEASRGPNVFMGYLDEPELTAR------ALDNEGWYYSGDLCRMDeDGYIKITGRKKDIIIRGGENISSREVEDILLQHP 457
Cdd:cd05931 384 EIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAH 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 458 ---RIHDACVVAMPDERlGERSCAYVVLKPPHLSLTLEEVIAFFsRKRVAKYK--YPERIVIVE--KLPRTASGKVQKFL 530
Cdd:cd05931 463 palRPGCVAAFSVPDDG-EERLVVVAEVERGADPADLAAIAAAI-RAAVAREHgvAPADVVLVRpgSIPRTSSGKIQRRA 540
|
...
gi 604198150 531 LRQ 533
Cdd:cd05931 541 CRA 543
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
38-532 |
6.52e-50 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 180.42 E-value: 6.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDN-HGASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELV 115
Cdd:PLN02574 53 NGDTALIDSsTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 116 WVLNKCQAKIFFAPTvfkqnRPVDLILPLQNQLRHLTHIVGVDKLAPATTALAlSQIIDRSEPLQSDInIHGDELAAVLF 195
Cdd:PLN02574 133 KRVVDCSVGLAFTSP-----ENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFY-ELIKEDFDFVPKPV-IKQDDVAAIMY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNIL----------ASERAYCARLNltwqdVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 265
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIamvelfvrfeASQYEYPGSDN-----VYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPAD-LSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPH 342
Cdd:PLN02574 281 ASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SMVNLGDSTSRMMNTDGYAATGVEIKIVD-EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRM 421
Cdd:PLN02574 361 GTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 422 DEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlKPPHLSLTLEEVIAFFSrK 501
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-RRQGSTLSQEAVINYVA-K 518
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 502 RVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PLN02574 519 QVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
194-532 |
1.01e-49 |
|
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: 177.95 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVM--LTHNNILASERAYCArLNLTWQ--DVFLMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPEAC 269
Cdd:cd05929 131 LYSGGTTGRPKGIKrgLPGGPPDNDTLMAAA-LGFGPGadSVYLSPAPLYHAAPFRWSMTALFM-GGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTLLAQQRCTCMSGATPFIYDLLCAVEQQPA--DLSSLRFFLCGGTIIPKKVARD-CQQRGIKLLSIYGSTESSPHSMVN 346
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKLPEAVRNayDLSSLKRVIHAAAPCPPWVKEQwIDWGGPIIWEYYGGTEGQGLTIIN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 347 lGDSTSRMMNTDGYAATGvEIKIVDEDRNTLPAGHEGEEASRGPNVFMgYLDEPELTARALDNEGWYYSGDLCRMDEDGY 426
Cdd:cd05929 289 -GEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 427 IKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTL--EEVIAFFsRKRVA 504
Cdd:cd05929 366 LYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaEELIAFL-RDRLS 444
|
330 340
....*....|....*....|....*...
gi 604198150 505 KYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
63-539 |
3.36e-49 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 178.45 E-value: 3.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 63 LANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAElvwvlnkcqakiffAPTVFKQNRPVDLIL 142
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEE--------------AKSAMLLVRPVMLVT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 143 ---------PLQN-QLRHLTHIVGVDKLAPaTTALALSQIIDRSE-------PLQSDINIHGDELAAVLFTSGTEGMPKG 205
Cdd:PLN02860 111 detcsswyeELQNdRLPSLMWQVFLESPSS-SVFIFLNSFLTTEMlkqralgTTELDYAWAPDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 206 VMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMSGAT 285
Cdd:PLN02860 190 VTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGG-LSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 286 PFIYDLL--CAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQ--RGIKLLSIYGSTES-SPHSMVNLGDSTSRMMNTD-- 358
Cdd:PLN02860 269 AMMADLIslTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTEAcSSLTFMTLHDPTLESPKQTlq 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 359 ------------------GYAATGVEIKIVDEDrntlpAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCR 420
Cdd:PLN02860 349 tvnqtksssvhqpqgvcvGKPAPHVELKIGLDE-----SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGW 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 421 MDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLK---------PPH----L 487
Cdd:PLN02860 424 IDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRdgwiwsdneKENakknL 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 604198150 488 SLTLEEVIAFFSRKRVAKYKYPERIVIVEK-LPRTASGKVQKFLLRQDIIERL 539
Cdd:PLN02860 504 TLSSETLRHHCREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREVLSHL 556
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-528 |
5.00e-49 |
|
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: 175.57 E-value: 5.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd17643 1 PEAVAVVDED-RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAkiffaptvfkqnrpvdlilplqnqlrhlthivgvdklapattALALSQiidrseplqsdinihGDELAAVLFTS 197
Cdd:cd17643 80 LADSGP------------------------------------------SLLLTD---------------PDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMpaplGHATGF------LHGvtaPFLIGARSVLLDIFT---PEA 268
Cdd:cd17643 103 GSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTL----FHSYAFdfsvweIWG---ALLHGGRLVVVPYEVarsPED 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSgATP--FiYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR----GIKLLSIYGSTESSPH 342
Cdd:cd17643 176 FARLLRDEGVTVLN-QTPsaF-YQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRfgldRPQLVNMYGITETTVH 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SmvnlgdSTSRMMNTDGYAATGVEI---------KIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR-----ALD 408
Cdd:cd17643 254 V------TFRPLDAADLPAAAASPIgrplpglrvYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanPFG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 409 NEG--WYYSGDLCRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlkPP 485
Cdd:cd17643 328 GPGsrMYRTGDLARRLPDGELEYLGRADEqVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV--AD 404
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 604198150 486 HLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17643 405 DGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
34-533 |
2.17e-48 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 175.72 E-value: 2.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAvSVPLL------P 107
Cdd:PRK13382 53 AQRCPDRPGLIDELG-TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLntsfagP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 108 AWREaelVWVLNKCQAKIF---FAPTVFK--QNRPvdlilplqnqlrHLTHIVGVDKLAPATTALALsqiidRSEPLQSD 182
Cdd:PRK13382 131 ALAE---VVTREGVDTVIYdeeFSATVDRalADCP------------QATRIVAWTDEDHDLTVEVL-----IAAHAGQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 INIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTApFLIGARSVLLD 262
Cdd:PRK13382 191 PEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLA-ASLACTIVTRR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 IFTPEACLTLLAQQRCTCMSgATPFIYD-LLCAVEQ--QPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTE 338
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLA-VVPVMFDrIMDLPAEvrNRYSGRSLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 SSPHSMVNLGDsTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYldepelTARALDN--EGWYYSG 416
Cdd:PRK13382 349 AGMIATATPAD-LRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGSTKDfhDGFMASG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 417 DLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIA 496
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK-PGASATPETLKQ 500
|
490 500 510
....*....|....*....|....*....|....*..
gi 604198150 497 FFsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK13382 501 HV-RDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
38-531 |
3.79e-48 |
|
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: 174.05 E-value: 3.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVdNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd17655 11 PDHTAVV-FEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIFFAptvfkqnrpvdlilplQNQLRHLTHIVG-VDKLAPATTAlalsqiIDRSEPLQSDINIhgDELAAVLFT 196
Cdd:cd17655 90 LEDSGADILLT----------------QSHLQPPIAFIGlIDLLDEDTIY------HEESENLEPVSKS--DDLAYVIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 197 SGTEGMPKGVMLTH----NNILASERAYcarlNLTWQDVFLMPAPLgHATGFLHGVTAPFLIGARSVLL---DIFTPEAC 269
Cdd:cd17655 146 SGSTGKPKGVMIEHrgvvNLVEWANKVI----YQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVrkeTVLDGQAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTLLAQQRCTCMSGaTPFIYDLLCAVEQQPAdlSSLRFFLCGGTIIPKKVAR---DCQQRGIKLLSIYGSTESSPHSMVN 346
Cdd:cd17655 221 TQYIRQNRITIIDL-TPAHLKLLDAADDSEG--LSLKHLIVGGEALSTELAKkiiELFGTNPTITNAYGPTETTVDASIY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 347 LGDSTSRMMNTD--GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARA-LDN-----EGWYYSGDL 418
Cdd:cd17655 298 QYEPETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfVDDpfvpgERMYRTGDL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 419 CRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlsLTLEEVIAF 497
Cdd:cd17655 378 ARWLPDGNIEFLGRIDHqVKIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE---LPVAQLREF 453
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 498 FSRKrVAKYKYPERIVIVEKLPRTASGKVQKFLL 531
Cdd:cd17655 454 LARE-LPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
192-532 |
3.90e-48 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 175.80 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNilaserAYCARLN--LTWQ----DVFLMPAPLGHATGFLHGVTAPFLIGArSVLLDIFT 265
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRG------AYLMALSnaLIWGmnegAVYLWTLPMFHCNGWCFTWTLAALCGT-NICLRQVT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSGATPFIYDLLCA-VEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSM 344
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPST 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 V--------NLGDST-SRMMNTDGYAATGVE-IKIVD-EDRNTLPAGHE--GEEASRGPNVFMGYLDEPELTARALDNeG 411
Cdd:PLN02479 352 VcawkpewdSLPPEEqARLNARQGVRYIGLEgLDVVDtKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAFAN-G 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKP---PHLS 488
Cdd:PLN02479 431 WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPgvdKSDE 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 604198150 489 LTLEEVIAFFSRKRVAKYKYPeRIVIVEKLPRTASGKVQKFLLR 532
Cdd:PLN02479 511 AALAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVLR 553
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
191-528 |
1.55e-46 |
|
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: 165.90 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNN-ILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGAR----------SV 259
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCvtggenttykSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 260 LLDIFTPEACLTLLAQqrcTCMSGATPFIYDLLCAVEQqpadlssLRFFLCGGT-IIPKKVARDCQQRGIKLLSIYGSTE 338
Cdd:cd17635 84 FKILTTNAVTTTCLVP---TLLSKLVSELKSANATVPS-------LRLIGYGGSrAIAADVRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 SSPHSMVNLGDStSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALdNEGWYYSGDL 418
Cdd:cd17635 154 TGTALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 419 CRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVL---KPPHLSLTLEEVI 495
Cdd:cd17635 232 GERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAIRALKHTI 311
|
330 340 350
....*....|....*....|....*....|...
gi 604198150 496 affsRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17635 312 ----RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-525 |
8.87e-46 |
|
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: 164.48 E-value: 8.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 193 VLFTSGTEGMPKGVMLTHNNI---LASERAYCARLNLTWQD-----------VFLMPAPLGHATGFLHGVTApFLIGARS 258
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDahkaaaaaagtVMFPAPPLMHGTGSWTAFGG-LLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 259 VLLDI-FTPEACLTLLAQQRCTCMS--G---ATPFIYDLlcaVEQQPADLSSLRFFLCGGTIIPKKVardcQQR------ 326
Cdd:cd05924 87 VLPDDrFDPEEVWRTIEKHKVTSMTivGdamARPLIDAL---RDAGPYDLSSLFAISSGGALLSPEV----KQGllelvp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 GIKLLSIYGSTESSphsmvNLGDSTSRMMNTDGYAATGV--EIKIVDEDRNTLPAGHEGEE--ASRGpNVFMGYLDEPEL 402
Cdd:cd05924 160 NITLVDAFGSSETG-----FTGSGHSAGSGPETGPFTRAnpDTVVLDDDGRVVPPGSGGVGwiARRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 403 TARA---LDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAY 479
Cdd:cd05924 234 TAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 604198150 480 VVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGK 525
Cdd:cd05924 314 VQLREGA-GVDLEELRE-HCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
33-539 |
3.90e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 165.72 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 33 TARAVPDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPgDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREA 112
Cdd:PRK07638 10 HASLQPNKIAIKEND-RVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 113 ELVWVLNKCQAKIFFAPTvFKQNRPVDLILPlqnqlrhlthIVGVDKLAPATT--ALALSQIIDrsepLQSDINIHGdel 190
Cdd:PRK07638 88 ELKERLAISNADMIVTER-YKLNDLPDEEGR----------VIEIDEWKRMIEkyLPTYAPIEN----VQNAPFYMG--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 aavlFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATgFLHGVTAPFLIGARSVLLDIFTPEACL 270
Cdd:PRK07638 150 ----FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRKFIPNQVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 271 TLLAQQRCTCMSGaTPFIYDLLCAVEQQPAdlSSLRFFLCGG--TIIPKKVARDcQQRGIKLLSIYGSTESSPHSMVNLG 348
Cdd:PRK07638 225 DKLETENISVMYT-VPTMLESLYKENRVIE--NKMKIISSGAkwEAEAKEKIKN-IFPYAKLYEFYGASELSFVTALVDE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 349 DSTsRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELtARALDNEGWYYSGDLCRMDEDGYIK 428
Cdd:PRK07638 301 ESE-RRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL-ARELNADGWMTVRDVGYEDEEGFIY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 429 ITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVvlkppHLSLTLEEVIAfFSRKRVAKYKY 508
Cdd:PRK07638 379 IVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII-----KGSATKQQLKS-FCLQRLSSFKI 452
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 509 PERIVIVEKLPRTASGKVQKFLLRQDIIERL 539
Cdd:PRK07638 453 PKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-526 |
4.36e-45 |
|
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: 164.73 E-value: 4.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWreaelvwv 117
Cdd:cd17652 1 PDAPAVVFG-DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAY-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 lnkcqakiffaptvfkqnrpvdlilPLQnQLRHLthivgvdkLAPATTALALSQiidrseplqsdinihGDELAAVLFTS 197
Cdd:cd17652 72 -------------------------PAE-RIAYM--------LADARPALLLTT---------------PDNLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHgVTAPFLIGARSVLLD---IFTPEACLTLLA 274
Cdd:cd17652 103 GSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATLVLAPaeeLLPGEPLADLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSgATPfiyDLLCAVEqqPADLSSLRFFLCGGTIIPKK-VARDCQQRgiKLLSIYGSTESSPHSMVNLGDSTSR 353
Cdd:cd17652 182 EHRITHVT-LPP---AALAALP--PDDLPDLRTLVVAGEACPAElVDRWAPGR--RMINAYGPTETTVCATMAGPLPGGG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 MMnTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA-RALDN------EGWYYSGDLCRMDEDGY 426
Cdd:cd17652 254 VP-PIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAeRFVADpfgapgSRMYRTGDLARWRADGQ 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 427 IKITGRKKD-IIIRGgENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAK 505
Cdd:cd17652 333 LEFLGRADDqVKIRG-FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGA-APTAAELRA-HLAERLPG 409
|
490 500
....*....|....*....|.
gi 604198150 506 YKYPERIVIVEKLPRTASGKV 526
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKL 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
35-526 |
9.88e-45 |
|
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: 166.60 E-value: 9.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 35 RAVPDKIAVV---DNHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:cd17634 64 RENGDRTAIIyegDDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFF-APTVFKQNRPVDLIL----PLQNQLRHLTHIVGVDKLAPATTA-----LALSQIIDRSEPL 179
Cdd:cd17634 144 APEAVAGRIIDSSSRLLItADGGVRAGRSVPLKKnvddALNPNVTSVEHVIVLKRTGSDIDWqegrdLWWRDLIAKASPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNI---LASERAYCarLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGA 256
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYlvyAATTMKYV--FDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 257 RSVLLDIF----TPEACLTLLAQQRCTCMSGATPFIYDLLCA----VEQQpaDLSSLR-FFLCGGTIIPKKVA---RDCQ 324
Cdd:cd17634 302 TTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaIEGT--DRSSLRiLGSVGEPINPEAYEwywKKIG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 325 QRGIKLLSIYGSTESSPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGE---EASRGPNVFMGYLDEPE 401
Cdd:cd17634 380 KEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNlviTDPWPGQTRTLFGDHER 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 402 LTARALDN-EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYV 480
Cdd:cd17634 460 FEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYV 539
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 604198150 481 VLKP-----PHLSLTLEEVIaffsRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17634 540 VLNHgvepsPELYAELRNWV----RKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
52-534 |
2.20e-44 |
|
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: 163.30 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFaptv 131
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 fkqnrpvdlilpLQNqlrhlthivgvdklapattalalsqiidrseplqsdiniHGDELAAVLFTSGTEGMPKGVMLTHN 211
Cdd:cd17640 83 ------------VEN---------------------------------------DSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NILASERAYCARLNLTWQDVFLMPAPLGHA-------TGFLHGVTAPFlIGARSVLLDI--FTPeaclTLLAqqrctcms 282
Cdd:cd17640 112 NLLHQIRSLSDIVPPQPGDRFLSILPIWHSyersaeyFIFACGCSQAY-TSIRTLKDDLkrVKP----HYIV-------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 283 gATPFIYD-LLCAVEQQPADLSS--------------LRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNL 347
Cdd:cd17640 179 -SVPRLWEsLYSGIQKQVSKSSPikqflflfflsggiFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 348 GDSTSRmmNTDGYAATGVEIKIVDED-RNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGY 426
Cdd:cd17640 258 LKCNVR--GSVGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 427 IKITGRKKD-IIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLG-------ERSCAYVVLKPPHLSLTLEEVIAff 498
Cdd:cd17640 336 LVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGalivpnfEELEKWAKESGVKLANDRSQLLA-- 413
|
490 500 510
....*....|....*....|....*....|....*..
gi 604198150 499 SRKRVAKYKyPERIVIVEKLPRTASG-KVQKFLLRQD 534
Cdd:cd17640 414 SKKVLKLYK-NEIKDEISNRPGFKSFeQIAPFALLEE 449
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
195-526 |
7.46e-44 |
|
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: 158.34 E-value: 7.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLDIFTPEACLTLLA 274
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSGATPFIYDLlcAVEQQPadLSSLRFFLCGGTIIPKKVARDCQQ--RGIKLLSIYGSTESSPHSMvnLGDSTS 352
Cdd:cd17633 86 QYNATVIYLVPTMLQAL--ARTLEP--ESKIKSIFSSGQKLFESTKKKLKNifPKANLIEFYGTSELSFITY--NFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 353 RMMNTDGYAATGVEIKIVDEDrntlpAGHEGEEASRGPNVFMGYLDEPELTaraldNEGWYYSGDLCRMDEDGYIKITGR 432
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSN-----PDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 433 KKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpphlSLTLEEVIAFFsRKRVAKYKYPERI 512
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD----KLTYKQLKRFL-KQKLSRYEIPKKI 304
|
330
....*....|....
gi 604198150 513 VIVEKLPRTASGKV 526
Cdd:cd17633 305 IFVDSLPYTSSGKI 318
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
34-532 |
3.91e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 160.56 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAV-VDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTG----AVSVPLLPA 108
Cdd:PRK13390 7 AQIAPDRPAViVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGlyitAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 109 wreaELVWVLNKCQAKIFFAPTVfkqnrpvdlilplqnqLRHLTHIVGvdklAPATTALALSQIIDRSEPLQSDINIHGD 188
Cdd:PRK13390 87 ----EADYIVGDSGARVLVASAA----------------LDGLAAKVG----ADLPLRLSFGGEIDGFGSFEAALAGAGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 EL------AAVLFTSGTEGMPKGVM---------LTHNNILASERAYcarLNLTWQDVFLMPAPLGHAT-----GFLHGv 248
Cdd:PRK13390 143 RLteqpcgAVMLYSSGTTGFPKGIQpdlpgrdvdAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHA- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 249 tapflIGARSVLLDIFTPEACLTLLAQQRCTCMSGA-TPFIYDL-LCAVEQQPADLSSLRFFLCGGTIIPKkvarDCQQR 326
Cdd:PRK13390 219 -----LGGTVVLAKRFDAQATLGHVERYRITVTQMVpTMFVRLLkLDADVRTRYDVSSLRAVIHAAAPCPV----DVKHA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 GIKLL-----SIYGSTESSPHSMVNLGDSTSRMMNTdGYAATGvEIKIVDEDRNTLPAGHEGE---EASRGPnvfMGYLD 398
Cdd:PRK13390 290 MIDWLgpivyEYYSSTEAHGMTFIDSPDWLAHPGSV-GRSVLG-DLHICDDDGNELPAGRIGTvyfERDRLP---FRYLN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 399 EPELTARALD--NEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERS 476
Cdd:PRK13390 365 DPEKTAAAQHpaHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQV 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 604198150 477 CAYVVLKP---PHLSLTLEevIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK13390 445 KAVIQLVEgirGSDELARE--LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-545 |
9.36e-43 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 164.56 E-value: 9.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 30 WRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:PRK12467 518 IEAQARQHPERPALVFG-EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNkcqakiffaptvfkqNRPVDLILPLQNQLRHLTHIVGVDKLapaTTALALSQIIDRSEpLQSDINIHGDE 189
Cdd:PRK12467 597 PQDRLAYMLD---------------DSGVRLLLTQSHLLAQLPVPAGLRSL---CLDEPADLLCGYSG-HNPEVALDPDN 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 190 LAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGhATGFLHGVTAPFLIGARSVLLD---IFTP 266
Cdd:PRK12467 658 LAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA-FDLGVTELFGALASGATLHLLPpdcARDA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLTLLAQQRCTCMSgATPFIYDLLCAVEqQPADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPHSM 344
Cdd:PRK12467 737 EAFAALMADQGVTVLK-IVPSHLQALLQAS-RVALPRPQRALVCGGEALQVDLLARVRALgpGARLINHYGPTETTVGVS 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 V-NLGDSTSRMMNTD-GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR-------ALDNEGWYYS 415
Cdd:PRK12467 815 TyELSDEERDFGNVPiGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAErfvpdpfGADGGRLYRT 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 416 GDLCRMDEDGYIKITGRKKD-IIIRgGENISSREVEDILLQHPRIHDACVVAMPDERlGERSCAYVVL-------KPPHL 487
Cdd:PRK12467 895 GDLARYRADGVIEYLGRMDHqVKIR-GFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPaavadgaEHQAT 972
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 488 SLTLEEVIaffsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK12467 973 RDELKAQL----RQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVA 1026
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
51-465 |
8.34e-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: 157.25 E-value: 8.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFF--- 127
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 -------APTVfkQNRPVDLILPLqnqlrhlthivgvdkLAPATTALALSQIIDRSEPLQSDINIHGDELAAVLFTSGTE 200
Cdd:cd05932 87 lddwkamAPGV--PEGLISISLPP---------------PSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 201 GMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHAT--------GFLHGVTAPFligARSvlLDIFTPE---AC 269
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTervfveggSLYGGVLVAF---AES--LDTFVEDvqrAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 LTL---------LAQQRCTCMSGAT--------PFIYDLlcaVEQQPAD---LSSLRFFLCGGTIIPKKVARDCQQRGIK 329
Cdd:cd05932 225 PTLffsvprlwtKFQQGVQDKIPQQklnlllkiPVVNSL---VKRKVLKglgLDQCRLAGCGSAPVPPALLEWYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 330 LLSIYGSTESSPHSMVNL-GDstsRMMNTDGYAATGVEIKIVDEdrntlpagheGEEASRGPNVFMGYLDEPELTARALD 408
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYpGR---DKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFT 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 409 NEGWYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVEDILLQHPRIHDACVV 465
Cdd:cd05932 369 ADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
28-533 |
3.99e-41 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 154.62 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 28 DYWRQTARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLP 107
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 108 AWREAELVWVLNKCQAKIFFAptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrSEPlqsdinihg 187
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLT-----------------------------------------------SSP--------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAplGHAtgFlhGVTapfligarsvLLDIFTPe 267
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYT--F--DVS----------ILEIFTT- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 acltlLAQQRCTCM---------------------SGATPFIYDLLcaveqQPADLSSLRFFLCGGTIIPKKVARDCQQR 326
Cdd:cd05918 169 -----LAAGGCLCIpseedrlndlagfinrlrvtwAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWADR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 gIKLLSIYGSTESSPHSMVNLGDSTSRMMNTdGYAATGVeIKIVDEDRNT--LPAGHEGEEASRGPNVFMGYLDEPELTA 404
Cdd:cd05918 239 -VRLINAYGPAECTIAATVSPVVPSTDPRNI-GRPLGAT-CWVVDPDNHDrlVPIGAVGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 405 RA-LDNEGW------------YYSGDLCRMDEDGYIKITGRKKDII-IRGgenisSR----EVEDILLQH-PRIHDACV- 464
Cdd:cd05918 316 AAfIEDPAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVkIRG-----QRvelgEIEHHLRQSlPGAKEVVVe 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 465 ----------------VAMPDERLGERSCAYVVLKPPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd05918 391 vvkpkdgssspqlvafVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDR 470
|
....*
gi 604198150 529 FLLRQ 533
Cdd:cd05918 471 RALRE 475
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
62-539 |
4.95e-41 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 155.95 E-value: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 62 RLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAPTVFKQ-NRPVDL 140
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 141 ILPLQNQLRHLtHIVGVDKL----APATTALALSQIIDRSEP----LQSDINIHGDELAAVL-FTSGTEGMPKGVMLTHN 211
Cdd:PLN03102 131 LLSSEDSNLNL-PVIFIHEIdfpkRPSSEELDYECLIQRGEPtpslVARMFRIQDEHDPISLnYTSGTTADPKGVVISHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NilaserAYCARLNLT--WQ----DVFLMPAPLGHATGFLH--GVTAPfliGARSVLLDIFTPEACLTLLAQQRCTCMSg 283
Cdd:PLN03102 210 G------AYLSTLSAIigWEmgtcPVYLWTLPMFHCNGWTFtwGTAAR---GGTSVCMRHVTAPEIYKNIEMHNVTHMC- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 284 ATPFIYDLLC---AVEQQPAdlSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESS-PHSMVNLGDSTSRM---MN 356
Cdd:PLN03102 280 CVPTVFNILLkgnSLDLSPR--SGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgPVLFCEWQDEWNRLpenQQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 357 TDGYAATGVEI-KIVDED-RNT-----LPAGHE--GEEASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYI 427
Cdd:PLN03102 358 MELKARQGVSIlGLADVDvKNKetqesVPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAFKH-GWLNTGDVGVIHPDGHV 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 428 KITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLK--------PPHLSLTLEEVIAFFS 499
Cdd:PLN03102 437 EIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgettkedRVDKLVTRERDLIEYC 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 604198150 500 RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRqDIIERL 539
Cdd:PLN03102 517 RENLPHFMCPRKVVFLQELPKNGNGKILKPKLR-DIAKGL 555
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-545 |
1.87e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 157.81 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK12316 2013 AARAPEAIAVVFG-DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKIFFAptvfkqNRPVDLILPLQNQLRHLthivgvdklaPATTALALSQIIDRSEPLQsdinIHGDELAAV 193
Cdd:PRK12316 2092 LAYMLEDSGAALLLT------QRHLLERLPLPAGVARL----------PLDRDAEWADYPDTAPAVQ----LAGENLAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLD--IFTPEACLT 271
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSF-DGAHEQWFHPLLNGARVLIRDdeLWDPEQLYD 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 272 LLAQQRCTCMSGATPFIYDLL--CAVEQQPAdlsSLRFFLCGGTIIPKKVARDCQQ--RGIKLLSIYGSTESSPHSMVNL 347
Cdd:PRK12316 2231 EMERHGVTILDFPPVYLQQLAehAERDGRPP---AVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVVTPLLWK 2307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 348 GDStsrmmnTDGYAATGVEIK---------IVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR-----ALDNEG-- 411
Cdd:PRK12316 2308 CRP------QDPCGAAYVPIGralgnrrayILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAErfvpdPFSASGer 2381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMpDERLGERSCAYVVlkPPHLSLT 490
Cdd:PRK12316 2382 LYRTGDLARYRADGVVEYLGRiDHQVKIRGFR-IELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDAAED 2457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 604198150 491 LEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK12316 2458 LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA 2512
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
49-533 |
2.28e-40 |
|
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: 152.97 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 49 ASWTYAALDYA-------ASRLANWLLSQGIQPGDRVAF---QLPGWCEftlIYLACLKTGAVSVPLLPAWREAELVWVL 118
Cdd:cd05915 16 RLHTGEVHRTTyaevyqrARRLMGGLRALGVGVGDRVATlgfNHFRHLE---AYFAVPGMGAVLHTANPRLSPKEIAYIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 119 NKCQAKIFFAPTVFKQNRPVDLIL---PLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPLqsdinihgdelaAVLF 195
Cdd:cd05915 93 NHAEDKVLLFDPNLLPLVEAIRGElktVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAAC------------GMAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNILASERAYCARLNLTWQD--VFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLL 273
Cdd:cd05915 161 TTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 274 AQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTES---------SPHSM 344
Cdd:cd05915 241 DGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETspvvvqnfvKSHLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPagHEGEE----ASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCR 420
Cdd:cd05915 321 SLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVP--KDGKAlgevQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 421 MDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSltLEEVIAFFSR 500
Cdd:cd05915 399 WDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPT--PEELNEHLLK 476
|
490 500 510
....*....|....*....|....*....|...
gi 604198150 501 KRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05915 477 AGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-528 |
4.02e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 156.66 E-value: 4.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK12316 4561 ARMTPDAVAVVFD-EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLnkcqakiffaptvfkQNRPVDLILPLQNQLRHLTHIVGVDKLApattalalsqiIDRSEPLQS------DINIHG 187
Cdd:PRK12316 4640 LAYMM---------------EDSGAALLLTQSHLLQRLPIPDGLASLA-----------LDRDEDWEGfpahdpAVRLHP 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLD--IFT 265
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF-DGSHEGLYHPLINGASVVIRDdsLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQpADLSSLRFFLCGGtiipKKVARDCQQRGIK------LLSIYGSTES 339
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD-GEPPSLRVYCFGG----EAVAQASYDLAWRalkpvyLFNGYGPTET 4847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 ---SPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR-----ALDNEG 411
Cdd:PRK12316 4848 tvtVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPG 4927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 --WYYSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMPDErLGERSCAYVVLKPPHLS 488
Cdd:PRK12316 4928 grLYRTGDLARYRADGVIDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPALA 5005
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 489 LTLEEVIAFFS------RKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK12316 5006 DADEAQAELRDelkaalRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
29-509 |
8.55e-40 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 150.41 E-value: 8.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 29 YWRQTAravPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAfqLPGWCEFTLI--YLACLKTGAVSVPLL 106
Cdd:PRK09029 11 HWAQVR---PQAIALRLN-DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVA--LRGKNSPETLlaYLALLQCGARVLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 107 PAWREAELVWVLNKCQakiffaptvfkqnrpVDLILPLQnqlrhlthivgvDKLAPATTALALSQIIDRSEPLQsdinIH 186
Cdd:PRK09029 85 PQLPQPLLEELLPSLT---------------LDFALVLE------------GENTFSALTSLHLQLVEGAHAVA----WQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 187 GDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGflHGVTAPFLI-GARSVLLDIFT 265
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG--QGIVWRWLYaGATLVVRDKQP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLtllaqQRCTCMSGATPFIYDLLcaveQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSphSMV 345
Cdd:PRK09029 212 LEQAL-----AGCTHASLVPTQLWRLL----DNRSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA--STV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 346 --NLGDSTSRMmntdGYAATGVEIKIVDedrntlpagheGEEASRGPNVFMGYLDEPELTArALDNEGWYYSGDLCRMDe 423
Cdd:PRK09029 281 caKRADGLAGV----GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 424 DGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpphlSLTLEEVIAFFSRKRV 503
Cdd:PRK09029 344 NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESD----SEAAVVNLAEWLQDKL 419
|
....*.
gi 604198150 504 AKYKYP 509
Cdd:PRK09029 420 ARFQQP 425
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-528 |
1.50e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 154.73 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 19 GYWGDASLGDYWRQTARAVPDKIAVVdnHGA-SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLK 97
Cdd:PRK12316 506 EYPLQRGVHRLFEEQVERTPEAPALA--FGEeTLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 98 TGAVSVPLLPAWREAELVWVLnkcqakiffaptvfkQNRPVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSe 177
Cdd:PRK12316 584 AGGAYVPLDPEYPAERLAYML---------------EDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 178 plqSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAP----LGHATGFLhgvtaPFL 253
Cdd:PRK12316 648 ---PGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPfsfdVSVWEFFW-----PLM 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 254 IGARSVLL---DIFTPEACLTLLAQQRCTCMSgatpFIYDLLCAVEQQP--ADLSSLRFFLCGGTIIPKKVARDCQQR-- 326
Cdd:PRK12316 720 SGARLVVAapgDHRDPAKLVELINREGVDTLH----FVPSMLQAFLQDEdvASCTSLRRIVCSGEALPADAQEQVFAKlp 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 GIKLLSIYGSTESSphsmVNLGDSTSRMMNTD----GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPEL 402
Cdd:PRK12316 796 QAGLYNLYGPTEAA----IDVTHWTCVEEGGDsvpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGL 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 403 TARAL------DNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLgers 476
Cdd:PRK12316 872 TAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL---- 947
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 604198150 477 CAYVVLKPPHLSltLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK12316 948 VGYVVLESEGGD--WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
40-526 |
1.65e-39 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 154.35 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 40 KIAVVDNHGASWTYAALDYAASRLANwLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGavSVPLLPAWrEAELVWVLN 119
Cdd:PRK06814 648 KLAVEDPVNGPLTYRKLLTGAFVLGR-KLKKNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMINF-SAGIANILS 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 120 KCQA---KIFFAPTVF-KQNRPVDLILPLQNQLRhlthIVGVDKL-APATTALALSQIIDRSEPLQSDINIHGDELAAVL 194
Cdd:PRK06814 724 ACKAaqvKTVLTSRAFiEKARLGPLIEALEFGIR----IIYLEDVrAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVIL 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL----LDI-FTPEac 269
Cdd:PRK06814 800 FTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLypspLHYrIIPE-- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 270 ltLLAQQRCTCMSGATPFI--YdllcAVEQQPADLSSLRFFLCGGtiipKKVaRDCQQR------GIKLLSIYGSTESSP 341
Cdd:PRK06814 878 --LIYDTNATILFGTDTFLngY----ARYAHPYDFRSLRYVFAGA----EKV-KEETRQtwmekfGIRILEGYGVTETAP 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNlgdstSRMMN---TDGYAATGVEIKIVDedrntLPAGHEGEEAS-RGPNVFMGYLD--------EPEltaraldn 409
Cdd:PRK06814 947 VIALN-----TPMHNkagTVGRLLPGIEYRLEP-----VPGIDEGGRLFvRGPNVMLGYLRaenpgvlePPA-------- 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 410 EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDI--LLQHPRIHdaCVVAMPDERLGERscayVVLKPPHL 487
Cdd:PRK06814 1009 DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELaaELWPDALH--AAVSIPDARKGER----IILLTTAS 1082
|
490 500 510
....*....|....*....|....*....|....*....
gi 604198150 488 SLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:PRK06814 1083 DATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
34-533 |
2.21e-39 |
|
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: 149.00 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:cd17653 7 AAAHPDAVAVESL-GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKiffaptvfkqnrpvdLILPLQNqlrhlthivgvdklapattalalsqiidrseplqsdinihGDELAAV 193
Cdd:cd17653 86 IQAILRTSGAT---------------LLLTTDS----------------------------------------PDDLAYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNNILASERAYCARLNLT-------------WQDVFLMPAPLGH-ATGFLHGVTAPFLIGARSV 259
Cdd:cd17653 111 IFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGpgsrvaqvlsiafDACIGEIFSTLCNgGTLVLADPSDPFAHVARTV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 260 LLDIFTPEACLTLlaqqrctcmsgatpfiydllcaveqQPADLSSLRFFLCGGTIIPKKVArDCQQRGIKLLSIYGSTES 339
Cdd:cd17653 191 DALMSTPSILSTL-------------------------SPQDFPNLKTIFLGGEAVPPSLL-DRWSPGRRLYNAYGPTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 SphsmvnLGDSTSRMM----NTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL----DNEG 411
Cdd:cd17653 245 T------ISSTMTELLpgqpVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 W--YYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVED-ILLQHPRIHDACVVaMPDERLgersCAYVVlkpphlS 488
Cdd:cd17653 319 SrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-VVNGRL----VAFVT------P 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 489 LTL-EEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd17653 388 ETVdVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-528 |
2.61e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 151.08 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAvPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWR 110
Cdd:PRK12467 3103 AQVART-PEAPALVFG-DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 111 EAELVWVLnkcqakiffaptvfkQNRPVDLILPLQNQLRHLTHIVGVdklapatTALALSQIIDRSEPLQS-DINIHGDE 189
Cdd:PRK12467 3181 RERLAYMI---------------EDSGVKLLLTQAHLLEQLPAPAGD-------TALTLDRLDLNGYSENNpSTRVMGEN 3238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 190 LAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLL--DIFTPE 267
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSF-DGAQERFLWTLICGGCLVVRdnDLWDPE 3317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 ACLTLLAQQRCTCMSGATPFIYDLlcAVEQQPADLSSLRFFLCGGTIIP----KKVARDCQQRGikLLSIYGSTESSPHS 343
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPAYLQQF--AEDAGGADCASLDIYVFGGEAVPpaafEQVKRKLKPRG--LTNGYGPTEAVVTV 3393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 344 MVNLGDSTSRMMNTD---GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA-RALDN------EGWY 413
Cdd:PRK12467 3394 TLWKCGGDAVCEAPYapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAeRFVADpfsgsgGRLY 3473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 414 YSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMPDERlGERSCAYVVLKPPhlSLTLE 492
Cdd:PRK12467 3474 RTGDLARYRADGVIEYLGRiDHQVKIRGFR-IELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPADP--QGDWR 3549
|
490 500 510
....*....|....*....|....*....|....*.
gi 604198150 493 EVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR 3585
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
24-532 |
4.00e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 149.03 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDKIavvdnhgaswTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSV 103
Cdd:PRK06060 14 ASEAGWYDRPAFYAADVV----------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 104 PLLPAWREAELVWVLNKCQAKIFFAPTvfkqnrpvdlilPLQNQLRHLTHIVGVDKLAPATtalalsqiidRSEPLQSDI 183
Cdd:PRK06060 84 LANPELHRDDHALAARNTEPALVVTSD------------ALRDRFQPSRVAEAAELMSEAA----------RVAPGGYEP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 184 nIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCAR-LNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLD 262
Cdd:PRK06060 142 -MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 I-FTPEACLTLLAQQRCTCMSGATPFIYDLLCAVeqQPADLSSLRFFLCGGTIIPKKVARDCQQ--RGIKLLSIYGSTES 339
Cdd:PRK06060 221 ApVTPEAAAILSARFGPSVLYGVPNFFARVIDSC--SPDSFRSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTEV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 SPHSMVNLGDSTSrmMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPEltaRALDNEGWYYSGDLC 419
Cdd:PRK06060 299 GQTFVSNRVDEWR--LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 420 RMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlkPPHLSLTLEEVIAFFS 499
Cdd:PRK06060 374 CIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLH 451
|
490 500 510
....*....|....*....|....*....|....*.
gi 604198150 500 RK---RVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK06060 452 RGllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-545 |
1.99e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 148.39 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 17 ESGYWGDASLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACL 96
Cdd:PRK12467 1567 HTGYPLARLVHQLIEDQAAATPEAVALVFG-EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAIL 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 97 KTGAVSVPLLPAWREAELVWVLNKCQAKIFFAptvfkqNRPVDLILPLQNQLRhlthivgvdklapattALALSQIIDRS 176
Cdd:PRK12467 1646 KAGGAYVPLDPEYPRERLAYMIEDSGIELLLT------QSHLQARLPLPDGLR----------------SLVLDQEDDWL 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 177 E---PLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPL---GHATGFLHgvta 250
Cdd:PRK12467 1704 EgysDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFafdVSVWELFW---- 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 251 PFLIGARSVLLDIFT---PEACLTLLAQQRCTcMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR- 326
Cdd:PRK12467 1780 PLINGARLVIAPPGAhrdPEQLIQLIERQQVT-TLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERl 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 327 -GIKLLSIYGSTESS---PHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPEL 402
Cdd:PRK12467 1859 pDTGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 403 TAR-------ALDNEGWYYSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMpDERLGE 474
Cdd:PRK12467 1939 TAErfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRiDHQVKIRGFR-IELGEIEARLREQGGVREAVVIAQ-DGANGK 2016
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 475 RSCAYVVLKPPHLSLTLEEVIAFFSRKRVA------KYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK12467 2017 QLVAYVVPTDPGLVDDDEAQVALRAILKNHlkaslpEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVA 2093
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
34-531 |
2.52e-37 |
|
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: 143.23 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNHGaSWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:cd12115 9 AARTPDAIALVCGDE-SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAkiffaptvfkqnrpvdlilplqnqlrhlthivgvdklapattALALSQiidrseplqsdinihGDELAAV 193
Cdd:cd12115 88 LRFILEDAQA------------------------------------------RLVLTD---------------PDDLAYV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNN-------------------ILASErAYCARLNltwqdVFLMPAPLghATG----FLHGVTA 250
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNaaaflqwaaaafsaeelagVLAST-SICFDLS-----VFELFGPL--ATGgkvvLADNVLA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 251 PFLIGARSVLLDIFT-PEACLTLLAQqrctcmsGATPfiydllcaveqqpadlSSLRFFLCGGTIIPKKVARDCQQR--G 327
Cdd:cd12115 183 LPDLPAAAEVTLINTvPSAAAELLRH-------DALP----------------ASVRVVNLAGEPLPRDLVQRLYARlqV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 328 IKLLSIYGSTESSPHS---MVNLGDSTSrmmNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA 404
Cdd:cd12115 240 ERVVNLYGPSEDTTYStvaPVPPGASGE---VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 405 ------RALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCA 478
Cdd:cd12115 317 erflpdPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 604198150 479 YVVLKPPhLSLTLEEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLL 531
Cdd:cd12115 397 YIVAEPG-AAGLVEDLRRHL-GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
32-528 |
4.28e-37 |
|
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: 142.69 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 32 QTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWRE 111
Cdd:cd17645 6 EQVERTPDHVAVVDR-GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 112 AELVWVLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalaLSQiidrseplqsdinihGDELA 191
Cdd:cd17645 85 ERIAYMLADSSAKIL------------------------------------------LTN---------------PDDLA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARsvlLDIFTPEACLT 271
Cdd:cd17645 108 YVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAA---LHVVPSERRLD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 272 LLAQQRCTCMSGAT-PFIYDLLCavEQQPA-DLSSLRFFLCGGTIIPKKVardcqQRGIKLLSIYGSTESS--------- 340
Cdd:cd17645 184 LDALNDYFNQEGITiSFLPTGAA--EQFMQlDNQSLRVLLTGGDKLKKIE-----RKGYKLVNNYGPTENTvvatsfeid 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 341 -PHSMVNLGDSTSRmmntdgyaatgVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARA------LDNEGWY 413
Cdd:cd17645 257 kPYANIPIGKPIDN-----------TRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 414 YSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlkpPHLSLTLEE 493
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT---APEEIPHEE 402
|
490 500 510
....*....|....*....|....*....|....*
gi 604198150 494 VIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17645 403 LREWL-KNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-526 |
7.26e-37 |
|
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: 142.22 E-value: 7.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd17650 1 PDAIAVSDAT-RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIFfaptvfkqnrpvdLILPlqnqlrhlthivgvdklapattalalsqiidrseplqsdinihgDELAAVLFTS 197
Cdd:cd17650 80 LEDSGAKLL-------------LTQP--------------------------------------------EDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNIlaseraycARLNLTWQDVFLMPAplghatgflhgvTAPFLIGARSVLLDIFTPEACLTLLA--- 274
Cdd:cd17650 103 GTTGKPKGVMVEHRNV--------AHAAHAWRREYELDS------------FPVRLLQMASFSFDVFAGDFARSLLNggt 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 --------------------QQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR---GIKLL 331
Cdd:cd17650 163 lvicpdevkldpaalydlilKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARfgqGMRII 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 332 SIYGSTESSPHS------MVNLGDSTsrmMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA- 404
Cdd:cd17650 243 NSYGVTEATIDStyyeegRDPLGDSA---NVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAe 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 405 RALDN-----EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAY 479
Cdd:cd17650 320 RFVENpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAY 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 604198150 480 VVlkpPHLSLTLEEVIAFFSrKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17650 400 VV---AAATLNTAELRAFLA-KELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-533 |
1.45e-36 |
|
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: 143.61 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 31 RQTARAVPDKIAV-----VDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL 105
Cdd:cd05967 58 RHVEAGRGDQIALiydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 106 LPAWREAELVWVLNKCQAKIFFAPTV-FKQNRPVDLiLPLqnqlrhlthivgVDKlapattALALSQ-------IIDRS- 176
Cdd:cd05967 138 FGGFAAKELASRIDDAKPKLIVTASCgIEPGKVVPY-KPL------------LDK------ALELSGhkphhvlVLNRPq 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 177 ---EPLQSDINIHGDELAA-----------------VLFTSGTEGMPKGVMLTHNnilaserAYCARLNLTWQ------- 229
Cdd:cd05967 199 vpaDLTKPGRDLDWSELLAkaepvdcvpvaatdplyILYTSGTTGKPKGVVRDNG-------GHAVALNWSMRniygikp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 230 -DVFLMPAPLGHATGFLHGVTAPFLIGARSVLLD---IFTPE--ACLTLLAQQRCTCMSGATPFIYdllcAVEQQPA--- 300
Cdd:cd05967 272 gDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEgkpVGTPDpgAFWRVIEKYQVNALFTAPTAIR----AIRKEDPdgk 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 301 -----DLSSLR-FFLCGGTIIPKKVARDCQQRGIKLLSIYGSTES-SP--HSMVNLGDSTSRMmNTDGYAATGVEIKIVD 371
Cdd:cd05967 348 yikkyDLSSLRtLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPitANPVGLEPLPIKA-GSPGKPVPGYQVQVLD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 372 EDRNTLPAGHEGEEASRGP---NVFMGYLDEPELTARALDNE--GWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISS 446
Cdd:cd05967 427 EDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLST 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 447 REVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKpPHLSLTLEEV---IAFFSRKRVAKYKYPERIVIVEKLPRTAS 523
Cdd:cd05967 507 GEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLK-EGVKITAEELekeLVALVREQIGPVAAFRLVIFVKRLPKTRS 585
|
570
....*....|
gi 604198150 524 GKVQKFLLRQ 533
Cdd:cd05967 586 GKILRRTLRK 595
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
67-535 |
3.35e-36 |
|
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: 141.09 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 67 LLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL---------LPAWReaelVWvlNKCqakiffaptvfkqNRP 137
Cdd:cd05908 32 LQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVsigsneehkLKLNK----VW--NTL-------------KNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 138 VdLILPLQNQlrhlthivgvDKLApattalalsqiidrseplqsdinihgDELAAVLFTSGTEGMPKGVMLTHNNILASE 217
Cdd:cd05908 93 Y-LITEEEVL----------CELA--------------------------DELAFIQFSSGSTGDPKGVMLTHENLVHNM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 218 RAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL----LDIFTPEACLTLLAQQRCTCMSG---ATPFIYD 290
Cdd:cd05908 136 FAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmptrLFIRRPILWLKKASEHKATIVSSpnfGYKYFLK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 291 LLCAVEQQPADLSSLRFFLCGGTIIPKKVARD----CQQRGIK---LLSIYGSTESS-----------------PHSMVN 346
Cdd:cd05908 216 TLKPEKANDWDLSSIRMILNGAEPIDYELCHEfldhMSKYGLKrnaILPVYGLAEASvgaslpkaqspfktitlGRRHVT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 347 LGDSTSRMMNTD---------GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGD 417
Cdd:cd05908 296 HGEPEPEVDKKDsecltfvevGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 418 LCRMdEDGYIKITGRKKDIIIRGGENISSREVEDILLQhprihdacvvaMPDERLGErscayVVLKPPHLSLTL-EEVIA 496
Cdd:cd05908 376 LGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEE-----------LEGVELGR-----VVACGVNNSNTRnEEIFC 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 497 FFSRKRVAKYKYP-----------------ERIVIVEKLPRTASGKVQKFLLRQDI 535
Cdd:cd05908 439 FIEHRKSEDDFYPlgkkikkhlnkrggwqiNEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
32-526 |
3.96e-36 |
|
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: 140.26 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 32 QTARAvPDKIAVVDnHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWRE 111
Cdd:cd17644 9 QVERT-PDAVAVVF-EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 112 AELVWVLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalaLSQiidrseplqsdinihGDELA 191
Cdd:cd17644 87 ERLTYILEDAQISVL------------------------------------------LTQ---------------PENLA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGfLHGVTAPFLIGARSVL---LDIFTPEA 268
Cdd:cd17644 110 YVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVLrpeEMRSSLED 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADL-SSLRFFLCGG-TIIPKKVARDCQQRG--IKLLSIYGSTESSPHSM 344
Cdd:cd17644 189 FVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGeAVQPELVRQWQKNVGnfIQLINVYGPTEATIAAT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 V-NLGDSTSRMMN--TDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDN--------EGWY 413
Cdd:cd17644 269 VcRLTQLTERNITsvPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIShpfnssesERLY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 414 YSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLE 492
Cdd:cd17644 349 KTGDLARYLPDGNIEYLGRiDNQVKIRGFR-IELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEE-SPSTV 426
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 493 EVIAFFSRKrVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17644 427 ELRQFLKAK-LPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
25-532 |
9.45e-36 |
|
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: 141.47 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTAravPDKIAVV----DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGA 100
Cdd:cd05968 65 QLLDKWLADT---RTRPALRwegeDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 101 VSVPLLPAWREAELVWVLNKCQAKIFFAPTVF-KQNRPVDLILPLQNQLRH---LTHIVGVDKLA---PATTALALSQII 173
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFtRRGREVNLKEEADKACAQcptVEKVVVVRHLGndfTPAKGRDLSYDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 174 DRSEPLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNI---LASERAYCARLN----LTW-QDVFLMPAPLGHATGFL 245
Cdd:cd05968 222 EKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQFDLKpgdlLTWfTDLGWMMGPWLIFGGLI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 246 HGVTAPFLIGARsvllDIFTPEACLTLLAQQRCTCMsGATPFIYDLLCAVEQQPA---DLSSLRFFlcGGT---IIPKKV 319
Cdd:cd05968 302 LGATMVLYDGAP----DHPKADRLWRMVEDHEITHL-GLSPTLIRALKPRGDAPVnahDLSSLRVL--GSTgepWNPEPW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 320 ARDCQQRGIKLLSIY---GSTESSPHSmvnLGDSTSRMMNTDGYAAT--GVEIKIVDEDRNTLPaGHEGEEASRGPNVFM 394
Cdd:cd05968 375 NWLFETVGKGRNPIInysGGTEISGGI---LGNVLIKPIKPSSFNGPvpGMKADVLDESGKPAR-PEVGELVLLAPWPGM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 395 --GYLDEPEltaRALDN-----EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAM 467
Cdd:cd05968 451 trGFWRDED---RYLETywsrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 468 PDERLGERSCAYVVLKPPH-LSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:cd05968 528 PHPVKGEAIVCFVVLKPGVtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
87-532 |
9.78e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 140.20 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 87 EFTLIYLACLKTGAVSVPLLPAWREAELV--WVLNKCQakiffapTVFKQNRPVDLILPLQNQLRHlthivgVDKLAPAT 164
Cdd:PRK07867 66 EFSLLLGAAALSGIVPVGLNPTRRGAALArdIAHADCQ-------LVLTESAHAELLDGLDPGVRV------INVDSPAW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 165 TALalsqIIDRSEPLQSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGF 244
Cdd:PRK07867 133 ADE----LAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 245 LHGVTAPFLIGARSVLLDIFTPEaclTLLAQQRctcMSGATPFIY-----DLLCAVEQQPADLS-SLRFfLCGGTIIPKK 318
Cdd:PRK07867 209 MAGWAVALAAGASIALRRKFSAS---GFLPDVR---RYGATYANYvgkplSYVLATPERPDDADnPLRI-VYGNEGAPGD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 319 VARDCQQRGIKLLSIYGSTEssphsmvnLGDSTSRMMNTD----GYAATGVEIKIVDEDRNTLPAGHE------GEEA-- 386
Cdd:PRK07867 282 IARFARRFGCVVVDGFGSTE--------GGVAITRTPDTPpgalGPLPPGVAIVDPDTGTECPPAEDAdgrllnADEAig 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 387 ----SRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDA 462
Cdd:PRK07867 354 elvnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 604198150 463 CVVAMPDERLGERSCAYVVLKpPHLSLTLEEVIAFF-SRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK07867 433 AVYAVPDPVVGDQVMAALVLA-PGAKFDPDAFAEFLaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
38-533 |
1.08e-35 |
|
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: 141.16 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVV-----DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV-SVpLLPAWRE 111
Cdd:cd05966 67 GDKVAIIwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhSV-VFAGFSA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 112 AELVWVLNKCQAKIFF-APTVFKQNRPVDLILPLQNQLRHLTHI--VGVDKLAPATTAL----------ALSQIIDRSEP 178
Cdd:cd05966 146 ESLADRINDAQCKLVItADGGYRGGKVIPLKEIVDEALEKCPSVekVLVVKRTGGEVPMtegrdlwwhdLMAKQSPECEP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 179 LQSDINihgDELAaVLFTSGTEGMPKGVMLTHNNILAseraYCAR-----LNLTWQDVFLMPAPLGHATGFLHGVTAPFL 253
Cdd:cd05966 226 EWMDSE---DPLF-ILYTSGSTGKPKGVVHTTGGYLL----YAATtfkyvFDYHPDDIYWCTADIGWITGHSYIVYGPLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 254 IGARSVLL----DIFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPA--DLSSLRFFlcgGT----IIP------- 316
Cdd:cd05966 298 NGATTVMFegtpTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKkhDLSSLRVL---GSvgepINPeawmwyy 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 317 KKVAR-DCQqrgikLLSIYGSTESSPHSMVNLGDSTSrmmnTDGYAAT----GVEIKIVDEDRNTLPAGHEGEEASRG-- 389
Cdd:cd05966 375 EVIGKeRCP-----IVDTWWQTETGGIMITPLPGATP----LKPGSATrpffGIEPAILDEEGNEVEGEVEGYLVIKRpw 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 390 PNVFMGYLDEPEltaRALDN-----EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV 464
Cdd:cd05966 446 PGMARTIYGDHE---RYEDTyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAV 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 465 VAMPDERLGERSCAYVVLKPPH-LSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05966 523 VGRPHDIKGEAIYAFVTLKDGEePSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-545 |
2.87e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.02 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 32 QTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWRE 111
Cdd:PRK12316 3065 EQVERTPDAVALAFG-EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 112 AELVWVLNKCQAkiffaptvfkqnrpvdLILPLQNQLRhLTHIVGVDKLApattalaLSQIIDRSEPLQSDINIHGDELA 191
Cdd:PRK12316 3144 ERLAYMLEDSGA----------------QLLLSQSHLR-LPLAQGVQVLD-------LDRGDENYAEANPAIRTMPENLA 3199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHaTGFLHGVTAPFLIGARSVLLDI---FTPEA 268
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGARVVLAGPedwRDPAL 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSGATPFIYDLLcaVEQQPADLSSLRFFLCGGTIIPKkvarDCQQR---GIKLLSIYGSTESSPHSMV 345
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFL--EEEDAHRCTSLKRIVCGGEALPA----DLQQQvfaGLPLYNLYGPTEATITVTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 346 NLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL------DNEGWYYSGDLC 419
Cdd:PRK12316 3353 WQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLA 3432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 420 RMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLgersCAYVVLKPPhlSLTLEEVIAFFS 499
Cdd:PRK12316 3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQL----VAYVVPEDE--AGDLREALKAHL 3506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 500 RKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK12316 3507 KASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVA 3552
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
194-532 |
1.88e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 136.70 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVtAPFLI-GARSVLLDIFTPEAcltL 272
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGW-APAVAsGAAVALPAKFSASG---F 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 273 LAQQRctcMSGATPFIY-----DLLCAVEQQPADL-SSLR--FflcGGTIIPKKVARDCQQRGIKLLSIYGSTESSphSM 344
Cdd:PRK13388 232 LDDVR---RYGATYFNYvgkplAYILATPERPDDAdNPLRvaF---GNEASPRDIAEFSRRFGCQVEDGYGSSEGA--VI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDSTSRmmNTDGYAATGVEIkiVDEDRNTL-------PAGH--EGEEA------SRGPNVFMGYLDEPELTARALDN 409
Cdd:PRK13388 304 VVREPGTPP--GSIGRGAPGVAI--YNPETLTEcavarfdAHGAllNADEAigelvnTAGAGFFEGYYNNPEATAERMRH 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 410 eGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSL 489
Cdd:PRK13388 380 -GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGA-TF 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 604198150 490 TLEEVIAFFSRKRVAKYKYPERIV-IVEKLPRTASGKVQKFLLR 532
Cdd:PRK13388 458 DPDAFAAFLAAQPDLGTKAWPRYVrIAADLPSTATNKVLKRELI 501
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-533 |
4.79e-34 |
|
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: 133.85 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPllpawreaelvwvlnkcqakiffaptv 131
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 fkqnrpvdlilplqnqlrhlthivgvdklapATTALALSQIIDRSEP-----LQSDINIHGDELAAVLFTSGTEGMPKGV 206
Cdd:cd05974 55 -------------------------------ATTLLTPDDLRDRVDRggavyAAVDENTHADDPMLLYFTSGTTSKPKLV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 207 MLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDI--FTPEACLTLLAQQRCTCMSgA 284
Cdd:cd05974 104 EHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYarFDAKRVLAALVRYGVTTLC-A 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 285 TPFIYDLLCaveQQpaDLSSLRFFL-----CGGTIIPKKVARDCQQRGIKLLSIYGSTESSphsmVNLGDSTSRMMNTD- 358
Cdd:cd05974 183 PPTVWRMLI---QQ--DLASFDVKLrevvgAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT----ALVGNSPGQPVKAGs 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 359 -GYAATGVEIKIVDEDRNtlpAGHEGE-----EASRGPNVFMGYLDEPELTARALDNeGWYYSGDLCRMDEDGYIKITGR 432
Cdd:cd05974 254 mGRPLPGYRVALLDPDGA---PATEGEvaldlGDTRPVGLMKGYAGDPDKTAHAMRG-GYYRTGDIAMRDEDGYLTYVGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 433 KKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPD-ERLGERScAYVVL-----KPPHLSLTLEEviafFSRKRVAKY 506
Cdd:cd05974 330 ADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDpVRLSVPK-AFIVLragyePSPETALEIFR----FSRERLAPY 404
|
490 500
....*....|....*....|....*..
gi 604198150 507 KYPERIVIVEkLPRTASGKVQKFLLRQ 533
Cdd:cd05974 405 KRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
34-460 |
4.88e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 135.80 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNHG---------ASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVP 104
Cdd:PRK09274 16 AQERPDQLAVAVPGGrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 105 LLPAWReaelVWVLNKCqakiffaptvFKQNRPVDLI-LPLQNQLRHL--------THIVGVD--KLAPATTalaLSQII 173
Cdd:PRK09274 96 VDPGMG----IKNLKQC----------LAEAQPDAFIgIPKAHLARRLfgwgkpsvRRLVTVGgrLLWGGTT---LATLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 174 DRSEPLQSDI-NIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLghatgF-LHGvtaP 251
Cdd:PRK09274 159 RDGAAAPFPMaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL-----FaLFG---P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 252 FLiGARSVLLDI-FT------PEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQ 324
Cdd:PRK09274 231 AL-GMTSVIPDMdPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 325 Q---RGIKLLSIYGSTESSPHSMV----NLGDSTSRmmnTD-------GYAATGVEIKIVD---------EDRNTLPAGH 381
Cdd:PRK09274 310 AmlpPDAEILTPYGATEALPISSIesreILFATRAA---TDngagicvGRPVDGVEVRIIAisdapipewDDALRLATGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 382 EGEEASRGPNVFMGYLDEPELTARA--LDNEG--WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHP 457
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHP 466
|
...
gi 604198150 458 RIH 460
Cdd:PRK09274 467 GVK 469
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
117-451 |
5.72e-34 |
|
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: 135.95 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 117 VLNKCQAKIFfaptVFKQNRPVDLILPLQNQLRHLTHIV-----------------GVDKLAPATTALALSQIIDRSEPl 179
Cdd:cd05933 75 VAETSEANIL----VVENQKQLQKILQIQDKLPHLKAIIqykeplkekepnlyswdEFMELGRSIPDEQLDAIISSQKP- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 qsdinihgDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTW----QDVFLMPAPLGHA--------TGFLHG 247
Cdd:cd05933 150 --------NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPatvgQESVVSYLPLSHIaaqildiwLPIKVG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 248 VTAPF-------------------------------------LIGARSVLLD--IFTPEACLTLLAQQrcTCMSGATPFI 288
Cdd:cd05933 222 GQVYFaqpdalkgtlvktlrevrptafmgvprvwekiqekmkAVGAKSGTLKrkIASWAKGVGLETNL--KLMGGESPSP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 289 Y------DLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESS-PHSMVNLGdstSRMMNTDGYA 361
Cdd:cd05933 300 LfyrlakKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSgPHTISNPQ---AYRLLSCGKA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 362 ATGVEIKIVDEDRNtlpaGHeGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIR-G 440
Cdd:cd05933 377 LPGCKTKIHNPDAD----GI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaG 451
|
410
....*....|.
gi 604198150 441 GENISSREVED 451
Cdd:cd05933 452 GENVPPVPIED 462
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-525 |
8.24e-34 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 137.10 E-value: 8.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVS 102
Cdd:PRK10252 457 ETTLSALVAQQAAKTPDAPALADAR-YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLLPAWREAELVWVLnkcqakiffaptvfKQNRPVdLILPLQNQLRHLTHIVGVDKLAPAtTALALSQiidrSEPLQSD 182
Cdd:PRK10252 536 LPLDTGYPDDRLKMML--------------EDARPS-LLITTADQLPRFADVPDLTSLCYN-APLAPQG----AAPLQLS 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 iniHGDELAAVLFTSGTEGMPKGVMLTHnnilaseRAYCARL-------NLTWQDVFLMPAPLGHATG----FLhgvtaP 251
Cdd:PRK10252 596 ---QPHHTAYIIFTSGSTGRPKGVMVGQ-------TAIVNRLlwmqnhyPLTADDVVLQKTPCSFDVSvwefFW-----P 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 252 FLIGARSVLL------DiftPEACLTLLAQQRCTcmsgATPFIYDLLCA------VEQQPADLSSLRFFLCGGTIIPKKV 319
Cdd:PRK10252 661 FIAGAKLVMAepeahrD---PLAMQQFFAEYGVT----TTHFVPSMLAAfvasltPEGARQSCASLRQVFCSGEALPADL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 320 ARDCQQR-GIKLLSIYGSTESS------PHSMVNLGDSTSRMMNTdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNV 392
Cdd:PRK10252 734 CREWQQLtGAPLHNLYGPTEAAvdvswyPAFGEELAAVRGSSVPI-GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQL 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 393 FMGYLDEPELTA-RALDN-----EGWYYSGDLCRMDEDGYIKITGRKKDII-IRgGENISSREVEDILLQHPRIH----D 461
Cdd:PRK10252 813 AQGYLGRPDLTAsRFIADpfapgERMYRTGDVARWLDDGAVEYLGRSDDQLkIR-GQRIELGEIDRAMQALPDVEqavtH 891
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 462 ACVVAMPDERLGE--RSCAYVVlkpPHLSLTLE-EVIAFFSRKRVAKYKYPERIVIVEKLPRTASGK 525
Cdd:PRK10252 892 ACVINQAAATGGDarQLVGYLV---SQSGLPLDtSALQAQLRERLPPHMVPVVLLQLDQLPLSANGK 955
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-533 |
6.49e-33 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 132.82 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 53 YAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL-LPAW---REA---ELVWVLNKCQAKI 125
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLpLPMGfggRESyiaQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 126 FFAPTVFkqnrpVDLILPLQNQLRHLTHIVGVDKLAPATTALALSQIidrsEPlqsdinihgDELAAVLFTSGTEGMPKG 205
Cdd:PRK09192 132 IITPDEL-----LPWVNEATHGNPLLHVLSHAWFKALPEADVALPRP----TP---------DDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 206 VMLTHNNILASERAY-CARLNLTWQDVFLMPAPLGHATGFLHGVTAPFligARSVLLDIFT-------PEACLTLLAQQR 277
Cdd:PRK09192 194 VIITHRALMANLRAIsHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPV---ATQLSVDYLPtrdfarrPLQWLDLISRNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 278 CTcMSGATPFIYDLlCA--VEQQPA---DLSSLRFFLCGGTIIP----KKVARDCQQRGIK---LLSIYGSTES------ 339
Cdd:PRK09192 271 GT-ISYSPPFGYEL-CArrVNSKDLaelDLSCWRVAGIGADMIRpdvlHQFAEAFAPAGFDdkaFMPSYGLAEAtlavsf 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 SPHS------------------MVNLGDST--SRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDE 399
Cdd:PRK09192 349 SPLGsgivveevdrdrleyqgkAVAPGAETrrVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 400 PElTARALDNEGWYYSGDLCRMdEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIH--DACVVAMPDErlGERSC 477
Cdd:PRK09192 429 EE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE--NGEKI 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 478 AYVV---LKPPHLSLTLEEVIA--FFSRKRVAkykyperiVIVE-----KLPRTASGKVQKFLLRQ 533
Cdd:PRK09192 505 VLLVqcrISDEERRGQLIHALAalVRSEFGVE--------AAVElvpphSLPRTSSGKLSRAKAKK 562
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
188-493 |
1.28e-32 |
|
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: 130.80 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLN--LTWQDVFLMPAPLGH-------ATGFLHGVTapflIGARS 258
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHifelaaeNVCLYRGGT----IGYGS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 259 VLldiftpeaCLTLLAQQRC---------TCMSGaTPFIYDLLC-AVEQQPADLSS------------------------ 304
Cdd:cd17639 164 PR--------TLTDKSKRGCkgdltefkpTLMVG-VPAIWDTIRkGVLAKLNPMGGlkrtlfwtayqsklkalkegpgtp 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 305 -----------------LRFFLCGGTIIpkkvARDCQqrgiKLLSI--------YGSTESSPHSMV-NLGDSTSrmmNTD 358
Cdd:cd17639 235 lldelvfkkvraalggrLRYMLSGGAPL----SADTQ----EFLNIvlcpviqgYGLTETCAGGTVqDPGDLET---GRV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 359 GYAATGVEIKIVD-EDRNTLPAGHE--GEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKD 435
Cdd:cd17639 304 GPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 604198150 436 II-IRGGENISSREVEDILLQHPRIHDACVVAMPDErlgERSCAYVVLKPPHLSLTLEE 493
Cdd:cd17639 384 LVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDK---SYPVAIVVPNEKHLTKLAEK 439
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
188-526 |
1.31e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 128.24 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAplGHATGF---LHGVTApfliGARSVLLDI- 263
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLALPA--HHIAGLqvlVRSVIA----GSEPVELDVs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 --FTPEACLTLLAQqrctcMSGatPFIYDLLCAVE-----QQPADLSSLRFF---LCGGTIIPKKVARDCQQRGIKLLSI 333
Cdd:PRK07824 109 agFDPTALPRAVAE-----LGG--GRRYTSLVPMQlakalDDPAATAALAELdavLVGGGPAPAPVLDAAAAAGINVVRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 334 YGSTEssphsmvnlgdsTSRMMNTDGYAATGVEIKIVDEdRNTLPaghegeeasrGPNVFMGYLDEPELTARAldNEGWY 413
Cdd:PRK07824 182 YGMSE------------TSGGCVYDGVPLDGVRVRVEDG-RIALG----------GPTLAKGYRNPVDPDPFA--EPGWF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 414 YSGDLCRMDeDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAyVVLKPPHLSLTLEE 493
Cdd:PRK07824 237 RTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA-AVVGDGGPAPTLEA 314
|
330 340 350
....*....|....*....|....*....|...
gi 604198150 494 VIAFFSRkRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:PRK07824 315 LRAHVAR-TLDRTAAPRELHVVDELPRRGIGKV 346
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-528 |
1.93e-32 |
|
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: 129.90 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHgASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWV 117
Cdd:cd17656 2 PDAVAVVFEN-QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 118 LNKCQAKIffaptVFKQNRPVDLilPLQNQLRHLthivgvdklapattalalsqIIDRSEPLQSDINI----HGDELAAV 193
Cdd:cd17656 81 MLDSGVRV-----VLTQRHLKSK--LSFNKSTIL--------------------LEDPSISQEDTSNIdyinNSDDLLYI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 LFTSGTEGMPKGVMLTHNNI---LASERAYCarLNLTWQDVFLMPAPlghatGF---LHGVTAPFLIGARSVLLDIFTP- 266
Cdd:cd17656 134 IYTSGTTGKPKGVQLEHKNMvnlLHFEREKT--NINFSDKVLQFATC-----SFdvcYQEIFSTLLSGGTLYIIREETKr 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 --EACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLSSLRFFLCGGT--IIPKKVARDCQQRGIKLLSIYGSTESSPH 342
Cdd:cd17656 207 dvEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEqlVITNEFKEMLHEHNVHLHNHYGPSETHVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SM--VNLGDSTSRMMNTdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL------DNEGWYY 414
Cdd:cd17656 287 TTytINPEAEIPELPPI-GKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 415 SGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVlkpPHLSLTLEEV 494
Cdd:cd17656 366 TGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---MEQELNISQL 442
|
490 500 510
....*....|....*....|....*....|....
gi 604198150 495 IAFFSrKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17656 443 REYLA-KQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
52-528 |
3.68e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 130.12 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFqlpgwceftliyLAclktgAVSVPLLPAwreAELVWVLNKcqakiffAPTV 131
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAV------------LA-----GAPVEIAPT---AQGLWMRGA-------SLTM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FKQNRP-VDLILPLQNQLRHLTHI------VG--VDKLAP-----ATTALALSQIIDrSEPLqSDINIHGDELAAVLFTS 197
Cdd:PRK07768 84 LHQPTPrTDLAVWAEDTLRVIGMIgakavvVGepFLAAAPvleekGIRVLTVADLLA-ADPI-DPVETGEDDLALMQLTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARLNLTWQ-DVFLMPAPLGHATGFLHGVTAPFLIGARSVLLdifTPEACL------ 270
Cdd:PRK07768 162 GSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV---TPMDFLrdpllw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 271 -TLLAQQRCTcMSGATPFIYDLLCAVEQQPA-----DLSSLRFFLCGGTII-PKKVARDCQQ------RGIKLLSIYGST 337
Cdd:PRK07768 239 aELISKYRGT-MTAAPNFAYALLARRLRRQAkpgafDLSSLRFALNGAEPIdPADVEDLLDAgarfglRPEAILPAYGMA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 338 ES------SP------------------HSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVF 393
Cdd:PRK07768 318 EAtlavsfSPcgaglvvdevdadllaalRRAVPATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 394 MGYLDePELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLG 473
Cdd:PRK07768 398 PGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 474 ERSCAYVVLkpphlsltleEVIAFFS-------RKRVAKYKY------PERIVIVEK--LPRTASGKVQK 528
Cdd:PRK07768 477 SREGFAVAV----------ESNAFEDpaevrriRHQVAHEVVaevgvrPRNVVVLGPgsIPKTPSGKLRR 536
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-526 |
8.17e-32 |
|
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: 127.90 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVVDNHgASWTYAALDYAASRLANWLLSQG-IQPGDRVAFQLPGwCEFTLI-YLACLKTGAVSVPLLPAWREAELV 115
Cdd:cd17648 1 PDRVAVVYGD-KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 116 WVLNKCQAKIffaptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqIIDRSEplqsdinihgdELAAVLF 195
Cdd:cd17648 79 FILEDTGARV----------------------------------------------VITNST-----------DLAYAIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNILASERAYCARlnltwqdvFLMPAPLGHATGFLHG-VTAPF-------LIGARSVLL----DI 263
Cdd:cd17648 102 TSGTTGKPKGVLVEHGSVVNLRTSLSER--------YFGRDNGDEAVLFFSNyVFDFFveqmtlaLLNGQKLVVppdeMR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMSGaTPFI---YDLlcaveqqpADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTES 339
Cdd:cd17648 174 FDPDRFYAYINREKVTYLSG-TPSVlqqYDL--------ARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTET 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 SPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTA-RALDN--------- 409
Cdd:cd17648 245 TVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAeRFLPNpfqteqera 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 410 EG----WYYSGDLCRMDEDGYIKITGRKK-DIIIRgGENISSREVEDILLQHPRIHDACVVA-----MPDERLGERSCAY 479
Cdd:cd17648 325 RGrnarLYKTGDLVRWLPSGELEYLGRNDfQVKIR-GQRIEPGEVEAALASYPGVRECAVVAkedasQAQSRIQKYLVGY 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 604198150 480 VVLKPPHLSltlEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:cd17648 404 YLPEPGHVP---ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
188-525 |
1.19e-31 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 128.40 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVL-LDIFTP 266
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFaYNPLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLTLLAQQRCTCMsGATPFIYD-LLCAVEQQPADLSSLRFFLCGGTIIpKKVARDCQQR---GIKLLSIYGSTESSPH 342
Cdd:PRK06334 263 KKIVEMIDEAKVTFL-GSTPVFFDyILKTAKKQESCLPSLRFVVIGGDAF-KDSLYQEALKtfpHIQLRQGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SMVNLGDStSRMMNTDGYAATGVEIKIVDEDRNT-LPAGHEGEEASRGPNVFMGYLDE-PELTARALDNEGWYYSGDLCR 420
Cdd:PRK06334 341 ITINTVNS-PKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWYVTGDLGY 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 421 MDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDA------CVVAMPDERlgERSCAYVVLkPPHLSlTLEEV 494
Cdd:PRK06334 420 VDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhagplVVCGLPGEK--VRLCLFTTF-PTSIS-EVNDI 495
|
330 340 350
....*....|....*....|....*....|.
gi 604198150 495 IAFFSRKRVAKYKYPERiviVEKLPRTASGK 525
Cdd:PRK06334 496 LKNSKTSSILKISYHHQ---VESIPMLGTGK 523
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
188-533 |
3.30e-31 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 128.29 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGAR-----SVLLD 262
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEvflypSPLHY 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 IFTPEacltLLAQQRCTCMSGATPFIYDllCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSP 341
Cdd:PRK08043 445 RIVPE----LVYDRNCTVLFGTSTFLGN--YARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGVTECAP 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSMVNLGDSTSRmmNTDGYAATGVEIKIVdedrnTLPAGHEGEEAS-RGPNVFMGYL--DEP-ELTARALDNE------G 411
Cdd:PRK08043 519 VVSINVPMAAKP--GTVGRILPGMDARLL-----SVPGIEQGGRLQlKGPNIMNGYLrvEKPgVLEVPTAENArgemerG 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERscayVVLKPPHLSLTL 491
Cdd:PRK08043 592 WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEA----LVLFTTDSELTR 667
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 604198150 492 EEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK08043 668 EKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
51-465 |
3.76e-31 |
|
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: 127.54 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 WTYAALDYAASRLANWLLSQGIQPGDRVAF---QLPGWCEFTLIYLAClktGAVSVPLLPAWREAELVWVLNKCQAKIFF 127
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAIlgdNRPEWVWAELAAQAI---GALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 AptvfKQNRPVDLILPLQNQLRHLTHIVGVD----------KLAPATTALALSQIIDRSEPLQSDINI---HGDELAAVL 194
Cdd:cd17641 89 A----EDEEQVDKLLEIADRIPSVRYVIYCDprgmrkyddpRLISFEDVVALGRALDRRDPGLYEREVaagKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFL--------------------I 254
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVcgfivnfpeepetmmedlreI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 GARSVLLdifTPEACLTLLAQQRCTcMSGATPF---IYDLLCAVEQQPAD------------------------------ 301
Cdd:cd17641 245 GPTFVLL---PPRVWEGIAADVRAR-MMDATPFkrfMFELGMKLGLRALDrgkrgrpvslwlrlaswladallfrplrdr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 302 --LSSLRFFLCGGTIIPKKVARDCQQRGIKLLSIYGSTESSPHSMVNL-GDSTSrmmNTDGYAATGVEIKIVDedrntlp 378
Cdd:cd17641 321 lgFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRdGDVDP---DTVGVPFPGTEVRIDE------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 379 aghEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDI-IIRGGENISSREVEDILLQHP 457
Cdd:cd17641 391 ---VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSP 467
|
....*...
gi 604198150 458 RIHDACVV 465
Cdd:cd17641 468 YIAEAVVL 475
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-469 |
5.12e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 127.30 E-value: 5.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVP 104
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFE-DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 105 LLPAWREAELVWVLNKCQAKIF-----FAPTvFKQNRPvdlilPLQNQLRHLTHIVGVDKLAPATTALALSQIIDRSEPL 179
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLivgeeLVEA-FEEARA-----DLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 180 QSDINIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSV 259
Cdd:PRK08279 191 ASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 260 LLDIFT-----PEAcltllaqQRctcmSGATPFIY--DL---LCAVEQQPADLS-SLRffLCGGTIIPKKVARDCQQR-G 327
Cdd:PRK08279 271 LRRKFSasrfwDDV-------RR----YRATAFQYigELcryLLNQPPKPTDRDhRLR--LMIGNGLRPDIWDEFQQRfG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 328 I-KLLSIYGSTESsphsmvNLGdstsrMMNTDGYA-ATG-------VEIKIV--DEDRNT---------LPAG-HE---- 382
Cdd:PRK08279 338 IpRILEFYAASEG------NVG-----FINVFNFDgTVGrvplwlaHPYAIVkyDVDTGEpvrdadgrcIKVKpGEvgll 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 383 -GEEASRGPnvFMGYLDePELTARAL------DNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQ 455
Cdd:PRK08279 407 iGRITDRGP--FDGYTD-PEASEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
|
490
....*....|....*.
gi 604198150 456 HPRIHDACV--VAMPD 469
Cdd:PRK08279 484 FPGVEEAVVygVEVPG 499
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
32-528 |
6.12e-31 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 126.66 E-value: 6.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 32 QTARAVPDKIAVVDNHGAS-WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL---LP 107
Cdd:PRK05857 22 EQARQQPEAIALRRCDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAdgnLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 108 AWREAELVWVLNKCQAKIFFAPTVFKQNRPVDLilplqnqlrHLTHIVGVDKLApATTALALSQIIDRsepLQSDINIHG 187
Cdd:PRK05857 102 IAAIERFCQITDPAAALVAPGSKMASSAVPEAL---------HSIPVIAVDIAA-VTRESEHSLDAAS---LAGNADQGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARlNLTWQD-----VFLMPAPLGHA-------TGFLHGvtAPFLIG 255
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKE-GLNWVTwvvgeTTYSPLPATHIgglwwilTCLMHG--GLCVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 256 A------RSVLLDIFTPEACL--TLLAQQRCTCMSGATpfiydllcaveqqpaDLSSLRFFLCGGTIIPKKVARDCQQRG 327
Cdd:PRK05857 246 GenttslLEILTTNAVATTCLvpTLLSKLVSELKSANA---------------TVPSLRLVGYGGSRAIAADVRFIEATG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 328 IKLLSIYGSTESSPHSMVNLGD--STSRM-MNTDGYAATGVEIKIVDEDRNTLPAGHEGEEASRG------PNVFMGYLD 398
Cdd:PRK05857 311 VRTAQVYGLSETGCTALCLPTDdgSIVKIeAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASFGtlwiksPANMLGYWN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 399 EPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCA 478
Cdd:PRK05857 391 NPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 604198150 479 YVVLKPP---HLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK05857 470 AVVASAEldeSAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-528 |
9.91e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 127.98 E-value: 9.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAE 113
Cdd:PRK05691 1141 ARQTPERIALVWD-GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 114 LVWVLNKCQAKIFfaptvfkqnrpvdlilplqnqlrhLTHIVGVDKL--APATTALALSQIIDRSEPLQSD-INIHGDEL 190
Cdd:PRK05691 1220 LAYMLADSGVELL------------------------LTQSHLLERLpqAEGVSAIALDSLHLDSWPSQAPgLHLHGDNL 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 191 AAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATG----FLhgvtaPFLIGARSVLL---DI 263
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSvwecFW-----PLITGCRLVLAgpgEH 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMSgatpFIYDLLCAVEQQP--ADLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTES 339
Cdd:PRK05691 1351 RDPQRIAELVQQYGVTTLH----FVPPLLQLFIDEPlaAACTSLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTET 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 340 SphsmVNLGDSTSRMMNTD----GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR-----ALDNE 410
Cdd:PRK05691 1427 A----INVTHWQCQAEDGErspiGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGED 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 411 G--WYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDAcVVAMPDERLGERSCAYVVL------ 482
Cdd:PRK05691 1503 GarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA-AVLVREGAAGAQLVGYYTGeagqea 1581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 604198150 483 KPPHLSLTLEEviaffsrkRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:PRK05691 1582 EAERLKAALAA--------ELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
52-533 |
4.42e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 124.12 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFA-P 129
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAdP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 TVFKQNRPvdlILPLQNQLRHLTHIVGVDKLAPAT------TALALSQIID-RSE----PLQSDinihgDELAAVLFTSG 198
Cdd:PRK05620 120 RLAEQLGE---ILKECPCVRAVVFIGPSDADSAAAhmpegiKVYSYEALLDgRSTvydwPELDE-----TTAAAICYSTG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 199 TEGMPKGVMLTHNNIlaseraYCARLNLTWQDVFlmpaPLGHATGFLHGV-----------TAPFLIGARSVLLDiftPE 267
Cdd:PRK05620 192 TTGAPKGVVYSHRSL------YLQSLSLRTTDSL----AVTHGESFLCCVpiyhvlswgvpLAAFMSGTPLVFPG---PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 ACLTLLAQQRCTCMS----GATPFIYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPH 342
Cdd:PRK05620 259 LSAPTLAKIIATAMPrvahGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETSPV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 343 SMVN------LGDSTSRMMNTDGYAATGVEIKIVDE-------DRNtlpaghEGEEASRGPNVFMGYLDEP--------- 400
Cdd:PRK05620 339 GTVArppsgvSGEARWAYRVSQGRFPASLEYRIVNDgqvmestDRN------EGEIQVRGNWVTASYYHSPteegggaas 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 401 ELTARALDNE-------GWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLG 473
Cdd:PRK05620 413 TFRGEDVEDAndrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 474 ERSCAYVVLKP--PHLSLTLEEvIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK05620 493 ERPLAVTVLAPgiEPTRETAER-LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
48-534 |
4.47e-29 |
|
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: 119.77 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFF 127
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 AptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsdinihgdELAAVLFTSGTEGMPKGVM 207
Cdd:cd05940 81 V------------------------------------------------------------DAALYIYTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 208 LTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTCMsgatPF 287
Cdd:cd05940 101 ISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIF----QY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 288 IYDL---LCAVEQQPADLS-SLRFfLCGGTIIPKkVARDCQQR-GI-KLLSIYGSTESSPhSMVNLGDSTSRMMNTDGYA 361
Cdd:cd05940 177 IGELcryLLNQPPKPTERKhKVRM-IFGNGLRPD-IWEEFKERfGVpRIAEFYAATEGNS-GFINFFGKPGAIGRNPSLL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 362 ATGVEIKIV--DEDRNTLPAGHEG--EEASRGP-----------NVFMGYLDEPELTARAL-----DNEGWYYSGDLCRM 421
Cdd:cd05940 254 RKVAPLALVkyDLESGEPIRDAEGrcIKVPRGEpgllisrinplEPFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 422 DEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERS-CAYVVLKPPHlSLTLEeviAFFSR 500
Cdd:cd05940 334 DGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNE-EFDLS---ALAAH 409
|
490 500 510
....*....|....*....|....*....|....*.
gi 604198150 501 --KRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:cd05940 410 leKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
33-526 |
8.28e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 120.10 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 33 TARAVPDKIAVVDNHGAsWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREA 112
Cdd:PRK13383 44 TAARWPGRTAIIDDDGA-LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 113 ELVWVLNKCQAKIFFAPTVFkqnrpvdlilplqnqlrhlthivgVDKLAPATTALAlsqIIDRSEPLQSDINIHGDELAA 192
Cdd:PRK13383 123 ALAAALRAHHISTVVADNEF------------------------AERIAGADDAVA---VIDPATAGAEESGGRPAVAAP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 193 ---VLFTSGTEGMPKGVMLTH--NNILASERAYCARLNLTWQDVFLMPAPLGHATGFlHGVTAPFLIGARSVLLDIFTPE 267
Cdd:PRK13383 176 griVLLTSGTTGKPKGVPRAPqlRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGL-GMLMLTIALGGTVLTHRHFDAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 ACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPA--DLSSLRFFLCGGTII-PKKVARDCQQRGIKLLSIYGSTESSPHSM 344
Cdd:PRK13383 255 AALAQASLHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDRLdPTLGQRFMDTYGDILYNGYGSTEVGIGAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 345 VNLGDsTSRMMNTDGYAATGVEIKIVDedRNTLPAGHE--------GEEASRGpnvfmgYLDEpelTARALdNEGWYYSG 416
Cdd:PRK13383 335 ATPAD-LRDAPETVGKPVAGCPVRILD--RNNRPVGPRvtgrifvgGELAGTR------YTDG---GGKAV-VDGMTSTG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 417 DLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlSLTLEEVIA 496
Cdd:PRK13383 402 DMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG--SGVDAAQLR 479
|
490 500 510
....*....|....*....|....*....|
gi 604198150 497 FFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:PRK13383 480 DYLKDRVSRFEQPRDINIVSSIPRNPTGKV 509
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
34-526 |
2.32e-28 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 118.46 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVvDNHGASWTYAALDYAASRLANWLLSQgiQPGDRVAFQLPGWCEFTLI--YLACLKTGAVSVPL---LPA 108
Cdd:PRK04813 12 AQTQPDFPAY-DYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVFGHMSPEMLatFLGAVKAGHAYIPVdvsSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 109 WReaeLVWVLNKCQAKIFFAPTVFkqnrPVDlilplqnqlrhlthivgvDKLAPATTALALSQIIDRSEPLQSDINIHGD 188
Cdd:PRK04813 89 ER---IEMIIEVAKPSLIIATEEL----PLE------------------ILGIPVITLDELKDIFATGNPYDFDHAVKGD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 189 ELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGhatgFLHGVTA--PFLI-GARSVLLD--- 262
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYS----FDLSVMDlyPTLAsGGTLVALPkdm 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 ------IFTpeaclTLLAQQRCTCMSgaTPFIYDLlCAV-----EQQPADLSslRFFLCGgTIIPKKVARDCQQR--GIK 329
Cdd:PRK04813 220 tanfkqLFE-----TLPQLPINVWVS--TPSFADM-CLLdpsfnEEHLPNLT--HFLFCG-EELPHKTAKKLLERfpSAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 330 LLSIYGSTESS-PHSMVNLgdsTSRMMNTD-----GYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELT 403
Cdd:PRK04813 289 IYNTYGPTEATvAVTSIEI---TDEMLDQYkrlpiGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 404 ARA---LDNEGWYYSGDLCRMDeDGYIKITGRkKDIIIR-GGENISSREVEDILLQHPRIHDACVVA-MPDERLgERSCA 478
Cdd:PRK04813 366 AEAfftFDGQPAYHTGDAGYLE-DGLLFYQGR-IDFQIKlNGYRIELEEIEQNLRQSSYVESAVVVPyNKDHKV-QYLIA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 604198150 479 YVVLKPPHLS--LTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV 526
Cdd:PRK04813 443 YVVPKEEDFEreFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-522 |
7.28e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 110.63 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVwvlnKCQAKIffAPTV 131
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLK----QCLQEA--EPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FkqnrpvdlilplqnqlrhlthiVGVDKlapattalalsqiidrseplqsdinihGDELAAVLFTSGTEGMPKGVMLTHN 211
Cdd:cd05910 78 F----------------------IGIPK---------------------------ADEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVT--APFLIGARSVLLDiftPEACLTLLAQQRCTCMSGaTPFIY 289
Cdd:cd05910 109 TFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTsvIPDMDPTRPARAD---PQKLVGAIRQYGVSIVFG-SPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 290 DLLCAV-EQQPADLSSLRFFLCGGTIIPKKVA---RDCQQRGIKLLSIYGSTESSPHSMVnlGDS---TSRMMNTDGYAA 362
Cdd:cd05910 185 ERVARYcAQHGITLPSLRRVLSAGAPVPIALAarlRKMLSDEAEILTPYGATEALPVSSI--GSRellATTTAATSGGAG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 363 T-------GVEIKIVD---------EDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARA----LDNEGWYYSGDLCRMD 422
Cdd:cd05910 263 TcvgrpipGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAkiddNSEGFWHRMGDLGYLD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 423 EDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAmpderLGERSCAYVVLKPPHLSLTLEEVIAFFSRKR 502
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG-----VGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
490 500
....*....|....*....|
gi 604198150 503 VAKYKYPERIVIVEKLPRTA 522
Cdd:cd05910 418 ALAKDYPHTQRIGRFLIHPS 437
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
36-545 |
7.81e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.95 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 36 AVPDKIaVVDNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAF------QLPGwceftlIYLACLKTGAVSVPLLPAW 109
Cdd:PRK05691 3732 AHPQRI-AASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALlaerglDLLG------MIVGSFKAGAGYLPLDPGL 3804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 REAELVWVLNKCQAKIFF-APTVFKQNRPVDLILPLQNQLRhlthivgvdklapattaLALSQIIDRSEPLQSDINIHG- 187
Cdd:PRK05691 3805 PAQRLQRIIELSRTPVLVcSAACREQARALLDELGCANRPR-----------------LLVWEEVQAGEVASHNPGIYSg 3867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 -DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPfLIGARSVLL--DI- 263
Cdd:PRK05691 3868 pDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAP-LFGARVEIVpnAIa 3946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 FTPEACLTLLAQQRCTCMSGATPFIYDLLcAVEQQPadLSSLRFFLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSP 341
Cdd:PRK05691 3947 HDPQGLLAHVQAQGITVLESVPSLIQGML-AEDRQA--LDGLRWMLPTGEAMPPELARQWLQRypQIGLVNAYGPAECSD 4023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 342 HSM---VNLGDSTSRMMNTdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARAL-------DNEG 411
Cdd:PRK05691 4024 DVAffrVDLASTRGSYLPI-GSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGER 4102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 412 WYYSGDLCRMDEDGYIKITGR-KKDIIIRgGENISSREVEDILLQHPRIHDAcVVAMPDERLGERSCAYVV-LKPPHLSL 489
Cdd:PRK05691 4103 LYRTGDLARRRSDGVLEYVGRiDHQVKIR-GYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVpHQTVLAQG 4180
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 490 TLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKV-QKFLLRQDIIERLRQEHTA 545
Cdd:PRK05691 4181 ALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLdRKALPALDIGQLQSQAYLA 4237
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
22-424 |
9.10e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 111.68 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 22 GDASLGDYWRQTARAVPDKIAVVD---NHGaSW---TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLAC 95
Cdd:PRK12582 47 YPRSIPHLLAKWAAEAPDRPWLAQrepGHG-QWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 96 LKTGAVSVPLLPAWR-----EAELVWVLNKCQAKIFFA---PTVFKQNRPVDLILPlqnqlrhltHIVGVDKLAPATTAL 167
Cdd:PRK12582 126 MQAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFAqsgAPFARALAALDLLDV---------TVVHVTGPGEGIASI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 168 ALSQIIdrSEPLQSDIN-----IHGDELAAVLFTSGTEGMPKGVMLTHNnILASERAYCARLNLTWQD----VFLMPAPL 238
Cdd:PRK12582 197 AFADLA--ATPPTAAVAaaiaaITPDTVAKYLFTSGSTGMPKAVINTQR-MMCANIAMQEQLRPREPDppppVSLDWMPW 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 239 GHATGFLHGVTaPFLIGARSVLLDIFTP-----EACLTLLAQQRCTCMsGATPFIYDLLC-AVEQQPADLSS----LRFF 308
Cdd:PRK12582 274 NHTMGGNANFN-GLLWGGGTLYIDDGKPlpgmfEETIRNLREISPTVY-GNVPAGYAMLAeAMEKDDALRRSffknLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 309 LCGGTIIPKKVARDCQQ-------RGIKLLSIYGSTESSPHSmVNLGDSTSRMmNTDGYAATGVEIKIVdedrntlPAGH 381
Cdd:PRK12582 352 AYGGATLSDDLYERMQAlavrttgHRIPFYTGYGATETAPTT-TGTHWDTERV-GLIGLPLPGVELKLA-------PVGD 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 604198150 382 EGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCR-MDED 424
Cdd:PRK12582 423 KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPD 466
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
48-533 |
1.70e-25 |
|
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: 109.44 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIF 126
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 127 FAptvfkqnrpvdlilplqnqlrhlthivgvdklapattalalsqiidrseplqsDInihgDELAAVLFTSGTEGMPKGV 206
Cdd:cd05937 83 IV-----------------------------------------------------DP----DDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 207 MLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGvTAPFLIGARSVLL------DIFTPEACLtllaqqrctc 280
Cdd:cd05937 106 AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLG-ACNCLMSGGTLALsrkfsaSQFWKDVRD---------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 281 mSGATPFIY-----DLLCAVEQQPADLSSlRFFLCGGTIIPKKVARDCQQR-GIKLL-SIYGSTESsPHSMVNL--GDST 351
Cdd:cd05937 175 -SGATIIQYvgelcRYLLSTPPSPYDRDH-KVRVAWGNGLRPDIWERFRERfNVPEIgEFYAATEG-VFALTNHnvGDFG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 352 ----------SRMMNTDGYAatgveikIVDEDRNT--------------LPAGHEGEEASRGPNV----FMGYLDEPELT 403
Cdd:cd05937 252 agaighhgliRRWKFENQVV-------LVKMDPETddpirdpktgfcvrAPVGEPGEMLGRVPFKnreaFQGYLHNEDAT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 404 ARAL------DNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV--VAMP--DERLG 473
Cdd:cd05937 325 ESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPghDGRAG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 474 ersCAYVVLKPPHLSLTLE--EVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05937 405 ---CAAITLEESSAVPTEFtkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
34-539 |
2.00e-25 |
|
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: 110.21 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 34 ARAVPDKIAVVDNHGA-SW---TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAW 109
Cdd:cd05921 5 ARQAPDRTWLAEREGNgGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 110 R-----EAELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQnqlrhlTHIVGVDKLAPATTALALSQIIDRSEPLQSDiN 184
Cdd:cd05921 85 SlmsqdLAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLG------TPLVVSRNAVAGRGAISFAELAATPPTAAVD-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 185 IHG----DELAAVLFTSGTEGMPKGVMLTHNNILASEraycARLNLTWQD------VFLMPAPLGHATGFLHGVTaPFLI 254
Cdd:cd05921 158 AFAavgpDTVAKFLFTSGSTGLPKAVINTQRMLCANQ----AMLEQTYPFfgeeppVLVDWLPWNHTFGGNHNFN-LVLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 GARSVLLDIFTPEACL--TLLAQQR--CTCMSGATPFIYD-LLCAVEQQPA----DLSSLRFFLCGGTIIPKKV------ 319
Cdd:cd05921 233 NGGTLYIDDGKPMPGGfeETLRNLReiSPTVYFNVPAGWEmLVAALEKDEAlrrrFFKRLKLMFYAGAGLSQDVwdrlqa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 320 --ARDCQQRgIKLLSIYGSTESSPHSMVNLGDsTSRMMNTdGYAATGVEIKIVdedrntlPAGHEGEEASRGPNVFMGYL 397
Cdd:cd05921 313 laVATVGER-IPMMAGLGATETAPTATFTHWP-TERSGLI-GLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 398 DEPELTARALDNEGWYYSGDLCRM--DED---GYIkITGR-KKDIIIRGGENIS--SREVEDILLQHPRIHDAcVVAMPD 469
Cdd:cd05921 383 RQPELTAQAFDEEGFYCLGDAAKLadPDDpakGLV-FDGRvAEDFKLASGTWVSvgPLRARAVAACAPLVHDA-VVAGED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 470 -ERLGerscAYVVLKP---------PHLS----LTLEEVIAFFSRkRVAKYKYP--------ERIVIVEKLPRTASGKV- 526
Cdd:cd05921 461 rAEVG----ALVFPDLlacrrlvglQEASdaevLRHAKVRAAFRD-RLAALNGEatgsssriARALLLDEPPSIDKGEIt 535
|
570 580
....*....|....*....|.
gi 604198150 527 ------QKFLL--RQDIIERL 539
Cdd:cd05921 536 dkgyinQRAVLerRAALVERL 556
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-545 |
2.46e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.41 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAVVDNhGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVS 102
Cdd:PRK05691 2187 DQTLHGLFAAQAARTPQAPALTFA-GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 103 VPLLPAWREAELVWVLnkcqakiffaptvfkQNRPVDLILPLQNQLRHLTHI-VGVDKLAPATTALALSQIIDRSEPlqs 181
Cdd:PRK05691 2266 VPLDPEYPLERLHYMI---------------EDSGIGLLLSDRALFEALGELpAGVARWCLEDDAAALAAYSDAPLP--- 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 182 diNIHG-DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFL--MPAPLGHATGFLhgvTAPFLIGARS 258
Cdd:PRK05691 2328 --FLSLpQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELhfYSINFDAASERL---LVPLLCGARV 2402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 259 VL--LDIFTPEACLTLLAQQRCTCMsGATPFIYDLLCAVEQQPADLSSLRFFLCGG-TIIPKKVARDCQQ-RGIKLLSIY 334
Cdd:PRK05691 2403 VLraQGQWGAEEICQLIREQQVSIL-GFTPSYGSQLAQWLAGQGEQLPVRMCITGGeALTGEHLQRIRQAfAPQLFFNAY 2481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 335 GSTESSPHSMVNLGDSTSRmmntDGYAAtgVEIK---------IVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTAR 405
Cdd:PRK05691 2482 GPTETVVMPLACLAPEQLE----EGAAS--VPIGrvvgarvayILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAE 2555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 406 -------ALDNEGWYYSGDLCRMDEDGYIKITGR-KKDIIIRGGEnISSREVEDILLQHPRIHDACVVAMpDERLGERSC 477
Cdd:PRK05691 2556 rfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRiDHQVKIRGFR-IELGEIESRLLEHPAVREAVVLAL-DTPSGKQLA 2633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 478 AYVVLKPPHLS----LTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQDIIERLRQEHTA 545
Cdd:PRK05691 2634 GYLVSAVAGQDdeaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQA 2705
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
188-464 |
3.80e-25 |
|
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: 109.23 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNILASerayCARLNLTW--------QDVFLMPAPLGH-------ATGFLHGVTAPF 252
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSN----VAGVFKILeilnkinpTDVYISYLPLAHifervveALFLYHGAKIGF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 253 LIGARSVLLD-----------------------IFTPEACLTLLAQ-------QRCTCM-----SGATPFIYDLLCAVEQ 297
Cdd:cd05927 190 YSGDIRLLLDdikalkptvfpgvprvlnriydkIFNKVQAKGPLKRklfnfalNYKLAElrsgvVRASPFWDKLVFNKIK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 298 QpADLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESS-PHSMVNLGDSTsrmMNTDGYAATGVEIKIVD-EDR 374
Cdd:cd05927 270 Q-ALGGNVRLMLTGSAPLSPEVLEFLRVAlGCPVLEGYGQTECTaGATLTLPGDTS---VGHVGGPLPCAEVKLVDvPEM 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 375 NTLPAGH--EGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVED 451
Cdd:cd05927 346 NYDAKDPnpRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIEN 425
|
330
....*....|...
gi 604198150 452 ILLQHPRIHDACV 464
Cdd:cd05927 426 IYARSPFVAQIFV 438
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
49-531 |
2.23e-24 |
|
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: 106.02 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 49 ASWTYAALDYAASRLANWLLSQGiQPGDR-VAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFf 127
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKF-QTEERaIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 128 aptvfkqnrpvdlilpLQNQLrhlthiVGVDKLapattalalsqiIDRSEPLQSDINiHGDELAAVLFTSGTEGMPKGVM 207
Cdd:cd17654 93 ----------------LQNKE------LDNAPL------------SFTPEHRHFNIR-TDECLAYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 208 LTHNNILASERAYCARLNLTWQDVFLMPAPLgHATGFLHGVTAPFLIGAR--SVLLDIFTPEACLT--LLAQQRCTCMsG 283
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATllIVPTSVKVLPSKLAdiLFKRHRITVL-Q 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 284 ATPFIYDLLCAVEQQPADLS---SLRFFLCGGTIIPKKVARDC---QQRGIKLLSIYGSTESSPHSM---VNLGDSTSRM 354
Cdd:cd17654 216 ATPTLFRRFGSQSIKSTVLSatsSLRVLALGGEPFPSLVILSSwrgKGNRTRIFNIYGITEVSCWALaykVPEEDSPVQL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 355 mntdGYAATGVEIKIVDEDRNTLPAGHEGEEASRGpnvfmGYLDEPELTARALdnegWYYSGDLCRMdEDGYIKITGRKK 434
Cdd:cd17654 296 ----GSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV-----CILDDEVTVPKGT----MRATGDFVTV-KDGELFFLGRKD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 435 DIIIRGGENISSREVEDILLQHPRIhDACVVAMPDErlgERSCAYVVLKPPHlSLTLEEVIAFfsrkRVAKYKYPERIVI 514
Cdd:cd17654 362 SQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSS-SRIHKELQLT----LLSSHAIPDTFVQ 432
|
490
....*....|....*..
gi 604198150 515 VEKLPRTASGKVQKFLL 531
Cdd:cd17654 433 IDKLPLTSHGKVDKSEL 449
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
48-534 |
3.79e-24 |
|
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: 106.22 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQ-GIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIF 126
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 127 FAPTVFKQNrpVDLILP-LQNQ------LRHLTHIVGVDKLAPAttalaLSQIIDRSEPLQSDINIHGDELAAVLFTSGT 199
Cdd:cd05938 83 VVAPELQEA--VEEVLPaLRADgvsvwyLSHTSNTEGVISLLDK-----VDAASDEPVPASLRAHVTIKSPALYIYTSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 200 EGMPKGVMLTHNNILASERAYCARlNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTP----EACLtllaQ 275
Cdd:cd05938 156 TGLPKAARISHLRVLQCSGFLSLC-GVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSAsqfwDDCR----K 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 276 QRCTCMSgatpFIYDL---LCAVEQQPADLS-SLRffLCGGTIIPKKVARDCQQR--GIKLLSIYGSTESSPhSMVNLGD 349
Cdd:cd05938 231 HNVTVIQ----YIGELlryLCNQPQSPNDRDhKVR--LAIGNGLRADVWREFLRRfgPIRIREFYGSTEGNI-GFFNYTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 350 ---STSRMMNTDGYAATGVEIKI-VDED---RNtlPAGHeGEEASRGP-----------NVFMGYLDEPELTARAL---- 407
Cdd:cd05938 304 kigAVGRVSYLYKLLFPFELIKFdVEKEepvRD--AQGF-CIPVAKGEpgllvakitqqSPFLGYAGDKEQTEKKLlrdv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 408 --DNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV--VAMPDERlGERSCAYVVLK 483
Cdd:cd05938 381 fkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPGHE-GRIGMAAVKLK 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 604198150 484 PPHlSLTLEEVIAFFSRKRVAkYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:cd05938 460 PGH-EFDGKKLYQHVREYLPA-YARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
13-452 |
1.77e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 104.41 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 13 KTYRESGYWG-----DASLGDYwrqtaravpdkiavvdnhgaSW-TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWC 86
Cdd:PLN02736 55 ETFRDYKYLGtrirvDGTVGEY--------------------KWmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 87 EFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQ-AKIFFAPtvfkQNRPVDL-ILPLQNQLRHLTHIVGVDKLAPAT 164
Cdd:PLN02736 115 EWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvAAIFCVP----QTLNTLLsCLSEIPSVRLIVVVGGADEPLPSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 165 TALALSQIIDRSEPL-QSDINIHG------DELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAP 237
Cdd:PLN02736 191 PSGTGVEIVTYSKLLaQGRSSPQPfrppkpEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 238 LGH-------ATGFLHGVTAPFLIGARSVLLD--------IFTPEACL------------------------TLLAQQRC 278
Cdd:PLN02736 271 LAHiyervnqIVMLHYGVAVGFYQGDNLKLMDdlaalrptIFCSVPRLynriydgitnavkesgglkerlfnAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 279 TCMSGATPF-IYDLLCAVEQQPADLSSLRFFLCGGTIIPKKVA---RDCqqRGIKLLSIYGSTESS-PHSMVNLGDSTSR 353
Cdd:PLN02736 351 ALENGKNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMeflRIC--FGGRVLEGYGMTETScVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 354 MMntdGYAATGVEIKIVD--------EDRnTLPaghEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDG 425
Cdd:PLN02736 429 HV---GSPNPACEVKLVDvpemnytsEDQ-PYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGG 501
|
490 500
....*....|....*....|....*...
gi 604198150 426 YIKITGRKKDII-IRGGENISSREVEDI 452
Cdd:PLN02736 502 RLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
376-540 |
4.90e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 101.99 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 376 TLPAGHEGEEASRGPNVFMGYLdePELtaraLDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQ 455
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 456 HPRIHDACVVAMPDERLGERSCAYVVLKPPHLSL-TLEEVIAffsrKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLeELKTAIK----DQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
....*.
gi 604198150 535 IIERLR 540
Cdd:PRK07445 445 AVQRLG 450
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
448-525 |
3.29e-22 |
|
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: 90.30 E-value: 3.29e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 448 EVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHlSLTLEEVIAfFSRKRVAKYKYPERIVIVEKLPRTASGK 525
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-ELLEEELVA-HVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
39-533 |
4.25e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 100.22 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 39 DKIAVV---DNHGAS--WTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV-SV------Pll 106
Cdd:PRK00174 82 DKVAIIwegDDPGDSrkITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhSVvfggfsA-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 107 pawrEAeLVWVLNKCQAK-IFFAPTVFKQNRPVdlilPLQNQlrhlthivgVDKlapattALALSQIIDRSEPLQ---SD 182
Cdd:PRK00174 160 ----EA-LADRIIDAGAKlVITADEGVRGGKPI----PLKAN---------VDE------ALANCPSVEKVIVVRrtgGD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 INIHG------DELAA------------------VLFTSGTEGMPKGVM-----------LTHNNILaseraycarlNLT 227
Cdd:PRK00174 216 VDWVEgrdlwwHELVAgasdecepepmdaedplfILYTSGSTGKPKGVLhttggylvyaaMTMKYVF----------DYK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 228 WQDVFLMPAPLGHATGFLHGVTAPFLIGARSVlldIFtpEACLTLLAQQRCTCM---SGATPF------IYDLLCAVEQQ 298
Cdd:PRK00174 286 DGDVYWCTADVGWVTGHSYIVYGPLANGATTL---MF--EGVPNYPDPGRFWEVidkHKVTIFytaptaIRALMKEGDEH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 299 PA--DLSSLRFFlcgGT----IIP-------KKVARD-C-------QQR--GIKLLSIYGSTESSPHSmvnlgdstsrmm 355
Cdd:PRK00174 361 PKkyDLSSLRLL---GSvgepINPeawewyyKVVGGErCpivdtwwQTEtgGIMITPLPGATPLKPGS------------ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 356 ntdgyaAT----GVEIKIVDEDRNTLPAGHEGeeasrgpnvfmgYL--DEP-ELTARAL--DNE-----------GWYYS 415
Cdd:PRK00174 426 ------ATrplpGIQPAVVDEEGNPLEGGEGG------------NLviKDPwPGMMRTIygDHErfvktyfstfkGMYFT 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 416 GDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLK---PPHLSLTlE 492
Cdd:PRK00174 488 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKggeEPSDELR-K 566
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 604198150 493 EVIAFFSRK--RVAKykyPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PRK00174 567 ELRNWVRKEigPIAK---PDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-533 |
5.92e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.01 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 25 SLGDYWRQTARAVPDKIAV-----VDNHGASWTYAALDYAASRLANWLLSQGiQPGDRVAFQLPGWCEFTLIYLACLKTG 99
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALrfladDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 100 AVSVPLLPA-----WREAELVWVLNKCQAKIFFAPTvfkqnrpvDLILPLQnQLRHLT-----HIVGVDKLAPATTAlal 169
Cdd:PRK05691 89 VIAVPAYPPesarrHHQERLLSIIADAEPRLLLTVA--------DLRDSLL-QMEELAaanapELLCVDTLDPALAE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 170 sqiiDRSEPlqsdiNIHGDELAAVLFTSGTEGMPKGVMLTHNNILASE----RAYcaRLNLTWQDVFLMPAPLGHATGFL 245
Cdd:PRK05691 157 ----AWQEP-----ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEqlirHGF--GIDLNPDDVIVSWLPLYHDMGLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 246 HGVTAPFLIGARSVLLD----IFTPEACLTLLAQQRCTcMSGATPFIYDLlC-------AVEQ-------------QPAD 301
Cdd:PRK05691 226 GGLLQPIFSGVPCVLMSpayfLERPLRWLEAISEYGGT-ISGGPDFAYRL-CservsesALERldlsrwrvaysgsEPIR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 302 LSSLRFFL-----CGGTiiPKK-------------VARDCQQRGIKLLSIYGSTESSPHSMVNLGdstSRMMNTdGYAAT 363
Cdd:PRK05691 304 QDSLERFAekfaaCGFD--PDSffasyglaeatlfVSGGRRGQGIPALELDAEALARNRAEPGTG---SVLMSC-GRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 364 GVEIKIVDEDR-NTLPAGHEGEEASRGPNVFMGYLDEPELTARA---LDNEGWYYSGDLCRMdEDGYIKITGRKKDIIIR 439
Cdd:PRK05691 378 GHAVLIVDPQSlEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 440 GGENISSREVEDIL------LQHPRIHDACVVAMPDERLG-----ERSCAYVVlKPPHLSLTLEEVIAffsrkrVAKYKY 508
Cdd:PRK05691 457 RGHNLYPQDIEKTVerevevVRKGRVAAFAVNHQGEEGIGiaaeiSRSVQKIL-PPQALIKSIRQAVA------EACQEA 529
|
570 580
....*....|....*....|....*..
gi 604198150 509 PERIVIVE--KLPRTASGKVQKFLLRQ 533
Cdd:PRK05691 530 PSVVLLLNpgALPKTSSGKLQRSACRL 556
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
26-424 |
2.10e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 98.03 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 26 LGDYWRQT-------ARAVPDKIAVVD-NHGASW---TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLA 94
Cdd:PRK08180 34 LGDYPRRLtdrlvhwAQEAPDRVFLAErGADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 95 CLKTGAVSVPLLPAWRE-----AELVWVLNKCQAKIFFAPTVFKQNRPVDLILPLQnqlrhlTHIVGVDKLAPATTALAL 169
Cdd:PRK08180 114 AMYAGVPYAPVSPAYSLvsqdfGKLRHVLELLTPGLVFADDGAAFARALAAVVPAD------VEVVAVRGAVPGRAATPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 170 SQIIDRSEPLQSDI---NIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAycarLNLTWQD------VFLMPAPLGH 240
Cdd:PRK08180 188 AALLATPPTAAVDAahaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQM----LAQTFPFlaeeppVLVDWLPWNH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 241 ATGFLHGVT----------------APFLIgARSV--LLDIfTPEACLTllaqqrctcmsgaTPFIYDLLCAVEQQPADL 302
Cdd:PRK08180 264 TFGGNHNLGivlynggtlyiddgkpTPGGF-DETLrnLREI-SPTVYFN-------------VPKGWEMLVPALERDAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 303 -----SSLRFFLCGGTIIPKKV--------ARDCQQRgIKLLSIYGSTESSPHSMvNLGDSTSRMMNTdGYAATGVEIKI 369
Cdd:PRK08180 329 rrrffSRLKLLFYAGAALSQDVwdrldrvaEATCGER-IRMMTGLGMTETAPSAT-FTTGPLSRAGNI-GLPAPGCEVKL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 370 VdedrntlPAGHEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRM-DED 424
Cdd:PRK08180 406 V-------PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPA 454
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-533 |
3.21e-21 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 97.66 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 49 ASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFA 128
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 129 PTVFKQN-RPVDLILPLQNQL-RHLTHIVGVDKLAPATTALALS--------------QIIDRSEPLQSDIN-IHGDELA 191
Cdd:PLN02654 199 CNAVKRGpKTINLKDIVDAALdESAKNGVSVGICLTYENQLAMKredtkwqegrdvwwQDVVPNYPTKCEVEwVDAEDPL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVLFTSGTEGMPKGVMLTHNN-ILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGArSVLLDIFTPE--- 267
Cdd:PLN02654 279 FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGA-TVLVFEGAPNypd 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 268 --ACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADLS--SLRFF-LCGGTIIPK------KVARDCQqrgIKLLSIYGS 336
Cdd:PLN02654 358 sgRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLgSVGEPINPSawrwffNVVGDSR---CPISDTWWQ 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 337 TESSPHSMVNLGDSTSRMMNTDGYAATGVEIKIVDEDRNTLpaghEGEEA------SRGPNVF---MGYLDEPELTARAl 407
Cdd:PLN02654 435 TETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEI----EGECSgylcvkKSWPGAFrtlYGDHERYETTYFK- 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 408 DNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKP--P 485
Cdd:PLN02654 510 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEgvP 589
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 604198150 486 HlSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:PLN02654 590 Y-SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
195-531 |
2.13e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 93.56 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLA 274
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 275 QQRCTCMSGATPFIY---DLLCAVEQQPADLSSlrfflcgGTIIPKKVARDCQQRGIKLLSIYGSTESsphsmvnlgdst 351
Cdd:PRK08308 188 NTPQHILYAVPLMLHilgRLLPGTFQFHAVMTS-------GTPLPEAWFYKLRERTTYMMQQYGCSEA------------ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 352 srmmntdGYAATGVEIKIVDEDRNTLPagHEGEEASRGPNvfmgyldEP-ELTARALDNEgwYYSGDLCRMDEDGYIKIT 430
Cdd:PRK08308 249 -------GCVSICPDMKSHLDLGNPLP--HVSVSAGSDEN-------APeEIVVKMGDKE--IFTKDLGYKSERGTLHFM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 431 GRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEviafFSRKRVAKYKYPE 510
Cdd:PRK08308 311 GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLRE----WCIQHLAPYQVPH 386
|
330 340
....*....|....*....|.
gi 604198150 511 RIVIVEKLPRTASGKVQKFLL 531
Cdd:PRK08308 387 EIESVTEIPKNANGKVSRKLL 407
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
71-510 |
1.63e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 92.35 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 71 GIQPGDRVA-FQLPGWCEFTLIYlACLKTGAVSV---------PLLPAWREAElvwvlnkCQAKIFFAPTVfkqnrpVDL 140
Cdd:PTZ00216 142 GLTKGSNVAiYEETRWEWLASIY-GIWSQSMVAAtvyanlgedALAYALRETE-------CKAIVCNGKNV------PNL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 141 ILPLQNQLRHLTHIVGVDKLAPATTA-----LALSQIIDRSEPLQSDINIHG----DELAAVLFTSGTEGMPKGVMLTHN 211
Cdd:PTZ00216 208 LRLMKSGGMPNTTIIYLDSLPASVDTegcrlVAWTDVVAKGHSAGSHHPLNIpennDDLALIMYTSGTTGDPKGVMHTHG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 212 NILASERAYCARLN-----LTWQDVFLMPAPLGHATGFlhGVTAPFLigARSVLLDIFTPEaclTL----------LAQQ 276
Cdd:PTZ00216 288 SLTAGILALEDRLNdligpPEEDETYCSYLPLAHIMEF--GVTNIFL--ARGALIGFGSPR---TLtdtfarphgdLTEF 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 277 RCTCMSGaTPFIYDLLC-AVEQQPADLSSL-----------------------------------------RFFLCGGTI 314
Cdd:PTZ00216 361 RPVFLIG-VPRIFDTIKkAVEAKLPPVGSLkrrvfdhayqsrlralkegkdtpywnekvfsapravlggrvRAMLSGGGP 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 315 IPKK------VARDCQQRGikllsiYGSTESsphsmVNLGdSTSRMMNTDgYAATG-----VEIKIVDED--RNTLPAGH 381
Cdd:PTZ00216 440 LSAAtqefvnVVFGMVIQG------WGLTET-----VCCG-GIQRTGDLE-PNAVGqllkgVEMKLLDTEeyKHTDTPEP 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 382 EGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRG-GENISSREVEDILLQHPRI- 459
Cdd:PTZ00216 507 RGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEALYGQNELVv 586
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 604198150 460 -HDACVVAMPDerlgeRS--CAyvvlkpphLSLTLEEVIAFFSRKRVAKYKYPE 510
Cdd:PTZ00216 587 pNGVCVLVHPA-----RSyiCA--------LVLTDEAKAMAFAKEHGIEGEYPA 627
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
48-534 |
2.18e-19 |
|
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: 90.95 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 48 GASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLN--KCQAKI 125
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITvsKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 126 FfaptvfkqnrpvDLILPLQNQlrhlthivgvdklapattalalsqiIDRSEPLQSDINIHgDELAAVlFTSGTEGMPKG 205
Cdd:cd05939 81 F------------NLLDPLLTQ-------------------------SSTEPPSQDDVNFR-DKLFYI-YTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 206 VMLTHNNIL--ASERAYCARLNLtwQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLAQQRCTcmsg 283
Cdd:cd05939 122 AVIVHSRYYriAAGAYYAFGMRP--EDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCT---- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 284 ATPFIYDL---LCAVEQQPADLS-SLRFFLCGG---TIIPKKVARdcqqRGIKLLS-IYGSTESsphsmvnlgdsTSRMM 355
Cdd:cd05939 196 IVQYIGEIcryLLAQPPSEEEQKhNVRLAVGNGlrpQIWEQFVRR----FGIPQIGeFYGATEG-----------NSSLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 356 NTDGY-AATG-----------VEIKIVDEDRNTLPAGHEGEEASRGPN----------------VFMGYLDEPELTARAL 407
Cdd:cd05939 261 NIDNHvGACGfnsrilpsvypIRLIKVDEDTGELIRDSDGLCIPCQPGepgllvgkiiqndplrRFDGYVNEGATNKKIA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 408 DN-----EGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV--VAMPdERLGERSCAYV 480
Cdd:cd05939 341 RDvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVP-GVEGRAGMAAI 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 604198150 481 VlkPPHLSLTLEEVIAFFsRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQD 534
Cdd:cd05939 420 V--DPERKVDLDRFSAVL-AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
38-528 |
1.55e-18 |
|
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: 88.73 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVV------DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWRE 111
Cdd:cd17647 2 PERTCVVetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 112 AelvwvlnkcqakiffaptvfKQN------RPVDLILplqnqLRHLTHIVGVDklapattalalsqiidrSEPLQSdini 185
Cdd:cd17647 82 A--------------------RQNiylgvaKPRGLIV-----IRAAGVVVGPD-----------------SNPTLS---- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 186 hgdelaavlFTSGTEGMPKGVMLTHNNIlaserAY-----CARLNLTWQDVFLMPAPLGHATgFLHGVTAPFLIGARsvL 260
Cdd:cd17647 116 ---------FTSGSEGIPKGVLGRHFSL-----AYyfpwmAKRFNLSENDKFTMLSGIAHDP-IQRDMFTPLFLGAQ--L 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 261 L-----DIFTPEACLTLLAQQRCTcMSGATPFIYDLLCAVEQQPADLSSLRFFLcgGTIIPKkvaRDCQQ-----RGIKL 330
Cdd:cd17647 179 LvptqdDIGTPGRLAEWMAKYGAT-VTHLTPAMGQLLTAQATTPFPKLHHAFFV--GDILTK---RDCLRlqtlaENVRI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 331 LSIYGSTE--------------SSPHSMVNLGDStsrMMNtdGYAATGVEIKIVDE-DRNTLPA-GHEGEEASRGPNVFM 394
Cdd:cd17647 253 VNMYGTTEtqravsyfevpsrsSDPTFLKNLKDV---MPA--GRGMLNVQLLVVNRnDRTQICGiGEVGEIYVRAGGLAE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 395 GYLDEPELTARAL-----------------DNEGW-----------YYSGDLCRMDEDGYIKITGRKKD-IIIRGGEnIS 445
Cdd:cd17647 328 GYRGLPELNKEKFvnnwfvepdhwnyldkdNNEPWrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDqVKIRGFR-IE 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 446 SREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPHLSLTLEEVIAF-------------------------FSR 500
Cdd:cd17647 407 LGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQEDVpkevstdpivkgligyrklikdireFLK 486
|
570 580
....*....|....*....|....*...
gi 604198150 501 KRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:cd17647 487 KRLASYAIPSLIVVLDKLPLNPNGKVDK 514
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
52-533 |
6.53e-17 |
|
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: 83.86 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGwCEFTLIylACLKT---GAVSVPLLPAWREAELVWVLNKCQAKIFFA 128
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPN-IPEAVV--AMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 129 -PTVFKQNRPVDL---ILPLQNQLRHLTHIVGVDKLAPATT--------ALALSQIIDRSEPLQSDIN-IHGDELAAVLF 195
Cdd:cd05943 177 vDAYTYNGKRHDVrekVAELVKGLPSLLAVVVVPYTVAAGQpdlskiakALTLEDFLATGAAGELEFEpLPFDHPLYILY 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNILA---SERAYCArlNLTWQDVFLMPAplghATGFL--HGVTAPFLIGARSVLLD----IFTP 266
Cdd:cd05943 257 SSGTTGLPKCIVHGAGGTLLqhlKEHILHC--DLRPGDRLFYYT----TCGWMmwNWLVSGLAVGATIVLYDgspfYPDT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 267 EACLTLLAQQRCTCMsGATPFIYDLLCAVEQQPA---DLSSLRFFLCGGTIIPKKVAR---DCQQRGIKLLSIYGSTE-- 338
Cdd:cd05943 331 NALWDLADEEGITVF-GTSAKYLDALEKAGLKPAethDLSSLRTILSTGSPLKPESFDyvyDHIKPDVLLASISGGTDii 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 339 -----SSPHSMVNLGDSTSRMMntdgyaatGVEIKIVDEDRNTLPaGHEGEEASRGPNVFM--GYLDEPELT-------A 404
Cdd:cd05943 410 scfvgGNPLLPVYRGEIQCRGL--------GMAVEAFDEEGKPVW-GEKGELVCTKPFPSMpvGFWNDPDGSryraayfA 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 405 RaldNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKP 484
Cdd:cd05943 481 K---YPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRE 557
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 604198150 485 PH-LSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFLLRQ 533
Cdd:cd05943 558 GVeLDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKK 607
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
301-531 |
3.21e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 81.71 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 301 DLSSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHSMVNLGdSTSRMMNTDGYAATGVEIKIVDEDRNTLPA 379
Cdd:PTZ00237 378 DLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGYGQTEIGITYLYCYG-HINIPYNATGVPSIFIKPSILSEDGKELNV 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 380 GHEGEEASR--GPNVFMGYLDEPELTARALDNE--GWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQ 455
Cdd:PTZ00237 457 NEIGEVAFKlpMPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 456 HPRIHDACVVAMPDERLGERSCAYVVLKPP----HLSLT-LEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQKFL 530
Cdd:PTZ00237 537 HPLVLECCSIGIYDPDCYNVPIGLLVLKQDqsnqSIDLNkLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQI 616
|
.
gi 604198150 531 L 531
Cdd:PTZ00237 617 I 617
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
193-464 |
3.94e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 81.40 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 193 VLFTSGTEGMPKGVMLTHNNILASERAYCARLN-----LTWQDVFLMPAPLGH---------------ATGFLHG----- 247
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHildrmieeyffrkgaSVGYYHGdlnal 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 248 ------VTAPFLIGARSVLLDIFtpEACLTLLAQ--------------------QRCTCMSGATPFIyDLLcAVEQQPAD 301
Cdd:PLN02430 305 rddlmeLKPTLLAGVPRVFERIH--EGIQKALQElnprrrlifnalykyklawmNRGYSHKKASPMA-DFL-AFRKVKAK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 302 LSS-LRFFLCGGTIIPKKVardcqQRGIKLLSI------YGSTESSPHSMVNLGDSTSrMMNTDGYAATGVEIKI--VDE 372
Cdd:PLN02430 381 LGGrLRLLISGGAPLSTEI-----EEFLRVTSCafvvqgYGLTETLGPTTLGFPDEMC-MLGTVGAPAVYNELRLeeVPE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 373 -DRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVE 450
Cdd:PLN02430 455 mGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLE 533
|
330
....*....|....
gi 604198150 451 DILLQHPRIHDACV 464
Cdd:PLN02430 534 NVYGQNPIVEDIWV 547
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
50-535 |
7.33e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 80.76 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 50 SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAV-SVpllpawreaelvwvlnkcqakIF-- 126
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhSV---------------------VFgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 127 FAPTVFKQN----RPVdLIL---------------PLQNQLRHL-----THIVGVDK-LAPATT--------ALALSQII 173
Cdd:PRK10524 143 FASHSLAARiddaKPV-LIVsadagsrggkvvpykPLLDEAIALaqhkpRHVLLVDRgLAPMARvagrdvdyATLRAQHL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 174 DRSEP---LQSDinihgdELAAVLFTSGTEGMPKGVMLT---HNNILAS--ERAYCARLNltwqDVFLMPAPLGHATGFL 245
Cdd:PRK10524 222 GARVPvewLESN------EPSYILYTSGTTGKPKGVQRDtggYAVALATsmDTIFGGKAG----ETFFCASDIGWVVGHS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 246 HGVTAPFLIGARSVL---LDIfTPEACL--TLLAQQRCTCMSGATPFIYDLlcaVEQQPA-----DLSSLRFFLCGGTII 315
Cdd:PRK10524 292 YIVYAPLLAGMATIMyegLPT-RPDAGIwwRIVEKYKVNRMFSAPTAIRVL---KKQDPAllrkhDLSSLRALFLAGEPL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 316 PKKVARDCQQR-GIKLLSIYGSTESSPHSMVN---LGDSTSRMmNTDGYAATGVEIKIVDE-DRNTLPAGHEGEEASRGP 390
Cdd:PRK10524 368 DEPTASWISEAlGVPVIDNYWQTETGWPILAIargVEDRPTRL-GSPGVPMYGYNVKLLNEvTGEPCGPNEKGVLVIEGP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 391 --NVFMG--YLDEPEL--TARALDNEGWYYSGDLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQHPRIHDACV 464
Cdd:PRK10524 447 lpPGCMQtvWGDDDRFvkTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 604198150 465 VAMPDERLGERSCAYVVLK------PPHLSLTLEEVIAFFSRKRVAKYKYPERIVIVEKLPRTASGKvqkfLLRQDI 535
Cdd:PRK10524 527 VGVKDALKGQVAVAFVVPKdsdslaDREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGK----LLRRAI 599
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
192-535 |
7.55e-16 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 80.20 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 192 AVL-FTSGTEGMPKGVMLTHNNILASERAYCARLNLTW-QDVFLMPAPLGHATGFLHGVTApFLIGARSVL--LDIFT-- 265
Cdd:PRK05851 155 AVLqGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDMGLAFLLTA-ALAGAPLWLapTTAFSas 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 PEACLTLLAQQRCTcMSGATPFIYDLL--CAVEQQPADLSSLRFFLCGGTIIpkkvarDCQ--QRGIKLLS--------- 332
Cdd:PRK05851 234 PFRWLSWLSDSRAT-LTAAPNFAYNLIgkYARRVSDVDLGALRVALNGGEPV------DCDgfERFATAMApfgfdagaa 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 333 --IYGSTESS-----PHSMVNL---------GDSTSRMMNTdGYAATGVEIKIVDEDRNTLPAGHE-GEEASRGPNVFMG 395
Cdd:PRK05851 307 apSYGLAESTcavtvPVPGIGLrvdevttddGSGARRHAVL-GNPIPGMEVRISPGDGAAGVAGREiGEIEIRGASMMSG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 396 YLDEPeltarALDNEGWYYSGDLCRMDEDGYIkITGRKKDIIIRGGENISSREVEDILLQHPRIHDACVVAMPDERLGER 475
Cdd:PRK05851 386 YLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSAR 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 604198150 476 SCAYVVL--KPPHLSLTLEEVIaffsrKRVAKY--KYPERIVIVE--KLPRTASGKVQKFLLRQDI 535
Cdd:PRK05851 460 PGLVIAAefRGPDEAGARSEVV-----QRVASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKRSL 520
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
18-528 |
4.56e-15 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 78.57 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 18 SGYWGdaSLGDYWRQTARAVPDKIAVVDNHGA--------SWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFT 89
Cdd:TIGR03443 232 SGFRG--AIHDIFADNAEKHPDRTCVVETPSFldpssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 90 LIYLACLKTGAV-SV--PLLPAWREAELVWVlNKCQAKIFFA------PTVfkqnrpVDLIlplQNQLRHLTHIVGVDKL 160
Cdd:TIGR03443 310 VAVMGVLKAGATfSVidPAYPPARQTIYLSV-AKPRALIVIEkagtldQLV------RDYI---DKELELRTEIPALALQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 161 APAT-TALALSQiiDRSEPLQSDINIHGDELAAVL---------FTSGTEGMPKGVMLTHNNIlaserAY-----CARLN 225
Cdd:TIGR03443 380 DDGSlVGGSLEG--GETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSL-----AYyfpwmAKRFG 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 226 LTWQDVFLMpaplghATGFLH-----GVTAPFLIGARsvLL-----DIFTPEACLTLLAQQRCTcMSGATPFIYDLLCAv 295
Cdd:TIGR03443 453 LSENDKFTM------LSGIAHdpiqrDMFTPLFLGAQ--LLvptadDIGTPGRLAEWMAKYGAT-VTHLTPAMGQLLSA- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 296 eQQPADLSSLR--FFLcgGTIIPKkvaRDCQQ-----RGIKLLSIYGSTE--------------SSPHSMVNLGDStsrM 354
Cdd:TIGR03443 523 -QATTPIPSLHhaFFV--GDILTK---RDCLRlqtlaENVCIVNMYGTTEtqravsyfeipsrsSDSTFLKNLKDV---M 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 355 MntdgyAATG---VEIKIVDE-DRNTLPA-GHEGEEASRGPNVFMGYLDEPELTARAL-----------------DNEGW 412
Cdd:TIGR03443 594 P-----AGKGmknVQLLVVNRnDRTQTCGvGEVGEIYVRAGGLAEGYLGLPELNAEKFvnnwfvdpshwidldkeNNKPE 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 413 -----------YYSGDLCRMDEDGYIKITGRKKD-IIIRGGEnISSREVEDILLQHPRIHDACVVAMPDERLGERSCAYV 480
Cdd:TIGR03443 669 refwlgprdrlYRTGDLGRYLPDGNVECCGRADDqVKIRGFR-IELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYI 747
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 481 V--LKPPHLSLTLEEV----------------------IAFFSRKRVAKYKYPERIVIVEKLPRTASGKVQK 528
Cdd:TIGR03443 748 VpqDKSDELEEFKSEVddeessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDK 819
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
51-464 |
6.64e-15 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 77.85 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 51 W-TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKiffap 129
Cdd:PLN02387 106 WiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT----- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 130 TVFKQNRPVDLILPLQNQLRHLTHIVGVDKLAPAT----------TALALSQI--IDRSEPLQSDINIHGDeLAAVLFTS 197
Cdd:PLN02387 181 TVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSdsslsgssnwTVSSFSEVekLGKENPVDPDLPSPND-IAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 198 GTEGMPKGVMLTHNNILASERAYCARL-NLTWQDVFLMPAPLGH-----ATGFLHGVTAPFLIGARSVLLDIFT------ 265
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHilelaAESVMAAVGAAIGYGSPLTLTDTSNkikkgt 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 266 ----PEACLTLLA-------------QQRCTCMSGATPFIYDL-----LCAVE--------------------QQPADLS 303
Cdd:PLN02387 340 kgdaSALKPTLMTavpaildrvrdgvRKKVDAKGGLAKKLFDIaykrrLAAIEgswfgawglekllwdalvfkKIRAVLG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 304 -SLRFFLCGGTiipkKVARDCQQ-----RGIKLLSIYGSTESSPHSMVNLGDSTS--RMmntdGYAATGVEIKIVDEDR- 374
Cdd:PLN02387 420 gRIRFMLSGGA----PLSGDTQRfinicLGAPIGQGYGLTETCAGATFSEWDDTSvgRV----GPPLPCCYVKLVSWEEg 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 375 ------NTLPaghEGEEASRGPNVFMGYLDEPELTARA--LDNEG--WYYSGDLCRMDEDGYIKITGRKKDII-IRGGEN 443
Cdd:PLN02387 492 gylisdKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEY 568
|
490 500 510
....*....|....*....|....*....|.
gi 604198150 444 IS----------SREVEDILLQHPRIHDACV 464
Cdd:PLN02387 569 VSlgkveaalsvSPYVDNIMVHADPFHSYCV 599
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
12-452 |
5.41e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 74.67 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 12 RKTYRESGY----WGDASLGDYWRQTARAVPD-----KIAVVDNHGASW---TYAALDYAASRLANWLLSQGIQPGDRVA 79
Cdd:PLN02614 29 RSIFAKDGFpnpiEGMDSCWDVFRMSVEKYPNnpmlgRREIVDGKPGKYvwqTYQEVYDIVIKLGNSLRSVGVKDEAKCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 80 FQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIFFAptvfKQNRPVDLILPLQNQLRHLTHIVGVDK 159
Cdd:PLN02614 109 IYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFV----EEKKISELFKTCPNSTEYMKTVVSFGG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 160 LAP---------ATTALALSQIIDRSEPLQSDINIHG-DELAAVLFTSGTEGMPKGVMLTHNNILASERAYC-----ARL 224
Cdd:PLN02614 185 VSReqkeeaetfGLVIYAWDEFLKLGEGKQYDLPIKKkSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 225 NLTWQDVFLMPAPLGH---------------ATGFLHGVTA----------PFLIGARSVLLD----------------- 262
Cdd:PLN02614 265 ALTVKDVYLSYLPLAHifdrvieecfiqhgaAIGFWRGDVKlliedlgelkPTIFCAVPRVLDrvysglqkklsdggflk 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 263 --IFTPEACLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADlSSLRFFLCGGTIIPK------KVARDCQqrgikLLSIY 334
Cdd:PLN02614 345 kfVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLAShvesflRVVACCH-----VLQGY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 335 GSTESSPHSMVNLGDSTSrMMNTDGYAATGVEIK---IVDEDRNTLPAGHEGEEASRGPNVFMGYLDEPELTARALDnEG 411
Cdd:PLN02614 419 GLTESCAGTFVSLPDELD-MLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLI-DG 496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 604198150 412 WYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVEDI 452
Cdd:PLN02614 497 WLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
52-459 |
3.03e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 72.57 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIffaptV 131
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSI-----A 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 132 FKQNRPVDLILPLQNQLR-HLTHIVGVDKLAPATTALALSQII------DRSEPLQSDINI---HGDELAAVLFTSGTEG 201
Cdd:PLN02861 154 FVQESKISSILSCLPKCSsNLKTIVSFGDVSSEQKEEAEELGVscfsweEFSLMGSLDCELppkQKTDICTIMYTSGTTG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 202 MPKGVMLTHNNILASERAYCARLNLT-----WQDVFLMPAPLGH---------------ATGFLHGVTAPFLIGARSVLL 261
Cdd:PLN02861 234 EPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHvydqvietyciskgaSIGFWQGDIRYLMEDVQALKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 262 DIF--TPEACLTLLAQQRCTCMSG---------------------------ATPFIyDLLCAVEQQPADLSSLRFFLCGG 312
Cdd:PLN02861 314 TIFcgVPRVYDRIYTGIMQKISSGgmlrkklfdfaynyklgnlrkglkqeeASPRL-DRLVFDKIKEGLGGRVRLLLSGA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 313 TIIPKKVARDCQQRGIKLLSI-YGSTESSPHSMVNLGDSTSrMMNTDGYAATGVEIKIV---DEDRNTLPAGHEGEEASR 388
Cdd:PLN02861 393 APLPRHVEEFLRVTSCSVLSQgYGLTESCGGCFTSIANVFS-MVGTVGVPMTTIEARLEsvpEMGYDALSDVPRGEICLR 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 604198150 389 GPNVFMGYLDEPELTARALdNEGWYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVEDILLQHPRI 459
Cdd:PLN02861 472 GNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 542
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
24-539 |
4.52e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.51 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 24 ASLGDYWRQTARAVPDKIAV------VDNHGA--SWTYAALDYAASRLANWLLSQGiQPGDRVAFQLPGWCEFTLIYLAC 95
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFtfidyeQDPAGVaeTLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 96 LKTGAVSVPL---LPAWREAELVWVLNKCqakiffAPTVfkqnrpvdlILPLQNQLRHLTHIVGVDKLAPATTALALSQI 172
Cdd:PRK05850 80 LQAGLIAVPLsvpQGGAHDERVSAVLRDT------SPSV---------VLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 173 iDRSEPLQSDINIHGDELAAVL-FTSGTEGMPKGVMLTHNNILA----SERAY------CARLNLT---WqdvflmpAPL 238
Cdd:PRK05850 145 -DLDSPRGSDARPRDLPSTAYLqYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYfgdtggVPPPDTTvvsW-------LPF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 239 GHATGFLHGVTAPFLIGARSVLLdifTPEACLT-------LLAQqRCTCMSGATPFIYDLlcAV----EQQPA--DLSSL 305
Cdd:PRK05850 217 YHDMGLVLGVCAPILGGCPAVLT---SPVAFLQrparwmqLLAS-NPHAFSAAPNFAFEL--AVrktsDDDMAglDLGGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 306 RFFLCGGTII-PKKVARDCQQ------RGIKLLSIYG----------STESSPHSMVNLgD----STSRMMNTDGYAAT- 363
Cdd:PRK05850 291 LGIISGSERVhPATLKRFADRfapfnlRETAIRPSYGlaeatvyvatREPGQPPESVRF-DyeklSAGHAKRCETGGGTp 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 364 ----GV----EIKIVDEDRNT-LPAGHEGEEASRGPNVFMGYLDEPELTAR----ALDN------EG-WYYSGDLCRMDE 423
Cdd:PRK05850 370 lvsyGSprspTVRIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERtfgaTLVDpspgtpEGpWLRTGDLGFISE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 424 DGYIkITGRKKDIIIRGGENISSrevEDIllqhprihDACV----------VAMPDERlGERSCAYVVLKPPH------- 486
Cdd:PRK05850 450 GELF-IVGRIKDLLIVDGRNHYP---DDI--------EATIqeitggrvaaISVPDDG-TEKLVAIIELKKRGdsdeeam 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 604198150 487 --LSLTLEEVIAFFSRK---RVAKykyperIVIVE--KLPRTASGKVQKF----LLRQDIIERL 539
Cdd:PRK05850 517 drLRTVKREVTSAISKShglSVAD------LVLVApgSIPITTSGKIRRAacveQYRQDEFTRL 574
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
52-425 |
2.04e-12 |
|
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: 69.79 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 52 TYAALDYAASRLANWL-LSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKIF---- 126
Cdd:cd17632 69 TYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLavsa 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 127 -------------FAPT---VFKQNRPVDlilplqnqlrhlTHIVGVD----KLAP---ATTALALSQIIDRSEPLQSDI 183
Cdd:cd17632 149 ehldlaveavlegGTPPrlvVFDHRPEVD------------AHRAALEsareRLAAvgiPVTTLTLIAVRGRDLPPAPLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 184 NI--HGDELAAVLFTSGTEGMPKGVMLTHNNIlaserAYCARLNLTWQDVFLMPA------PLGHATG-------FLHGV 248
Cdd:cd17632 217 RPepDDDPLALLIYTSGSTGTPKGAMYTERLV-----ATFWLKVSSIQDIRPPASitlnfmPMSHIAGrislygtLARGG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 249 TAPFLIGAR-SVLLD----------IFTPEAClTLLAQQRCTCMSGATPFIYDLLCAVEQQPADlssLRFFLCGGTIIPK 317
Cdd:cd17632 292 TAYFAAASDmSTLFDdlalvrptelFLVPRVC-DMLFQRYQAELDRRSVAGADAETLAERVKAE---LRERVLGGRLLAA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 318 KVAR---DCQQR-------GIKLLSIYGSTESsphSMVNLGDSTSRMMNTD---------GYAATgveikivdeDRntlP 378
Cdd:cd17632 368 VCGSaplSAEMKafmesllDLDLHDGYGSTEA---GAVILDGVIVRPPVLDyklvdvpelGYFRT---------DR---P 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 604198150 379 agH-EGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLcrMDEDG 425
Cdd:cd17632 433 --HpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV--MAELG 476
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
60-541 |
5.29e-11 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 65.49 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 60 ASRLANWLLSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVLNKCQAKiffapTVFKQnrpvD 139
Cdd:PLN03052 218 VSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAK-----AIFTQ----D 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 140 LILPLQNQLRHLTHIVGvdklAPATTALALSQI------------------IDRSEPLQSdinihGDELAAV-------- 193
Cdd:PLN03052 289 VIVRGGKSIPLYSRVVE----AKAPKAIVLPADgksvrvklregdmswddfLARANGLRR-----PDEYKAVeqpveaft 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 194 --LFTSGTEGMPKGVMLTHNN-ILASERAYCaRLNLTWQDVFLMPAPLGHATG-FLhgVTAPFLIGARSVL-----LDI- 263
Cdd:PLN03052 360 niLFSSGTTGEPKAIPWTQLTpLRAAADAWA-HLDIRKGDIVCWPTNLGWMMGpWL--VYASLLNGATLALyngspLGRg 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 264 ---FTPEACLTLL--------AQQRCTCMSGAtpfiydllcaveqqpaDLSSLRFFlcGGTIIPKKVARD---CQQRGIK 329
Cdd:PLN03052 437 fakFVQDAKVTMLgtvpsivkTWKNTNCMAGL----------------DWSSIRCF--GSTGEASSVDDYlwlMSRAGYK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 330 -LLSIYGSTEssphsmvnLGDS--TSRMMNTDGYAA-----TGVEIKIVDEDRNTLPAGHEGE-EASRGPNVFMGyldep 400
Cdd:PLN03052 499 pIIEYCGGTE--------LGGGfvTGSLLQPQAFAAfstpaMGCKLFILDDSGNPYPDDAPCTgELALFPLMFGA----- 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 401 elTARAL--DNEGWYYSG-------------DLCRMDEDGYIKITGRKKDIIIRGGENISSREVEDILLQ-HPRIHDACV 464
Cdd:PLN03052 566 --SSTLLnaDHYKVYFKGmpvfngkilrrhgDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 465 VAMPDERLG-ERSCAYVVLK-PPHLSLTLEEVIAFFSRKRVAK----YKYpERIVIVEKLPRTASGKVQKFLLRQDIIER 538
Cdd:PLN03052 644 IGVPPPGGGpEQLVIAAVLKdPPGSNPDLNELKKIFNSAIQKKlnplFKV-SAVVIVPSFPRTASNKVMRRVLRQQLAQE 722
|
...
gi 604198150 539 LRQ 541
Cdd:PLN03052 723 LSR 725
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
196-459 |
1.21e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 60.55 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 196 TSGTEGMPKGVMLTHNNILAS----ERAYCArLNLTWQDVFLMPAPLGHATGFL---HGVTApflIGARSVLLDIFTPEA 268
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWaelfARSLRA-AGVRPGDRVQNAFGYGLFTGGLglhYGAER---LGATVIPAGGGNTER 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 269 CLTLLAQQRCTCMSGATPFIYDLLCAVEQQPADL--SSLRFFLCGGTIIPKKVARDCQQR-GIKLLSIYGSTESSPHsmv 345
Cdd:COG1541 167 QLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERwGIKAYDIYGLTEVGPG--- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 346 nlgdstsrmMNTDGYAATG---------VEikIVD-EDRNTLPAGHEGeeasrgpnvfmgyldepELTARALDNEGW--- 412
Cdd:COG1541 244 ---------VAYECEAQDGlhiwedhflVE--IIDpETGEPVPEGEEG-----------------ELVVTTLTKEAMpli 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 604198150 413 -YYSGDLCRMDED------GYI---KITGRKKD-IIIRGGeNISSREVEDILLQHPRI 459
Cdd:COG1541 296 rYRTGDLTRLLPEpcpcgrTHPrigRILGRADDmLIIRGV-NVFPSQIEEVLLRIPEV 352
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
23-443 |
2.05e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.13 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 23 DASLGDYWRQTARAVPDKIAvvdnhgaswtYAALDYAASRLA-----NWL------------LSQGIQPGDRVAFQLPGW 85
Cdd:PRK07769 20 NTNLVRHVERWAKVRGDKLA----------YRFLDFSTERDGvardlTWSqfgarnravgarLQQVTKPGDRVAILAPQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 86 CEFTLIYLACLKTGAVSVPL----LPAWREaELVWVLNKCQAKIFFAPT-----VFKQNRPvdliLPLQNQLRhlthIVG 156
Cdd:PRK07769 90 LDYLIAFFGALYAGRIAVPLfdpaEPGHVG-RLHAVLDDCTPSAILTTTdsaegVRKFFRA----RPAKERPR----VIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 157 VDKLaPATTALALSQIidrseplqsdiNIHGDELAAVLFTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPA 236
Cdd:PRK07769 161 VDAV-PDEVGATWVPP-----------EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 237 PLGHATGFLHgVTAPFLIGARsvlLDIFTPEA-------CLTLLAQQ---RCTCMSGATPFIYDLlCAVE------QQPA 300
Cdd:PRK07769 229 PFFHDMGLIT-VLLPALLGHY---ITFMSPAAfvrrpgrWIRELARKpggTGGTFSAAPNFAFEH-AAARglpkdgEPPL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 301 DLSSLRFFLCGGTIIP----KKVARDCQQRGIKLLSI---YG---------STESSPHSMVNLGDSTS----RMMNTDGY 360
Cdd:PRK07769 304 DLSNVKGLLNGSEPVSpasmRKFNEAFAPYGLPPTAIkpsYGmaeatlfvsTTPMDEEPTVIYVDRDElnagRFVEVPAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 361 AATGVE------------IKIVDEDRNT-LPAGHEGEEASRGPNVFMGYLDEPELTARALDN-----------EG----- 411
Cdd:PRK07769 384 APNAVAqvsagkvgvsewAVIVDPETASeLPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaEGapdda 463
|
490 500 510
....*....|....*....|....*....|...
gi 604198150 412 -WYYSGDLcRMDEDGYIKITGRKKDIIIRGGEN 443
Cdd:PRK07769 464 lWVRTGDY-GVYFDGELYITGRVKDLVIIDGRN 495
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
38-210 |
2.22e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 56.73 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 38 PDKIAVV----DNHGASWTYAALDYAASRLANWLLSQGIQPGDRVAFQLPGWCEfTLI-YLACLKTGAvsvpllpawrea 112
Cdd:PRK03584 98 DDRPAIIfrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPE-TVVaMLATASLGA------------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 113 elVW-----------VLNKCQA---KIFFA-PTVFKQNRPVDL---ILPLQNQLRHLTHIVGVDKLAPATTALALSQIID 174
Cdd:PRK03584 165 --IWsscspdfgvqgVLDRFGQiepKVLIAvDGYRYGGKAFDRrakVAELRAALPSLEHVVVVPYLGPAAAAAALPGALL 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 604198150 175 RSEPLQsdiNIHGDELAA----------VLFTSGTEGMPK-------GVMLTH 210
Cdd:PRK03584 243 WEDFLA---PAEAAELEFepvpfdhplwILYSSGTTGLPKcivhghgGILLEH 292
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
188-465 |
1.31e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 54.34 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 188 DELAAVLFTSGTEGMPKGVMLTHNNIL-----ASERAYCARLNLTWQDVFLmpaPLGHA-------TGFLHGVT------ 249
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLYntvvpLCKHSIFKKYNPKTHLSYL---PISHIyerviayLSFMLGGTiniwsk 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 250 -------------APFLIGARSVLLDIFT-----------PEACL--TLLAQQRCTCMSGATPFIyDLLCAVEQQPADL- 302
Cdd:PTZ00342 381 dinyfskdiynskGNILAGVPKVFNRIYTnimteinnlppLKRFLvkKILSLRKSNNNGGFSKFL-EGITHISSKIKDKv 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 303 -SSLRFFLCGGTIIPKKVARD-CQQRGIKLLSIYGSTESSPHSMVNLGDSTsRMMNTDGYAATGVEIKIVD----EDRNT 376
Cdd:PTZ00342 460 nPNLEVILNGGGKLSPKIAEElSVLLNVNYYQGYGLTETTGPIFVQHADDN-NTESIGGPISPNTKYKVRTwetyKATDT 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 377 LPaghEGEEASRGPNVFMGYLDEPELTARALDNEGWYYSGDLCRMDEDGYIKITGRKKDII-IRGGENISSREVEDILLQ 455
Cdd:PTZ00342 539 LP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIETDMLNNLYSQ 615
|
330
....*....|
gi 604198150 456 HPRIHDaCVV 465
Cdd:PTZ00342 616 ISFINF-CVV 624
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
43-306 |
4.52e-07 |
|
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: 52.74 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 43 VVDNHGA---SWTYAALDYAASRLANWLL-SQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPLLPAWREAELVWVL 118
Cdd:cd05905 4 LLDSKGKeatTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 119 NKCQAKIFFAPTVFKQNRPVDLILPLQN----QLRHLTHIVGVDKLAPATTALALSQIIDrsePLQSDinihgDELAAVL 194
Cdd:cd05905 84 GTCKVRVALTVEACLKGLPKKLLKSKTAaeiaKKKGWPKILDFVKIPKSKRSKLKKWGPH---PPTRD-----GDTAYIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 195 FTSGTEGMPKGVMLTHNNILASERAYCARLNLTWQDVFLMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPEACLTLLA 274
Cdd:cd05905 156 YSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 604198150 275 QQ------RCTCMSGATpfIY----DLLCAVEQQPA---DLSSLR 306
Cdd:cd05905 236 QTlsqykvRDAYVKLRT--LHwclkDLSSTLASLKNrdvNLSSLR 278
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
44-443 |
1.45e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.81 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 44 VDNHGASWTYAALDYAASRLA-----NWL------------LSQGIQPGDRVAFQLPGWCEFTLIYLACLKTGAVSVPL- 105
Cdd:PRK12476 44 IANVGDTVAYRYLDHSHSAAGcavelTWTqlgvrlravgarLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLf 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 106 ---LPAWREaELVWVLNKCQAKIFFAPTVFKQnrpvdlilPLQNQLRHLTHivgvdklAPATTALALSQIIDRSEPLQSD 182
Cdd:PRK12476 124 apeLPGHAE-RLDTALRDAEPTVVLTTTAAAE--------AVEGFLRNLPR-------LRRPRVIAIDAIPDSAGESFVP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 183 INIHGDELAAVLFTSGTEGMPKGVMLTHnnilaseRAYCARL--------NLTWQDVFLMPAPLGHATGFLHgVTAPFLI 254
Cdd:PRK12476 188 VELDTDDVSHLQYTSGSTRPPVGVEITH-------RAVGTNLvqmilsidLLDRNTHGVSWLPLYHDMGLSM-IGFPAVY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 255 GARSVLLDiftPEACL--------TLLAQQRCTCMSGATP-FIYDLLCA------------------VEQQPADLSSLRF 307
Cdd:PRK12476 260 GGHSTLMS---PTAFVrrpqrwikALSEGSRTGRVVTAAPnFAYEWAAQrglpaegddidlsnvvliIGSEPVSIDAVTT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 308 F-------------------LCGGTIIPKKVARDCQQRGIKL----LSIYGSTE---SSPHSMVNLgdstsrmmnTDGYA 361
Cdd:PRK12476 337 FnkafapyglprtafkpsygIAEATLFVATIAPDAEPSVVYLdreqLGAGRAVRvaaDAPNAVAHV---------SCGQV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 362 ATGVEIKIVDEDRNT-LPAGHEGEEASRGPNVFMGYLDEPELT------------------ARALDNEGWYYSGDLcRMD 422
Cdd:PRK12476 408 ARSQWAVIVDPDTGAeLPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGDL-GVY 486
|
490 500
....*....|....*....|.
gi 604198150 423 EDGYIKITGRKKDIIIRGGEN 443
Cdd:PRK12476 487 LDGELYITGRIADLIVIDGRN 507
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
430-532 |
2.02e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 43.60 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 604198150 430 TGRK-KDIIIRGGENISSRE------------VEDILLQHPRIHDACVVAMPDERLGERSCAYVVLKPPhlslTLEEVIa 496
Cdd:PRK09188 213 TGKKvYNFITRGLFSWSDGEgtgdridneapaIQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELP----ADEKSL- 287
|
90 100 110
....*....|....*....|....*....|....*....
gi 604198150 497 ffsRKRVAKY---KYPERIVIVEKLPRTASGKVQKFLLR 532
Cdd:PRK09188 288 ---RARLAGAkppKPPEHIQPVAALPRDADGTVRDDILR 323
|
|
| |
