|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-600 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 847.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 1 MREFSvppivTVGDAANLTDPVWENAEVAPDTVQFVRPGAGtdAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSR 80
Cdd:COG1022 1 MSEFS-----DVPPADTLPDLLRRRAARFPDRVALREKEDG--IWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 81 TRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLREVWQIDLGA------ 154
Cdd:COG1022 74 NRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGlrddpr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 155 ---VDDLVAAGASV-DRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFL 230
Cdd:COG1022 154 llsLDELLALGREVaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP--LGPGDRTLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 231 PLAHAFARLIQVGVVHARATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIA 308
Cdd:COG1022 232 PLAHVFERTVSYYALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGglKRKLFRWALAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 309 WSEAQELPGGPGLGLRAQHALFDKLVYRKLRAAMGGRCRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANL 388
Cdd:COG1022 312 YARARLAGKSPSLLLRLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 389 PTGTRIGTVGRPLPGVTIRIDDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVT 468
Cdd:COG1022 392 PGDNRIGTVGPPLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVT 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 469 AGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALVTIDEEALPKWLAGQGRPEtTSMAELREDAALRAEVQSAIDQA 548
Cdd:COG1022 472 SGGKNVAPQPIENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPY-TSYAELAQDPEVRALIQEEVDRA 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 549 NQAVSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYRG 600
Cdd:COG1022 551 NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
47-586 |
0e+00 |
|
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: 619.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 47 DVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVE 126
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 stahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIY 206
Cdd:cd05907 85 ---------------------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNIL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 207 SDIANAVPVLPnlFRQGASTLLFLPLAHAFA-RLIQVGVVHARATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYNG 285
Cdd:cd05907 114 SNALALAERLP--ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVPRVWEKVYAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 286 ARQKAEAEGKGKIFDRAekvaiawseaqelpggpglglraqhalfdklvyrklraaMGGRCRDAISGGAPLGARLGHFFR 365
Cdd:cd05907 192 IKVKAVPGLKRKLFDLA---------------------------------------VGGRLRFAASGGAPLPAELLHFFR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 366 GVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTG 445
Cdd:cd05907 233 ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 446 DLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALVTIDEEALPKWLAGQGRPET 525
Cdd:cd05907 313 DLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEEHGIAYT 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 526 TsMAELREDAALRAEVQSAIDQANQAVSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVV 586
Cdd:cd05907 393 D-VAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
55-599 |
3.10e-114 |
|
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: 351.52 E-value: 3.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 55 DEVVAVAQGLIAAGV--SPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEstahat 132
Cdd:cd05927 13 ERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 133 lvAGVrdrlpdlrEVWQIDlgavdDLVAAGASVDRAEVEtrrslSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIA-- 210
Cdd:cd05927 87 --AGV--------KVYSLE-----EFEKLGKKNKVPPPP-----PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAgv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 211 NAVPVLPNLFRQGASTLLFLPLAHAFARLIQVGVVHARATMA-HCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQK 289
Cdd:cd05927 147 FKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGfYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 290 AEAEG--KGKIFDRAEKVAIAWSEAqelpggpglGLRAQHALFDKLVYRKLRAAMGGRCRDAISGGAPLGARLGHFFRGV 367
Cdd:cd05927 227 VQAKGplKRKLFNFALNYKLAELRS---------GVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 368 -GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD-------------DGEVLIAGDIVFQGYWHNDAATA 433
Cdd:cd05927 298 lGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnydakdpnpRGEVCIRGPNVFSGYYKDPEKTA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 434 EAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDR-QPFIAALVTIDEEA 512
Cdd:cd05927 378 EALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSlKSFLVAIVVPDPDV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 513 LPKWLAGQGRpETTSMAELREDAALRAEVQSAIDQ-ANQA-VSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTY 590
Cdd:cd05927 458 LKEWAASKGG-GTGSFEELCKNPEVKKAILEDLVRlGKENgLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYY 536
|
....*....
gi 2504840381 591 ASEIAEIYR 599
Cdd:cd05927 537 KKQIDEMYK 545
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
48-590 |
1.14e-107 |
|
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: 335.16 E-value: 1.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVES 127
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 TAHATLVAGVRDRLPDLREVWQID-----------LGAVDDLVAAGASVDRAE---VETRRSLSKADDVATIIYTSGTTG 193
Cdd:cd17641 92 EEQVDKLLEIADRIPSVRYVIYCDprgmrkyddprLISFEDVVALGRALDRRDpglYEREVAAGKGEDVAVLCTTSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 194 RPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQVG-VVHARATMAHCADTKNLVAELQDFKPTFV 272
Cdd:cd17641 172 KPKLAMLSHGNFLGHCAAYLAADP--LGPGDEYVSVLPLPWIGEQMYSVGqALVCGFIVNFPEEPETMMEDLREIGPTFV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 273 LSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKLVYRKLRAAMG-GRCRDA 349
Cdd:cd17641 250 LLPPRVWEGIAADVRARMMDATpfKRFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLRDRLGfSRLRSA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 350 ISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDDGEVLIAGDIVFQGYWHND 429
Cdd:cd17641 330 ATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSPGVFVGYYKNP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 430 AATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALVTID 509
Cdd:cd17641 410 EATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFICID 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 510 EEALPKWLAGQGRPETTSmaelrEDAALRAEVQSAI----DQANQAVSKAEAIKVFRILPQDFTEATGELTPSLKVKRQV 585
Cdd:cd17641 490 YAIVGKWAEQRGIAFTTY-----TDLASRPEVYELIrkevEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRKVRRGV 564
|
....*
gi 2504840381 586 VHKTY 590
Cdd:cd17641 565 IAEKY 569
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
46-598 |
4.55e-107 |
|
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: 334.33 E-value: 4.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 ESTAHATLVAGVRDRLPDLREVWQI---------DLGAVDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRPK 196
Cdd:cd05933 87 ENQKQLQKILQIQDKLPHLKAIIQYkeplkekepNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 197 GCVLTHRNIYSDIANAVPVLP-NLFRQGASTLL-FLPLAHAFARLIQVgvvHARATMAHC-------ADTKNLVAELQDF 267
Cdd:cd05933 167 GVMLSHDNITWTAKAASQHMDlRPATVGQESVVsYLPLSHIAAQILDI---WLPIKVGGQvyfaqpdALKGTLVKTLREV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 268 KPTFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAI-AWSEAQELPGGPGLGLRaqhaLFDKLVYRKLRAAMG- 343
Cdd:cd05933 244 RPTAFMGVPRVWEKIQEKMKAVGAKSGtlKRKIASWAKGVGLeTNLKLMGGESPSPLFYR----LAKKLVFKKVRKALGl 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 344 GRCRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRI-----DDDGEVLIAG 418
Cdd:cd05933 320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIhnpdaDGIGEICFWG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 419 DIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAH-PLISQCVVVGD 497
Cdd:cd05933 400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 498 RQPFIAALVTIDEEALPK--------------WLAGQGRPETTSmAEL--REDAALRAEVQSAIDQAN-QAVSKAEAIKV 560
Cdd:cd05933 480 KRKFLSMLLTLKCEVNPEtgepldelteeaieFCRKLGSQATRV-SEIagGKDPKVYEAIEEGIKRVNkKAISNAQKIQK 558
|
570 580 590
....*....|....*....|....*....|....*...
gi 2504840381 561 FRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIY 598
Cdd:cd05933 559 WVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
48-586 |
4.29e-106 |
|
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: 327.78 E-value: 4.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVES 127
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 TAhatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskaDDVATIIYTSGTTGRPKGCVLTHRNIYS 207
Cdd:cd17640 86 DS--------------------------------------------------DDLATIIYTSGTTGNPKGVMLTHANLLH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 208 DIANAVPVLPNlfRQGASTLLFLPLAHAFARLIQVgVVHARATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGAR 287
Cdd:cd17640 116 QIRSLSDIVPP--QPGDRFLSILPIWHSYERSAEY-FIFACGCSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 288 QKAEAEGKGKIFdraekvaiawseaqelpggpglglraqhaLFDKLVyrklraaMGGRCRDAISGGAPLGARLGHFFRGV 367
Cdd:cd17640 193 KQVSKSSPIKQF-----------------------------LFLFFL-------SGGIFKFGISGGGALPPHVDTFFEAI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 368 GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAEAI 436
Cdd:cd17640 237 GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDpegnvvlppgeKGIVWVRGPQVMKGYYKNPEATSKVL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 437 TTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALVTIDEEALPKW 516
Cdd:cd17640 317 DSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFEELEKW 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504840381 517 LAGQG----RPETTSMAELREDAALRAEVQSAIDQANQAvSKAEAIKVFRILPQDFTEAtGELTPSLKVKRQVV 586
Cdd:cd17640 397 AKESGvklaNDRSQLLASKKVLKLYKNEIKDEISNRPGF-KSFEQIAPFALLEEPFIEN-GEMTQTMKIKRNVV 468
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
46-590 |
1.24e-104 |
|
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: 325.19 E-value: 1.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 ESTAH-ATLVAGVRDRLPdLREVWQIDLGAV----DDLVAagasvdRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVL 200
Cdd:cd05932 85 GKLDDwKAMAPGVPEGLI-SISLPPPSAANCqyqwDDLIA------QHPPLEERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 201 ThrniYSDIANAVPVLPNLFRQGASTLLF--LPLAHAFAR-LIQVGVVHARATMAHCADTKNLVAELQDFKPTFVLSVPR 277
Cdd:cd05932 158 T----FGSFAWAAQAGIEHIGTEENDRMLsyLPLAHVTERvFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 278 VFEKVYNGARQKAeaeGKGKIfDRAEKVAIawseaqelpggpglglraqhalFDKLVYRKLRAAMG-GRCRDAISGGAPL 356
Cdd:cd05932 234 LWTKFQQGVQDKI---PQQKL-NLLLKIPV----------------------VNSLVKRKVLKGLGlDQCRLAGCGSAPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 357 GARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDDGEVLIAGDIVFQGYWHNDAATAEAI 436
Cdd:cd05932 288 PPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 437 TTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALVTIDEEALPKW 516
Cdd:cd05932 368 TADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504840381 517 LAGqgrpettsmaelrEDAALRAEVQSAIDQANQAVSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTY 590
Cdd:cd05932 448 DAF-------------ARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
22-469 |
6.11e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 312.71 E-value: 6.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 22 VWENAEVAPDTVQFVrpgagTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVP 101
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 102 IYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLREVWQIDLGAVDDL-VAAGASVDRAEVETRRSLSKAD 180
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEePLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGAST--LLFLPLAHAFARLIQV-GVVHARATM-----A 252
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDrvLSTLPLFHDFGLSLGLlGPLLAGATVvlppgF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEGkgkifdraekvaiawseaqelpggpglGLRAqhalfdk 332
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS---------------------------SLRL------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 333 lvyrklraamggrcrdAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTGTR---IGTVGRPLPGVTIRI 408
Cdd:pfam00501 282 ----------------VLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKI 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 409 DDD-----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTA 469
Cdd:pfam00501 346 VDDetgepvppgepGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
43-586 |
3.94e-99 |
|
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: 311.07 E-value: 3.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 43 DAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETssaeqaawiLGDSGava 122
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYAT---------LGEDA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 vvvesTAHAtlvagvrdrlpdLREvwqidlgavddlvaagasvdrAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:cd17639 69 -----LIHS------------LNE---------------------TECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVLPNLFRQGASTLLFLPLAH---------AFARLIQVGVVHAR----ATMAHCAdtknlvAELQDFKP 269
Cdd:cd17639 111 GNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaaenvCLYRGGTIGYGSPRtltdKSKRGCK------GDLTEFKP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 270 TFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIAWSEaqELPGGPglglraqhaLFDKLVYRKLRAAMGGRCR 347
Cdd:cd17639 185 TLMVGVPAIWDTIRKGVLAKLNPMGglKRTLFWTAYQSKLKALK--EGPGTP---------LLDELVFKKVRAALGGRLR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 348 DAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD-------------DGEV 414
Cdd:cd17639 254 YMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDweeggystdkpppRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQ-CV 493
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNiCV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 494 VVGDRQPFIAALVTIDEEALPKWLAGQGRPETTsMAELREDAALRAEVQSAIDQANQA--VSKAEAIKVFRILPQDFTEA 571
Cdd:cd17639 414 YADPDKSYPVAIVVPNEKHLTKLAEKHGVINSE-WEELCEDKKLQKAVLKSLAETARAagLEKFEIPQGVVLLDEEWTPE 492
|
570
....*....|....*
gi 2504840381 572 TGELTPSLKVKRQVV 586
Cdd:cd17639 493 NGLVTAAQKLKRKEI 507
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
41-600 |
1.23e-90 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 293.16 E-value: 1.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 41 GTDAREDVTCRQFR--------DEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAA 112
Cdd:PLN02736 64 GTRIRVDGTVGEYKwmtygeagTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 113 WILgDSGAVAVVVESTAHATLVAGVRDRLPDLREVwqIDLGAVDDLV---AAGASV-----DRAEVETRRSL-----SKA 179
Cdd:PLN02736 144 FIV-NHAEVAAIFCVPQTLNTLLSCLSEIPSVRLI--VVVGGADEPLpslPSGTGVeivtySKLLAQGRSSPqpfrpPKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQVGVVHARATMA-HCADTK 258
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGfYQGDNL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 259 NLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKvaiawSEAQELPGGpglglRAQHALFDKLVYR 336
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGglKERLFNAAYN-----AKKQALENG-----KNPSPMWDRLVFN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 337 KLRAAMGGRCRDAISGGAPLGARLGHFFR-GVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD----- 410
Cdd:PLN02736 369 KIKAKLGGRVRFMSSGASPLSPDVMEFLRiCFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemn 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 ---------DGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLED 481
Cdd:PLN02736 449 ytsedqpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 482 QVRAHPLISQCVVVGDR-QPFIAALVTIDEEALPKWLAGQGRPeTTSMAELREDAALRAEVQSAID-QANQAVSKA-EAI 558
Cdd:PLN02736 529 VYAKCKFVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIK-YEDLKQLCNDPRVRAAVLADMDaVGREAQLRGfEFA 607
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2504840381 559 KVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYRG 600
Cdd:PLN02736 608 KAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-583 |
6.61e-90 |
|
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: 285.49 E-value: 6.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 estahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslSKADDVATIIYTSGTTGRPKGCVLTHRNI 205
Cdd:cd05914 86 ---------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 206 YSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQ-VGVVHARATMAHCADTKNLVAELQDF---KPTFVLSVPRVFEK 281
Cdd:cd05914 115 VSNVDGVKEVVL--LGKGDKILSILPLHHIYPLTFTlLLPLLNGAHVVFLDKIPSAKIIALAFaqvTPTLGVPVPLVIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 282 VYngarqkaeaegkgkIFDRAEKVAIAWseaqelpggpgLGLRAQHALFD----KLVYRKLRAAMGGRCRDAISGGAPLG 357
Cdd:cd05914 193 IF--------------KMDIIPKLTLKK-----------FKFKLAKKINNrkirKLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 358 ARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD------DGEVLIAGDIVFQGYWHNDAA 431
Cdd:cd05914 248 PDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSpdpatgEGEIIVRGPNVMKGYYKNPEA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 432 TAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHP--LISQCVVVGDRqpfIAALVTID 509
Cdd:cd05914 328 TAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPfvLESLVVVQEKK---LVALAYID 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504840381 510 eealpkwlagqgrPETTSMAELREDAALRAEVQSAIDQANQAVSKAEAIKVFRILPQDFteatgELTPSLKVKR 583
Cdd:cd05914 405 -------------PDFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKEEF-----EKTPKGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
18-520 |
9.77e-88 |
|
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: 279.39 E-value: 9.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 18 LTDPVWENAEVAPDTVQFVRPGagtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGA 97
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 98 VTVPIYETSSAEQAAWILGDSGAVAVVVestahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrsls 177
Cdd:COG0318 75 VVVPLNPRLTAEELAYILEDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 kaddvATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQV-GVVHARATMAHCA- 255
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLVLLPr 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 256 -DTKNLVAELQDFKPTFVLSVPRVFEKVyngarqkaeaegkgkifdraekvaiawseaqelpggpglglrAQHALFDKLV 334
Cdd:COG0318 176 fDPERVLELIERERVTVLFGVPTMLARL------------------------------------------LRHPEFARYD 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 335 YRKLRAAmggrcrdaISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANL--PTGTRIGTVGRPLPGVTIRIDDD 411
Cdd:COG0318 214 LSSLRLV--------VSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ----------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLED 481
Cdd:COG0318 286 dgrelppgevGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEE 363
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2504840381 482 QVRAHPLISQCVVVGDRQPF----IAALV------TIDEEALPKWLAGQ 520
Cdd:COG0318 364 VLAAHPGVAEAAVVGVPDEKwgerVVAFVvlrpgaELDAEELRAFLRER 412
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
17-519 |
1.08e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 263.20 E-value: 1.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 17 NLTDPVWENAEVAPDTVQFVRPGAGTdaredvTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSR--TRYEWTLFdyAIWA 94
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRT------TYAELDERVNRLANALRALGVKKGDRVAVFDWnsHEYLEAYF--AVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 95 AGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTaHATLVAGVRDRLPDLREVWQIDLGAVDDLVA---------AGASV 165
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVIVEGDGPAAPLAPevgeyeellAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 166 DRAEVETrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVpvLPNLFRQGASTLLFLPLAHAFARLIQVGVV 245
Cdd:PRK06187 158 TFDFPDI-----DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVC--AWLKLSRDDVYLVIVPMFHVHAWGLPYLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 246 HARAT--MAHCADTKNLVAELQDFKPTFVLSVPRVFEKVyngarqkaeaegkgkifdraekvaiawseaqelpggpglgL 323
Cdd:PRK06187 231 MAGAKqvIPRRFDPENLLDLIETERVTFFFAVPTIWQML----------------------------------------L 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 324 RAQHALFDKLvyrklraamgGRCRDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPT------GTRIGT 396
Cdd:PRK06187 271 KAPRAYFVDF----------SSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSPVVSVLPPEdqlpgqWTKRRS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 397 VGRPLPGVTIRI-DDD-----------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKE 464
Cdd:PRK06187 341 AGRPLPGVEARIvDDDgdelppdggevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 465 IIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG------DRQPFiAALV-----TIDEEALPKWLAG 519
Cdd:PRK06187 420 VIIS-GGENIYPRELEDALYGHPAVAEVAVIGvpdekwGERPV-AVVVlkpgaTLDAKELRAFLRG 483
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
49-520 |
5.20e-79 |
|
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: 257.11 E-value: 5.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEST 128
Cdd:cd05936 26 TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 ahatlvagvrdrlpdlrevwqidlgaVDDLVAAGASVDRAEVETrrslskADDVATIIYTSGTTGRPKGCVLTHRNIYSD 208
Cdd:cd05936 106 --------------------------FTDLLAAGAPLGERVALT------PEDVAVLQYTSGTTGVPKGAMLTHRNLVAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 209 IANAVPVLPNLFRQGASTLLFLPLAHAFArLIQVGVVHARA----TMAHCADTKNLVAELQDFKPTFVLSVPRVFekvyn 284
Cdd:cd05936 154 ALQIKAWLEDLLEGDDVVLAALPLFHVFG-LTVALLLPLALgatiVLIPRFRPIGVLKEIRKHRVTIFPGVPTMY----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 285 garqkaeaegkgkifdraekVAIAwseaqelpggpglglraQHALFDKLVYRKLRAAmggrcrdaISGGAPLGARLGHFF 364
Cdd:cd05936 228 --------------------IALL-----------------NAPEFKKRDFSSLRLC--------ISGGAPLPVEVAERF 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 365 RGV-GVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAAT 432
Cdd:cd05936 263 EELtGVPIVEGYGLTETSPVVAVNPLDGpRKPGSIGIPLPGTEVKIVDDdgeelppgevGELWVRGPQVMKGYWNRPEET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 433 AEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVtAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPF----IAALV-- 506
Cdd:cd05936 343 AEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsgeaVKAFVvl 420
|
490
....*....|....*...
gi 2504840381 507 ----TIDEEALPKWLAGQ 520
Cdd:cd05936 421 kegaSLTEEEIIAFCREQ 438
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
43-599 |
1.58e-74 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 251.43 E-value: 1.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 43 DAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVA 122
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 VVVESTAHATLVAGVR------------DRLPDLREVWQIDLGAVDDLVAAGASvdRAEVETRRSLSKADDVATIIYTSG 190
Cdd:PTZ00216 197 IVCNGKNVPNLLRLMKsggmpnttiiylDSLPASVDTEGCRLVAWTDVVAKGHS--AGSHHPLNIPENNDDLALIMYTSG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 191 TTGRPKGCVLTHRNIYSDIANAVPVLPNLF---RQGASTLLFLPLAHAFaRLIQVGVVHARATMAHCADTKNLV------ 261
Cdd:PTZ00216 275 TTGDPKGVMHTHGSLTAGILALEDRLNDLIgppEEDETYCSYLPLAHIM-EFGVTNIFLARGALIGFGSPRTLTdtfarp 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 262 -AELQDFKPTFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAI-AWSEAQELPggpglglraqhaLFDKLVYRK 337
Cdd:PTZ00216 354 hGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGslKRRVFDHAYQSRLrALKEGKDTP------------YWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 LRAAMGGRCRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD------- 410
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDteeykht 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 D-----GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRA 485
Cdd:PTZ00216 502 DtpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQ 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 486 HPLISQ---CVVVGDRQPFIAALVTIDeEALPKWLAGQGRPETTSMAELREDAALRAEVQSAIDQANQAVSKA-EAIKVF 561
Cdd:PTZ00216 582 NELVVPngvCVLVHPARSYICALVLTD-EAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSfEIVRHV 660
|
570 580 590
....*....|....*....|....*....|....*...
gi 2504840381 562 RILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYR 599
Cdd:PTZ00216 661 RVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
48-496 |
3.67e-74 |
|
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: 245.20 E-value: 3.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVES 127
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 TAHATLVAGVRdRLPDLREVWQID-----LGAVDDLVAAGASVDRAEVETRRSLSKaDDVATIIYTSGTTGRPKGCVLTH 202
Cdd:cd05911 91 DGLEKVKEAAK-ELGPKDKIIVLDdkpdgVLSIEDLLSPTLGEEDEDLPPPLKDGK-DDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVLPNLFRQGASTLLFLPLAHAFARLIQVGVVHARAT--MAHCADTKNLVAELQDFKPTFVLSVPRVFe 280
Cdd:cd05911 169 RNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATviIMPKFDSELFLDLIEKYKITFLYLVPPIA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 281 kvyngarqkaeaegkgkifdraekVAIAwseaqelpggpglglraQHALFDKLVYRKLRAAMggrcrdaiSGGAPLGARL 360
Cdd:cd05911 248 ------------------------AALA-----------------KSPLLDKYDLSSLRVIL--------SGGAPLSKEL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 361 GHFF--RGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRI-DDD----------GEVLIAGDIVFQGYWH 427
Cdd:cd05911 279 QELLakRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIvDDDgkdslgpnepGEICVRGPQVMKGYYN 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 428 NDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05911 359 NPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELI-KYKGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
14-496 |
3.38e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 240.58 E-value: 3.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 14 DAANLTDPVWENAEVAPDTVQFVrpgagtDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIW 93
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKEAYV------FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 94 AAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVrDRLPDLREV----------WQIDLGAVDDLVAAGA 163
Cdd:PRK07656 77 KAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAT-TRLPALEHVviceteeddpHTEKMKTFTDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 164 SVDRA-EVetrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIYSDiANAVPVLPNLfRQGASTLLFLPLAHAFArlIQV 242
Cdd:PRK07656 156 PAERApEV-------DPDDVADILFTSGTTGRPKGAMLTHRQLLSN-AADWAEYLGL-TEGDRYLAANPFFHVFG--YKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 243 GVVHAR---ATMAhcadtknlvaelqdfkPTFVLSVPRVFEKVyngarqkaeaegkgkifdRAEKVAIawseaqeLPGGP 319
Cdd:PRK07656 225 GVNAPLmrgATIL----------------PLPVFDPDEVFRLI------------------ETERITV-------LPGPP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 320 GLglraQHALFDklvYRKLRAAMGGRCRDAISGGAPLGARLGHFFR---GVGvTICEGYGLTETSPAAAANLPTGTRI-- 394
Cdd:PRK07656 264 TM----YNSLLQ---HPDRSAEDLSSLRLAVTGAASMPVALLERFEselGVD-IVLTGYGLSEASGVTTFNRLDDDRKtv 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 395 -GTVGRPLPGVTIRI----------DDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKK 463
Cdd:PRK07656 336 aGTIGTAIAGVENKIvnelgeevpvGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKK 415
|
490 500 510
....*....|....*....|....*....|....
gi 2504840381 464 E-IIVtaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK07656 416 DmFIV--GGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
55-598 |
6.45e-70 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 239.25 E-value: 6.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 55 DEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLV 134
Cdd:PLN02387 114 ERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 135 AgVRDRLPDLREVWQIDLGAVDDLVAAGASVDR-----AEVE-------TRRSLSKADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PLN02387 194 D-ISSQLETVKRVIYMDDEGVDSDSSLSGSSNWtvssfSEVEklgkenpVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVLPNLfRQGASTLLFLPLAHAF-----ARLIQVGVVHARATMAHCADTKNLV-----AELQDFKPTFV 272
Cdd:PLN02387 273 GNIVATVAGVMTVVPKL-GKNDVYLAYLPLAHILelaaeSVMAAVGAAIGYGSPLTLTDTSNKIkkgtkGDASALKPTLM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 273 LSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIAWSEAQELpGGPGLglraQHALFDKLVYRKLRAAMGGRCRDAI 350
Cdd:PLN02387 352 TAVPAILDRVRDGVRKKVDAKGglAKKLFDIAYKRRLAAIEGSWF-GAWGL----EKLLWDALVFKKIRAVLGGRIRFML 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 351 SGGAPLGARLGHFFR-GVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTI----------RIDDD----GEVL 415
Cdd:PLN02387 427 SGGAPLSGDTQRFINiCLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVklvsweeggyLISDKpmprGEIV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 416 IAGDIVFQGYWHNDAATAEAITTDG----WFRTGDLGQLDENGYLSITGRKKEII-VTAG-----GK-----NVAPAVLE 480
Cdd:PLN02387 507 IGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGeyvslGKveaalSVSPYVDN 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 481 DQVRAHPLISQCVvvgdrqpfiaALVTIDEEALPKWLAGQGRpETTSMAELREDAALRAEVQSAIDQANQA--VSKAEAI 558
Cdd:PLN02387 587 IMVHADPFHSYCV----------ALVVPSQQALEKWAKKAGI-DYSNFAELCEKEEAVKEVQQSLSKAAKAarLEKFEIP 655
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2504840381 559 KVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIY 598
Cdd:PLN02387 656 AKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
49-599 |
4.08e-69 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 236.25 E-value: 4.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETssaeqaawiLGdSGAVAVVVEst 128
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDT---------LG-PGAVDYIVD-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 aHATL-VAGVRDRlpDLREVWQIDLGAVDDLVAAGASVDRAEVETRRSLS-------------------------KADDV 182
Cdd:PLN02430 146 -HAEIdFVFVQDK--KIKELLEPDCKSAKRLKAIVSFTSVTEEESDKASQigvktyswidflhmgkenpsetnppKPLDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 183 ATIIYTSGTTGRPKGCVLTHRNIYSdIANAVPVLPNLFRQGAST----LLFLPLAHAFARLIQVGVVHARATMAHC-ADT 257
Cdd:PLN02430 223 CTIMYTSGTSGDPKGVVLTHEAVAT-FVRGVDLFMEQFEDKMTHddvyLSFLPLAHILDRMIEEYFFRKGASVGYYhGDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 KNLVAELQDFKPTFVLSVPRVFEKVYNGArQKAEAE---GKGKIFDRAEKVAIAWSEAqelpggpGLGLRAQHALFDKLV 334
Cdd:PLN02430 302 NALRDDLMELKPTLLAGVPRVFERIHEGI-QKALQElnpRRRLIFNALYKYKLAWMNR-------GYSHKKASPMADFLA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 335 YRKLRAAMGGRCRDAISGGAPLGARLGHFFRgvgVTIC----EGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVTIRID 409
Cdd:PLN02430 374 FRKVKAKLGGRLRLLISGGAPLSTEIEEFLR---VTSCafvvQGYGLTETLGPTTLGFPDEmCMLGTVGAPAVYNELRLE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 410 D-------------DGEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAP 476
Cdd:PLN02430 451 EvpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVAL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 477 AVLEDQVRAHPLISQCVVVGDR-QPFIAALVTIDEEALPKW--LAGQGRP--ETTSMAELREdaALRAEVQSAIDQANqa 551
Cdd:PLN02430 530 EYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKWakDNGFTGSfeELCSLPELKE--HILSELKSTAEKNK-- 605
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2504840381 552 VSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYR 599
Cdd:PLN02430 606 LRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
25-496 |
2.90e-67 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 225.18 E-value: 2.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 25 NAEVAPDTVQFVRPGagtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYE-WTLFdYAIWAAGAVTVPIY 103
Cdd:cd17631 4 RARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEfLELL-FAAARLGAVFVPLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAWILGDSGAVAVVvestahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskaDDVA 183
Cdd:cd17631 77 FRLTPPEVAYILADSGAKVLF-------------------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAH-AFARLIQVGVVHARAT--MAHCADTKNL 260
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALD--LGPDDVLLVVAPLFHiGGLGVFTLPTLLRGGTvvILRKFDPETV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 261 VAELQDFKPTFVLSVPRVFEKVyngarqkaeaegkgkifdraekvaiawseaqelpggpglglrAQHALFDKLVYRKLRA 340
Cdd:cd17631 180 LDLIERHRVTSFFLVPTMIQAL------------------------------------------LQHPRFATTDLSSLRA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 341 AmggrcrdaISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTG--TRIGTVGRPLPGVTIRI-DDD------ 411
Cdd:cd17631 218 V--------IYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIvDPDgrevpp 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ---GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPL 488
Cdd:cd17631 290 gevGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVLYEHPA 367
|
....*...
gi 2504840381 489 ISQCVVVG 496
Cdd:cd17631 368 VAEVAVIG 375
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
49-599 |
1.24e-63 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 221.43 E-value: 1.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVE-- 126
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 -----------STAHATLV---AGVRDRLPDLREVWQIDLGAVDDLVAAGASVdraevETRRSLSKADDVATIIYTSGTT 192
Cdd:PLN02614 161 kiselfktcpnSTEYMKTVvsfGGVSREQKEEAETFGLVIYAWDEFLKLGEGK-----QYDLPIKKKSDICTIMYTSGTT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 193 GRPKGCVLTHRNIYSDIANAVPVLPNL---FRQGASTLLFLPLAHAFARLIQVGVVHARATMAHC-ADTKNLVAELQDFK 268
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLKSAnaaLTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWrGDVKLLIEDLGELK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 269 PTFVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIAWSEAqelpggpGLGLRAQHALFDKLVYRKLRAAMGGRC 346
Cdd:PLN02614 316 PTIFCAVPRVLDRVYSGLQKKLSDGGflKKFVFDSAFSYKFGNMKK-------GQSHVEASPLCDKLVFNKVKQGLGGNV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAPLGARLGHFFRGVG-VTICEGYGLTETSPAAAANLPTGT-RIGTVGRPLPGVTIRIDD-------------D 411
Cdd:PLN02614 389 RIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRLESvpemeydalastpR 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 GEVLIAGDIVFQGYWHNDAATAEaITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQ 491
Cdd:PLN02614 469 GEICIRGKTLFSGYYKREDLTKE-VLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDS 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 492 CVVVGDR-QPFIAALVTIDEEALPKWLAGQGrpETTSMAELREDAALRAEVQSA-IDQANQAVSKA-EAIKVFRILPQDF 568
Cdd:PLN02614 548 VWVYGNSfESFLVAIANPNQQILERWAAENG--VSGDYNALCQNEKAKEFILGElVKMAKEKKMKGfEIIKAIHLDPVPF 625
|
570 580 590
....*....|....*....|....*....|.
gi 2504840381 569 TEATGELTPSLKVKRQVVHKTYASEIAEIYR 599
Cdd:PLN02614 626 DMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
48-599 |
2.34e-63 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 220.48 E-value: 2.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG-AVAVVVE 126
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEvSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 STAHATLvAGVRDRLPDLREVwqIDLGAVDDLVAAGAS---VDRAEVETRRSLSKAD---------DVATIIYTSGTTGR 194
Cdd:PLN02861 158 SKISSIL-SCLPKCSSNLKTI--VSFGDVSSEQKEEAEelgVSCFSWEEFSLMGSLDcelppkqktDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 195 PKGCVLTHRNIYSDIANAVPVLPNLFRQGA---STLLFLPLAHAFARLIQVGVVHARATMAHC-ADTKNLVAELQDFKPT 270
Cdd:PLN02861 235 PKGVILTNRAIIAEVLSTDHLLKVTDRVATeedSYFSYLPLAHVYDQVIETYCISKGASIGFWqGDIRYLMEDVQALKPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 271 FVLSVPRVFEKVYNGARQKAEAEG--KGKIFDRAEKVAIAWSEAqelpggpglGLRAQHA--LFDKLVYRKLRAAMGGRC 346
Cdd:PLN02861 315 IFCGVPRVYDRIYTGIMQKISSGGmlRKKLFDFAYNYKLGNLRK---------GLKQEEAspRLDRLVFDKIKEGLGGRV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAPLGARLGHFFRgvgVTIC----EGYGLTETSPAAAANLP-TGTRIGTVGRPLPGVTIRIDD----------- 410
Cdd:PLN02861 386 RLLLSGAAPLPRHVEEFLR---VTSCsvlsQGYGLTESCGGCFTSIAnVFSMVGTVGVPMTTIEARLESvpemgydalsd 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 --DGEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPL 488
Cdd:PLN02861 463 vpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 489 ISQCVVVGDR-QPFIAALVTIDEEALPKWLAGQGrpETTSMAELREDAALRAEVQsaiDQANQAVSKA-----EAIKVFR 562
Cdd:PLN02861 542 IASIWVYGNSfESFLVAVVVPDRQALEDWAANNN--KTGDFKSLCKNLKARKYIL---DELNSTGKKLqlrgfEMLKAIH 616
|
570 580 590
....*....|....*....|....*....|....*..
gi 2504840381 563 ILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYR 599
Cdd:PLN02861 617 LEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
6-516 |
3.98e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 212.55 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 6 VPPIVTVGDAAnLTDPVWENAEVAPDTVQFVRPGAGTdaredvTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEW 85
Cdd:PRK05605 23 TPHDLDYGDTT-LVDLYDNAVARFGDRPALDFFGATT------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 86 TLFDYAIWAAGAVTV---PIYetsSAEQAAWILGDSGAVAVVVESTAhATLVAGVRDRLPdLREVWQIDL---------- 152
Cdd:PRK05605 96 IVAFYAVLRLGAVVVehnPLY---TAHELEHPFEDHGARVAIVWDKV-APTVERLRRTTP-LETIVSVNMiaampllqrl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 153 -----------------GAVDDLV--------AAGASVDRAEVETRRslskADDVATIIYTSGTTGRPKGCVLTHRNIYS 207
Cdd:PRK05605 171 alrlpipalrkaraaltGPAPGTVpwetlvdaAIGGDGSDVSHPRPT----PDDVALILYTSGTTGKPKGAQLTHRNLFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 208 DIANAVPVLPNLFRQGASTLLFLPLAHAFA-RLIQVGVVHARATMA--HCADTKNLVAELQDFKPTFVLSVPRVFEKVYN 284
Cdd:PRK05605 247 NAAQGKAWVPGLGDGPERVLAALPMFHAYGlTLCLTLAVSIGGELVllPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 285 GARQKaeaegkgkifdraekvaiawseaqelpggpGLGLRAqhalfdklvyrklraamggrCRDAISGGAPLGARLGHFF 364
Cdd:PRK05605 327 AAEER------------------------------GVDLSG--------------------VRNAFSGAMALPVSTVELW 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 365 RGV-GVTICEGYGLTETSPAAAANlPTGT--RIGTVGRPLPGVTIRIDD------------DGEVLIAGDIVFQGYWHND 429
Cdd:PRK05605 357 EKLtGGLLVEGYGLTETSPIIVGN-PMSDdrRPGYVGVPFPDTEVRIVDpedpdetmpdgeEGELLVRGPQVFKGYWNRP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 430 AATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQP-----FIAA 504
Cdd:PRK05605 436 EETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLREHPGVEDAAVVGLPREdgseeVVAA 513
|
570
....*....|....*..
gi 2504840381 505 LV-----TIDEEALPKW 516
Cdd:PRK05605 514 VVlepgaALDPEGLRAY 530
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
181-518 |
1.04e-59 |
|
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: 202.13 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQVGVVHARATMAHCA--DTK 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPkfDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 259 NLVAELQDFKPTFVLSVPRVFEKVyngarqkaeaegkgkifdraekvaiawseaqelpggpglglrAQHALFDKLVYRKL 338
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARL------------------------------------------LKAPESAGYDLSSL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 339 RAAmggrcrdaISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTG--TRIGTVGRPLPGVTIRI-DDD--- 411
Cdd:cd04433 117 RAL--------VSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIvDPDgge 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ------GEVLIAGDIVFQGYWHNDAATAEAiTTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRA 485
Cdd:cd04433 189 lppgeiGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLLG 266
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2504840381 486 HPLISQCVVVG----DRQPFIAALV------TIDEEALPKWLA 518
Cdd:cd04433 267 HPGVAEAAVVGvpdpEWGERVVAVVvlrpgaDLDAEELRAHVR 309
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
17-496 |
3.78e-59 |
|
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: 205.55 E-value: 3.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 17 NLTDPVWENAEVAPDTVQFVrpGAGTDARedVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAG 96
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALI--DAATGRA--LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 97 AVTVPIYETSSAEQAAWILGDSGAV-AVVVESTAHatlvagvrdRLPDLrevwQIDLGAVDDLVAAGASVDRA-----EV 170
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAKlAFTTAELAE---------KLASL----ALPVVLLDSAEFDSLSFSDLlfeadEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 171 ETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGASTLLFLPLAHAFA-RLIQVGVVHARA 249
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 T---MAHcADTKNLVAELQDFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekVAIAwseaqelpggpglglraQ 326
Cdd:cd05904 229 TvvvMPR-FDLEELLAAIERYKVTHLPVVPPIV-------------------------LALV-----------------K 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 327 HALFDKLVYRKLRAAMggrcrdaiSGGAPLGARLGHFFRGV--GVTICEGYGLTETSPAAAANLPTG---TRIGTVGRPL 401
Cdd:cd05904 266 SPIVDKYDLSSLRQIM--------SGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFAPEkdrAKYGSVGRLV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 402 PGVTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAG 470
Cdd:cd05904 338 PNVEAKIVDpetgeslppnqTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI-KYK 416
|
490 500
....*....|....*....|....*.
gi 2504840381 471 GKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05904 417 GFQVAPAELEALLLSHPEILDAAVIP 442
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
49-496 |
1.25e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 205.43 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTV---PIYETSSAEQAawiLGDSGAVAVVV 125
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRLSELEYA---LNQSGCKALIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 ----ESTAHATLVAGVR-------------DRLPDLREVWQIDLGA------VDDLVAAGASVDRAEVETRRSLSKADDV 182
Cdd:PRK08315 122 adgfKDSDYVAMLYELApelatcepgqlqsARLPELRRVIFLGDEKhpgmlnFDELLALGRAVDDAELAARQATLDPDDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 183 ATIIYTSGTTGRPKGCVLTHRNIYSD---IANA----------VPVlpnlfrqgastllflPLAHAFARLIQV-GVVHAR 248
Cdd:PRK08315 202 INIQYTSGTTGFPKGATLTHRNILNNgyfIGEAmklteedrlcIPV---------------PLYHCFGMVLGNlACVTHG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 249 ATMahcadtknlVAELQDFKPTFVLS------------VPRVFekvyngarqkaeaegkgkifdraekvaIAwseaqELp 316
Cdd:PRK08315 267 ATM---------VYPGEGFDPLATLAaveeerctalygVPTMF---------------------------IA-----EL- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 317 ggpglglraQHALFDKLVYRKLRAAmggrcrdaISGGAPLGARLghfFRGV-------GVTICegYGLTETSP---AAAA 386
Cdd:PRK08315 305 ---------DHPDFARFDLSSLRTG--------IMAGSPCPIEV---MKRVidkmhmsEVTIA--YGMTETSPvstQTRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 387 NLPTGTRIGTVGRPLPGVTIRIDDD-----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGY 455
Cdd:PRK08315 363 DDPLEKRVTTVGRALPHLEVKIVDPetgetvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGY 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2504840381 456 LSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK08315 443 VNIVGRIKDMIIR-GGENIYPREIEEFLYTHPKIQDVQVVG 482
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
42-518 |
1.16e-56 |
|
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: 198.69 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 42 TDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAV 121
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 122 AVVVESTAHAT-LVAGVRDRLPDLREVWQI-DLGAVDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCV 199
Cdd:cd05926 89 LVLTPKGELGPaSRAASKLGLAILELALDVgVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHRNIYSDIANAVpvlpNLFRQGAS--TLLFLPLAHAFArliQVGVVHA------RATMAHCADTKNLVAELQDFKPTF 271
Cdd:cd05926 169 LTHRNLAASATNIT----NTYKLTPDdrTLVVMPLFHVHG---LVASLLStlaaggSVVLPPRFSASTFWPDVRDYNATW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 272 VLSVPRVfekvyngarqkaeaegkgkifdraekVAIAWSEAQELPGGPGLGLRaqhalFdklvyrklraamggrCRdaiS 351
Cdd:cd05926 242 YTAVPTI--------------------------HQILLNRPEPNPESPPPKLR-----F---------------IR---S 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 352 GGAPLG-ARLGHFFRGVGVTICEGYGLTETSPAAAAN-LPTGTR-IGTVGRPLpGVTIRIDDD----------GEVLIAG 418
Cdd:cd05926 273 CSASLPpAVLEALEATFGAPVLEAYGMTEAAHQMTSNpLPPGPRkPGSVGKPV-GVEVRILDEdgeilppgvvGEICLRG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 419 DIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVGDR 498
Cdd:cd05926 352 PNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI-NRGGEKISPLEVDGVLLSHPAVLEAVAFGVP 430
|
490 500 510
....*....|....*....|....*....|
gi 2504840381 499 QPF----IAALV------TIDEEALPKWLA 518
Cdd:cd05926 431 DEKygeeVAAAVvlregaSVTEEELRAFCR 460
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
49-523 |
5.25e-54 |
|
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: 190.19 E-value: 5.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVS-PGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVves 127
Cdd:cd05941 13 TYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 tahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskadDVATIIYTSGTTGRPKGCVLTHRNIYS 207
Cdd:cd05941 90 -----------------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 208 DIAnavpVLPNL--FRQGASTLLFLPLAHAFarliqvGVVHA-------RATMAH----CADTKNLVAELQDFkpTFVLS 274
Cdd:cd05941 117 NVR----ALVDAwrWTEDDVLLHVLPLHHVH------GLVNAllcplfaGASVEFlpkfDPKEVAISRLMPSI--TVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 275 VPRVFEKVyngarqkaeaegkgkifdraekvaiawSEAQELPGGPGLGLRAQHAlfdklvyRKLRAAMggrcrdaiSGGA 354
Cdd:cd05941 185 VPTIYTRL---------------------------LQYYEAHFTDPQFARAAAA-------ERLRLMV--------SGSA 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 355 PLGARLGHFFRGV-GVTICEGYGLTETSpAAAANLPTGTRI-GTVGRPLPGVTIRIDDD-----------GEVLIAGDIV 421
Cdd:cd05941 223 ALPVPTLEEWEAItGHTLLERYGMTEIG-MALSNPLDGERRpGTVGMPLPGVQARIVDEetgeplprgevGEIQVRGPSV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 422 FQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQP- 500
Cdd:cd05941 302 FKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPd 381
|
490 500 510
....*....|....*....|....*....|...
gi 2504840381 501 ---FIAALV-------TIDEEALPKWLAGQGRP 523
Cdd:cd05941 382 wgeRVVAVVvlragaaALSLEELKEWAKQRLAP 414
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
49-496 |
2.34e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 191.14 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV--- 125
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICada 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 --ESTAHATLV------------AGVRDRLPDLREVWQID------LGAVDDLVAAGASVDRAEVETRRSLSKADDVATI 185
Cdd:PRK12583 127 fkTSDYHAMLQellpglaegqpgALACERLPELRGVVSLApapppgFLAWHELQARGETVSREALAERQASLDRDDPINI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 186 IYTSGTTGRPKGCVLTHRNIysdIANAVPVLPNLFRQGASTLLF-LPLAHAFarliqvGVVHAR-ATMAHCAdtkNLVAE 263
Cdd:PRK12583 207 QYTSGTTGFPKGATLSHHNI---LNNGYFVAESLGLTEHDRLCVpVPLYHCF------GMVLANlGCMTVGA---CLVYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 264 LQDFKPTFVLsvprvfekvyngarQKAEAEgkgkifdraekvaiawsEAQELPGGPGLGL-RAQHALFDKLVYRKLRAAm 342
Cdd:PRK12583 275 NEAFDPLATL--------------QAVEEE-----------------RCTALYGVPTMFIaELDHPQRGNFDLSSLRTG- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 343 ggrcrdaISGGAP----LGARLGHFFRGVGVTIceGYGLTETSPAA---AANLPTGTRIGTVGRPLPGVTIR-IDDDGEV 414
Cdd:PRK12583 323 -------IMAGAPcpieVMRRVMDEMHMAEVQI--AYGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKvVDPDGAT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDI---------VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRA 485
Cdd:PRK12583 394 VPRGEIgelctrgysVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIEEFLFT 472
|
490
....*....|.
gi 2504840381 486 HPLISQCVVVG 496
Cdd:PRK12583 473 HPAVADVQVFG 483
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
42-586 |
6.70e-50 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 181.85 E-value: 6.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 42 TDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAV 121
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 122 AVVVES--------TAHATLVAGVRDRLPDLREVWQIDLGAV----------DDLVAAgASVDRAEVETrrslsKADDVA 183
Cdd:COG0365 114 VLITADgglrggkvIDLKEKVDEALEELPSLEHVIVVGRTGAdvpmegdldwDELLAA-ASAEFEPEPT-----DADDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNI----------------------YSDIANAVpVLPNLF----RQGASTLLF-----LPL 232
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYlvhaattakyvldlkpgdvfwcTADIGWAT-GHSYIVygplLNGATVVLYegrpdFPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 233 AHAFARLIQvgvvharatmahcadtknlvaelqDFKPTFVLSVP---RVFEKVyngarqkaeaegkgkifdraekvaiaw 309
Cdd:COG0365 267 PGRLWELIE------------------------KYGVTVFFTAPtaiRALMKA--------------------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 310 seaqelpggpGLGLRAQHALfdklvyRKLRAAMggrcrdaiSGGAPLGARLGH-FFRGVGVTICEGYGLTETSPAAAANL 388
Cdd:COG0365 296 ----------GDEPLKKYDL------SSLRLLG--------SAGEPLNPEVWEwWYEAVGVPIVDGWGQTETGGIFISNL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 389 PTG-TRIGTVGRPLPGVTIRI-DDDGEVLIA---GDIV--------FQGYWHNDAATAEAI--TTDGWFRTGDLGQLDEN 453
Cdd:COG0365 352 PGLpVKPGSMGKPVPGYDVAVvDEDGNPVPPgeeGELVikgpwpgmFRGYWNDPERYRETYfgRFPGWYRTGDGARRDED 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 454 GYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVVVG----DRQPFIAALVTIDEEALPkwlagqgrpettsma 529
Cdd:COG0365 432 GYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVVGvpdeIRGQVVKAFVVLKPGVEP--------------- 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 530 elreDAALRAEVQSAIDQanqavsKAEAIKVFRILpqdftEATGEL--TPSLKVKRQVV 586
Cdd:COG0365 496 ----SDELAKELQAHVRE------ELGPYAYPREI-----EFVDELpkTRSGKIMRRLL 539
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
60-520 |
5.58e-49 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 177.76 E-value: 5.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEwTLFDY-AIWAAGAVTVPIyetSSAEQAAWI---LGDSGAVAVVVESTAHATlVA 135
Cdd:PRK07514 41 LANLLVALGVKPGDRVAVQVEKSPE-ALALYlATLRAGAVFLPL---NTAYTLAELdyfIGDAEPALVVCDPANFAW-LS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 136 GVRDRLPdLREVWQIDLGAVDDL--VAAGASVDRAEVETrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIYSdiaNAV 213
Cdd:PRK07514 116 KIAAAAG-APHVETLDADGTGSLleAAAAAPDDFETVPR-----GADDLAAILYTSGTTGRSKGAMLSHGNLLS---NAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 214 pVLPNLFRQGASTLLF--LPLAHAFARLIQVGVV-HARATMAHCadtknlvaelqdfkptfvlsvPRvfekvyngarqka 290
Cdd:PRK07514 187 -TLVDYWRFTPDDVLIhaLPIFHTHGLFVATNVAlLAGASMIFL---------------------PK------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 291 eaegkgkiFDRAEkvAIAW-SEAQELPGGPGLGLRA-QHALFDklvyRKLRAAMggrcRDAISGGAPL--------GARL 360
Cdd:PRK07514 232 --------FDPDA--VLALmPRATVMMGVPTFYTRLlQEPRLT----REAAAHM----RLFISGSAPLlaethrefQERT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 361 GHffrgvgvTICEGYGLTETspaaaaNLPT-----GTRI-GTVGRPLPGVTIRIDD--DGEVLIAGDI---------VFQ 423
Cdd:PRK07514 294 GH-------AILERYGMTET------NMNTsnpydGERRaGTVGFPLPGVSLRVTDpeTGAELPPGEIgmievkgpnVFK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 424 GYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQP-F- 501
Cdd:PRK07514 361 GYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEIDELPGVVESAVIGVPHPdFg 439
|
490 500
....*....|....*....|....*..
gi 2504840381 502 ---IAALV-----TIDEEALPKWLAGQ 520
Cdd:PRK07514 440 egvTAVVVpkpgaALDEAAILAALKGR 466
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-519 |
1.97e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 176.77 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 15 AANLTDPVWENAEVAPDTVQFVRpGAGTdaredVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtLFD--YAI 92
Cdd:PRK07470 6 VMNLAHFLRQAARRFPDRIALVW-GDRS-----WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQ--MFEsmFAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 93 WAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEStAHATLVAGVRDRLPDLRevWQIDLGA------VDDLVA--AGAS 164
Cdd:PRK07470 78 FRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHA-DFPEHAAAVRAASPDLT--HVVAIGGaragldYEALVArhLGAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 165 VDRAEVEtrrslskADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAV-PVLPNLFRQGAStLLFLPLAHAFArliqvg 243
Cdd:PRK07470 155 VANAAVD-------HDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLaDLMPGTTEQDAS-LVVAPLSHGAG------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 244 vVHARATMAHCADTKNLVAE----------LQDFKPTFVLSVPRVfekvyngarqkaeaegkgkifdraekvaiawseaq 313
Cdd:PRK07470 221 -IHQLCQVARGAATVLLPSErfdpaevwalVERHRVTNLFTVPTI----------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 314 elpggpgLGLRAQHALFDKLVYRKLRAAmggrcrdaISGGAP------------LGARLGHFFrGVG-VTICegygLTET 380
Cdd:PRK07470 265 -------LKMLVEHPAVDRYDHSSLRYV--------IYAGAPmyradqkralakLGKVLVQYF-GLGeVTGN----ITVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 381 SPAA-AANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQ 449
Cdd:PRK07470 325 PPALhDAEDGPDARIGTCGFERTGMEVQIQDDegrelppgetGEICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLGH 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 450 LDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPF-----IAALV-----TIDEEALPKWLAG 519
Cdd:PRK07470 404 LDARGFLYITGRASDMYIS-GGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwgevgVAVCVardgaPVDEAELLAWLDG 482
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
21-512 |
2.36e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 177.07 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 21 PVWENAEVA----PDTVQFVRPGAgtdareDVTCRQFRDEVVAVAQGLI-AAGVSPGDRVGLMSRTRYEWTLFDYAIWAA 95
Cdd:PRK08314 11 SLFHNLEVSarryPDKTAIVFYGR------AISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 96 GAVTVPIYETSSAEQAAWILGDSGAVAVVVES-------TAHATL------VAGVRDRLPDLREVwqidlgAVDDLVAAG 162
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSelapkvaPAVGNLrlrhviVAQYSDYLPAEPEI------AVPAWLRAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 163 ASVDRAEVETRRSLSKA--------------DDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVpvlpnLFRQGAS--- 225
Cdd:PRK08314 159 PPLQALAPGGVVAWKEAlaaglappphtagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV-----LWSNSTPesv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 226 TLLFLPLAHAfarliqVGVVHARATMAHCADT--------KNLVAEL-QDFKPTFVLSVPRVfekvyngarqkaeaegkg 296
Cdd:PRK08314 234 VLAVLPLFHV------TGMVHSMNAPIYAGATvvlmprwdREAAARLiERYRVTHWTNIPTM------------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 297 kIFDraekvaiawseaqeLPGGPGLglraqhALFD--KLVYrklraaMGGrcrdaisGGAPL----GARLghfFRGVGVT 370
Cdd:PRK08314 290 -VVD--------------FLASPGL------AERDlsSLRY------IGG-------GGAAMpeavAERL---KELTGLD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 371 ICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAEA-ITT 438
Cdd:PRK08314 333 YVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpetleelppgeVGEIVVHGPQVFKGYWNRPEATAEAfIEI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 439 DG--WFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGDRQPF----IAALVTIDEEA 512
Cdd:PRK08314 413 DGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFK-VWPAEVENLLYKHPAIQEACVIATPDPRrgetVKAVVVLRPEA 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-520 |
6.31e-48 |
|
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: 172.86 E-value: 6.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVest 128
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 ahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskadDVATIIYTSGTTGRPKGCVLTHRNIYSD 208
Cdd:cd05934 82 ----------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 209 IANAVPVLPnlFRQGASTLLFLPLAHAFARLIQVG---VVHARATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYng 285
Cdd:cd05934 110 GYYSARRFG--LGEDDVYLTVLPLFHINAQAVSVLaalSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLL-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 286 arqkaeaegkgkifdraekvaiawseAQelpggPGLGLRAQHalfdklvyrKLRAAMGGrcrdaisggAPLGARLGHFFR 365
Cdd:cd05934 186 --------------------------AQ-----PPSPDDRAH---------RLRAAYGA---------PNPPELHEEFEE 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 366 GVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLI---AGDIVFQGYWHNDAAT 432
Cdd:cd05934 217 RFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDdgqelpagepGELVIrglRGWGFFKGYYNMPEAT 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 433 AEAItTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPF----IAALV-- 506
Cdd:cd05934 297 AEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI-RRRGENISSAEVERAILRHPAVREAAVVAVPDEVgedeVKAVVvl 374
|
490
....*....|....*...
gi 2504840381 507 ----TIDEEALPKWLAGQ 520
Cdd:cd05934 375 rpgeTLDPEELFAFCEGQ 392
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
60-496 |
7.64e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 175.71 E-value: 7.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVA----VVVESTAHATLVA 135
Cdd:PRK06087 62 LANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMffapTLFKQTRPVDLIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 136 GVRDRLPDLREVWqidlgAVDDLVAAGASVDRAEV-ETRRSLSK-----ADDVATIIYTSGTTGRPKGCVLTHRNIysdI 209
Cdd:PRK06087 142 PLQNQLPQLQQIV-----GVDKLAPATSSLSLSQIiADYEPLTTaitthGDELAAVLFTSGTEGLPKGVMLTHNNI---L 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 210 ANAVPVLPNLFRQGASTLLF-LPLAHA---FARLIQVGVVHARATMahcadtknlvaeLQDFKPTFVLSVPRvfekvyng 285
Cdd:PRK06087 214 ASERAYCARLNLTWQDVFMMpAPLGHAtgfLHGVTAPFLIGARSVL------------LDIFTPDACLALLE-------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 286 aRQKaeaegkgkifdraekvaIAWSeaqeLPGGPGL-----GLRAQHALFDKLvyrklraamggrcRDAISGGAPLGARL 360
Cdd:PRK06087 274 -QQR-----------------CTCM----LGATPFIydllnLLEKQPADLSAL-------------RFFLCGGTTIPKKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 361 GHFFRGVGVTICEGYGLTETSPAAAANL--PTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHN 428
Cdd:PRK06087 319 ARECQQRGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGVEIKVVDEarktlppgceGEEASRGPNVFMGYLDE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 429 DAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK06087 399 PELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSREVEDILLQHPKIHDACVVA 465
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
47-496 |
9.21e-46 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 170.20 E-value: 9.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 47 DVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTV---PIYETSSAEQAawiLGDSGAVAV 123
Cdd:PRK07059 48 AITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTPRELEHQ---LKDSGAEAI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VV-ESTAHA------------TLVAGVRD--------------RLPDLREVWQIDlGAV--DDLVAAGASVDRAEVETrr 174
Cdd:PRK07059 125 VVlENFATTvqqvlaktavkhVVVASMGDllgfkghivnfvvrRVKKMVPAWSLP-GHVrfNDALAEGARQTFKPVKL-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 175 slsKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGA-----STLLFLPLAHAFArLIQVGVVHARA 249
Cdd:PRK07059 202 ---GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPrpdqlNFVCALPLYHIFA-LTVCGLLGMRT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 -----TMAHCADTKNLVAELQDFKPTfvlSVPRVfEKVYNGARQKAEaegkgkifdraekvaiawseaqelpggpglglr 324
Cdd:PRK07059 278 ggrniLIPNPRDIPGFIKELKKYQVH---IFPAV-NTLYNALLNNPD--------------------------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 325 aqhalFDKLVYRKLRAAMGGrcrdaisGGA---PLGARlghFFRGVGVTICEGYGLTETSPAAAANLPTGTRI-GTVGRP 400
Cdd:PRK07059 321 -----FDKLDFSKLIVANGG-------GMAvqrPVAER---WLEMTGCPITEGYGLSETSPVATCNPVDATEFsGTIGLP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 401 LPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAg 470
Cdd:PRK07059 386 LPSTEVSIRDDdgndlplgepGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS- 464
|
490 500
....*....|....*....|....*.
gi 2504840381 471 GKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAVG 490
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
26-500 |
3.22e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 167.34 E-value: 3.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVrpgagtDAREDVTCRQFRDEVVAVAQGLI-AAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYE 104
Cdd:PRK06839 12 AYLHPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 105 TSSAEQAAWILGDSGAVAVVVESTAHATlVAGVRDRLPDLREVWQIDLGAVDDLVAAGAsVDRAEvetrrslskaDDVAT 184
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNM-ALSMQKVSYVQRVISITSLKEIEDRKIDNF-VEKNE----------SASFI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 185 IIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAH-------AFARLIQVGVVharaTMAHCADT 257
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAID--LTMHDRSIVLLPLFHiggiglfAFPTLFAGGVI----IVPRKFEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 KNLVAELQDFKPTFVLSVPRVFEKVYNGARqkaeaegkgkiFDRAEKVAIAWseaqelpggpglglraqhalfdklVYrk 337
Cdd:PRK06839 228 TKALSMIEKHKVTVVMGVPTIHQALINCSK-----------FETTNLQSVRW------------------------FY-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 lraamggrcrdaiSGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTR--IGTVGRPLPGVTIR-IDDD--- 411
Cdd:PRK06839 271 -------------NGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYElIDENknk 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRA 485
Cdd:PRK06839 338 vevgevGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINK 415
|
490
....*....|....*
gi 2504840381 486 HPLISQCVVVGDRQP 500
Cdd:PRK06839 416 LSDVYEVAVVGRQHV 430
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
61-496 |
3.53e-45 |
|
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: 165.70 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 61 AQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGavavvvestahatlVAGVRDR 140
Cdd:TIGR01923 13 AKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD--------------VQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 141 LPDLREVWQIDlgAVDDLVAAgasvDRAEVETRRSLSkADDVATIIYTSGTTGRPKGCVLTHRNIYsdiANAVPVLPNL- 219
Cdd:TIGR01923 79 SLLEEKDFQAD--SLDRIEAA----GRYETSLSASFN-MDQIATLMFTSGTTGKPKAVPHTFRNHY---ASAVGSKENLg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 FRQGASTLLFLPLAHafarliqvgvvharatmahcadtknlvaelqdfkptfVLSVPRVFEKVYNGARQKAeAEGKGKIF 299
Cdd:TIGR01923 149 FTEDDNWLLSLPLYH-------------------------------------ISGLSILFRWLIEGATLRI-VDKFNQLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 300 DraekvAIAwseaqelpggpglGLRAQHA-LFDKLVYRKLRAamGGRC---RDAISGGAPLGARLGHFFRGVGVTICEGY 375
Cdd:TIGR01923 191 E-----MIA-------------NERVTHIsLVPTQLNRLLDE--GGHNenlRKILLGGSAIPAPLIEEAQQYGLPIYLSY 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 376 GLTET-SPAAAANLPTGTRIGTVGRPLPGVTIRIDDD-----GEVLIAGDIVFQGYWHNDAATaEAITTDGWFRTGDLGQ 449
Cdd:TIGR01923 251 GMTETcSQVTTATPEMLHARPDVGRPLAGREIKIKVDnkeghGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGE 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2504840381 450 LDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:TIGR01923 330 LDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLYQHPGIQEAVVVP 375
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-496 |
4.39e-45 |
|
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: 163.22 E-value: 4.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIysdIANAVPV-LPNLFRQGASTLLFLPLAHAFARLIQV-GVVHARATMAHCA-- 255
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI---VNNGYFIgERLGLTEQDRLCIPVPLFHCFGSVLGVlACLTHGATMVFPSps 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 256 -DTKNLVAELQDFKPTFVLSVPRVFEKVYNgarqkaeaegkgkifdraekvaiawseaqelpggpglglraqHALFDKLV 334
Cdd:cd05917 79 fDPLAVLEAIEKEKCTALHGVPTMFIAELE------------------------------------------HPDFDKFD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 335 YRKLRAAmggrcrdaISGGAP----LGARLGHFFRGVGVTICegYGLTETSPAAAANLPTGT---RIGTVGRPLPGVTIR 407
Cdd:cd05917 117 LSSLRTG--------IMAGAPcppeLMKRVIEVMNMKDVTIA--YGMTETSPVSTQTRTDDSiekRVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 408 IDDD-----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAP 476
Cdd:cd05917 187 IVDPeggivppvgvpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYP 265
|
330 340
....*....|....*....|
gi 2504840381 477 AVLEDQVRAHPLISQCVVVG 496
Cdd:cd05917 266 REIEEFLHTHPKVSDVQVVG 285
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
18-521 |
8.71e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.15 E-value: 8.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 18 LTDPVWENAEVAPDTVQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGA 97
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 98 VTVPIYETSSAEQAAWILGDSGAVAVVVEST----AHATLVAGVRDRLPDLREVWQIDlGAVDDLVAAGASVDRAEVETR 173
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfDHAAMARRLRPELPALRHVVVVG-GDGADSFEALLITPAWEQEPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 174 ------RSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANavpvLPNLFRQGASTLLFL--PLAHafarliQVGVV 245
Cdd:PRK13295 185 apailaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVP----YAERLGLGADDVILMasPMAH------QTGFM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 246 H-------ARATMAhcadtknlvaeLQDfkptfvlsvprvfekVYNGARQKAEAEGKGKIFDRAEKVAIA-WSEAQELPG 317
Cdd:PRK13295 255 YglmmpvmLGATAV-----------LQD---------------IWDPARAAELIRTEGVTFTMASTPFLTdLTRAVKESG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 318 GPGLGLRAqhalFdklvyrklraamggrcrdaISGGAPL-GARLGHFFRGVGVTICEGYGLTETSPAAAANL--PTGTRI 394
Cdd:PRK13295 309 RPVSSLRT----F-------------------LCAGAPIpGALVERARAALGAKIVSAWGMTENGAVTLTKLddPDERAS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 395 GTVGRPLPGVTIRI-DDDGEVLIAGDI---------VFQGYWHNDAATAEAitTDGWFRTGDLGQLDENGYLSITGRKKE 464
Cdd:PRK13295 366 TTDGCPLPGVEVRVvDADGAPLPAGQIgrlqvrgcsNFGGYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKD 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504840381 465 IIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG--DR--QPFIAALV------TIDEEALPKWLAGQG 521
Cdd:PRK13295 444 VIIR-GGENIPVVEIEALLYRHPAIAQVAIVAypDErlGERACAFVvprpgqSLDFEEMVEFLKAQK 509
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
68-496 |
1.15e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 167.25 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 68 GVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTV---PIYetsSAEQAAWILGDSGAVAVVV-ESTAHA------------ 131
Cdd:PRK05677 71 DLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY---TAREMEHQFNDSGAKALVClANMAHLaekvlpktgvkh 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 132 TLVAGVRDRLPDLRE-------------VWQIDL-GAV--DDLVAAGASVDRAEVEtrrslSKADDVATIIYTSGTTGRP 195
Cdd:PRK05677 148 VIVTEVADMLPPLKRllinavvkhvkkmVPAYHLpQAVkfNDALAKGAGQPVTEAN-----PQADDVAVLQYTGGTTGVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 196 KGCVLTHRNIYSDIANAVPVLPNLFRQGASTLLF-LPLAHAFARliqvgVVHARATM---AHCA------DTKNLVAELQ 265
Cdd:PRK05677 223 KGAMLTHRNLVANMLQCRALMGSNLNEGCEILIApLPLYHIYAF-----TFHCMAMMligNHNIlisnprDLPAMVKELG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 266 DFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekVAIAWSEAqelpggpglglraqhalFDKLVYRKLRAAmggr 345
Cdd:PRK05677 298 KWKFSGFVGLNTLF-------------------------VALCNNEA-----------------FRKLDFSALKLT---- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 346 crdaISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIR-IDDDGEVLIAGDI--- 420
Cdd:PRK05677 332 ----LSGGMALQLATAERWKEVtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKvIDDDGNELPLGEVgel 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 421 ------VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVV 494
Cdd:PRK05677 408 cvkgpqVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLAALPGVLQCAA 486
|
..
gi 2504840381 495 VG 496
Cdd:PRK05677 487 IG 488
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
26-521 |
4.83e-44 |
|
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: 164.34 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGTDAREdvTCRQFRDEVVAVAQGLIAAGVSPGDRVG-LMSRTRYEWTLFdYAIWAAGAVTVPIYE 104
Cdd:cd12119 6 ARLHGDREIVSRTHEGEVHRY--TYAEVAERARRLANALRRLGVKPGDRVAtLAWNTHRHLELY-YAVPGMGAVLHTINP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 105 TSSAEQAAWILGDSGAVAVVVESTAhATLVAGVRDRLPDLREVWQID------------LGAVDDLVAAGASV-DRAEVE 171
Cdd:cd12119 83 RLFPEQIAYIINHAEDRVVFVDRDF-LPLLEAIAPRLPTVEHVVVMTddaampepagvgVLAYEELLAAESPEyDWPDFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 172 TRrslskadDVATIIYTSGTTGRPKGCVLTHRNIY--SDIANAVPVLPnlFRQGASTLLFLPLAHAFARliqvGVVHArA 249
Cdd:cd12119 162 EN-------TAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLG--LSESDVVLPVVPMFHVNAW----GLPYA-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 TMAHCA--------DTKNLVAELQDFKPTFVLSVPrvfeKVYNGARQKAEAEGkgkifdraekvaiawseaQELPGGpgl 321
Cdd:cd12119 228 AMVGAKlvlpgpylDPASLAELIEREGVTFAAGVP----TVWQGLLDHLEANG------------------RDLSSL--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 322 glraqhalfdklvyrklraamggrcRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIG------ 395
Cdd:cd12119 283 -------------------------RRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeq 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 396 -----TVGRPLPGVTIRIDDD------------GEVLIAGDIVFQGYWHNDAATaEAITTDGWFRTGDLGQLDENGYLSI 458
Cdd:cd12119 338 lalraKQGRPVPGVELRIVDDdgrelpwdgkavGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTI 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 459 TGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVG------DRQPFiaALV------TIDEEALPKWLAGQG 521
Cdd:cd12119 417 TDRSKDVI-KSGGEWISSVELENAIMAHPAVAEAAVIGvphpkwGERPL--AVVvlkegaTVTAEELLEFLADKV 488
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
52-520 |
5.85e-44 |
|
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: 162.26 E-value: 5.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 52 QFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVestaha 131
Cdd:cd05935 6 ELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 132 tlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrsLSKADDVATIIYTSGTTGRPKGCVLTHRNIysdIAN 211
Cdd:cd05935 80 --------------------------------------------GSELDDLALIPYTSGTTGLPKGCMHTHFSA---AAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 212 AV-PVLPNLFRQGASTLLFLPLAHA--FARLIQVGVVhARATMAHCA--DTKNLVAELQDFKPTFVLSVPRVFEKVYNGA 286
Cdd:cd05935 113 ALqSAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVY-VGGTYVLMArwDRETALELIEKYKVTFWTNIPTMLVDLLATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 287 RqkaeaegkgkifdraekvaiawseaqelpggpglglraqhalFDKLVYRKLRAAMGGrcrdaisgGAPLGARLGHFFRG 366
Cdd:cd05935 192 E------------------------------------------FKTRDLSSLKVLTGG--------GAPMPPAVAEKLLK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 367 V-GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAE 434
Cdd:cd05935 222 LtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDietgrelppneVGEIVVRGPQIFKGYWNRPEETEE 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 435 AITTDG---WFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGDRQPFIA----ALV- 506
Cdd:cd05935 302 SFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEVEAKLYKHPAI*EVCVISVPDERVGeevkAFIv 380
|
490 500
....*....|....*....|.
gi 2504840381 507 -------TIDEEALPKWLAGQ 520
Cdd:cd05935 381 lrpeyrgKVTEEDIIEWAREQ 401
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
46-513 |
2.07e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 160.10 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 EStAHATLVAGVRDRLPDLREVWQIDLG---------AVDDLVAAGaSVDRAEVETRrslskADDVATIIYTSGTTGRPK 196
Cdd:PRK08316 115 DP-ALAPTAEAALALLPVDTLILSLVLGgreapggwlDFADWAEAG-SVAEPDVELA-----DDDLAQILYTSGTESLPK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 197 GCVLTHRNIysdIANAVPVLPNL-FRQGASTLLFLPLAHAFAR------LIQVGvvharATmahcadtkNLVAElqdfKP 269
Cdd:PRK08316 188 GAMLTHRAL---IAEYVSCIVAGdMSADDIPLHALPLYHCAQLdvflgpYLYVG-----AT--------NVILD----AP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 270 TfvlsVPRVFEKVyngarqkaEAEGKGKIFdRAEKVAIAWseaqelpggpglglrAQHALFDKLVYRKLRAAMGGRcrdA 349
Cdd:PRK08316 248 D----PELILRTI--------EAERITSFF-APPTVWISL---------------LRHPDFDTRDLSSLRKGYYGA---S 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 350 ISGGAPLgARLGHFFRGVGVTICegYGLTETSPAAAANLPTG--TRIGTVGRPLPGVTIRI-DDDGEVLIA---GDIVFQ 423
Cdd:PRK08316 297 IMPVEVL-KELRERLPGLRFYNC--YGQTEIAPLATVLGPEEhlRRPGSAGRPVLNVETRVvDDDGNDVAPgevGEIVHR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 424 ------GYWHNDAATAEAItTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGD 497
Cdd:PRK08316 374 spqlmlGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVEEALYTHPAVAEVAVIGL 451
|
490 500
....*....|....*....|....*.
gi 2504840381 498 RQPF----IAALV------TIDEEAL 513
Cdd:PRK08316 452 PDPKwieaVTAVVvpkagaTVTEDEL 477
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
26-500 |
2.34e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 161.66 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPD--TVQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwTLFdyAIWAAGA--VTVP 101
Cdd:PRK07529 35 AARHPDapALSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE-THF--ALWGGEAagIANP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 102 IYETSSAEQAAWILGDSGA-VAVVVESTAHATL---VAGVRDRLPDLREVWQIDLG-----------------AVDDLVA 160
Cdd:PRK07529 112 INPLLEPEQIAELLRAAGAkVLVTLGPFPGTDIwqkVAEVLAALPELRTVVEVDLArylpgpkrlavplirrkAHARILD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 161 AGASVDRAEVETRRS--LSKADDVATIIYTSGTTGRPKGCVLTHRNiysDIANAVPVLPNLFRQGASTLLF-LPLAHAFA 237
Cdd:PRK07529 192 FDAELARQPGDRLFSgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGN---EVANAWLGALLLGLGPGDTVFCgLPLFHVNA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 238 RLIQVGVVHARAtmAHC-------ADTKNLVAEL----QDFKPTFVLSVPrvfeKVYNGARQkaeaegkgkifdraekva 306
Cdd:PRK07529 269 LLVTGLAPLARG--AHVvlatpqgYRGPGVIANFwkivERYRINFLSGVP----TVYAALLQ------------------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 307 iawseaqelpggpglglraqhalfdklvyRKLRAAMGGRCRDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAA 385
Cdd:PRK07529 325 -----------------------------VPVDGHDISSLRYALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTEATCVSS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 386 ANLPTG-TRIGTVGRPLPGVTIRI---------------DDDGEVLIAGDIVFQGYW---HNDAATAEaittDGWFRTGD 446
Cdd:PRK07529 376 VNPPDGeRRIGSVGLRLPYQRVRVvilddagrylrdcavDEVGVLCIAGPNVFSGYLeaaHNKGLWLE----DGWLNTGD 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2504840381 447 LGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGdrQP 500
Cdd:PRK07529 452 LGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEALLRHPAVALAAAVG--RP 502
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
49-494 |
1.13e-41 |
|
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: 155.50 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAA-GVSPGDRVGLMSRtRYEWTLFDY-AIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVE 126
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLE-RSAELVVAIlAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 StAHATLVAGV--RDRLPDLREVWQIDlgavddlvaagasvDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRN 204
Cdd:TIGR01733 80 S-ALASRLAGLvlPVILLDPLELAALD--------------DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 205 iysdIANAVPVLPNLF--RQGASTLLFLPLAH------AFARLIQ-VGVVHARATMAHcaDTKNLVAELQD-FKPTFVLS 274
Cdd:TIGR01733 145 ----LVNLLAWLARRYglDPDDRVLQFASLSFdasveeIFGALLAgATLVVPPEDEER--DDAALLAALIAeHPVTVLNL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 275 VPRVFEKVyngarqkaeaegkgkifdraekvaiawsEAQELPGGPGLglraqhalfdklvyrklraamggrcRDAISGGA 354
Cdd:TIGR01733 219 TPSLLALL----------------------------AAALPPALASL-------------------------RLVILGGE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 355 PLGARLGHFFRGV--GVTICEGYGLTETSPAAAANL-----PTGTRIGTVGRPLPGVTIRIDDD----------GEVLIA 417
Cdd:TIGR01733 246 ALTPALVDRWRARgpGARLINLYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRLYVLDDdlrpvpvgvvGELYIG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 418 GDIVFQGYWHNDAATAEAITTDG--------WFRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLI 489
Cdd:TIGR01733 326 GPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGRIDD-QVKIRGYRIELGEIEAALLRHPGV 404
|
....*
gi 2504840381 490 SQCVV 494
Cdd:TIGR01733 405 REAVV 409
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
47-525 |
4.76e-41 |
|
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: 153.66 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 47 DVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAvavvve 126
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 stahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIY 206
Cdd:cd05912 75 ---------------------------------------------------KLDDIATIMYTSGTTGKPKGVQQTFGNHW 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 207 sdiANAVPVLPNL-FRQGASTLLFLPLAHAFARLIQV-GVVHA-RATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVy 283
Cdd:cd05912 104 ---WSAIGSALNLgLTEDDNWLCALPLFHISGLSILMrSVIYGmTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 ngarqkaeaegkgkifdraekvaiawseAQELPGGpglglraQHALFdklvyrklraamggRCrdAISGGAPLGARLGHF 363
Cdd:cd05912 180 ----------------------------LEILGEG-------YPNNL--------------RC--ILLGGGPAPKPLLEQ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 364 FRGVGVTICEGYGLTETSPAAAANLP--TGTRIGTVGRPLPGVTIRIDDD-------GEVLIAGDIVFQGYWHNDAATAE 434
Cdd:cd05912 209 CKEKGIPVYQSYGMTETCSQIVTLSPedALNKIGSAGKPLFPVELKIEDDgqppyevGEILLKGPNVTKGYLNRPDATEE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 435 AITtDGWFRTGDLGQLDENGYLSITGRKKEIIVtAGGKNVAPAVLEDQVRAHPLISQCVVVG--DRQ----P--FIAALV 506
Cdd:cd05912 289 SFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPAIKEAGVVGipDDKwgqvPvaFVVSER 366
|
490 500
....*....|....*....|...
gi 2504840381 507 TIDEEAL----PKWLAGQGRPET 525
Cdd:cd05912 367 PISEEELiaycSEKLAKYKVPKK 389
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
71-496 |
8.92e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 156.14 E-value: 8.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 71 PGDRVGLMSRTRYEWTLFDYAIWAAGAVTV---PIYetsSAEQAAWILGDSGAVAVV--------VESTAHATLV----- 134
Cdd:PRK12492 74 PGDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLY---TAREMRHQFKDSGARALVylnmfgklVQEVLPDTGIeylie 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 135 AGVRDRLPDLREvWQID--LGAVDDLVAA-----GASVDRAEVETRRSLSKA-----DDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PRK12492 151 AKMGDLLPAAKG-WLVNtvVDKVKKMVPAyhlpqAVPFKQALRQGRGLSLKPvpvglDDIAVLQYTGGTTGLAKGAMLTH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIysdIANAVPVLPN----------LFRQGASTLLF-LPLAHAFA-----RLIQVGVVHaRATMAHCADTKNLVAELQD 266
Cdd:PRK12492 230 GNL---VANMLQVRAClsqlgpdgqpLMKEGQEVMIApLPLYHIYAftancMCMMVSGNH-NVLITNPRDIPGFIKELGK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 267 FKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekVAIAwseaqelpggpglglraQHALFDKLVYRKLRAAMGGrc 346
Cdd:PRK12492 306 WRFSALLGLNTLF-------------------------VALM-----------------DHPGFKDLDFSALKLTNSG-- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 rdaisGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANlPTGT--RIGTVGRPLPGVTIRIDDD----------GEV 414
Cdd:PRK12492 342 -----GTALVKATAERWEQLTGCTIVEGYGLTETSPVASTN-PYGElaRLGTVGIPVPGTALKVIDDdgnelplgerGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVV 494
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEIEDVVMAHPKVANCAA 494
|
..
gi 2504840381 495 VG 496
Cdd:PRK12492 495 IG 496
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
26-513 |
1.07e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 154.35 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYET 105
Cdd:PRK03640 12 AFLTPDRT------AIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 106 SSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLrevwqidlgavddlvAAGASVDRAEVETrrslSKADDVATI 185
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAEL---------------MNGPKEEAEIQEE----FDLDEVATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 186 IYTSGTTGRPKGCVLTHRN-IYSDIANAVpvlpNL-FRQGASTLLFLPLAH-----AFARLIQVG---VVHARAtmahca 255
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNhWWSAVGSAL----NLgLTEDDCWLAAVPIFHisglsILMRSVIYGmrvVLVEKF------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 256 DTKNLVAELQDFKPTFVLSVPRVFEKVyngarqkaeaegkgkifdraekvaiawseAQELPGGPglglraQHALFdklvy 335
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVSTMLQRL-----------------------------LERLGEGT------YPSSF----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 336 rklraamggRCrdAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTG--TRIGTVGRPLPGVTIRIDDD-- 411
Cdd:PRK03640 257 ---------RC--MLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVTLSPEDalTKLGSAGKPLFPCELKIEKDgv 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 -------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVR 484
Cdd:PRK03640 326 vvppfeeGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLL 403
|
490 500 510
....*....|....*....|....*....|....*..
gi 2504840381 485 AHPLISQCVVVG--DRQ----P--FIAALVTIDEEAL 513
Cdd:PRK03640 404 SHPGVAEAGVVGvpDDKwgqvPvaFVVKSGEVTEEEL 440
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
26-496 |
1.61e-40 |
|
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: 154.45 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPgAGTdaredVTCRQFRDEVVAVAQGLIAAGVSPGDRVGL-MSRTRYEWTLFDYAIWAaGAVTVPIYE 104
Cdd:cd05959 14 NEGRGDKTAFIDD-AGS-----LTYAELEAEARRVAGALRALGVKREERVLLiMLDTVDFPTAFLGAIRA-GIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 105 TSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGASVDRAEVETRRSLS-KADDVA 183
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAtHADDPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNIY---------------SDIANAVPVLpnLFRQGASTLLFLPLAHAFARLIQVGvvhaR 248
Cdd:cd05959 167 FWLYSSGSTGRPKGVVHLHADIYwtaelyarnvlgireDDVCFSAAKL--FFAYGLGNSLTFPLSVGATTVLMPE----R 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 249 ATMAHCADTknlvaeLQDFKPTFVLSVPrvfeKVYNGarqkaeaegkgkifdraekvaiawseaqeLPGGPGLGLRAQHA 328
Cdd:cd05959 241 PTPAAVFKR------IRRYRPTVFFGVP----TLYAA-----------------------------MLAAPNLPSRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 329 LfdklvyrklraamggrcRDAISGGAPLGARLGHFFRG-VGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIR 407
Cdd:cd05959 282 L-----------------RLCVSAGEALPAEVGERWKArFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 408 IDDD----------GEVLIAGDIVFQGYWHNDAATAEAItTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPA 477
Cdd:cd05959 345 LRDEdggdvadgepGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDML-KVSGIWVSPF 422
|
490
....*....|....*....
gi 2504840381 478 VLEDQVRAHPLISQCVVVG 496
Cdd:cd05959 423 EVESALVQHPAVLEAAVVG 441
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-496 |
2.44e-40 |
|
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: 152.53 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVES 127
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 tahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIys 207
Cdd:cd05903 82 -----------------------------------------RFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTL-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 208 dIANAVPVLPNL-FRQGASTLLFLPLAHafarliQVGVVHAratmahcadtknlvaelqdFKPTFVLSVPRVFEKVYNGA 286
Cdd:cd05903 119 -SASIRQYAERLgLGPGDVFLVASPMAH------QTGFVYG-------------------FTLPLLLGAPVVLQDIWDPD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 287 RQKAEAEGKGKIFdraekvaiawseaqelpggpglGLRAQHALFDKLVYRKLRAAMGGRCRDAISGGAPLGARLG-HFFR 365
Cdd:cd05903 173 KALALMREHGVTF----------------------MMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLArRAAE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 366 GVGVTICEGYGLTETSPAAAANLPT--GTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATA 433
Cdd:cd05903 231 LLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDDtgatlapgveGELLSRGPSVFLGYLDRPDLTA 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 434 EAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05903 311 DAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
17-496 |
2.61e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 154.55 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 17 NLTDPVWENAEVAPDTVQFVRPGAGTdaredvTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAG 96
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGNTT------TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 97 AVTVPIYETSSAEQAAWILGDSGAVAVVVEsTAHATLVAGVRDRLPDLREVWQIDlGAVDDLVAAGASVDRAEVETRRSL 176
Cdd:PRK07786 92 AIAVPVNFRLTPPEIAFLVSDCGAHVVVTE-AALAPVATAVRDIVPLLSTVVVAG-GSSDDSVLGYEDLLAEAGPAHAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDV-ATIIYTSGTTGRPKGCVLTHRNIYSDianavpVLPNLFRQGAST-----LLFLPLAH-AFARLIQVGVVHARA 249
Cdd:PRK07786 170 DIPNDSpALIMYTSGTTGRPKGAVLTHANLTGQ------AMTCLRTNGADInsdvgFVGVPLFHiAGIGSMLPGLLLGAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 TMAH---CADTKNLVAELQDFKPTFVLSVPRVFEKVYngarqkAEAEGKGKifDRAEKVaIAWSEAqelPGGPGLgLRAQ 326
Cdd:PRK07786 244 TVIYplgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVC------AEQQARPR--DLALRV-LSWGAA---PASDTL-LRQM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 327 HALFDklvyrklraamggrcrdaisggaplgarlghffrgvGVTICEGYGLTETSPAAAANLPTGT--RIGTVGRPLPGV 404
Cdd:PRK07786 311 AATFP------------------------------------EAQILAAFGQTEMSPVTCMLLGEDAirKLGSVGKVIPTV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 TIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAItTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNV 474
Cdd:PRK07786 355 AARVVDEnmndvpvgevGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENI 432
|
490 500
....*....|....*....|..
gi 2504840381 475 APAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK07786 433 YCAEVENVLASHPDIVEVAVIG 454
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
68-496 |
3.44e-40 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 154.44 E-value: 3.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 68 GVSPGDRVGLM--SRTRYEWTLFdyAIWAAGAVTV---PIYETSSAEQAawiLGDSGAVAVVVESTAHATLVAGVRDrlP 142
Cdd:PRK08974 70 GLKKGDRVALMmpNLLQYPIALF--GILRAGMIVVnvnPLYTPRELEHQ---LNDSGAKAIVIVSNFAHTLEKVVFK--T 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 143 DLREVWQIDLGavDDLVAA-GASVDRA---------------EVETRRSLSKA------------DDVATIIYTSGTTGR 194
Cdd:PRK08974 143 PVKHVILTRMG--DQLSTAkGTLVNFVvkyikrlvpkyhlpdAISFRSALHKGrrmqyvkpelvpEDLAFLQYTGGTTGV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 195 PKGCVLTHRNIYSDIANAVPVLPNLFRQGAS-TLLFLPLAHAFAR------LIQVGVVHARATMAHcaDTKNLVAELQDF 267
Cdd:PRK08974 221 AKGAMLTHRNMLANLEQAKAAYGPLLHPGKElVVTALPLYHIFALtvncllFIELGGQNLLITNPR--DIPGFVKELKKY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 268 KPTFVLSVPRVFEkvyngarqkaeaegkgkifdraekvaiAWSEAQElpggpglglraqhalFDKLVYRKLRAAMGGrcr 347
Cdd:PRK08974 299 PFTAITGVNTLFN---------------------------ALLNNEE---------------FQELDFSSLKLSVGG--- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 348 daisgGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANlPTGTRI--GTVGRPLPGVTIRIDDD----------GEV 414
Cdd:PRK08974 334 -----GMAVQQAVAERWVKLtGQYLLEGYGLTECSPLVSVN-PYDLDYysGSIGLPVPSTEIKLVDDdgnevppgepGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVV 494
Cdd:PRK08974 408 WVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPKVLEVAA 485
|
..
gi 2504840381 495 VG 496
Cdd:PRK08974 486 VG 487
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
49-496 |
9.90e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 152.45 E-value: 9.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEST 128
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 AHATLVAGVRDRLPDLREVwqIDLGAVDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIysd 208
Cdd:PRK06188 119 PFVERALALLARVPSLKHV--LTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 209 IANAVPVLPNL-FRQGASTLLFLPLAHAFARLIQVGVVHARAT-MAHCADTKNLVAELQDFKPTFVLSVPRVfekVYnga 286
Cdd:PRK06188 194 ATMAQIQLAEWeWPADPRFLMCTPLSHAGGAFFLPTLLRGGTViVLAKFDPAEVLRAIEEQRITATFLVPTM---IY--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 287 rqkaeaegkgKIFDRAEkvaiawSEAQELPGgpglglraqhalFDKLVYRKlrAAMG-GRCRDAISggaplgaRLGHFFR 365
Cdd:PRK06188 268 ----------ALLDHPD------LRTRDLSS------------LETVYYGA--SPMSpVRLAEAIE-------RFGPIFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 366 GVgvticegYGLTEtSPAAAANLPTG-------TRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHN 428
Cdd:PRK06188 311 QY-------YGQTE-APMVITYLRKRdhdpddpKRLTSCGRPTPGLRVALLDEdgrevaqgevGEICVRGPLVMDGYWNR 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 429 DAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK06188 383 PEETAEAFR-DGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
48-506 |
2.58e-37 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 143.63 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEs 127
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 tahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCVLTHRNIYS 207
Cdd:cd05972 80 ---------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 208 DIANAVPVLPnlfrqgastllflplahafarliqvgvVHARATMAHCADTKNLVAELQDFKPTFVLSVPRVfekVYNGAR 287
Cdd:cd05972 109 HIPTAAYWLG---------------------------LRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVF---VYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 288 QKAEaegkgKIFDRAEKVAIawseaQELPGGPglglraqhalfdkLVYRKLRAAMG-----GRCRDAISGGAPLGARLGH 362
Cdd:cd05972 159 FDAE-----RILELLERYGV-----TSFCGPP-------------TAYRMLIKQDLssykfSHLRLVVSAGEPLNPEVIE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 363 FFRG-VGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRI-DDDGEVLIA---GDIV--------FQGYWHND 429
Cdd:cd05972 216 WWRAaTGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIiDDDGRELPPgeeGDIAiklpppglFLGYVGDP 295
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504840381 430 AATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAALV 506
Cdd:cd05972 296 EKTEASIR-GDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVV 370
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
48-496 |
5.48e-37 |
|
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: 144.01 E-value: 5.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQgLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGaVAVVVES 127
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAG-IKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 128 TA---HATLVAGVRDR-------LPDLREvwqiDLGAVDDLVAAGASVDRAEVETRRSLS---KADDVATIIYTSGTTGR 194
Cdd:cd05909 86 KQfieKLKLHHLFDVEydarivyLEDLRA----KISKADKCKAFLAGKFPPKWLLRIFGVapvQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 195 PKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAF--------ARLIQVGVVHAratmAHCADTKNLVAELQD 266
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFD--PNPEDVVFGALPFFHSFgltgclwlPLLSGIKVVFH----PNPLDYKKIPELIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 267 FKPTFVLSVPrVFEKVYNGARQKAEAEGKGKIFDRAEKVaiawseaqelpggpglglraQHALFDKlvyrklraamggrc 346
Cdd:cd05909 236 KKATILLGTP-TFLRGYARAAHPEDFSSLRLVVAGAEKL--------------------KDTLRQE-------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 rdaisggaplgarlghFFRGVGVTICEGYGLTETSPAAAANLP-TGTRIGTVGRPLPGVTIRIDD-----------DGEV 414
Cdd:cd05909 281 ----------------FQEKFGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPLPGMEVKIVSvetheevpigeGGLL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAH-PLISQCV 493
Cdd:cd05909 345 LVRGPNVMLGYLNEPELTSFAFG-DGWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEIlPEDNEVA 422
|
...
gi 2504840381 494 VVG 496
Cdd:cd05909 423 VVS 425
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
181-520 |
1.64e-36 |
|
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: 139.00 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYsdiANAVPVLPNL-FRQGASTLLFLPLAH--AFARLIQVGVVHARATMAHCADT 257
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLL---ASAAGLHSRLgFGGGDSWLLSLPLYHvgGLAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 knLVAELQDFKPTFVLSVPRVFEKVYngarqkaeaegkgkifdrAEKVAIAWSEaqelpggpglGLRAqhalfdklvyrk 337
Cdd:cd17630 78 --LAEDLAPPGVTHVSLVPTQLQRLL------------------DSGQGPAALK----------SLRA------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 lraamggrcrdAISGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDDGEVLIA 417
Cdd:cd17630 116 -----------VLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 418 GDIVFQGYWHNDaaTAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG- 496
Cdd:cd17630 185 GASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHPAVRDAFVVGv 261
|
330 340 350
....*....|....*....|....*....|.
gi 2504840381 497 -DR---QPFIAALVT---IDEEALPKWLAGQ 520
Cdd:cd17630 262 pDEelgQRPVAVIVGrgpADPAELRAWLKDK 292
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
72-496 |
5.01e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 142.32 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 72 GDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATlvagVRDRLPD--LREVWQ 149
Cdd:PRK08751 76 GDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTT----VQQVIADtpVKQVIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 150 IDLGAVDDLvAAGASVD---------------RAEVETRRSLS------------KADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PRK08751 152 TGLGDMLGF-PKAALVNfvvkyvkklvpeyriNGAIRFREALAlgrkhsmptlqiEPDDIAFLQYTGGTTGVAKGAMLTH 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVL--PNLFRQGASTLLF-LPLAHAFArLIQVGVVHARA-----TMAHCADTKNLVAELQDFKPTFVLS 274
Cdd:PRK08751 231 RNLVANMQQAHQWLagTGKLEEGCEVVITaLPLYHIFA-LTANGLVFMKIggcnhLISNPRDMPGFVKELKKTRFTAFTG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 275 VPRVFEKVYNgarqkaeaegkgkifdraekvaiawseaqeLPGgpglglraqhalFDKLVYRKLRAAMGGrcrdaisGGA 354
Cdd:PRK08751 310 VNTLFNGLLN------------------------------TPG------------FDQIDFSSLKMTLGG-------GMA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 355 PLGARLGHFFRGVGVTICEGYGLTETSPAAAAN-LPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQ 423
Cdd:PRK08751 341 VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLPIPSTDACIKDDagtvlaigeiGELCIKGPQVMK 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 424 GYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK08751 421 GYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
43-518 |
1.42e-35 |
|
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: 139.20 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 43 DAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVA 122
Cdd:cd05930 8 DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 VVVEstahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:cd05930 88 VLTD----------------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVLPNLFR----QGAS-------TLLFLPLAHAfARLIQVGVVHARatmahcaDTKNLVAELQDFKPTF 271
Cdd:cd05930 116 RGLVNLLLWMQEAYPLTPGdrvlQFTSfsfdvsvWEIFGALLAG-ATLVVLPEEVRK-------DPEALADLLAEEGITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 272 VLSVPrvfekvyngarqkaeaegkgkifdraekvaiawSEAQELpgGPGLGLRAQHALfdklvyrklraamggrcRDAIS 351
Cdd:cd05930 188 LHLTP---------------------------------SLLRLL--LQELELAALPSL-----------------RLVLV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 352 GGAPLGARLGHFFRGV--GVTICEGYGLTETS-PAAAANLPTGTRIG---TVGRPLPGVTIRIDDD----------GEVL 415
Cdd:cd05930 216 GGEALPPDLVRRWRELlpGARLVNLYGPTEATvDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDEnlrpvppgvpGELY 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 416 IAGDIVFQGYWHNDAATAEAITTDGWF------RTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLI 489
Cdd:cd05930 296 IGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDD-QVKIRGYRIELGEIEAALLAHPGV 374
|
490 500 510
....*....|....*....|....*....|....*....
gi 2504840381 490 SQCVVV----GDRQPFIAALVT------IDEEALPKWLA 518
Cdd:cd05930 375 REAAVVaredGDGEKRLVAYVVpdeggeLDEEELRAHLA 413
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
178-461 |
1.46e-35 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 143.14 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 KADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQ--------VGVV-HAR 248
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN--LRNDDVILSSLPFFHSFGLTVTlwlpllegIKVVyHPD 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 249 ATMAhcADTKNLVAElqdFKPTFVLSVPRVFekvyngarqkaeaegkgKIFDRAEKVaiawseaqelpggpglglraqha 328
Cdd:PRK08633 858 PTDA--LGIAKLVAK---HRATILLGTPTFL-----------------RLYLRNKKL----------------------- 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 329 lfDKLVYRKLRAAmggrcrdaISGGAPLGARLGHFFR-GVGVTICEGYGLTETSPAAAANLP----------TGTRIGTV 397
Cdd:PRK08633 893 --HPLMFASLRLV--------VAGAEKLKPEVADAFEeKFGIRILEGYGATETSPVASVNLPdvlaadfkrqTGSKEGSV 962
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 398 GRPLPGVTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAEAITT---DGWFRTGDLGQLDENGYLSITGR 461
Cdd:PRK08633 963 GMPLPGVAVRIVDpetfeelppgeDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
46-511 |
2.02e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 140.55 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVV- 124
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 125 -------VESTAHAT-----LVAGVRDRLPDLREVW-------QIDL---GAVDDLVAAGASVDRaEVETRRSL--SKAD 180
Cdd:PRK06710 128 ldlvfprVTNVQSATkiehvIVTRIADFLPFPKNLLypfvqkkQSNLvvkVSESETIHLWNSVEK-EVNTGVEVpcDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGASTLLFLPLAHAFArliqvgvvhARATMahcadtkNL 260
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYG---------MTAVM-------NL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 261 vAELQDFK----PTFVLSVprVFEKVyngarqkaeaegkgkifdRAEKVAIawseaqeLPGGPGLGLraqhALFDKLVYR 336
Cdd:PRK06710 271 -SIMQGYKmvliPKFDMKM--VFEAI------------------KKHKVTL-------FPGAPTIYI----ALLNSPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 337 KLRAAmggRCRDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTGTRI-GTVGRPLP-----------G 403
Cdd:PRK06710 319 EYDIS---SIRACISGSAPLPVEVQEKFETVtGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPdteamimsletG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 404 VTIRIDDDGEVLIAGDIVFQGYWHNDAATAeAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVtAGGKNVAPAVLEDQV 483
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEEVL 473
|
490 500 510
....*....|....*....|....*....|..
gi 2504840381 484 RAHPLISQCVVVGDRQPF----IAALVTIDEE 511
Cdd:PRK06710 474 YEHEKVQEVVTIGVPDPYrgetVKAFVVLKEG 505
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
21-516 |
2.25e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 140.06 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 21 PVWENAEVAPDTVQFVrpgagtDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtlFDYAIWAAGAVTV 100
Cdd:PRK07788 54 LVAHAARRAPDRAALI------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRG---FVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 101 PIY---ETSSAEQAAWILGDSGAVAVVVESTaHATLVAGVRDRLPDLReVWQidlGAVDDLVAAGASVDR-AEVETRRSL 176
Cdd:PRK07788 125 RIIllnTGFSGPQLAEVAAREGVKALVYDDE-FTDLLSALPPDLGRLR-AWG---GNPDDDEPSGSTDETlDDLIAGSST 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDVAT----IIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFarliqvGVVHARATMA 252
Cdd:PRK07788 200 APLPKPPKpggiVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVP--FRAGETTLLPAPMFHAT------GWAHLTLAMA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HCA--------DTKNLVAELQDFKPTFVLSVP----RVFEkvyngarqkAEAEGKGKIFDRAEK-VAIAWSeaqelPGGP 319
Cdd:PRK07788 272 LGStvvlrrrfDPEATLEDIAKHKATALVVVPvmlsRILD---------LGPEVLAKYDTSSLKiIFVSGS-----ALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 320 GLGLRAQHALfdklvyrklraamggrcrdaisggaplgarlghffrgvGVTICEGYGLTETSPAAAANlPTGTRI--GTV 397
Cdd:PRK07788 338 ELATRALEAF--------------------------------------GPVLYNLYGSTEVAFATIAT-PEDLAEapGTV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 398 GRPLPGVTIRIDDD----------GEVLIAGDIVFQGYwhNDAATAEAIttDGWFRTGDLGQLDENGYLSITGRKKEIIV 467
Cdd:PRK07788 379 GRPPKGVTVKILDEngnevprgvvGRIFVGNGFPFEGY--TDGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 468 TaGGKNVAPAVLEDQVRAHPLISQCVVVG--DRQPF--IAALV------TIDEEALPKW 516
Cdd:PRK07788 455 S-GGENVFPAEVEDLLAGHPDVVEAAVIGvdDEEFGqrLRAFVvkapgaALDEDAIKDY 512
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
45-568 |
7.32e-35 |
|
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: 139.13 E-value: 7.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 45 REDVTCRQFRDEVVAVAQGLIAAG-VSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWIL-------- 115
Cdd:cd17632 65 FETITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILaeteprll 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 116 --------------GDSGAVAVVV------ESTAHATLVAGVRDRLPDL-REVWQIDLGAVDDLVAAGASVDRAEVETrr 174
Cdd:cd17632 145 avsaehldlaveavLEGGTPPRLVvfdhrpEVDAHRAALESARERLAAVgIPVTTLTLIAVRGRDLPPAPLFRPEPDD-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 175 slskaDDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNlFRQGASTLLFLPLAHAFARLIQVGVVHARAT--MA 252
Cdd:cd17632 223 -----DPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDI-RPPASITLNFMPMSHIAGRISLYGTLARGGTayFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HCADTKNLVAELQDFKPTFVLSVPRVFEKVYngarQKAEAEGKGKIFDRAEKVAIAWSEAQElpggpglgLRAQhalfdk 332
Cdd:cd17632 297 AASDMSTLFDDLALVRPTELFLVPRVCDMLF----QRYQAELDRRSVAGADAETLAERVKAE--------LRER------ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 333 lvyrklraAMGGRCRDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSpaaaanlpTGTRIGTVGRPlPGVTIRIDD- 410
Cdd:cd17632 359 --------VLGGRLLAAVCGSAPLSAEMKAFMESLlDLDLHDGYGSTEAG--------AVILDGVIVRP-PVLDYKLVDv 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 -------------DGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPA 477
Cdd:cd17632 422 pelgyfrtdrphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVA 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 478 VLEDQVRAHPLISQCVVVG--DRQPFIAALVTIDEealpkwlAGQGRPettsmaelreDAALRAEVQSAIdqanQAVSKA 555
Cdd:cd17632 502 RLEAVFAASPLVRQIFVYGnsERAYLLAVVVPTQD-------ALAGED----------TARLRAALAESL----QRIARE 560
|
570
....*....|...
gi 2504840381 556 EAIKVFRIlPQDF 568
Cdd:cd17632 561 AGLQSYEI-PRDF 572
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
44-496 |
1.87e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 135.64 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 44 AREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAV 123
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VVEStahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCVLTHR 203
Cdd:cd05971 83 VTDG---------------------------------------------------SDDPALIIYTSGTTGPPKGALHAHR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 204 NIYSDIANaVPVLPNLFRQGAStLLFLPlahafarliqvgvvharatmahcADTKNLVAELQDFKPTFVLSVPRVFEKvy 283
Cdd:cd05971 112 VLLGHLPG-VQFPFNLFPRDGD-LYWTP-----------------------ADWAWIGGLLDVLLPSLYFGVPVLAHR-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 ngaRQKAEAegkgkifDRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKLVYRKLRAAmggrcrdaISGGAPLGAR-LGH 362
Cdd:cd05971 165 ---MTKFDP-------KAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAI--------ATGGESLGEElLGW 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 363 FFRGVGVTICEGYGLTEtspaaaANLPTGT-------RIGTVGRPLPGVTIRI-DDDGEVLIAGD-----------IVFQ 423
Cdd:cd05971 227 AREQFGVEVNEFYGQTE------CNLVIGNcsalfpiKPGSMGKPIPGHRVAIvDDNGTPLPPGEvgeiavelpdpVAFL 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 424 GYWHNDAATAEAITTDgWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05971 301 GYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR-IGPAEIEECLLKHPAVLMAAVVG 371
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
59-494 |
1.93e-34 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 137.58 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 59 AVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEStAHATLVAGVR 138
Cdd:PRK06155 58 AAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEA-ALLAALEAAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 139 DRLPDLREVWQID---LGAVD------DLVAAGASVDRAEVetrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIYSDI 209
Cdd:PRK06155 137 PGDLPLPAVWLLDapaSVSVPagwstaPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 210 ANAVPVLpnlfRQGASTLLF--LPLAH--AFARLIQVGVVHARATMAHCADTKNLVAELQDFKPTFVLsvprvfekvYNG 285
Cdd:PRK06155 210 RNSAEDL----EIGADDVLYttLPLFHtnALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTY---------LLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 286 A------RQKAEAEgkgkifDRAEKVAIAWSeaqelPGGPGlglraqhalfdklvyrKLRAAMGGRCrdaisggaplgar 359
Cdd:PRK06155 277 AmvsillSQPARES------DRAHRVRVALG-----PGVPA----------------ALHAAFRERF------------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 360 lghffrgvGVTICEGYGLTETSPAAAANLPTgTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVF---QGYW 426
Cdd:PRK06155 317 --------GVDLLDGYGSTETNFVIAVTHGS-QRPGSMGRLAPGFEARVVDEhdqelpdgepGELLLRADEPFafaTGYF 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 427 HNDAATAEAiTTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVV 494
Cdd:PRK06155 388 GMPEKTVEA-WRNLWFHTGDRVVRDADGWFRFVDRIKDAI-RRRGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
30-496 |
2.08e-34 |
|
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: 137.27 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 30 PDTVQFVRPGAGtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAE 109
Cdd:cd17642 31 PGTIAFTDAHTG----VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 110 QAAWILGDSGAvAVVVESTAHATLVAGVRDRLPDLREVWQID-------LGAVDDLVAAGASVDRAEVE-TRRSLSKADD 181
Cdd:cd17642 107 ELDHSLNISKP-TIVFCSKKGLQKVLNVQKKLKIIKTIIILDskedykgYQCLYTFITQNLPPGFNEYDfKPPSFDRDEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 182 VATIIYTSGTTGRPKGCVLTHRNIYSDIANAV-PVLPNLFRQGASTLLFLPLAHAFARLIQVG--VVHARATMAHCADTK 258
Cdd:cd17642 186 VALIMNSSGSTGLPKGVQLTHKNIVARFSHARdPIFGNQIIPDTAILTVIPFHHGFGMFTTLGylICGFRVVLMYKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 259 NLVAELQDFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekvaiawseaqelpggpglGLRAQHALFDKLVYRKL 338
Cdd:cd17642 266 LFLRSLQDYKVQSALLVPTLF------------------------------------------AFFAKSTLVDKYDLSNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 339 RaamggrcrDAISGGAPLGARLGHFF-RGVGVT-ICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDD------ 410
Cdd:cd17642 304 H--------EIASGGAPLSKEVGEAVaKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDldtgkt 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 -----DGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRA 485
Cdd:cd17642 376 lgpneRGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLI-KYKGYQVPPAELESILLQ 454
|
490
....*....|.
gi 2504840381 486 HPLISQCVVVG 496
Cdd:cd17642 455 HPKIFDAGVAG 465
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-518 |
2.18e-34 |
|
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: 133.76 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIysdIANA-VPVLPNLFRQGASTLLFLPLAHAFARLIQVGVVHARAtmAHC---- 254
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNE---VYNAwMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG--AHVvlag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 -------ADTKNLVAELQDFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekvaiawSEAQELPGGPGLGlraqh 327
Cdd:cd05944 77 pagyrnpGLFDNFWKLVERYRITSLSTVPTVY------------------------------AALLQVPVNADIS----- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 328 alfdklvyrKLRAAMggrcrdaiSGGAPLGARLGHFFR-GVGVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVT 405
Cdd:cd05944 122 ---------SLRFAM--------SGAAPLPVELRARFEdATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYAR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 406 IRI---------------DDDGEVLIAGDIVFQGYWHNDAATaEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaG 470
Cdd:cd05944 185 VRIkvldgvgrllrdcapDEVGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-G 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 471 GKNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAAL----------VTIDEEALPKWLA 518
Cdd:cd05944 263 GHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELpvayvqlkpgAVVEEEELLAWAR 320
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
181-516 |
3.16e-34 |
|
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: 132.62 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRN---IYSDIANAVPVlpnlfRQGASTLLFLPLAHAFArliqvgvvharatmahcadt 257
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQtlrAAAAWADCADL-----TEDDRYLIINPFFHTFG-------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 knlvaelqdFKPTFVLSVprvfekvYNGARQKAEAegkgkIFD-RAEKVAIAWSEAQELPGGPGLglraQHALFDKLVYR 336
Cdd:cd17638 56 ---------YKAGIVACL-------LTGATVVPVA-----VFDvDAILEAIERERITVLPGPPTL----FQSLLDHPGRK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 337 KLRAAmggRCRDAISGGAPLGARLGHFFRG-VGV-TICEGYGLTEtspaaaANLPTGTRIG--------TVGRPLPGVTI 406
Cdd:cd17638 111 KFDLS---SLRAAVTGAATVPVELVRRMRSeLGFeTVLTAYGLTE------AGVATMCRPGddaetvatTCGRACPGFEV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 407 RIDDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVtAGGKNVAPAVLEDQVRAH 486
Cdd:cd17638 182 RIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAEH 260
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2504840381 487 PLISQCVVVG---DR-----QPFIAAL--VTIDEEALPKW 516
Cdd:cd17638 261 PGVAQVAVIGvpdERmgevgKAFVVARpgVTLTEEDVIAW 300
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
22-496 |
4.22e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 135.97 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 22 VWEN-AEVAPDTVQFVRPGAGTDAREdVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTV 100
Cdd:PRK08008 12 MWDDlADVYGHKTALIFESSGGVVRR-YSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 101 PIYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLREVWQIDlgAVDDLVAAGASVDR------AEVETRR 174
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTR--VALPADDGVSSFTQlkaqqpATLCYAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 175 SLSkADDVATIIYTSGTTGRPKGCVLTHRNI-----YSDIANA-------VPVLPNL---FRQGAStllfLPLAHAFARL 239
Cdd:PRK08008 169 PLS-TDDTAEILFTSGTTSRPKGVVITHYNLrfagyYSAWQCAlrdddvyLTVMPAFhidCQCTAA----MAAFSAGATF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 240 IQVGVVHARAtmahcadtknLVAELQDFKPTFVLSVPRVFEKVyngARQKAEAegkgkiFDRaekvaiawseaqelpggp 319
Cdd:PRK08008 244 VLLEKYSARA----------FWGQVCKYRATITECIPMMIRTL---MVQPPSA------NDR------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 320 glglraQHALFDKLVYRKLRAAMggrcRDAisggaplgarlghFFRGVGVTICEGYGLTETSPAAAANLPTGTR-IGTVG 398
Cdd:PRK08008 287 ------QHCLREVMFYLNLSDQE----KDA-------------FEERFGVRLLTSYGMTETIVGIIGDRPGDKRrWPSIG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 399 RPLPGVTIRI-DDDGEVLIAGDI------------VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEI 465
Cdd:PRK08008 344 RPGFCYEAEIrDDHNRPLPAGEIgeicikgvpgktIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNM 423
|
490 500 510
....*....|....*....|....*....|.
gi 2504840381 466 IvTAGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK08008 424 I-KRGGENVSCVELENIIATHPKIQDIVVVG 453
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
55-496 |
6.18e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 135.32 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 55 DEVVAVAQGLIAA-GVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPI-YETSSAEQAAwILGDsgavavvvestAHAT 132
Cdd:PRK09088 29 DALVGRLAAVLRRrGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnWRLSASELDA-LLQD-----------AEPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 133 LVAGvRDRLPDLREVwqidlgaVDDLVAAGASVDRAEVETRRSLSkADDVATIIYTSGTTGRPKGCVLTHRNIYSdiana 212
Cdd:PRK09088 97 LLLG-DDAVAAGRTD-------VEDLAAFIASADALEPADTPSIP-PERVSLILFTSGTSGQPKGVMLSERNLQQ----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 213 vpvlpnlfrqgastllflpLAHAFARLIQVG---VVHARATMAHcadtknLVAELQDFKPTFV----LSVPRVFEKVYNG 285
Cdd:PRK09088 163 -------------------TAHNFGVLGRVDahsSFLCDAPMFH------IIGLITSVRPVLAvggsILVSNGFEPKRTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 286 ARQKAEAEGKGKIFDRAEKVAIawseaqelpggpglgLRAQHAlFDKLVYRKLRAAmggrcrdaISGGAPLGARLGHFFR 365
Cdd:PRK09088 218 GRLGDPALGITHYFCVPQMAQA---------------FRAQPG-FDAAALRHLTAL--------FTGGAPHAAEDILGWL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 366 GVGVTICEGYGLTETS-----PAAAANLptGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDA 430
Cdd:PRK09088 274 DDGIPMVDGFGMSEAGtvfgmSVDCDVI--RAKAGAAGIPTPTVQTRVVDDqgndcpagvpGELLLRGPNLSPGYWRRPQ 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 431 ATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK09088 352 ATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
43-496 |
6.75e-34 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 134.13 E-value: 6.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 43 DAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVA 122
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 VVVEstahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:cd05919 86 VVTS----------------------------------------------------ADDIAYLLYSSGTTGPPKGVMHAH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDI-ANAVPVL---PN---------LFRQGASTLLFLPLAHAFARLIQVGVVHARATMAhcadtkNLVAelqdFKP 269
Cdd:cd05919 114 RDPLLFAdAMAREALgltPGdrvfssakmFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLA------TLAR----FRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 270 TFVLSVPRVFekvyngARQKAEAEGkgkifdraekvaiawseaqelpggpglglrAQHALFDklvyrklraamggrCRDA 349
Cdd:cd05919 184 TVLYGVPTFY------ANLLDSCAG------------------------------SPDALRS--------------LRLC 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 350 ISGGAPLGARLGHFFRG-VGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAG 418
Cdd:cd05919 214 VSAGEALPRGLGERWMEhFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEeghtippgeeGDLLVRG 293
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 419 DIVFQGYWHNdAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05919 294 PSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPAVAEAAVVA 369
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
24-591 |
7.11e-34 |
|
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: 135.83 E-value: 7.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGvSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIY 103
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAW---ILGDSGAVAVVVeSTAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGASVDRAEvetrrslskAD 180
Cdd:cd05931 80 PPTPGRHAERlaaILADAGPRVVLT-TAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD---------PD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIysdIANAVPVLPNLFRQGASTLLF-LPLAHAFArLIQvGVVHARATMAHCadtkn 259
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNL---LANVRQIRRAYGLDPGDVVVSwLPLYHDMG-LIG-GLLTPLYSGGPS----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 260 lvaelqdfkptfVLSVPRVFekVYNGARQ-KAEAEGKGKIfdraekvaiawseaqelPGGPGLGlraqhalFDKLVYRKL 338
Cdd:cd05931 220 ------------VLMSPAAF--LRRPLRWlRLISRYRATI-----------------SAAPNFA-------YDLCVRRVR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 339 RAAMGG----RCRDAISGGAPLGAR-LGHF---FRGVGV---TICEGYGLTETS-------------------------- 381
Cdd:cd05931 262 DEDLEGldlsSWRVALNGAEPVRPAtLRRFaeaFAPFGFrpeAFRPSYGLAEATlfvsggppgtgpvvlrvdrdalagra 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 382 PAAAANLPTGTRIGTVGRPLPGVTIRIDDD-----------GEVLIAGDIVFQGYWHNDAATAE------AITTDGWFRT 444
Cdd:cd05931 342 VAVAADDPAARELVSCGRPLPDQEVRIVDPetgrelpdgevGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 445 GDLGQLDEnGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLisqcVVVGDRqpfiAALVTIDEEalpkwlagqGRPE 524
Cdd:cd05931 422 GDLGFLHD-GELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHP----ALRPGC----VAAFSVPDD---------GEER 482
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 525 TTSMAELREDAAlRAEVQSAIDQANQAVSKAEAIKVFRILpqdFTEAtGEL--TPSLKVKRQVVHKTYA 591
Cdd:cd05931 483 LVVVAEVERGAD-PADLAAIAAAIRAAVAREHGVAPADVV---LVRP-GSIprTSSGKIQRRACRAAYL 546
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
49-496 |
8.09e-34 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 135.70 E-value: 8.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRV---GLMSRTRYEWTLfdyAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVaiaALNSDLYLEWLL---AVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 ESTAHATLVAGVRDRLPDLRevWQIDLGAVDDLVAAGA-SVDRAEVETRRSLSKA--------DDVATIIYTSGTTGRPK 196
Cdd:PLN02860 111 DETCSSWYEELQNDRLPSLM--WQVFLESPSSSVFIFLnSFLTTEMLKQRALGTTeldyawapDDAVLICFTSGTTGRPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 197 GCVLTHRniysdiANAVPVLPNLFRQGAST----LLFLPLAH------AFARLIqVGVVHaraTMAHCADTKNLVAELQD 266
Cdd:PLN02860 189 GVTISHS------ALIVQSLAKIAIVGYGEddvyLHTAPLCHigglssALAMLM-VGACH---VLLPKFDAKAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 267 FKPTFVLSVPRVFEKVYNGARQKaeaeGKGKIFDRAEKVaiawseaqeLPGGPGLGLRAQHALFDKLVYRKLRAAMGgrC 346
Cdd:PLN02860 259 HNVTSMITVPAMMADLISLTRKS----MTWKVFPSVRKI---------LNGGGSLSSRLLPDAKKLFPNAKLFSAYG--M 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAplgarlghfFRGVGVTICEGYGLTETSPAAAANLPTGTRIGT-VGRPLPGVTIRIDDD-----GEVLIAGDI 420
Cdd:PLN02860 324 TEACSSLT---------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAPHVELKIGLDessrvGRILTRGPH 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 421 VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PLN02860 395 VMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-523 |
4.21e-33 |
|
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: 132.18 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 57 VVAVAQGLIAAGVSPGDR--VGLMSRTRYEWTLFD--YAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEstahAT 132
Cdd:cd05922 3 VSAAASALLEAGGVRGERvvLILPNRFTYIELSFAvaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLAD----AG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 133 LVAGVRDRLPDLRevwqiDLGAV---DDLVAAGASVDRAEVEtrrslskADDVATIIYTSGTTGRPKGCVLTHRNIYSDI 209
Cdd:cd05922 79 AADRLRDALPASP-----DPGTVldaDGIRAARASAPAHEVS-------HEDLALLLYTSGSTGSPKLVRLSHQNLLANA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 210 ANAVPVLPNLFRQGASTLLFLPLAHAFARLIQVGVVHARATMAhcadtknlvaelqdfkPTFVLsvprvfekvyngarqk 289
Cdd:cd05922 147 RSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT----------------NDGVL---------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 290 aeaegkgkifDRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKLVYRKLR--AAMGGRCRDAisggapLGARLGHFFRGV 367
Cdd:cd05922 195 ----------DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRylTQAGGRLPQE------TIARLRELLPGA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 368 GVTICegYGLTETSpAAAANLP---TGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAE 434
Cdd:cd05922 259 QVYVM--YGQTEAT-RRMTYLPperILEKPGSIGLAIPGGEFEILDDdgtptppgepGEIVHRGPNVMKGYWNDPPYRRK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 435 AITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGDRQPF---IAALVT---- 507
Cdd:cd05922 336 EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNR-ISPTEIEAAARSIGLIIEAAAVGLPDPLgekLALFVTapdk 414
|
490
....*....|....*.
gi 2504840381 508 IDEEALPKWLAGQGRP 523
Cdd:cd05922 415 IDPKDVLRSLAERLPP 430
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
49-496 |
5.12e-33 |
|
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: 132.42 E-value: 5.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV--E 126
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVdrE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 STAHATLVAGVRDRLPdlrevwqidLGAVDDlvaagasvdraevetrrslskaDDVATIIYTSGTTGRPKGCVLTHRNIY 206
Cdd:cd12118 111 FEYEDLLAEGDPDFEW---------IPPADE----------------------WDPIALNYTSGTTGRPKGVVYHHRGAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 207 -SDIANavpVLPNLFRQGASTLLFLPLAHAFARLIQVGVVHARATMAHC--ADTKNLVAELQDFKPTFVLSVPRVFEKVY 283
Cdd:cd12118 160 lNALAN---ILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLrkVDAKAIYDLIEKHKVTHFCGAPTVLNMLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 NGARqkaeaegkgkifdraekvaiawSEAQELPGgpglglRAQhalfdklvyrklraamggrcrdAISGGAPLGARLGHF 363
Cdd:cd12118 237 NAPP----------------------SDARPLPH------RVH----------------------VMTAGAPPPAAVLAK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 364 FRGVGVTICEGYGLTETSPAAAA--------NLPTGTR--------IGTVG------------RPLP--GVTIridddGE 413
Cdd:cd12118 267 MEELGFDVTHVYGLTETYGPATVcawkpewdELPTEERarlkarqgVRYVGleevdvldpetmKPVPrdGKTI-----GE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 414 VLIAGDIVFQGYWHNDAATAEAiTTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCV 493
Cdd:cd12118 342 IVFRGNIVMKGYLKNPEATAEA-FRGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVLYKHPAVLEAA 419
|
...
gi 2504840381 494 VVG 496
Cdd:cd12118 420 VVA 422
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
48-470 |
8.91e-33 |
|
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: 132.41 E-value: 8.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtlFDYAIWA---AGAVTVP-----IYETSSAEQA----AWIL 115
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNED---FIPAFWAcvlAGFVPAPltvppTYDEPNARLRklrhIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 116 GDSGAVavvvesTAHATLVAGVRDrlpdLREVWQIDlgavDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRP 195
Cdd:cd05906 117 LGSPVV------LTDAELVAEFAG----LETLSGLP----GIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 196 KGCVLTHRNIYSDIAnAVPVLPNLFRQGAsTLLFLPLAHAfarliqVGVV--HARATMAHCaDTKNLVAELqdfkptfVL 273
Cdd:cd05906 183 KAVPLTHRNILARSA-GKIQHNGLTPQDV-FLNWVPLDHV------GGLVelHLRAVYLGC-QQVHVPTEE-------IL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 274 SVPRVFekvyngarqkaeaegkgkiFDRAEK--VAIAWSeaqelpggPG--LGLraqhaLFDKLVYRKLRAAMGGRCRDA 349
Cdd:cd05906 247 ADPLRW-------------------LDLIDRyrVTITWA--------PNfaFAL-----LNDLLEEIEDGTWDLSSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 350 ISGGAPLGARLGHFF------RGVGVT-ICEGYGLTETS-------PAAAANLPTGTRIGTVGRPLPGVTIRI-DDDGEV 414
Cdd:cd05906 295 VNAGEAVVAKTIRRLlrllepYGLPPDaIRPAFGMTETCsgviysrSFPTYDHSQALEFVSLGRPIPGVSMRIvDDEGQL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 415 L---------IAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDeNGYLSITGRKKEIIVTAG 470
Cdd:cd05906 375 LpegevgrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNG 438
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
181-496 |
5.84e-32 |
|
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: 126.23 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSdiANAVPVLPNLFRQGASTLLFLPLAHAfarliqVGVVHARATMahCADTKNL 260
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIA--ANLQLIHAMGLTEADVYLNMLPLFHI------AGLNLALATF--HAGGANV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 261 VAE----------LQDFKPTFVLSVPRVFekvyngarqkaeaegkGKIFDRAEKVAIAWSEaqelpggpglglraqhalf 330
Cdd:cd17637 71 VMEkfdpaealelIEEEKVTLMGSFPPIL----------------SNLLDAAEKSGVDLSS------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 331 dklvyrkLRAAMGGRCRDAIsggaplgarlGHFFRGVGVTICEGYGLTETSpAAAANLPTGTRIGTVGRPLPGVTIRIDD 410
Cdd:cd17637 116 -------LRHVLGLDAPETI----------QRFEETTGATFWSLYGQTETS-GLVTLSPYRERPGSAGRPGPLVRVRIVD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 D----------GEVLIAGDIVFQGYWHNDAATAEAiTTDGWFRTGDLGQLDENGYLSITGRK--KEIIVTaGGKNVAPAV 478
Cdd:cd17637 178 DndrpvpagetGEIVVRGPLVFQGYWNLPELTAYT-FRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAE 255
|
330
....*....|....*...
gi 2504840381 479 LEDQVRAHPLISQCVVVG 496
Cdd:cd17637 256 VEKVILEHPAIAEVCVIG 273
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
18-496 |
1.20e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.94 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 18 LTDPVWENAEVAPDTVQFVRPGAG---TDAREDVTCRQfrdevvaVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWA 94
Cdd:PLN02246 25 LHDYCFERLSEFSDRPCLIDGATGrvyTYADVELLSRR-------VAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 95 AGAVTV---PIYeTSS--AEQAAwilgDSGAVAVVVESTAHatlvagvrDRLPDLRE-----VWQIDlGAVDDLVAAGAS 164
Cdd:PLN02246 98 RGAVTTtanPFY-TPAeiAKQAK----ASGAKLIITQSCYV--------DKLKGLAEddgvtVVTID-DPPEGCLHFSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 165 VDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVP-VLPNL-FRQGASTLLFLPLAHAFArLIQV 242
Cdd:PLN02246 164 TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLyFHSDDVILCVLPMFHIYS-LNSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 243 GVVHARATMA----HCADTKNLVAELQDFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekVAIAWSEAQElpgg 318
Cdd:PLN02246 243 LLCGLRVGAAilimPKFEIGALLELIQRHKVTIAPFVPPIV-------------------------LAIAKSPVVE---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 319 pglglraQHALfdklvyRKLRAAMggrcrdaiSGGAPLGARLGHFFRGV--GVTICEGYGLTETSPAAAANL-----PTG 391
Cdd:PLN02246 294 -------KYDL------SSIRMVL--------SGAAPLGKELEDAFRAKlpNAVLGQGYGMTEAGPVLAMCLafakePFP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 392 TR---IGTVGR--------PLPGVTIRIDDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITG 460
Cdd:PLN02246 353 VKsgsCGTVVRnaelkivdPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVD 432
|
490 500 510
....*....|....*....|....*....|....*.
gi 2504840381 461 RKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PLN02246 433 RLKELIKYKGFQ-VAPAELEALLISHPSIADAAVVP 467
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
15-600 |
1.98e-31 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 129.23 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 15 AANLTDPVWENAEVAPDTVQFVRPGAGTDAREdVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWA 94
Cdd:PRK08180 38 PRRLTDRLVHWAQEAPDRVFLAERGADGGWRR-LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 95 AGAVTVPI---YETSSAE-----------QAAWILGDSGAV---AVVVESTAHATLVAgVRDRLPDLREVwqidlgAVDD 157
Cdd:PRK08180 117 AGVPYAPVspaYSLVSQDfgklrhvlellTPGLVFADDGAAfarALAAVVPADVEVVA-VRGAVPGRAAT------PFAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 158 LVAA--GASVDRAEVETRrslskADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGASTLLFLPLAHA 235
Cdd:PRK08180 190 LLATppTAAVDAAHAAVG-----PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLPWNHT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 236 FARLIQVGVV----------HARATMAHCADTknlVAELQDFKPTFVLSVPRVFEKVYNGARQKAE-AEgkgKIFDRAEK 304
Cdd:PRK08180 265 FGGNHNLGIVlynggtlyidDGKPTPGGFDET---LRNLREISPTVYFNVPKGWEMLVPALERDAAlRR---RFFSRLKL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 305 VAIAwseaqelpgGPGLglrAQHaLFDKLvyrklraamggrcrDAISGgAPLGARlghffrgvgVTICEGYGLTETSPAA 384
Cdd:PRK08180 339 LFYA---------GAAL---SQD-VWDRL--------------DRVAE-ATCGER---------IRMMTGLGMTETAPSA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 385 AANLPTGTRIGTVGRPLPGVTIRI---DDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQL-DEN----GyL 456
Cdd:PRK08180 382 TFTTGPLSRAGNIGLPAPGCEVKLvpvGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAdperG-L 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 457 SITGRKKEIIVTAGGK--NVAPavledqVRAH------PLISQCVVVGDRQPFIAALVTIDEEALpKWLAGQgrPETTSM 528
Cdd:PRK08180 461 MFDGRIAEDFKLSSGTwvSVGP------LRARavsagaPLVQDVVITGHDRDEIGLLVFPNLDAC-RRLAGL--LADASL 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 529 AELREDAALRAEVQSAIDQAN-QAVSKAEAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYRG 600
Cdd:PRK08180 532 AEVLAHPAVRAAFRERLARLNaQATGSSTRVARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYAD 604
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
64-584 |
3.57e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 128.24 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 64 LIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAhATLVAGVRDRLPd 143
Cdd:PRK06178 75 LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRAETS- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 144 LREVWQIDLGAV-----------------------DDLVAAGASVDRAEVETRRSLskaDDVATIIYTSGTTGRPKGCVL 200
Cdd:PRK06178 153 LRHVIVTSLADVlpaeptlplpdslraprlaaagaIDLLPALRACTAPVPLPPPAL---DALAALNYTGGTTGMPKGCEH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 201 THRNIYSDIANAVPV-------------LPNLFRQGASTLLFLPL-------------AHAFARLIQvgvvHARATmaHC 254
Cdd:PRK06178 230 TQRDMVYTAAAAYAVavvggedsvflsfLPEFWIAGENFGLLFPLfsgatlvllarwdAVAFMAAVE----RYRVT--RT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 ADTKNLVAELQDFkptfvlsvPRVFEkvyngarqkaeaegkgkiFDraekvaiawseaqelpggpglgLRA-QHALFDKL 333
Cdd:PRK06178 304 VMLVDNAVELMDH--------PRFAE------------------YD----------------------LSSlRQVRVVSF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 334 VyRKLRAAMGGRCRDAisggaplgarlghffrgVGVTICEG-YGLTETSpaAAANLPTGTRIGT---------VGRPLPG 403
Cdd:PRK06178 336 V-KKLNPDYRQRWRAL-----------------TGSVLAEAaWGMTETH--TCDTFTAGFQDDDfdllsqpvfVGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 404 VTIRIDD-----------DGEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGK 472
Cdd:PRK06178 396 TEFKICDfetgellplgaEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 473 NVAPAVLEDQVRAHPLISQCVVVGdrQPfiaalvtiDEEalpkwlAGQgrpETTSMAELREDAALRAEVQSAIDQANQAV 552
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVG--RP--------DPD------KGQ---VPVAFVQLKPGADLTAAALQAWCRENMAV 534
|
570 580 590
....*....|....*....|....*....|..
gi 2504840381 553 SKAEAIKVFRILPqdfTEATGeltpslKVKRQ 584
Cdd:PRK06178 535 YKVPEIRIVDALP---MTATG------KVRKQ 557
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-521 |
1.67e-29 |
|
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: 122.56 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 18 LTDPVWENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGA 97
Cdd:COG1021 27 LGDLLRRRAERHPDRI------AVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 98 VtvPIY--------ETSS-AEQaawilgdSGAVAVVV----ESTAHATLVAGVRDRLPDLREVwqIDLGAVDDLVAAgAS 164
Cdd:COG1021 101 I--PVFalpahrraEISHfAEQ-------SEAVAYIIpdrhRGFDYRALARELQAEVPSLRHV--LVVGDAGEFTSL-DA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 165 VDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRN-IYS-----DIANavpvlpnlFRQGASTLLFLPLAHAFAR 238
Cdd:COG1021 169 LLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSvrasaEICG--------LDADTVYLAALPAAHNFPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 239 LIQV--GVVHARATMAHCADTKNLVA-EL-QDFKPTFVLSVPrvfekvyngarqkaeaegkgkifdraeKVAIAWSEAQE 314
Cdd:COG1021 241 SSPGvlGVLYAGGTVVLAPDPSPDTAfPLiERERVTVTALVP---------------------------PLALLWLDAAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 315 lpggpglglRAQHALFD-KLVYrklraamggrcrdaiSGGAPLGARLghfFRGV----GVTICEGYGLTE-----TSPAA 384
Cdd:COG1021 294 ---------RSRYDLSSlRVLQ---------------VGGAKLSPEL---ARRVrpalGCTLQQVFGMAEglvnyTRLDD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 385 aanlPTGTRIGTVGRPL-PGVTIRI-DDD---------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDEN 453
Cdd:COG1021 347 ----PEEVILTTQGRPIsPDDEVRIvDEDgnpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPD 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504840381 454 GYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFI-----AALVTIDEE----ALPKWLAGQG 521
Cdd:COG1021 423 GYLVVEGRAKDQINR-GGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerscAFVVPRGEPltlaELRRFLRERG 498
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
38-500 |
2.01e-29 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 122.20 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 38 PGAG--TDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWIL 115
Cdd:TIGR03098 14 PDATalVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 116 GDSGaVAVVVESTAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGASVdrAEVETRRSLSKA--------DDVATIIY 187
Cdd:TIGR03098 94 ADCN-VRLLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEP--ASWPKLLALGDAdpphpvidSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 188 TSGTTGRPKGCVLTHRNIysdIANAVPVLPNLFRQGASTLL-FLPLA--HAFARLIQVGVVHARATMAHCADTKNLVAEL 264
Cdd:TIGR03098 171 TSGSTGRPKGVVLSHRNL---VAGAQSVATYLENRPDDRLLaVLPLSfdYGFNQLTTAFYVGATVVLHDYLLPRDVLKAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 265 QDFKPTFVLSVPRVFEKVYNgarqkaeaegkgkifdraekvaIAWSEAqelpggpglglraqhalfdklVYRKLRaamgg 344
Cdd:TIGR03098 248 EKHGITGLAAVPPLWAQLAQ----------------------LDWPES---------------------AAPSLR----- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 345 rcRDAISGGA---PLGARLGHFFRGVGVTICegYGLTETspAAAANLP---TGTRIGTVGRPLPGVTIRI---------- 408
Cdd:TIGR03098 280 --YLTNSGGAmprATLSRLRSFLPNARLFLM--YGLTEA--FRSTYLPpeeVDRRPDSIGKAIPNAEVLVlredgsecap 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 409 DDDGEVLIAGDIVFQGYWHNDAATAEAittdgwFR-----------------TGDLGQLDENGYLSITGRKKEIIVTAGG 471
Cdd:TIGR03098 354 GEEGELVHRGALVAMGYWNDPEKTAER------FRplppfpgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGY 427
|
490 500
....*....|....*....|....*....
gi 2504840381 472 KnVAPAVLEDQVRAHPLISQCVVVGDRQP 500
Cdd:TIGR03098 428 R-VSPTEVEEVAYATGLVAEAVAFGVPDP 455
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-496 |
2.14e-29 |
|
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: 121.85 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGTDaredVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYET 105
Cdd:cd05923 11 ASRAPDACAIADPARGLR----LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 106 SSAEQAAWILGDSGAVAVVVEstahatlvagvrdrlpDLREVWQIDLGAVDDLVAAGASVDRAEVETRRSLSKA-----D 180
Cdd:cd05923 87 LKAAELAELIERGEMTAAVIA----------------VDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDpprepE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGASTLLFLPLAHAFArliqvgvvharatmahcadtknl 260
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIG----------------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 261 vaelqdFKPTFVLSVprvfekVYNGARQKAEAegkgkiFDRAEkvAIAWSEAQELPGgpglgLRAQHALFDKLVYRKLRA 340
Cdd:cd05923 208 ------FFAVLVAAL------ALDGTYVVVEE------FDPAD--ALKLIEQERVTS-----LFATPTHLDALAAAAEFA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 341 AMG-GRCRDAISGGA----PLGARLGHFFRGVGVTIcegYGLTETSPAAAANLPtgtRIGTVGRP-------------LP 402
Cdd:cd05923 263 GLKlSSLRHVTFAGAtmpdAVLERVNQHLPGEKVNI---YGTTEAMNSLYMRDA---RTGTEMRPgffsevrivriggSP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 403 GVTIRIDDDGEVLIA--GDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLE 480
Cdd:cd05923 337 DEALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQ-DGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIE 414
|
490
....*....|....*.
gi 2504840381 481 DQVRAHPLISQCVVVG 496
Cdd:cd05923 415 RVLSRHPGVTEVVVIG 430
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
26-514 |
4.90e-29 |
|
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: 120.91 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGTDARE-DVTCRQfrdevvaVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYE 104
Cdd:cd17651 5 AARTPDAPALVAEGRRLTYAElDRRANR-------LAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 105 TSSAEQAAWILGDSGAVAVVVEstAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGAsvdraevetrrslskADDVAT 184
Cdd:cd17651 78 AYPAERLAFMLADAGPVLVLTH--PALAGELAVELVAVTLLDQPGAAAGADAEPDPALD---------------ADDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 185 IIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFArliqvgVVHARATMAHCAdtknlvael 264
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANLVAWQARASS--LGPGARTLQFAGLGFDVS------VQEIFSTLCAGA--------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 265 qdfkpTFVLSVPRVfekvyngaRQKAEAegkgkifdraekvAIAWSEAQelpggpglglRAQHALFDKLVYRKLRAAM-- 342
Cdd:cd17651 204 -----TLVLPPEEV--------RTDPPA-------------LAAWLDEQ----------RISRVFLPTVALRALAEHGrp 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 343 ----GGRCRDAISGGAPL--GARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTGT----RIGTVGRPLPGVTIRIDDD 411
Cdd:cd17651 248 lgvrLAALRYLLTGGEQLvlTEDLREFCAGLpGLRLHNHYGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRVYVLDA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVA 475
Cdd:cd17651 328 alrpvppgvpGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADD-QVKIRGFRIE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2504840381 476 PAVLEDQVRAHPLISQCVVVGDR----QPFIAALVTIDEEALP 514
Cdd:cd17651 407 LGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPV 449
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-535 |
1.17e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 119.80 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 53 FRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVvestAHAT 132
Cdd:PRK12406 17 LAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI----AHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 133 LVAGVRDRLP------------DLREVWQID-------LGAVD--DLVAAGASVDRAEVETRrslskaddvATIIYTSGT 191
Cdd:PRK12406 93 LLHGLASALPagvtvlsvptppEIAAAYRISpalltppAGAIDweGWLAQQEPYDGPPVPQP---------QSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 192 TGRPKGCVLT-----HRNIYSDIANAVPVLPnlfrQGASTLLFLPLAH----AF----ARLIQVGVVHARAtmahcaDTK 258
Cdd:PRK12406 164 TGHPKGVRRAaptpeQAAAAEQMRALIYGLK----PGIRALLTGPLYHsapnAYglraGRLGGVLVLQPRF------DPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 259 NLVAELQDFKPTFVLSVPRVFEKvyngarqkaeaegkgkIFDRAEKVaiawseaqelpggpglglRAQHALfdklvyRKL 338
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPTMFIR----------------LLKLPEEV------------------RAKYDV------SSL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 339 RAAmggrcrdaISGGAPLGArlgHFFRGV----GVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVTIR-IDDDG 412
Cdd:PRK12406 274 RHV--------IHAAAPCPA---DVKRAMiewwGPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKAAPGAELRfVDEDG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 413 EVLIAGDI--VF---QGY----WHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQV 483
Cdd:PRK12406 343 RPLPQGEIgeIYsriAGNpdftYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVL 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 484 RAHPLISQCVVVG--DRQpFIAAL---------VTIDEEA----LPKWLAGQGRPE-TTSMAEL-REDA 535
Cdd:PRK12406 422 HAVPGVHDCAVFGipDAE-FGEALmavvepqpgATLDEADiraqLKARLAGYKVPKhIEIMAELpREDS 489
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
40-520 |
1.99e-28 |
|
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: 118.55 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 40 AGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLM-SRTRyEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDS 118
Cdd:cd12116 5 AVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYlPRSA-RLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 119 GAVAVVVESTAhatlvagvRDRLPDLREVWQidlgavDDLVAAGASVDRAEVETRrslskADDVATIIYTSGTTGRPKGC 198
Cdd:cd12116 84 EPALVLTDDAL--------PDRLPAGLPVLL------LALAAAAAAPAAPRTPVS-----PDDLAYVIYTSGSTGRPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 199 VLTHRNiysdianavpvLPNLFrqgastllflplaHAFARLIQVGvvharatmahcADTKNLVAElqdfKPTFVLSVPRV 278
Cdd:cd12116 145 VVSHRN-----------LVNFL-------------HSMRERLGLG-----------PGDRLLAVT----TYAFDISLLEL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 279 FEKVYNGARqkaeaegkgkifdraekVAIAWSEAQELPGGPGLGLR--------AQHALFDKLVYRKLRAAMGGRcrdAI 350
Cdd:cd12116 186 LLPLLAGAR-----------------VVIAPRETQRDPEALARLIEahsitvmqATPATWRMLLDAGWQGRAGLT---AL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 351 SGGAPLGARLGHFFRGVGVTICEGYGLTETSP-AAAANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGD 419
Cdd:cd12116 246 CGGEALPPDLAARLLSRVGSLWNLYGPTETTIwSTAARVTAAAGPIPIGRPLANTQVYVLDAalrpvppgvpGELYIGGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 420 IVFQGYWHNDAATAEAITTDG-------WFRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQC 492
Cdd:cd12116 326 GVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADG-QVKIRGHRIELGEIEAALAAHPGVAQA 404
|
490 500 510
....*....|....*....|....*....|....*..
gi 2504840381 493 VVVGDRQPFIAALV---------TIDEEALPKWLAGQ 520
Cdd:cd12116 405 AVVVREDGGDRRLVayvvlkagaAPDAAALRAHLRAT 441
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
181-494 |
8.75e-28 |
|
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: 114.67 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLfRQGASTLLFLPLAHAFARL-IQVGVVHARATMAHCADT-- 257
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW-VVGDVTYLPLPATHIGGLWwILTCLIHGGLCVTGGENTty 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 KNLVAELQDFKPTFVLSVPRVFEKVYNgarqkaeaegkgkifdrAEKVAIAWSEaqelpggpglglraqhalfdklvyrK 337
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVS-----------------ELKSANATVP-------------------------S 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 LRAAmggrcrdaISGGAPLGARLGHFFRGVGVT-ICEGYGLTETSpaAAANLPTG---TRIGTVGRPLPGVTIRI-DDDG 412
Cdd:cd17635 119 LRLI--------GYGGSRAIAADVRFIEATGLTnTAQVYGLSETG--TALCLPTDddsIEINAVGRPYPGVDVYLaATDG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 413 EVLIA---GDIVFQ------GYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVtAGGKNVAPAVLEDQV 483
Cdd:cd17635 189 IAGPSasfGTIWIKspanmlGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDEVERIA 266
|
330
....*....|.
gi 2504840381 484 RAHPLISQCVV 494
Cdd:cd17635 267 EGVSGVQECAC 277
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
54-496 |
9.42e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 116.63 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 54 RDEVVAVAqGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTahatl 133
Cdd:PRK07787 28 RSDLAGAA-TAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAP----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 134 vagvrdrlPDLREVWQIDLgavdDLVAAGASvdraevetRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDI---A 210
Cdd:PRK07787 102 --------DDPAGLPHVPV----RLHARSWH--------RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdalA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 211 NAVPVLPNlfrqgaSTLLF-LPLAHAFARLIQV-GVVHARATMAHCAD-TKNLVAELQDFKPTFVLSVPRVFEKVyngar 287
Cdd:PRK07787 162 EAWQWTAD------DVLVHgLPLFHVHGLVLGVlGPLRIGNRFVHTGRpTPEAYAQALSEGGTLYFGVPTVWSRI----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 288 qkaeaegkgkifdrAEKVAIAwseaqelpggpglglraqhalfdklvyRKLRAAmggrcRDAISGGAPLGARLGHFFRGV 367
Cdd:PRK07787 231 --------------AADPEAA---------------------------RALRGA-----RLLVSGSAALPVPVFDRLAAL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 368 -GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDD------------GEVLIAGDIVFQGYWHNDAATAE 434
Cdd:PRK07787 265 tGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEdggpvphdgetvGELQVRGPTLFDGYLNRPDATAA 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 435 AITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK07787 345 AFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
17-500 |
1.42e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.52 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 17 NLTDPVWENAEVAPDTVQFVRPGagtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAG 96
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 97 AVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDlrEVWQIDlgaVDDLVAAGASVDRAEVetrrsl 176
Cdd:PRK06145 77 AVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVID--AAAQAD---SRRLAQGGLEIPPQAA------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFArLIQVGVvharATMAHcad 256
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALG--LTASERLLVVGPLYHVGA-FDLPGI----AVLWV--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 257 tKNLVAELQDFKPTFVL-SVPRvfekvyngarqkaeaegkgkifdraEKVAIAWSEAQELPGGPGLGLRaqhalfDKLVY 335
Cdd:PRK06145 216 -GGTLRIHREFDPEAVLaAIER-------------------------HRLTCAWMAPVMLSRVLTVPDR------DRFDL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 336 RKLRAAMGG-------RCRDaisggaplgarLGHFFRGVgvTICEGYGLTETSpAAAANLPTG---TRIGTVGRPLPGVT 405
Cdd:PRK06145 264 DSLAWCIGGgektpesRIRD-----------FTRVFTRA--RYIDAYGLTETC-SGDTLMEAGreiEKIGSTGRALAHVE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 406 IRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVA 475
Cdd:PRK06145 330 IRIADGagrwlppnmkGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIA 407
|
490 500
....*....|....*....|....*
gi 2504840381 476 PAVLEDQVRAHPLISQCVVVGDRQP 500
Cdd:PRK06145 408 SSEVERVIYELPEVAEAAVIGVHDD 432
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-496 |
2.64e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 115.77 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtLFDyAIWAA---GAVTVPIYETSSAEQAAWILGDSGAVA 122
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPE--FFE-VYWAArrsGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 VVVeSTAHATLVAGVRDRLPDLREVWQIDLGAVD------DLVAAGASVDRAEvETRRslskaddvATIIYTSGTTGRPK 196
Cdd:PRK08276 87 LIV-SAALADTAAELAAELPAGVPLLLVVAGPVPgfrsyeEALAAQPDTPIAD-ETAG--------ADMLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 197 GCV--LTHRNIySDIANAVPVLPNLFRQGASTLLFL---PLAHAfARLIQVGVVHAratMAHcadtknlvaelqdfkpTF 271
Cdd:PRK08276 157 GIKrpLPGLDP-DEAPGMMLALLGFGMYGGPDSVYLspaPLYHT-APLRFGMSALA---LGG----------------TV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 272 VLSvprvfekvyngarQKAEAEGKGKIFDRaEKVaiawSEAQELPggpglglraqhALFDKLVyrKLRAAMGGR-----C 346
Cdd:PRK08276 216 VVM-------------EKFDAEEALALIER-YRV----THSQLVP-----------TMFVRML--KLPEEVRARydvssL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAP----LGARLGHFFrgvGVTICEGYGLTETSPAAAAN----LptgTRIGTVGRPLPGVtIRI-DDDGEVLIA 417
Cdd:PRK08276 265 RVAIHAAAPcpveVKRAMIDWW---GPIIHEYYASSEGGGVTVITsedwL---AHPGSVGKAVLGE-VRIlDEDGNELPP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 418 ---GDIVFQ--GY---WHND-AATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPL 488
Cdd:PRK08276 338 geiGTVYFEmdGYpfeYHNDpEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENLLVTHPK 416
|
....*...
gi 2504840381 489 ISQCVVVG 496
Cdd:PRK08276 417 VADVAVFG 424
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
40-506 |
9.51e-27 |
|
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: 113.91 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 40 AGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG 119
Cdd:cd12114 5 AVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVestahatlvagvrDRLPDLREVWQIDLgAVDDLVAAGASVDRAEVEtrrslSKADDVATIIYTSGTTGRPKGCV 199
Cdd:cd12114 85 ARLVLT-------------DGPDAQLDVAVFDV-LILDLDALAAPAPPPPVD-----VAPDDLAYVIFTSGSTGTPKGVM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHR---NIYSDIANAVPVLPNLFRQGASTL--------LFLPLAhAFARLIQVGVVHARATmAHCADTknlvaeLQDFK 268
Cdd:cd12114 146 ISHRaalNTILDINRRFAVGPDDRVLALSSLsfdlsvydIFGALS-AGATLVLPDEARRRDP-AHWAEL------IERHG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 269 PTFVLSVPRVFEKVYNGARQkaeaegkgkifdraekvaiawseAQELPGGpglglraqhalfdklvyrkLRAAMggrcrd 348
Cdd:cd12114 218 VTLWNSVPALLEMLLDVLEA-----------------------AQALLPS-------------------LRLVL------ 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 349 aISG---GAPLGARLGHFFRGVGVtICEGyGLTETS-----------PAAAANLPtgtrigtVGRPLPGVTIRIDDD--- 411
Cdd:cd12114 250 -LSGdwiPLDLPARLRALAPDARL-ISLG-GATEASiwsiyhpidevPPDWRSIP-------YGRPLANQRYRVLDPrgr 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 -------GEVLIAGDIVFQGYWHNDAATAEAITTDG----WFRTGDLGQLDENGYLSITGRkKEIIVTAGGKNVAPAVLE 480
Cdd:cd12114 320 dcpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGR-RDGQVKVRGYRIELGEIE 398
|
490 500
....*....|....*....|....*.
gi 2504840381 481 DQVRAHPLISQCVVVGDRQPFIAALV 506
Cdd:cd12114 399 AALQAHPGVARAVVVVLGDPGGKRLA 424
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
46-496 |
1.28e-25 |
|
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: 109.88 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVS-PGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG-AVAV 123
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARiTVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VVEStahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrsLSKADDVATIIYTSGTTGRPKGCVLTHR 203
Cdd:cd05958 89 CAHA------------------------------------------------LTASDDICILAFTSGTTGAPKATMHFHR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 204 NIysdIANAVPVLPNLFRQGASTLLF--LPLAHAFAR---LIQVGVVHARATMAHCADTKNLVAELQDFKPTFVLSVPRV 278
Cdd:cd05958 121 DP---LASADRYAVNVLRLREDDRFVgsPPLAFTFGLggvLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 279 FEkvyngarqkaeaegkgkifdraekvAIAWSEAQELPGGPGLglraqhalfdklvyrklraamggrcRDAISGGAPLGA 358
Cdd:cd05958 198 YR-------------------------AMLAHPDAAGPDLSSL-------------------------RKCVSAGEALPA 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 359 RLGH-FFRGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRI-DDDGEVLIAGDI---VFQG---YWHNDA 430
Cdd:cd05958 228 ALHRaWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVvDDEGNPVPDGTIgrlAVRGptgCRYLAD 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 431 ATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05958 308 KRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
26-600 |
1.86e-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: 110.60 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGTDAREdVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPI--- 102
Cdd:cd05921 5 ARQAPDRTWLAEREGNGGWRR-VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 103 YETSSAEQA--AWILGDSGAVAVVVESTA--HATLVAGVRDRLPDL---REVWQIDLGAVDDLVA--AGASVDRAevetr 173
Cdd:cd05921 84 YSLMSQDLAklKHLFELLKPGLVFAQDAApfARALAAIFPLGTPLVvsrNAVAGRGAISFAELAAtpPTAAVDAA----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 174 RSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnLFRQGASTLL-FLPLAHAFARLIQVGVVHARATMA 252
Cdd:cd05921 159 FAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYP-FFGEEPPVLVdWLPWNHTFGGNHNFNLVLYNGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HCADTKNL-------VAELQDFKPTFVLSVPRVFEKVYnGARQKAEAEgKGKIFDRAEKVAIawseaqelpGGPGLglrA 325
Cdd:cd05921 238 YIDDGKPMpggfeetLRNLREISPTVYFNVPAGWEMLV-AALEKDEAL-RRRFFKRLKLMFY---------AGAGL---S 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 326 QHalfdklVYRKLRAAMGGRCRDAIsggaPLGArlghffrgvgvticeGYGLTETSPAAAANLPTGTRIGTVGRPLPGVT 405
Cdd:cd05921 304 QD------VWDRLQALAVATVGERI----PMMA---------------GLGATETAPTATFTHWPTERSGLIGLPAPGTE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 406 IRI---DDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQL----DENGYLSITGRKKEIIVTAGGKNVAPAV 478
Cdd:cd05921 359 LKLvpsGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGP 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 479 LEDQVRAH--PLISQCVVVGDRQPFIAALVTIDeealPKWLAGQGRPETTSMAELREDAALRAEVQSAIDQAN-QAVSKA 555
Cdd:cd05921 439 LRARAVAAcaPLVHDAVVAGEDRAEVGALVFPD----LLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAALNgEATGSS 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2504840381 556 EAIKVFRILPQDFTEATGELTPSLKVKRQVVHKTYASEIAEIYRG 600
Cdd:cd05921 515 SRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
11-496 |
1.93e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 110.37 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 11 TVGDAANLTDPVWENAEVAPDT----VQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWT 86
Cdd:PRK09274 1 MMASMANIARHLPRAAQERPDQlavaVPGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 87 LFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHAtlvagVRdRLPDLREVWQIDLGAVDD-LVAAGASV 165
Cdd:PRK09274 81 ALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHL-----AR-RLFGWGKPSVRRLVTVGGrLLWGGTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 166 DRAEVETRRS-----LSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANA------------VPVLPnLFrqgastLL 228
Cdd:PRK09274 155 ATLLRDGAAApfpmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALredygiepgeidLPTFP-LF------AL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 229 FLPLAHA--------FARLIQVgvvharatmahcaDTKNLVAELQDFKPTFVLSVPRVFEKVyngARqkaEAEGKGKIFd 300
Cdd:PRK09274 228 FGPALGMtsvipdmdPTRPATV-------------DPAKLFAAIERYGVTNLFGSPALLERL---GR---YGEANGIKL- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 301 raekvaiawseaqelpggPGLglraqhalfdklvyrklraamggrcRDAISGGAPLGARLGHFFRGV---GVTICEGYGL 377
Cdd:PRK09274 288 ------------------PSL-------------------------RRVISAGAPVPIAVIERFRAMlppDAEILTPYGA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 378 TETSPAAA----ANLpTGTRIGT-------VGRPLPGVTIRI-----------DDD--------GEVLIAGDIVFQGYWH 427
Cdd:PRK09274 325 TEALPISSiesrEIL-FATRAATdngagicVGRPVDGVEVRIiaisdapipewDDAlrlatgeiGEIVVAGPMVTRSYYN 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 428 NDAATAEAITTDG----WFRTGDLGQLDENGYLSITGRKKEIIVTAGGkNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK09274 404 RPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG-TLYTIPCERIFNTHPGVKRSALVG 475
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
17-593 |
2.45e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 110.52 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 17 NLTDPVWENAEVAPDTVQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAG 96
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 97 AVTVPI---YETSSAEQA-----------AWILGDSG-----AVAVVVESTAHATLVAGVRDRLPDLRevwqidlgaVDD 157
Cdd:PRK12582 130 VPAAPVspaYSLMSHDHAklkhlfdlvkpRVVFAQSGapfarALAALDLLDVTVVHVTGPGEGIASIA---------FAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 158 LVaagASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLFRQGASTLL-FLPLAHAF 236
Cdd:PRK12582 201 LA---ATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdWMPWNHTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 237 ARLIQV-GVVHARATMaHCADTKNL-------VAELQDFKPTFVLSVPRVFEKVYnGARQKAEAEGKgKIFDRAEKVAIA 308
Cdd:PRK12582 278 GGNANFnGLLWGGGTL-YIDDGKPLpgmfeetIRNLREISPTVYGNVPAGYAMLA-EAMEKDDALRR-SFFKNLRLMAYG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 309 wseaqelpggpglGLRAQHALFDKLvYRKLRAAMGGRcrdaisggaplgarlghffrgvgVTICEGYGLTETSPaaaanL 388
Cdd:PRK12582 355 -------------GATLSDDLYERM-QALAVRTTGHR-----------------------IPFYTGYGATETAP-----T 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 389 PTGT-----RIGTVGRPLPGVTIRIDDDG---EVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQL----DENGYL 456
Cdd:PRK12582 393 TTGThwdteRVGLIGLPLPGVELKLAPVGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvdpdDPEKGL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 457 SITGRKKEIIVTAGGKNVAPAVLE-DQVRA-HPLISQCVVVGDRQPFIAALVTIDEEALPKwLAGQGRPettSMAELRED 534
Cdd:PRK12582 473 IFDGRVAEDFKLSTGTWVSVGTLRpDAVAAcSPVIHDAVVAGQDRAFIGLLAWPNPAACRQ-LAGDPDA---APEDVVKH 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 535 AALRAEVQSAIDQANQAVSKAEA-IKVFRILPQDFTEATGELT--------PSLKVKRQVVHKTYASE 593
Cdd:PRK12582 549 PAVLAILREGLSAHNAEAGGSSSrIARALLMTEPPSIDAGEITdkgyinqrAVLERRAALVERLYAEP 616
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
26-496 |
3.47e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 109.40 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtlFDYAIWAA---GAVTVPI 102
Cdd:PRK13391 7 AQTTPDKPAVIMASTG----EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLR---YLEVCWAAersGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 103 YETSSAEQAAWILGDSGAVAVVVeSTAHATLVAGVRDRLPDLREVWQID-LGAVDDLVAAGASVDRAEVETRRSLSKADD 181
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALIT-SAAKLDVARALLKQCPGVRHRLVLDgDGELEGFVGYAEAVAGLPATPIADESLGTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 182 vatIIYTSGTTGRPKGcvlthrnIYSDIANAVPVLP--------NLFRQGASTlLFL---PLAHAfARLIQVGVVHARA- 249
Cdd:PRK13391 159 ---MLYSSGTTGRPKG-------IKRPLPEQPPDTPlpltaflqRLWGFRSDM-VYLspaPLYHS-APQRAVMLVIRLGg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 ---TMAHcADTKNLVAELQDFKPTFVLSVPRVFekvyngarqkaeaegkgkifdraekvaiawSEAQELPggpglglRAQ 326
Cdd:PRK13391 227 tviVMEH-FDAEQYLALIEEYGVTHTQLVPTMF------------------------------SRMLKLP-------EEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 327 HALFDklvYRKLRAamggrcrdAISGGAPLGARLGH-FFRGVGVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGV 404
Cdd:PRK13391 269 RDKYD---LSSLEV--------AIHAAAPCPPQVKEqMIDWWGPIIHEYYAATEGLGFTACDSEEWlAHPGTVGRAMFGD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 TIRIDDDGEVLIAGD---IVFQG----YWHNDAA-TAEAITTDG-WFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVA 475
Cdd:PRK13391 338 LHILDDDGAELPPGEpgtIWFEGgrpfEYLNDPAkTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIY 416
|
490 500
....*....|....*....|.
gi 2504840381 476 PAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK13391 417 PQEAENLLITHPKVADAAVFG 437
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
25-500 |
3.66e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 109.33 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 25 NAEVAPDTVQFVRPGAGtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYE 104
Cdd:PRK13390 6 HAQIAPDRPAVIVAETG----EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 105 TSSAEQAAWILGDSGAvAVVVESTAHATLVAGVRDRLPdLREVWQidlGAVDDLvaagASVDRAEVETRRSLSKADDVAT 184
Cdd:PRK13390 82 HLTAPEADYIVGDSGA-RVLVASAALDGLAAKVGADLP-LRLSFG---GEIDGF----GSFEAALAGAGPRLTEQPCGAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 185 IIYTSGTTGRPKGCV--LTHRNIYSDIANAVPVLPNLFRQGASTLLF--LPLAHAfARLIQVGVVHA---RATMAHCADT 257
Cdd:PRK13390 153 MLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYssAPIYHA-APLRWCSMVHAlggTVVLAKRFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 KNLVAELQDFKPTFVLSVPRVFEKVYngarqKAEAEGKGKiFDRAEKVAIAWSeAQELPggpglgLRAQHALFDKLvyrk 337
Cdd:PRK13390 232 QATLGHVERYRITVTQMVPTMFVRLL-----KLDADVRTR-YDVSSLRAVIHA-AAPCP------VDVKHAMIDWL---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 lraamggrcrdaisggaplgarlghffrgvGVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVTIRIDDDGEVLI 416
Cdd:PRK13390 295 ------------------------------GPIVYEYYSSTEAHGMTFIDSPDWlAHPGSVGRSVLGDLHICDDDGNELP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 417 AGDI---VFQG-----YWHND---AATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRA 485
Cdd:PRK13390 345 AGRIgtvYFERdrlpfRYLNDpekTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQETENALTM 423
|
490
....*....|....*
gi 2504840381 486 HPLISQCVVVGDRQP 500
Cdd:PRK13390 424 HPAVHDVAVIGVPDP 438
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
180-598 |
8.13e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 109.42 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIYSDIanaVPVLPNLFRQGAST---LLFLPLAHAFARLIQVGVVHARATM-AHCA 255
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLYNTV---VPLCKHSIFKKYNPkthLSYLPISHIYERVIAYLSFMLGGTInIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 256 DTKNLVAELQDFKPTFVLSVPRVFEKVYNGARqkaeAE-GKGKIFDR--AEKVAiawseaqelpggpGLGLRAQHALFDK 332
Cdd:PTZ00342 381 DINYFSKDIYNSKGNILAGVPKVFNRIYTNIM----TEiNNLPPLKRflVKKIL-------------SLRKSNNNGGFSK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 333 L------VYRKLRAAMGGRCRDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPL-PGV 404
Cdd:PTZ00342 444 FlegithISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLlNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNT 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 --------TIRIDDD---GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKN 473
Cdd:PTZ00342 524 kykvrtweTYKATDTlpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEY 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 474 VAPAVLEDQVRAHPLISQCVVVGDRQ---PFiaALVTIDEEALPKWLAGQGRPETTSMAelrEDAALRAEVQsaiDQANQ 550
Cdd:PTZ00342 604 IETDMLNNLYSQISFINFCVVYGDDSmdgPL--AIISVDKYLLFKCLKDDNMLESTGIN---EKNYLEKLTD---ETINN 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 551 AV----SKAEAIKVFR-------------ILPQDFTEATGELTPSLKVKRQVVHKTYA---SEIAEIY 598
Cdd:PTZ00342 676 NIyvdyVKGKMLEVYKktnlnryniindiYLTSKVWDTNNYLTPTFKVKRFYVFKDYAffiDQVKKIY 743
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
24-538 |
8.91e-25 |
|
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: 108.13 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIY 103
Cdd:cd17646 6 EQAARTPDAP------AVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLpdlrevwqidlgaVDDLVAAGASVDRAEVETRRslskaDDVA 183
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVAL-------------LGDEALAAPPATPPLVPPRP-----DNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNIYSDIA---NAVPVLPN---LFRQGAST-----LLFLPLAHAfARLiqvgvVHARATmA 252
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGIVNRLLwmqDEYPLGPGdrvLQKTPLSFdvsvwELFWPLVAG-ARL-----VVARPG-G 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HcADTKNLVAELQDFKPTFVLSVPRVFEkvyngarqkaeaegkgkifdraekVAIAWSEAQELPGgpglglraqhalfdk 332
Cdd:cd17646 215 H-RDPAYLAALIREHGVTTCHFVPSMLR------------------------VFLAEPAAGSCAS--------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 333 lvyrklraamggrCRDAISGGAPLGARLG-HFFRGVGVTICEGYGLTETS---PAAAANLPTGTRIGTVGRPLPGVTIRI 408
Cdd:cd17646 255 -------------LRRVFCSGEALPPELAaRFLALPGAELHNLYGPTEAAidvTHWPVRGPAETPSVPIGRPVPNTRLYV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 409 DDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDgWF-------RTGDLGQLDENGYLSITGRKKEiIVTAGG 471
Cdd:cd17646 322 LDDalrpvpvgvpGELYLGGVQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRPDGALEFLGRSDD-QVKIRG 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504840381 472 KNVAPAVLEDQVRAHPLISQCVVVGDRQPFIAAlvtideeALPKWLAGQGRPETTSMAELREDAALR 538
Cdd:cd17646 400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA-------RLVGYVVPAAGAAGPDTAALRAHLAER 459
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
24-518 |
9.88e-25 |
|
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: 107.67 E-value: 9.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIY 103
Cdd:cd12117 5 EQAARTPDAV------AVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAWILGDSGAVAVVvestAHATLVAGVRDRLPDLREVWQIDlgavddlvAAGASVDRAEVEtrrslskADDVA 183
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLL----TDRSLAGRAGGLEVAVVIDEALD--------AGPAGNPAVPVS-------PDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNIysdianavpvlpnlfrqgastllflplahafarliqVGVVHARATMAHCADTKNLVAE 263
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGV------------------------------------VRLVKNTNYVTLGPDDRVLQTS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 264 lqdfKPTFVLSVPRVFEKVYNGARqkAEAEGKGKIFD--------RAEKVAIAWSEAqelpggpglglraqhALFDKLVy 335
Cdd:cd12117 184 ----PLAFDASTFEIWGALLNGAR--LVLAPKGTLLDpdalgaliAEEGVTVLWLTA---------------ALFNQLA- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 336 rKLRAAMGGRCRDAISGGAPLGARLghfFRGV-----GVTICEGYGLTETS-----------PAAAANLPtgtrigtVGR 399
Cdd:cd12117 242 -DEDPECFAGLRELLTGGEVVSPPH---VRRVlaacpGLRLVNGYGPTENTtfttshvvtelDEVAGSIP-------IGR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 400 PLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKK 463
Cdd:cd12117 311 PIANTRVYVLDEdgrpvppgvpGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRID 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 464 EiIVTAGGKNVAPAVLEDQVRAHPLISQCVVV------GDRQ--PFIAALVTIDEEALPKWLA 518
Cdd:cd12117 391 D-QVKIRGFRIELGEIEAALRAHPGVREAVVVvredagGDKRlvAYVVAEGALDAAELRAFLR 452
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
31-518 |
1.77e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.52 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 31 DTVQFVRPGAGTDARED--VTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSA 108
Cdd:PRK06164 17 DAHARARPDAVALIDEDrpLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 109 EQAAWILGDSGAVAVVVESTAH-----ATLVAGVRDRLPDLREVWQIDLGAVD-------DLVAAGASVDRAEVETRRSL 176
Cdd:PRK06164 97 HEVAHILGRGRARWLVVWPGFKgidfaAILAAVPPDALPPLRAIAVVDDAADAtpapapgARVQLFALPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDVATIIYT-SGTTGRPK------GCVLTHRNIysdIANAVPVLPnlfrqGASTLLFLPLAHAFARLIQVGVVHARA 249
Cdd:PRK06164 177 AADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARA---IARAYGYDP-----GAVLLAALPFCGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 250 T--MAHCADTKNLVAELQDFKPTFVLSVPRVFekvyngaRQKAEAEGKGKIFDRAEKVAIAwseaQELPGGPGLGLRAQH 327
Cdd:PRK06164 249 PlvCEPVFDAARTARALRRHRVTHTFGNDEML-------RRILDTAGERADFPSARLFGFA----SFAPALGELAALARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 328 AlfdklvyrklraamggrcrdaisgGAPLgarlghffRGVgvticegYGLTETSPAAA---ANLPTGTRIGTVGRPL-PG 403
Cdd:PRK06164 318 R------------------------GVPL--------TGL-------YGSSEVQALVAlqpATDPVSVRIEGGGRPAsPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 404 VTIRIDD--DGEVLIAGDI---------VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGK 472
Cdd:PRK06164 359 ARVRARDpqDGALLPDGESgeieirapsLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSL-RLGGF 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 473 NVAPAVLEDQVRAHPLISQCVVVG---DRQPFIAALV------TIDEEALPKWLA 518
Cdd:PRK06164 438 LVNPAEIEHALEALPGVAAAQVVGatrDGKTVPVAFViptdgaSPDEAGLMAACR 492
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
24-514 |
1.92e-24 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 108.79 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGL-MSRTryewtlFD-----YAIWAAGA 97
Cdd:COG1020 484 AQAARTPDAV------AVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVcLERS------LEmvvalLAVLKAGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 98 VTVPIYETSSAEQAAWILGDSGAVAVVVEStahatlvaGVRDRLPDLrevwQIDLGAVDDLVAAGASVDRAEVETRrsls 177
Cdd:COG1020 552 AYVPLDPAYPAERLAYMLEDAGARLVLTQS--------ALAARLPEL----GVPVLALDALALAAEPATNPPVPVT---- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 kADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTL-------------LFLPLAHAfARLiqvgv 244
Cdd:COG1020 616 -PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG--LGPGDRVLqfaslsfdasvweIFGALLSG-ATL----- 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 245 VHARATMAHcaDTKNLVAELQDFKPTFVLSVPRVFEkvyngarqkaeaegkgkifdraekvAIAWSEAQELPGgpglglr 324
Cdd:COG1020 687 VLAPPEARR--DPAALAELLARHRVTVLNLTPSLLR-------------------------ALLDAAPEALPS------- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 325 aqhalfdklvyrkLRAAMggrcrdaISGGAPLGARLGHFFRGV-GVTICEGYGLTETSPAAA-----ANLPTGTRIgTVG 398
Cdd:COG1020 733 -------------LRLVL-------VGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTyyevtPPDADGGSV-PIG 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 399 RPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEA-----ITTDG--WFRTGDLGQLDENGYLSITGR 461
Cdd:COG1020 792 RPIANTRVYVLDAhlqpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGR 871
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 462 kkeiivtaggknvapavLEDQV----------------RAHPLISQCVVV----GDRQPFIAALVTIDEEALP 514
Cdd:COG1020 872 -----------------ADDQVkirgfrielgeieaalLQHPGVREAVVVaredAPGDKRLVAYVVPEAGAAA 927
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
5-512 |
2.32e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 107.37 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 5 SVPPIVTVGDAANLTDPVWENAEVAPDTVQFVRPGAGtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYE 84
Cdd:PLN02330 17 SRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTG----KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 85 WTLFDYAIWAAGAV---TVPIYETSSAEQAAwilgDSGAVAVVVESTAHATLVAGVRdrLPDLREVWQIDLGAVD--DLV 159
Cdd:PLN02330 93 YGIVALGIMAAGGVfsgANPTALESEIKKQA----EAAGAKLIVTNDTNYGKVKGLG--LPVIVLGEEKIEGAVNwkELL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 160 AAGasvDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAV-PVLPNLFRQgASTLLFLPLAHAFAr 238
Cdd:PLN02330 167 EAA---DRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfSVGPEMIGQ-VVTLGLIPFFHIYG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 239 liQVGVVharatmahCADTKNlvaelqdfkptfvlsvprvfekvyngarqkaeaegKGKI-----FD-RAEKVAIAWSEA 312
Cdd:PLN02330 242 --ITGIC--------CATLRN-----------------------------------KGKVvvmsrFElRTFLNALITQEV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 313 QELPGGPGLGLR-AQHALFDK--LVYRKLRAAMggrcrdaiSGGAPLGARLGHFFRGV--GVTICEGYGLTETS------ 381
Cdd:PLN02330 277 SFAPIVPPIILNlVKNPIVEEfdLSKLKLQAIM--------TAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlth 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 382 --PAAAANLptgTRIGTVGRPLPGVTIR-IDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLG 448
Cdd:PLN02330 349 gdPEKGHGI---AKKNSVGFILPNLEVKfIDPDtgrslpkntpGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIG 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504840381 449 QLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVV--GDRQP--FIAALVTIDEEA 512
Cdd:PLN02330 426 YIDDDGDIFIVDRIKELIKYKGFQ-VAPAELEAILLTHPSVEDAAVVplPDEEAgeIPAACVVINPKA 492
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
26-496 |
2.52e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 106.89 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRpgagtDAREdVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYET 105
Cdd:PRK07798 13 ADAVPDRVALVC-----GDRR-LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 106 SSAEQAAWILGDSGAVAVVVESTaHATLVAGVRDRLPDLREVWQID--------LGAVD--DLVAAGASvDRAEVEtrRS 175
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYERE-FAPRVAEVLPRLPKLRTLVVVEdgsgndllPGAVDyeDALAAGSP-ERDFGE--RS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 176 lskADDVaTIIYTSGTTGRPKGCVLTHRNIY------SDIANAVPV-----LPNLFRQGASTLLFL--PLAHAFARLIqv 242
Cdd:PRK07798 163 ---PDDL-YLLYTGGTTGMPKGVMWRQEDIFrvllggRDFATGEPIedeeeLAKRAAAGPGMRRFPapPLMHGAGQWA-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 243 gvvharATMAHCADTKNLVAELQDFKPTFVLSVprvfekvyngarqkAEAEGKGKIFDRAEKVAIAWSEAQELPGGPGLG 322
Cdd:PRK07798 237 ------AFAALFSGQTVVLLPDVRFDADEVWRT--------------IEREKVNVITIVGDAMARPLLDALEARGPYDLS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 323 lraqhALFdklvyrklraamggrcrdAI-SGGAPLGARLGHFFRGV--GVTICEGYGLTET-----SPAAAANLPTGTRI 394
Cdd:PRK07798 297 -----SLF------------------AIaSGGALFSPSVKEALLELlpNVVLTDSIGSSETgfggsGTVAKGAVHTGGPR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 395 GTVGrplPGVTIrIDDDGEVLIAGD----------IVFQGYWHNDAATAEAITT-DG--WFRTGDLGQLDENGYLSITGR 461
Cdd:PRK07798 354 FTIG---PRTVV-LDEDGNPVEPGSgeigwiarrgHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGR 429
|
490 500 510
....*....|....*....|....*....|....*
gi 2504840381 462 KKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK07798 430 GSVCINTGGEK-VFPEEVEEALKAHPDVADALVVG 463
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
37-512 |
2.98e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 106.77 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 37 RPGAgTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwtlFDYAIWAAGAV--TVPIYETS-SAEQAAW 113
Cdd:PRK13382 59 RPGL-IDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRG---FVEALLAANRIgaDILLLNTSfAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 114 ILGDSGAVAVVVESTAHATLVAGVRDRLPDLREVWQIDlgAVDDLVAAGASVDRAEVETRRSLSKADdvaTIIYTSGTTG 193
Cdd:PRK13382 135 VVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTD--EDHDLTVEVLIAAHAGQRPEPTGRKGR---VILLTSGTTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 194 RPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHA--FARLIQVGVVHARATMAHCADTKNLVAELQDFKPTF 271
Cdd:PRK13382 210 TPKGARRSGPGGIGTLKAILDRTP--WRAEEPTVIVAPMFHAwgFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 272 VLSVPRVFEKvyngarqkaeaegkgkIFDRAEKVaiawseaqelpggpglglraqhalFDKLVYRKLR--AAMGGRCRDA 349
Cdd:PRK13382 288 LAVVPVMFDR----------------IMDLPAEV------------------------RNRYSGRSLRfaAASGSRMRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 350 IsggaplgarLGHFFRGVGVTICEGYGLTETSPAAAANlPTGTR--IGTVGRPLPGVTIRIDDD----------GEVLIA 417
Cdd:PRK13382 328 V---------VIAFMDQFGDVIYNNYNATEAGMIATAT-PADLRaaPDTAGRPAEGTEIRILDQdfrevptgevGTIFVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 418 GDIVFQGYwhNDAATAEaiTTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG- 496
Cdd:PRK13382 398 NDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMIVS-GGENVYPIEVEKTLATHPDVAEAAVIGv 472
|
490
....*....|....*....
gi 2504840381 497 DRQPF---IAALVTIDEEA 512
Cdd:PRK13382 473 DDEQYgqrLAAFVVLKPGA 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
26-515 |
3.02e-24 |
|
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: 105.79 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVrpgagtDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYET 105
Cdd:cd05945 1 AAANPDRPAVV------EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 106 SSAEQAAWILGDSGAVAVVVEStahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskaDDVATI 185
Cdd:cd05945 75 SPAERIREILDAAKPALLIADG----------------------------------------------------DDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 186 IYTSGTTGRPKGCVLTHRNIYSDIANAVPVLP----NLFRQGA------STL-LFLPLAHAfARLIQVGvvHARAtmahc 254
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPlgpgDVFLNQApfsfdlSVMdLYPALASG-ATLVPVP--RDAT----- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 ADTKNLVAELQDFKPTFVLSVPRVFEkvynGARQKAEaegkgkiFDraekvaiawseAQELPGgpglgLRaqHALFDKLV 334
Cdd:cd05945 175 ADPKQLFRFLAEHGITVWVSTPSFAA----MCLLSPT-------FT-----------PESLPS-----LR--HFLFCGEV 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 335 Y-----RKLRAAmggrcrdaisggAPlGARlghffrgvgvtICEGYGLTETSPAAAANLPTGTRIGT-----VGRPLPGV 404
Cdd:cd05945 226 LphktaRALQQR------------FP-DAR-----------IYNTYGPTEATVAVTYIEVTPEVLDGydrlpIGYAKPGA 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 TIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTD---GWFRTGDLGQLDENGYLSITGRKKEIIVTAGG 471
Cdd:cd05945 282 KLVILDEdgrpvppgekGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2504840381 472 KnVAPAVLEDQVRAHPLISQCVVV----GDRQPFIAALVTIDEEALPK 515
Cdd:cd05945 362 R-IELEEIEAALRQVPGVKEAVVVpkykGEKVTELIAFVVPKPGAEAG 408
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
49-506 |
3.17e-24 |
|
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: 105.66 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEqaawilgdsgavavvvest 128
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPE------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 ahatlvaGVRDRLpdlrevwqiDLGAVDDLVAAGASVDRAEVEtrrslskadDVATIIYTSGTTGRPKGCVLTHRNIYSD 208
Cdd:cd05969 63 -------AIRDRL---------ENSEAKVLITTEELYERTDPE---------DPTLLHYTSGTTGTPKGVLHVHDAMIFY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 209 IANAVPVLPnlfrqgastllflplahafarliqvgvVHARATMAHCADtknlvaelqdfkPTFVL-SVPRVFEKVYNGAr 287
Cdd:cd05969 118 YFTGKYVLD---------------------------LHPDDIYWCTAD------------PGWVTgTVYGIWAPWLNGV- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 288 QKAEAEGKgkiFD--------RAEKVAIaWSEAqelPGGPGLGLRAQHALFDKLVYRKLRAAMggrcrdaiSGGAPLG-- 357
Cdd:cd05969 158 TNVVYEGR---FDaeswygiiERVKVTV-WYTA---PTAIRMLMKEGDELARKYDLSSLRFIH--------SVGEPLNpe 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 358 -ARLGHffRGVGVTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGV-TIRIDDDGEVLIAGDI-----------VFQ 423
Cdd:cd05969 223 aIRWGM--EVFGVPIHDTWWQTETGSIMIANYPCMpIKPGSMGKPLPGVkAAVVDENGNELPPGTKgilalkpgwpsMFR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 424 GYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGDRQPFIA 503
Cdd:cd05969 301 GIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR-VGPFEVESALMEHPAVAEAGVIGKPDPLRG 378
|
...
gi 2504840381 504 ALV 506
Cdd:cd05969 379 EII 381
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
49-500 |
9.55e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.17 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEST 128
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 aHATLVAGVRDRLPDLREvW------------QIDLGAVDDLVAAGASVDRAEVETRRSLSkaddvaTIIYTSGTTGRPK 196
Cdd:PRK07008 121 -FLPLVDALAPQCPNVKG-WvamtdaahlpagSTPLLCYETLVGAQDGDYDWPRFDENQAS------SLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 197 GCVLTHRniySDIANAV-PVLPNLFRQGA--STLLFLPLAHAFARliqvGVVHArATMAHCA--------DTKNLVAELQ 265
Cdd:PRK07008 193 GALYSHR---STVLHAYgAALPDAMGLSArdAVLPVVPMFHVNAW----GLPYS-APLTGAKlvlpgpdlDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 266 DFKPTFVLSVPRVfekvyngarqkaeaegkgkifdraekvaiaWseaqelpggpgLGLrAQHALFDKLVYRKLRaamggr 345
Cdd:PRK07008 265 AERVTFSAGVPTV------------------------------W-----------LGL-LNHMREAGLRFSTLR------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 346 cRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSP--------AAAANLPTGTRIGTV---GRPLPGVTIRIDDD--- 411
Cdd:PRK07008 297 -RTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPlgtlcklkWKHSQLPLDEQRKLLekqGRVIYGVDMKIVGDdgr 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 ---------GEVLIAGDIVFQGYWHNDAATaeaiTTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQ 482
Cdd:PRK07008 376 elpwdgkafGDLQVRGPWVIDRYFRGDASP----LVDGWFPTGDVATIDADGFMQITDRSKDVI-KSGGEWISSIDIENV 450
|
490
....*....|....*...
gi 2504840381 483 VRAHPLISQCVVVGDRQP 500
Cdd:PRK07008 451 AVAHPAVAEAACIACAHP 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
52-512 |
1.16e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 105.31 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 52 QFRDEVVAVAQGLI-AAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSS-AEQAAWILGDSGAVAVVVESTA 129
Cdd:PLN02574 71 ELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSlGEIKKRVVDCSVGLAFTSPENV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 130 hatlvagvrDRLPDLR-------EVWQIDLGAVDDLVAAGASVDRAEVeTRRSLSKADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PLN02574 151 ---------EKLSPLGvpvigvpENYDFDSKRIEFPKFYELIKEDFDF-VPKPVIKQDDVAAIMYSSGTTGASKGVVLTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 203 RNIYSDIANAVPVLPNLFRQGAST---LLFLPLAHAFA-RLIQVGVVHARATMAHCA--DTKNLVAELQDFKPTFVLSVP 276
Cdd:PLN02574 221 RNLIAMVELFVRFEASQYEYPGSDnvyLAALPMFHIYGlSLFVVGLLSLGSTIVVMRrfDASDMVKVIDRFKVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 277 RVFEKVYNGARQKAeaegkGKIFDRAEKVAiawseaqelpggpglglraqhalfdklvyrklraamggrcrdaiSGGAPL 356
Cdd:PLN02574 301 PILMALTKKAKGVC-----GEVLKSLKQVS--------------------------------------------CGAAPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 357 GARLGHFFRGV--GVTICEGYGLTETSPAAAANLPT--GTRIGTVGRPLPGVTIRIDD-----------DGEVLIAGDIV 421
Cdd:PLN02574 332 SGKFIQDFVQTlpHVDFIQGYGMTESTAVGTRGFNTekLSKYSSVGLLAPNMQAKVVDwstgcllppgnCGELWIQGPGV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 422 FQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGdrqpf 501
Cdd:PLN02574 412 MKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQ-IAPADLEAVLISHPEIIDAAVTA----- 485
|
490
....*....|.
gi 2504840381 502 iaalvTIDEEA 512
Cdd:PLN02574 486 -----VPDKEC 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
40-512 |
1.23e-23 |
|
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: 103.93 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 40 AGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG 119
Cdd:cd17643 5 AVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVEstahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCV 199
Cdd:cd17643 85 PSLLLTD----------------------------------------------------PDDLAYVIYTSGSTGRPKGVV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHRNIYSDIANAVPVLPnlFRQGASTLLF-------------LPLAHAfARLIQVGVVHARATmahcADTKNLVAelqD 266
Cdd:cd17643 113 VSHANVLALFAATQRWFG--FNEDDVWTLFhsyafdfsvweiwGALLHG-GRLVVVPYEVARSP----EDFARLLR---D 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 267 FKPTFVLSVPRVFekvyngaRQKAEAEGKGkifdraekvaiawseaqelpggpglgLRAQHALfdklvyrklraamggrc 346
Cdd:cd17643 183 EGVTVLNQTPSAF-------YQLVEAADRD--------------------------GRDPLAL----------------- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAPLG-ARLGHFFRGVGV---TICEGYGLTETS------PAAAANLPTGTRiGTVGRPLPGVTIRIDDD----- 411
Cdd:cd17643 213 RYVIFGGEALEaAMLRPWAGRFGLdrpQLVNMYGITETTvhvtfrPLDAADLPAAAA-SPIGRPLPGLRVYVLDAdgrpv 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 -----GEVLIAGDIVFQGYWHNDAATAEAITTDGW-------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVL 479
Cdd:cd17643 292 ppgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADE-QVKIRGFRIELGEI 370
|
490 500 510
....*....|....*....|....*....|....*..
gi 2504840381 480 EDQVRAHPLISQCVVV----GDRQPFIAALVTIDEEA 512
Cdd:cd17643 371 EAALATHPSVRDAAVIvredEPGDTRLVAYVVADDGA 407
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
42-553 |
2.33e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 42 TDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAV 121
Cdd:PRK05852 38 TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGAR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 122 AVVVESTahatlvaGVRDRLPDLREVWQI--DLGAVDDLVAAGASVDR---AEVETRRSLSKA--DDVATIIYTSGTTGR 194
Cdd:PRK05852 118 VVLIDAD-------GPHDRAEPTTRWWPLtvNVGGDSGPSGGTLSVHLdaaTEPTPATSTPEGlrPDDAMIMFTGGTTGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 195 PKGCVLTHRNIYSDIaNAVPVLPNLFRQGAsTLLFLPLAHA-------FARLIQVGVVHARATMAHCADTknLVAELQDF 267
Cdd:PRK05852 191 PKMVPWTHANIASSV-RAIITGYRLSPRDA-TVAVMPLYHGhgliaalLATLASGGAVLLPARGRFSAHT--FWDDIKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 268 KPTFVLSVPRVFEKVYNGARQKAEAEGKGKI-FDRAEKVAIAWSEAQelpggpglglraqhALFDKLvyrklraamggrc 346
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAATEPSGRKPAALrFIRSCSAPLTAETAQ--------------ALQTEF------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 rdaisgGAPLGARLG--HFFRGVGVTICEGYGLTETsPAAAANL---PTGTRI---GTVGRPLPGVTIridddGEVLIAG 418
Cdd:PRK05852 320 ------AAPVVCAFGmtEATHQVTTTQIEGIGQTEN-PVVSTGLvgrSTGAQIrivGSDGLPLPAGAV-----GEVWLRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 419 DIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVGDR 498
Cdd:PRK05852 388 TTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELI-NRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504840381 499 QPF----IAALVTIDEEALP--KWLAGQGRPETTSM---AELREDAALRAEVQSAIDQanQAVS 553
Cdd:PRK05852 466 DQLygeaVAAVIVPRESAPPtaEELVQFCRERLAAFeipASFQEASGLPHTAKGSLDR--RAVA 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
49-500 |
1.01e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 102.14 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLM----SRTRYEWtlfdYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVV 124
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawntWRHLEAW----YGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 125 VESTaHATLVAGVRDRLPDLREVWQIDLGA------VDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGC 198
Cdd:PRK06018 117 TDLT-FVPILEKIADKLPSVERYVVLTDAAhmpqttLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 199 VLTHRN--IYSDIANAVPVLPnlFRQGASTLLFLPLAHAFARLIQVGV--VHARATMAHCADTKNLVAELQDF-KPTFVL 273
Cdd:PRK06018 196 LYSHRSnvLHALMANNGDALG--TSAADTMLPVVPLFHANSWGIAFSApsMGTKLVMPGAKLDGASVYELLDTeKVTFTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 274 SVPRVFEKVYngarQKAEAEGKgkifdraekvaiawseaqelpggpglglraqhalfdKLVYRKLraamggrcrdAISGG 353
Cdd:PRK06018 274 GVPTVWLMLL----QYMEKEGL------------------------------------KLPHLKM----------VVCGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 354 APLGARLGHFFRGVGVTICEGYGLTETSP--------AAAANLPTGTRIG---TVGRPLPGVTIRIDDD----------- 411
Cdd:PRK06018 304 SAMPRSMIKAFEDMGVEVRHAWGMTEMSPlgtlaalkPPFSKLPGDARLDvlqKQGYPPFGVEMKITDDagkelpwdgkt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 -GEVLIAGDIVFQGYWHNDAataEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLIS 490
Cdd:PRK06018 384 fGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVI-KSGGEWISSIDLENLAVGHPKVA 459
|
490
....*....|
gi 2504840381 491 QCVVVGDRQP 500
Cdd:PRK06018 460 EAAVIGVYHP 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
49-495 |
2.88e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 100.79 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILgDSGAVAVVVEST 128
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML-RHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 AHATLVAGVRDRLPDLREVwqidlgAVDDLVAAGASVDRA-EVETRRSLSKAD------------DVATIIYTSGTTGRP 195
Cdd:PRK08162 124 EFAEVAREALALLPGPKPL------VIDVDDPEYPGGRFIgALDYEAFLASGDpdfawtlpadewDAIALNYTSGTTGNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 196 KGCVLTHRNIYsdiANAVP-VLPNLFRQGASTLLFLPLAH----AFArliqvGVVHARATMAHCadtknlvaeLQDFKPt 270
Cdd:PRK08162 198 KGVVYHHRGAY---LNALSnILAWGMPKHPVYLWTLPMFHcngwCFP-----WTVAARAGTNVC---------LRKVDP- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 271 fvlsvprvfekvyngarqkaeaegkGKIFD--RAEKVAiawseaqELPGGPglglraqhalfdkLVYRKL-------RAA 341
Cdd:PRK08162 260 -------------------------KLIFDliREHGVT-------HYCGAP-------------IVLSALinapaewRAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 342 MGGRCRDAISGGAPLGARLGHFfRGVGVTICEGYGLTET-SPAAA-------ANLPTGTRIGTVGR------PLPGVTIr 407
Cdd:PRK08162 295 IDHPVHAMVAGAAPPAAVIAKM-EEIGFDLTHVYGLTETyGPATVcawqpewDALPLDERAQLKARqgvrypLQEGVTV- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 408 IDDD------------GEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVA 475
Cdd:PRK08162 373 LDPDtmqpvpadgetiGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENIS 450
|
490 500
....*....|....*....|
gi 2504840381 476 PAVLEDQVRAHPLISQCVVV 495
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVV 470
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
180-518 |
6.25e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 97.81 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIYSDiANAVPVlpnlfRQG--ASTLLFLPlAHAFARLiQVGVvhaRATMAhcadt 257
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAS-ADATHD-----RLGgpGQWLLALP-AHHIAGL-QVLV---RSVIA----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 258 knlvaelqDFKPTfVLSVPRVFEkVYNGARQKAEAEGkgkifDR--AEKVAIAWSEAQELPGGPglglrAQHALFDKLVY 335
Cdd:PRK07824 99 --------GSEPV-ELDVSAGFD-PTALPRAVAELGG-----GRryTSLVPMQLAKALDDPAAT-----AALAELDAVLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 336 rklraamggrcrdaisGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANlptgtrigtvGRPLPGVTIRIDDdGEVL 415
Cdd:PRK07824 159 ----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED-GRIA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 416 IAGDIVFQGYwhNDAATAEAITTDGWFRTGDLGQLDeNGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVV 495
Cdd:PRK07824 212 LGGPTLAKGY--RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAIST-GGLTVLPQVVEAALATHPAVADCAVF 287
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2504840381 496 G---DR---------------QPFIAALVTIDEEALPKWLA 518
Cdd:PRK07824 288 GlpdDRlgqrvvaavvgdggpAPTLEALRAHVARTLDRTAA 328
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
26-518 |
1.70e-21 |
|
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: 97.38 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYET 105
Cdd:cd17653 7 AAAHPDAV------AVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 106 SSAEQAAWILGDSGAVAVVvestahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrSLSKADDVATI 185
Cdd:cd17653 81 LPSARIQAILRTSGATLLL--------------------------------------------------TTDSPDDLAYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 186 IYTSGTTGRPKGCVLTHRNIysdiANAVPVLPNLFRQGASTLLFLPLAHAFarliQVGVVHARATMAHCAdtknlvaelq 265
Cdd:cd17653 111 IFTSGSTGIPKGVMVPHRGV----LNYVSQPPARLDVGPGSRVAQVLSIAF----DACIGEIFSTLCNGG---------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 266 dfkpTFVLSVPrvfekvyngarqkaeaegKGKIFDRAEKVAIawseaqeLPGGPGlglraqhalfdklVYRKLRAAMGGR 345
Cdd:cd17653 173 ----TLVLADP------------------SDPFAHVARTVDA-------LMSTPS-------------ILSTLSPQDFPN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 346 CRDAISGGAPLGARLGHFFRGvGVTICEGYGLTETSPAAA-ANLPTGTRIgTVGRPLPGVTIRIDD----------DGEV 414
Cdd:cd17653 211 LKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECTISSTmTELLPGQPV-TIGKPIPNSTCYILDadlqpvpegvVGEI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVLEDQVRAHPL 488
Cdd:cd17653 289 CISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE 368
|
490 500 510
....*....|....*....|....*....|....*
gi 2504840381 489 ISQ--CVVVGDRqpfIAALVT---IDEEALPKWLA 518
Cdd:cd17653 369 VTQaaAIVVNGR---LVAFVTpetVDVDGLRSELA 400
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
24-518 |
1.81e-21 |
|
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: 97.78 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVQFVRPGagtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIY 103
Cdd:cd17655 5 EQAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAWILGDSGAVAVVVESTahatlvagVRDRLPDLREVWQIDlgavDDLVAAGASVDRAEVetrrslSKADDVA 183
Cdd:cd17655 79 PDYPEERIQYILEDSGADILLTQSH--------LQPPIAFIGLIDLLD----EDTIYHEESENLEPV------SKSDDLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNlfRQGASTLLFLPLAhafarliqvgvvharatmahcadtknlvae 263
Cdd:cd17655 141 YVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ--GEHLRVALFASIS------------------------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 264 lqdfkptFVLSVPRVFEKVYNGAR---QKAEAEGKGKIF------DRAEKVAIAWSEAQELPggpglglRAQHALFDKLv 334
Cdd:cd17655 189 -------FDASVTEIFASLLSGNTlyiVRKETVLDGQALtqyirqNRITIIDLTPAHLKLLD-------AADDSEGLSL- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 335 yRKLraamggrcrdaISGGAPLGARL----GHFFrGVGVTICEGYGLTETSPAAAA-NLPTGTRIGT---VGRPLPGVTI 406
Cdd:cd17655 254 -KHL-----------IVGGEALSTELakkiIELF-GTNPTITNAYGPTETTVDASIyQYEPETDQQVsvpIGKPLGNTRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 407 RIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAG 470
Cdd:cd17655 321 YILDQygrpqpvgvaGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDH-QVKIR 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 471 GKNVAPAVLEDQVRAHPLISQCVVVG----DRQPFIAALVTIDEE----ALPKWLA 518
Cdd:cd17655 400 GYRIELGEIEARLLQHPDIKEAVVIArkdeQGQNYLCAYIVSEKElpvaQLREFLA 455
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-496 |
1.87e-21 |
|
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: 97.53 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 59 AVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIyetssaeqaawilgDSGAvavvvestahatlvagvr 138
Cdd:cd05910 14 RIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLI--------------DPGM------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 139 drlpDLREVWQidlgavddlvaagaSVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIAnavpVLPN 218
Cdd:cd05910 62 ----GRKNLKQ--------------CLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQID----ALRQ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 219 LF--RQGASTLLFLPLAHAFARLIqvGVVHARATMAHC----ADTKNLVAELQDFKPTFVLSVPRVFEKVyngarqkaea 292
Cdd:cd05910 120 LYgiRPGEVDLATFPLFALFGPAL--GLTSVIPDMDPTrparADPQKLVGAIRQYGVSIVFGSPALLERV---------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 293 egkgkifdraekvaIAWSEAQELPGgPGLglraqhalfdklvyrklraamggrcRDAISGGAPLGARLGHFFRGV---GV 369
Cdd:cd05910 188 --------------ARYCAQHGITL-PSL-------------------------RRVLSAGAPVPIALAARLRKMlsdEA 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 370 TICEGYGLTETSP----------AAAANLPTGTRIGTVGRPLPGVTIRI-----------DDD--------GEVLIAGDI 420
Cdd:cd05910 228 EILTPYGATEALPvssigsrellATTTAATSGGAGTCVGRPIPGVRVRIieiddepiaewDDTlelprgeiGEITVTGPT 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 421 VFQGYWHNDAATAEAITTDG----WFRTGDLGQLDENGYLSITGRKKEIIVTAGGKNVAPAVlEDQVRAHPLISQCVVVG 496
Cdd:cd05910 308 VTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPV-ERVFNTHPGVRRSALVG 386
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
178-463 |
1.93e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 99.27 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 KADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFrqGASTLLF--LPLAHAFarliqvGVvharatmahca 255
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--F--SPEDKVFnaLPVFHSF------GL----------- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 256 dTKNLVAELQDFKPTFVLSVPR----VFEKVYN-GArqkaeaegkgkifdraekvAIAWSEAQELPGGPglglRAQHAlF 330
Cdd:PRK06814 850 -TGGLVLPLLSGVKVFLYPSPLhyriIPELIYDtNA-------------------TILFGTDTFLNGYA----RYAHP-Y 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 331 DklvYRKLRAAmggrcrdaISGGAPLGARLGHFF-RGVGVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIR-- 407
Cdd:PRK06814 905 D---FRSLRYV--------FAGAEKVKEETRQTWmEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRle 973
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 408 ----IDDDGEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKK 463
Cdd:PRK06814 974 pvpgIDEGGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-588 |
3.23e-21 |
|
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: 96.43 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRV-GLMSRTRyEWTLFDYAIWAAGAVTVPIYeTSSAEQA-AWILGDSGAVAVVVE 126
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVaGLLPRTP-ELVVTILGIWRLGAVYQPLF-TAFGPKAiEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 127 stahatlvAGVRDRLpdlrevwqidlgavddlvaagasvdraevetrrslskADDVATIIYTSGTTGRPKGCVLTHRNIY 206
Cdd:cd05973 80 --------AANRHKL-------------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 207 SDIA---NAVPVLP-NLFRQGASTLLFLPLAHAFARLIQVGVvharatmahcadtknlvaelqdfkPTFVLSVPRVFEKV 282
Cdd:cd05973 115 AFGAylrDAVDLRPeDSFWNAADPGWAYGLYYAITGPLALGH------------------------PTILLEGGFSVEST 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 283 YngarqkaeaegkgkifDRAEKVAIAwseaqELPGGPglglraqhalfdkLVYRKLRAA-------MGGRCRDAISGGAP 355
Cdd:cd05973 171 W----------------RVIERLGVT-----NLAGSP-------------TAYRLLMAAgaevparPKGRLRRVSSAGEP 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 356 LGARLGHFFRG-VGVTICEGYGLTETSP--AAAANLPTGTRIGTVGRPLPGVTIRI-DDDGEVLIAGD------------ 419
Cdd:cd05973 217 LTPEVIRWFDAaLGVPIHDHYGQTELGMvlANHHALEHPVHAGSAGRAMPGWRVAVlDDDGDELGPGEpgrlaidiansp 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 420 -IVFQGYWHNDAATAEAittdGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVG-- 496
Cdd:cd05973 297 lMWFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR-IGPFDVESALIEHPAVAEAAVIGvp 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 497 --DRQPFIAALVTideealpkwLAGQGRPETtsmaelredaALRAEVQSAIDQANQAVSKAEAIKVFRILPQdfteatge 574
Cdd:cd05973 372 dpERTEVVKAFVV---------LRGGHEGTP----------ALADELQLHVKKRLSAHAYPRTIHFVDELPK-------- 424
|
570
....*....|....
gi 2504840381 575 lTPSLKVKRQVVHK 588
Cdd:cd05973 425 -TPSGKIQRFLLRR 437
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
371-496 |
4.58e-21 |
|
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: 94.39 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 371 ICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDD-----GEVLIAGDIVFQGYwhndaATAEAITTDGWFRTG 445
Cdd:cd17633 139 LIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNAdggeiGKIFVKSEMVFSGY-----VRGGFSNPDGWMSVG 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 446 DLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
26-496 |
8.01e-21 |
|
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: 96.03 E-value: 8.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 26 AEVAPDTVQFVRPGAGTDAReDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVP---- 101
Cdd:cd05970 27 AKEYPDKLALVWCDDAGEER-IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 102 ------IYETSSAEQAAWILGDSGAVAVVVEStAHATlvAGVRDRL----PDLREVWqIDLgavDDLVA-AGASVDRAEV 170
Cdd:cd05970 106 ltakdiVYRIESADIKMIVAIAEDNIPEEIEK-AAPE--CPSKPKLvwvgDPVPEGW-IDF---RKLIKnASPDFERPTA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 171 ETRrslSKADDVATIIYTSGTTGRPKgcVLTHRNIYsdianavpvlpnlfrqgastllflPLAH----AFARLIQVGVVH 246
Cdd:cd05970 179 NSY---PCGEDILLVYFSSGTTGMPK--MVEHDFTY------------------------PLGHivtaKYWQNVREGGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 247 ARAtmahcADTKNLVAELQDFKPTFVLSVPrVFekVYNGARQKAEAegkgkIFDRAEKVAIAwseaqelpggpglGLRAQ 326
Cdd:cd05970 230 LTV-----ADTGWGKAVWGKIYGQWIAGAA-VF--VYDYDKFDPKA-----LLEKLSKYGVT-------------TFCAP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 327 HALFDKLVYRKLRAAMGGRCRDAISGGAPLGARLGHFFRG-VGVTICEGYGLTETSpAAAANLP-TGTRIGTVGRPLPGV 404
Cdd:cd05970 284 PTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEkTGIKLMEGFGQTETT-LTIATFPwMEPKPGSMGKPAPGY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 TIR-IDDDG---EVLIAGDIV-----------FQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTA 469
Cdd:cd05970 363 EIDlIDREGrscEAGEEGEIVirtskgkpvglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
490 500
....*....|....*....|....*..
gi 2504840381 470 GGKnVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05970 442 GYR-IGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
177-548 |
1.61e-20 |
|
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: 94.92 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDVATIIYTSGTTGRPKGCVLTHRNIysdiANAVPVLPNLFRQGAST--LLFLplAHAFArliqVGVVHARATMAHC 254
Cdd:cd05918 103 SSPSDAAYVIFTSGSTGKPKGVVIEHRAL----STSALAHGRALGLTSESrvLQFA--SYTFD----VSILEIFTTLAAG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 A--------DTKN-LVAELQDFKPTFVLSVPRVfekvyngARQkaeaegkgkifdraekvaIAWSEAqelpggPGLglra 325
Cdd:cd05918 173 GclcipseeDRLNdLAGFINRLRVTWAFLTPSV-------ARL------------------LDPEDV------PSL---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 326 qhalfdklvyrklraamggrcRDAISGGAPLGARLGHFFRGvGVTICEGYGLTETSPAAAANLPT-GTRIGTVGRPLPGV 404
Cdd:cd05918 218 ---------------------RTLVLGGEALTQSDVDTWAD-RVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 405 TIRIDDD-----------GEVLIAGDIVFQGYWHNDAATAEA-ITTDGW------------FRTGDLGQLDENGYLSITG 460
Cdd:cd05918 276 CWVVDPDnhdrlvpigavGELLIEGPILARGYLNDPEKTAAAfIEDPAWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 461 RK----KeIivtaGGKNVAPAVLEDQVRAH-PLISQCVVV------GDRQPFIAALVTIDEEALpkwlaGQGRPETTSMA 529
Cdd:cd05918 356 RKdtqvK-I----RGQRVELGEIEHHLRQSlPGAKEVVVEvvkpkdGSSSPQLVAFVVLDGSSS-----GSGDGDSLFLE 425
|
410
....*....|....*....
gi 2504840381 530 ELREDAALRAEVQSAIDQA 548
Cdd:cd05918 426 PSDEFRALVAELRSKLRQR 444
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
16-480 |
2.93e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 94.68 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 16 ANLTDPVWENAEVAPDTVQFVRPgagtDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAA 95
Cdd:PRK07768 2 SRFTEKMYANARTSPRGMVTGEP----DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 96 GA-VTVPIYETSSAEQAAWIlGDSGAVAVVVEstAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGAsVDRAEVEtrr 174
Cdd:PRK07768 78 GAsLTMLHQPTPRTDLAVWA-EDTLRVIGMIG--AKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADP-IDPVETG--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 175 slskADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANavpvlpnlFRQGAS-------TLLFLPLAHafarliQVGVVHA 247
Cdd:PRK07768 151 ----EDDLALMQLTSGSTGSPKAVQITHGNLYANAEA--------MFVAAEfdvetdvMVSWLPLFH------DMGMVGF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 248 RATMAHCAdtknlvAELQDFKPTFVLSVPRVFEKV---YNG-------------ARQKAEAEGKGKiFDRAeKVAIAWSE 311
Cdd:PRK07768 213 LTVPMYFG------AELVKVTPMDFLRDPLLWAELiskYRGtmtaapnfayallARRLRRQAKPGA-FDLS-SLRFALNG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 312 AQELpggpglglraqhalfDKLVYRKLRAAMG--GRCRDAIS-----GGAPLGARLGHFFRGVGVTICEGYGLTETSPAA 384
Cdd:PRK07768 285 AEPI---------------DPADVEDLLDAGArfGLRPEAILpaygmAEATLAVSFSPCGAGLVVDEVDADLLAALRRAV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 385 AANLPTGTRIGTVGRPLPGVTIRI-DDDGEVL---------IAGDIVFQGYWHNDAAtAEAITTDGWFRTGDLGQLDENG 454
Cdd:PRK07768 350 PATKGNTRRLATLGPPLPGLEVRVvDEDGQVLpprgvgvieLRGESVTPGYLTMDGF-IPAQDADGWLDTGDLGYLTEEG 428
|
490 500
....*....|....*....|....*.
gi 2504840381 455 YLSITGRKKEIIVTaGGKNVAPAVLE 480
Cdd:PRK07768 429 EVVVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-496 |
7.94e-20 |
|
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: 92.78 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 18 LTDPVWENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGA 97
Cdd:cd05920 17 LGDLLARSAARHPDRI------AVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 98 VTV-PIYETSSAEQAAWIlGDSGAVAVVVESTAhatlvaGVRDRLPDLREVwqidlgavddlvaagasvdraevetrrsL 176
Cdd:cd05920 91 VPVlALPSHRRSELSAFC-AHAEAVAYIVPDRH------AGFDHRALAREL----------------------------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 177 SKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlFRQGASTLLFLPLAHAFArliqvgvvharatmahcad 256
Cdd:cd05920 136 ESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCG--LDQDTVYLAVLPAAHNFP------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 257 tknlvaelqdfkptfvLSVPRVFEKVYNGAR----QKAEAEGKGKIFDRaEKVAIAwseaqelpggpglglraqhALFDK 332
Cdd:cd05920 195 ----------------LACPGVLGTLLAGGRvvlaPDPSPDAAFPLIER-EGVTVT-------------------ALVPA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 333 LVYRKLRAAmgGRCRDAIS-------GGAPLGARLGHFFRGV-GVTICEGYGLTEtspaaaaNLPTGTR--------IGT 396
Cdd:cd05920 239 LVSLWLDAA--ASRRADLSslrllqvGGARLSPALARRVPPVlGCTLQQVFGMAE-------GLLNYTRlddpdeviIHT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 397 VGRPL-PGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEI 465
Cdd:cd05920 310 QGRPMsPDDEIRVVDEegnpvppgeeGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQ 389
|
490 500 510
....*....|....*....|....*....|.
gi 2504840381 466 IVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05920 390 INR-GGEKIAAEEVENLLLRHPAVHDAAVVA 419
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
29-520 |
1.82e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 92.05 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 29 APDTV-QFVRPGAGTDAR----ED--VTCRQFRDEVVAVAQGLiaAGVSPGDR---VGLMSRTRYEWTLFDYAIWAAGAV 98
Cdd:PRK07867 3 SAPTVaELLLPLAEDDDRglyfEDsfTSWREHIRGSAARAAAL--RARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 99 TVPIYET-SSAEQAAWIlgDSGAVAVVVESTAHATLVAGVrdrLPDLReVWQIDLGAVDDLVAAgasvdRAEVETRRSLS 177
Cdd:PRK07867 81 PVGLNPTrRGAALARDI--AHADCQLVLTESAHAELLDGL---DPGVR-VINVDSPAWADELAA-----HRDAEPPFRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 KADDVATIIYTSGTTGRPKGCVLTHRNIysdiANAVPVLPNLFRQGASTLLFL--PLAHAFARLIQVGV-VHARATMAHc 254
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKV----ASAGVMLAQRFGLGPDDVCYVsmPLFHSNAVMAGWAVaLAAGASIAL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 adtknlvaeLQDFKPTFVLSVPRVFEKVYngarqkAEAEGKgkifdraekvAIAWSEA-QELPGGpglglrAQHALfdkl 333
Cdd:PRK07867 225 ---------RRKFSASGFLPDVRRYGATY------ANYVGK----------PLSYVLAtPERPDD------ADNPL---- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 334 vyrklRAAMGGRcrdaisGGAPLGARLGHFFrgvGVTICEGYGLTETSpAAAANLPtGTRIGTVGRPLPGVTI------- 406
Cdd:PRK07867 270 -----RIVYGNE------GAPGDIARFARRF---GCVVVDGFGSTEGG-VAITRTP-DTPPGALGPLPPGVAIvdpdtgt 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 407 -----RIDDDGE----------VLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGG 471
Cdd:PRK07867 334 ecppaEDADGRLlnadeaigelVNTAGPGGFEGYYNDPEADAERMR-GGVYWSGDLAYRDADGYAYFAGRLGDWM-RVDG 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 472 KNVAPAVLEDQVRAHPLISQCVV-------VGDRqpFIAALV-----TIDEEALPKWLAGQ 520
Cdd:PRK07867 412 ENLGTAPIERILLRYPDATEVAVyavpdpvVGDQ--VMAALVlapgaKFDPDAFAEFLAAQ 470
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
363-520 |
2.52e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 91.63 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 363 FFRGVGVTICEGYGLTETspAAAANLPTGTRIGTVGRPLPGVTI------------RIDDDGEVLIA----GDIV----- 421
Cdd:PRK13388 283 FSRRFGCQVEDGYGSSEG--AVIVVREPGTPPGSIGRGAPGVAIynpetltecavaRFDAHGALLNAdeaiGELVntaga 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 422 --FQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVGDRQ 499
Cdd:PRK13388 361 gfFEGYYNNPEATAERMR-HGMYWSGDLAYRDADGWIYFAGRTADWM-RVDGENLSAAPIERILLRHPAINRVAVYAVPD 438
|
170 180 190
....*....|....*....|....*....|.
gi 2504840381 500 PF-----IAALV-----TIDEEALPKWLAGQ 520
Cdd:PRK13388 439 ERvgdqvMAALVlrdgaTFDPDAFAAFLAAQ 469
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
49-593 |
4.69e-19 |
|
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: 91.01 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVvesT 128
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI---T 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 129 AHATLVagvRDRLPDLREVwqidlgaVDDLVAAGASVDRAEVETR----------RSLSKADDVAT-------------- 184
Cdd:cd05968 170 ADGFTR---RGREVNLKEE-------ADKACAQCPTVEKVVVVRHlgndftpakgRDLSYDEEKETagdgaertesedpl 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 185 -IIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPNLfRQGASTLLFLPLAHAFARLIQVGVVHARATMAhcadtknlvae 263
Cdd:cd05968 240 mIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDL-KPGDLLTWFTDLGWMMGPWLIFGGLILGATMV----------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 264 lqdfkptfvlsvprvfekVYNGArqkAEAEGKGKIFDRAEKVAIAwseaqELPGGPGLgLRAQHALFDKLVYRKLRAAMg 343
Cdd:cd05968 308 ------------------LYDGA---PDHPKADRLWRMVEDHEIT-----HLGLSPTL-IRALKPRGDAPVNAHDLSSL- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 344 grcRDAISGGAPLGAR-LGHFFRGVG---VTICEGYGLTETSPAAAANLPTG-TRIGTVGRPLPGVTIRI-DDDGEVLI- 416
Cdd:cd05968 360 ---RVLGSTGEPWNPEpWNWLFETVGkgrNPIINYSGGTEISGGILGNVLIKpIKPSSFNGPVPGMKADVlDESGKPARp 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 417 -AGDIVF--------QGYWHNDAATAEAITT--DGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRA 485
Cdd:cd05968 437 eVGELVLlapwpgmtRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLNA 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 486 HPLISQCVVVGDRQPF----IAALVTIdeealpkwlagqgRPETTSMAELREDaaLRAEVQSAIDQAnqavSKAEAIKVF 561
Cdd:cd05968 516 HPAVLESAAIGVPHPVkgeaIVCFVVL-------------KPGVTPTEALAEE--LMERVADELGKP----LSPERILFV 576
|
570 580 590
....*....|....*....|....*....|..
gi 2504840381 562 RILPQdfteatgelTPSLKVKRQVVHKTYASE 593
Cdd:cd05968 577 KDLPK---------TRNAKVMRRVIRAAYLGK 599
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
185-496 |
9.60e-19 |
|
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: 87.74 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 185 IIYTSGTTGRPKGCVLTHRNIysdIANAVpvlpNLFRQGA--STLLFL---PLAHafarliqvgvvharatmahcadtkn 259
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAL---LAQAL----VLAVLQAidEGTVFLnsgPLFH------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 260 lVAELQDFKPTFVLSVPRVFekvyngARQkAEAEGKGKIFDrAEKVAIAW------SEAQELPGGPGLGLRAQHALFDKL 333
Cdd:cd17636 53 -IGTLMFTLATFHAGGTNVF------VRR-VDAEEVLELIE-AERCTHAFllpptiDQIVELNADGLYDLSSLRSSPAAP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 334 VYRKLRAAmggrcrDAisggAPLGARLGhffrgvgvticeGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRIDDD-- 411
Cdd:cd17636 124 EWNDMATV------DT----SPWGRKPG------------GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEdg 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 --------GEVLIAGDIVFQGYWHNDAATAEAiTTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQV 483
Cdd:cd17636 182 revpdgevGEIVARGPTVMAGYWNRPEVNARR-TRGGWHHTNDLGRREPDGSLSFVGPKTRMIKS-GAENIYPAEVERCL 259
|
330
....*....|...
gi 2504840381 484 RAHPLISQCVVVG 496
Cdd:cd17636 260 RQHPAVADAAVIG 272
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-545 |
1.09e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.79 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATL--VAGV 137
Cdd:PRK12316 4589 LAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpiPDGL 4668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 138 RDRLPDLREVWQiDLGAVDDLVAAgasvdraevetrrslsKADDVATIIYTSGTTGRPKGCVLTHRNIYSDIAnavpVLP 217
Cdd:PRK12316 4669 ASLALDRDEDWE-GFPAHDPAVRL----------------HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH----ATG 4727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 218 NLFRQGAS--TLLFLPLA------HAFARLIQVGVVHARATMAHcaDTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQK 289
Cdd:PRK12316 4728 ERYELTPDdrVLQFMSFSfdgsheGLYHPLINGASVVIRDDSLW--DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD 4805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 290 AEAegkgkifdraekvaiawseaqelpggpglgLRAQHALFdklvyrklraamGGrcrDAISGGAplgarLGHFFRGVGV 369
Cdd:PRK12316 4806 GEP------------------------------PSLRVYCF------------GG---EAVAQAS-----YDLAWRALKP 4835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 370 T-ICEGYGLTETSP-----AAAANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATA 433
Cdd:PRK12316 4836 VyLFNGYGPTETTVtvllwKARDGDACGAAYMPIGTPLGNRSGYVLDGqlnplpvgvaGELYLGGEGVARGYLERPALTA 4915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 434 EAITTDGW-------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGdrqpfiaalv 506
Cdd:PRK12316 4916 ERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDH-QVKIRGFRIELGEIEARLREHPAVREAVVIA---------- 4984
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2504840381 507 tiDEEALPKWLAGQGRPETTSMAELRE-DAALRAEVQSAI 545
Cdd:PRK12316 4985 --QEGAVGKQLVGYVVPQDPALADADEaQAELRDELKAAL 5022
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
51-543 |
1.51e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 89.29 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 51 RQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPI-YETSSAEQAAWI------LGDSGAVAV 123
Cdd:PRK09192 53 QTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLpLPMGFGGRESYIaqlrgmLASAQPAAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VvestAHATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGASVDRAevetrrslsKADDVATIIYTSGTTGRPKGCVLTHR 203
Cdd:PRK09192 133 I----TPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALPRP---------TPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 204 NIysdIANAVPVLPN--LFRQGASTLLFLPLAH------------------------AFAR-------LIQvgvvHARAT 250
Cdd:PRK09192 200 AL---MANLRAISHDglKVRPGDRCVSWLPFYHdmglvgflltpvatqlsvdylptrDFARrplqwldLIS----RNRGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 251 MAH--------CAdtknLVAELQDfKPTFVLSVPRVfekVYNGA--------RQKAEAEGKGKIFDRAEKvaiawseaqe 314
Cdd:PRK09192 273 ISYsppfgyelCA----RRVNSKD-LAELDLSCWRV---AGIGAdmirpdvlHQFAEAFAPAGFDDKAFM---------- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 315 lpggPGLGLrAQHALfdklvyrklraamggrcrdAISGgAPLGArlGHFFRGVGVTICEGYGLTETSPAAAANLPTgtrI 394
Cdd:PRK09192 335 ----PSYGL-AEATL-------------------AVSF-SPLGS--GIVVEEVDRDRLEYQGKAVAPGAETRRVRT---F 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 395 GTVGRPLPGVTIRI-DDDGEVL---------IAGDIVFQGYWhNDAATAEAITTDGWFRTGDLGQLdENGYLSITGRKKE 464
Cdd:PRK09192 385 VNCGKALPGHEIEIrNEAGMPLpervvghicVRGPSLMSGYF-RDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKD 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 465 IIVTaGGKNVAPAVLEDQVRAHPLISQcvvvGDrqpfIAALVTIDEEALPKWLAGQGRpetTSMAELREdaALRAEVQS 543
Cdd:PRK09192 463 LIII-NGRNIWPQDIEWIAEQEPELRS----GD----AAAFSIAQENGEKIVLLVQCR---ISDEERRG--QLIHALAA 527
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
51-520 |
1.67e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 88.90 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 51 RQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEqaawilgdsgAVAVVVESTAH 130
Cdd:PRK13383 64 RELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD----------ALAAALRAHHI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 131 ATLVAgvrdrlpdlrevwqiDLGAVDDLVAAGASV---DRAEVETRRSLSKADDVAT---IIYTSGTTGRPKGcVLTHRN 204
Cdd:PRK13383 134 STVVA---------------DNEFAERIAGADDAVaviDPATAGAEESGGRPAVAAPgriVLLTSGTTGKPKG-VPRAPQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 205 IYSDIANAVPVLPNL-FRQGASTLLFLPLAHAFArliqVGVVHARATMAHCADTKnlvaelqdfkptfvlsvpRVFEkvy 283
Cdd:PRK13383 198 LRSAVGVWVTILDRTrLRTGSRISVAMPMFHGLG----LGMLMLTIALGGTVLTH------------------RHFD--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 ngarqkAEAEGKGKIFDRAEK---VAIAWSEAQELPGGpglgLRAQHALfdklvyrklraamgGRCRDAISGGAPLGARL 360
Cdd:PRK13383 253 ------AEAALAQASLHRADAftaVPVVLARILELPPR----VRARNPL--------------PQLRVVMSSGDRLDPTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 361 GH-FFRGVGVTICEGYGLTETSPAAAANlPTGTRIG--TVGRPLPGVTIRIDD----------DGEVLIAGDIVFQGYwh 427
Cdd:PRK13383 309 GQrFMDTYGDILYNGYGSTEVGIGALAT-PADLRDApeTVGKPVAGCPVRILDrnnrpvgprvTGRIFVGGELAGTRY-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 428 NDAATAEAIttDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG--DRQ--PFIA 503
Cdd:PRK13383 386 TDGGGKAVV--DGMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVADNAVIGvpDERfgHRLA 462
|
490 500
....*....|....*....|...
gi 2504840381 504 ALVT------IDEEALPKWLAGQ 520
Cdd:PRK13383 463 AFVVlhpgsgVDAAQLRDYLKDR 485
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
352-520 |
4.57e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.97 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 352 GGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLP----TGTRigTVGRPLPGVTIRID--DDGEVLIAGDIVFQGY 425
Cdd:PRK07445 238 GGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPddflAGNN--SSGQVLPHAQITIPanQTGNITIQAQSLALGY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 426 WhndaatAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG--DR---QP 500
Cdd:PRK07445 316 Y------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLGlpDPhwgEV 388
|
170 180
....*....|....*....|....
gi 2504840381 501 FIAALV----TIDEEALPKWLAGQ 520
Cdd:PRK07445 389 VTAIYVpkdpSISLEELKTAIKDQ 412
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
61-538 |
6.23e-18 |
|
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: 86.54 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 61 AQGLIAAGVSPGDRVGL-MSRTrYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVvvestahatlvagvrd 139
Cdd:cd17652 26 ARLLAARGVGPERLVALaLPRS-AELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALL---------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 rlpdlrevwqidlgavddlvaagasvdraevetrrsLSKADDVATIIYTSGTTGRPKGCVLTHRNiysdianavpvLPNL 219
Cdd:cd17652 89 ------------------------------------LTTPDNLAYVIYTSGSTGRPKGVVVTHRG-----------LANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 FRqgastllflplahAFARLIQVGVvHARAtmahcadtknlvaeLQDFKPTFVLSVPRVFEKVYNGARqkaeaegkgkif 299
Cdd:cd17652 122 AA-------------AQIAAFDVGP-GSRV--------------LQFASPSFDASVWELLMALLAGAT------------ 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 300 draekVAIAWSEaqELPGGPGLG--LRAQHALFDKLVYRKLrAAMGGRC----RDAISGGAPLGARLGHFFrGVGVTICE 373
Cdd:cd17652 162 -----LVLAPAE--ELLPGEPLAdlLREHRITHVTLPPAAL-AALPPDDlpdlRTLVVAGEACPAELVDRW-APGRRMIN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 374 GYGLTETSPAA-AANLPTGTRIGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW- 441
Cdd:cd17652 233 AYGPTETTVCAtMAGPLPGGGVPPIGRPVPGTRVYVLDArlrpvppgvpGELYIAGAGLARGYLNRPGLTAERFVADPFg 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 442 ------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVV-VGDRQPFIAALVTideealp 514
Cdd:cd17652 313 apgsrmYRTGDLARWRADGQLEFLGRADD-QVKIRGFRIELGEVEAALTEHPGVAEAVVvVRDDRPGDKRLVA------- 384
|
490 500
....*....|....*....|....
gi 2504840381 515 kWLAGQGrPETTSMAELREDAALR 538
Cdd:cd17652 385 -YVVPAP-GAAPTAAELRAHLAER 406
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-495 |
6.55e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.29 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 61 AQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTahatlvagVRDR 140
Cdd:PRK12467 551 AHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH--------LLAQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 141 LPDLREVWQIDLGAVDDLVAAgasvdRAEVETRRSLSkADDVATIIYTSGTTGRPKGCVLTHRNiysdIANAVPVLPNLF 220
Cdd:PRK12467 623 LPVPAGLRSLCLDEPADLLCG-----YSGHNPEVALD-PDNLAYVIYTSGSTGQPKGVAISHGA----LANYVCVIAERL 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 221 RQGA--STLLFLPLA------HAFARLIQVGVVHARATMAHcADTKNLVAELQDFKPTFVLSVPRVFekvyngarqkaea 292
Cdd:PRK12467 693 QLAAddSMLMVSTFAfdlgvtELFGALASGATLHLLPPDCA-RDAEAFAALMADQGVTVLKIVPSHL------------- 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 293 egkgKIFDRAEKVAIAWSEAQELPGGPGLGLRAQhalfdklvyRKLRAAmggrcrdaisggaplgarlghffrGVGVTIC 372
Cdd:PRK12467 759 ----QALLQASRVALPRPQRALVCGGEALQVDLL---------ARVRAL------------------------GPGARLI 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 373 EGYGLTETS------PAAAANLPTGTriGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAI 436
Cdd:PRK12467 802 NHYGPTETTvgvstyELSDEERDFGN--VPIGQPLANLGLYILDHylnpvpvgvvGELYIGGAGLARGYHRRPALTAERF 879
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504840381 437 TTDGW-------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVV 495
Cdd:PRK12467 880 VPDPFgadggrlYRTGDLARYRADGVIEYLGRMDH-QVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
60-495 |
8.71e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGaVAVVVeSTAHatlvagVRD 139
Cdd:PRK12467 3133 LAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG-VKLLL-TQAH------LLE 3204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 RLPDLREVWQIDLgavdDLVAAGASVDRAEVetrrSLSKADDVATIIYTSGTTGRPKGCVLTHrniySDIANAVPVLPNL 219
Cdd:PRK12467 3205 QLPAPAGDTALTL----DRLDLNGYSENNPS----TRVMGENLAYVIYTSGSTGKPKGVGVRH----GALANHLCWIAEA 3272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 FRQGAST--LLFLPLA------HAFARLIQVGVVHARAtmAHCADTKNLVAELQDFKPTFVLSVPRVFEKvyngarqkae 291
Cdd:PRK12467 3273 YELDANDrvLLFMSFSfdgaqeRFLWTLICGGCLVVRD--NDLWDPEELWQAIHAHRISIACFPPAYLQQ---------- 3340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 292 aegkgkiFDRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKLVYRKLRaamggrcrdaisggaplgarlghffrgvgvti 371
Cdd:PRK12467 3341 -------FAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLT-------------------------------- 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 372 cEGYGLTET------------SPAAAANLPtgtrigtVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHND 429
Cdd:PRK12467 3382 -NGYGPTEAvvtvtlwkcggdAVCEAPYAP-------IGRPVAGRSIYVLDGqlnpvpvgvaGELYIGGVGLARGYHQRP 3453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 430 AATAEAITTDGW-------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVV 495
Cdd:PRK12467 3454 SLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDH-QVKIRGFRIELGEIEARLLQHPSVREAVVL 3525
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-496 |
1.37e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.10 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 41 GTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRV-GLMSRTR--YEWTLfdyAIWAAGAVTVPIYETSSAEQAAWILGD 117
Cdd:PRK04319 67 DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVfIFMPRIPelYFALL---GALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 118 SGAVAVVvesTAHATLVAGVRDRLPDLREVWQID--LGAVDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRP 195
Cdd:PRK04319 144 SEAKVLI---TTPALLERKPADDLPSLKHVLLVGedVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 196 KGCVLTHRNIYSDIANAVPVLPnlFRQ--------------GASTLLFLPLAHafarliqvGVVharatmahcadtkNLV 261
Cdd:PRK04319 221 KGVLHVHNAMLQHYQTGKYVLD--LHEddvywctadpgwvtGTSYGIFAPWLN--------GAT-------------NVI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 262 AElQDFKPtfvlsvprvfEKVYngarqkaeaegkgKIFDRaEKVAIaWSEAqelPG------GPGLGLRAQHALfdklvy 335
Cdd:PRK04319 278 DG-GRFSP----------ERWY-------------RILED-YKVTV-WYTA---PTairmlmGAGDDLVKKYDL------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 336 rklraamgGRCRDAISGGAPLGA---RLGHffRGVGVTICEGYGLTETSPAAAANLPT-GTRIGTVGRPLPGVTIRI-DD 410
Cdd:PRK04319 323 --------SSLRHILSVGEPLNPevvRWGM--KVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGIEAAIvDD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 411 DGEVLIAGDI-----------VFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVL 479
Cdd:PRK04319 393 QGNELPPNRMgnlaikkgwpsMMRGIWNNPEKYESYFA-GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEV 470
|
490
....*....|....*..
gi 2504840381 480 EDQVRAHPLISQCVVVG 496
Cdd:PRK04319 471 ESKLMEHPAVAEAGVIG 487
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
179-480 |
1.66e-17 |
|
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: 85.62 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 179 ADDVATIIYTSGTTGRPKGCVLTHRNIYS---DIANAVPVlpnlfRQGASTLLFLPLAHAFArLIQVGVVHARATMAH-- 253
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHnmfAILNSTEW-----KTKDRILSWMPLTHDMG-LIAFHLAPLIAGMNQyl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 254 ------CADTKNLVAELQDFKPTfVLSVP----RVFEKVYNgaRQKAEAEGKGKIfdraeKVAIAWSEaqelPGGPGLGl 323
Cdd:cd05908 179 mptrlfIRRPILWLKKASEHKAT-IVSSPnfgyKYFLKTLK--PEKANDWDLSSI-----RMILNGAE----PIDYELC- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 324 raqHALFDKLVYRKLRaamggrcRDAI---------SGGAPLGARLGHFFRgvgVTIC-EGYGLTETSPAAAANLPTGTR 393
Cdd:cd05908 246 ---HEFLDHMSKYGLK-------RNAIlpvyglaeaSVGASLPKAQSPFKT---ITLGrRHVTHGEPEPEVDKKDSECLT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 394 IGTVGRPLPGVTIRI-DDDGEVL---------IAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGqLDENGYLSITGRKK 463
Cdd:cd05908 313 FVEVGKPIDETDIRIcDEDNKILpdgyighiqIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREK 391
|
330
....*....|....*..
gi 2504840381 464 EIIVTaGGKNVAPAVLE 480
Cdd:cd05908 392 DIIFV-NGQNVYPHDIE 407
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
40-520 |
2.64e-17 |
|
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: 84.68 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 40 AGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG 119
Cdd:cd12115 17 ALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVEStahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskaDDVATIIYTSGTTGRPKGCV 199
Cdd:cd12115 97 ARLVLTDP----------------------------------------------------DDLAYVIYTSGSTGRPKGVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHRNIYSDIANAVPVLPNLFRQG--ASTL---------LFLPLAHAfARLIQV-GVVHARATMAHCadtknlvaelqdf 267
Cdd:cd12115 125 IEHRNAAAFLQWAAAAFSAEELAGvlASTSicfdlsvfeLFGPLATG-GKVVLAdNVLALPDLPAAA------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 268 KPTFVLSVPRVfekvyngARQKAEAEGkgkifdraekvaiawseaqeLPGGpglgLR----AQHALFDKLVyRKLRAAMG 343
Cdd:cd12115 191 EVTLINTVPSA-------AAELLRHDA--------------------LPAS----VRvvnlAGEPLPRDLV-QRLYARLQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 344 GRCrdaisggaplgarlghffrgvgvtICEGYGLTE-TSPAAAANLPTGT-RIGTVGRPLPGVTIRIDDD---------- 411
Cdd:cd12115 239 VER------------------------VVNLYGPSEdTTYSTVAPVPPGAsGEVSIGRPLANTQAYVLDRalqpvplgvp 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 GEVLIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRA 485
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADN-QVKVRGFRIELGEIEAALRS 373
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2504840381 486 HPLISQCVVV----GDRQPFIAALVT------IDEEALPKWLAGQ 520
Cdd:cd12115 374 IPGVREAVVVaigdAAGERRLVAYIVaepgaaGLVEDLRRHLGTR 418
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
68-496 |
2.97e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.22 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 68 GVSPGDRVGLM--SRTRYEWTLFdyAIWAAGAVTVPIYETSSAEQAAWILGDSgAVAVVVESTAHATLVAGVRDRLPDLR 145
Cdd:PRK05620 60 GITGDQRVGSMmyNCAEHLEVLF--AVACMGAVFNPLNKQLMNDQIVHIINHA-EDEVIVADPRLAEQLGEILKECPCVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 146 EVwqidlgavddLVAAGASVDRAEVETRRSLSKAD--------------------DVATIIYTSGTTGRPKGCVLTHRNI 205
Cdd:PRK05620 137 AV----------VFIGPSDADSAAAHMPEGIKVYSyealldgrstvydwpeldetTAAAICYSTGTTGAPKGVVYSHRSL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 206 YSDIANAVPVLPNLFRQGASTLLFLPLAH---------AF---ARLIQVGVVHARATMAHCADTknlvaelqdfkptfvl 273
Cdd:PRK05620 207 YLQSLSLRTTDSLAVTHGESFLCCVPIYHvlswgvplaAFmsgTPLVFPGPDLSAPTLAKIIAT---------------- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 274 SVPRVfekvyngarqkaeaegkgkifdrAEKVAIAWseaqelpggpgLGLraqhalfdkLVYRKLRAAMGGRCRDAISGG 353
Cdd:PRK05620 271 AMPRV-----------------------AHGVPTLW-----------IQL---------MVHYLKNPPERMSLQEIYVGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 354 APLGARLGHFFRG-VGVTICEGYGLTETSPaaaanlptgtrIGTVGRPLPGVT-------------------IRIDDDGE 413
Cdd:PRK05620 308 SAVPPILIKAWEErYGVDVVHVWGMTETSP-----------VGTVARPPSGVSgearwayrvsqgrfpasleYRIVNDGQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 414 VL-----------IAGDIVFQGYWHNDAAT----------------AEAITTDGWFRTGDLGQLDENGYLSITGRKKEII 466
Cdd:PRK05620 377 VMestdrnegeiqVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVI 456
|
490 500 510
....*....|....*....|....*....|
gi 2504840381 467 vTAGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PRK05620 457 -RSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-476 |
4.92e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 84.29 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 16 ANLTDPVWENAEVAPDTVQFVRpgagTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAA 95
Cdd:PRK05857 14 STVLDRVFEQARQQPEAIALRR----CDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 96 GAVTVPIYETSSAEQAAWI--LGDSGAVAVVVESTAHATLVAGVRDRLPDLRevwqIDLGAVDDLVAAGASVDRAEVETR 173
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFcqITDPAAALVAPGSKMASSAVPEALHSIPVIA----VDIAAVTRESEHSLDAASLAGNAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 174 rslSKADDVATIIYTSGTTGRPKGCVLTHRNIYSdianavpvLPNLFRQ----------GASTLLFLPLAHAFARL-IQV 242
Cdd:PRK05857 166 ---QGSEDPLAMIFTSGTTGEPKAVLLANRTFFA--------VPDILQKeglnwvtwvvGETTYSPLPATHIGGLWwILT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 243 GVVHARATMAHCADTKNLVAELQDFKPTFVLSVPrvfekvyngarqkaeaegkgkifdraekvaiawseaqelpggpglg 322
Cdd:PRK05857 235 CLMHGGLCVTGGENTTSLLEILTTNAVATTCLVP---------------------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 323 lraqhALFDKLVYR-KLRAAMGGRCRDAISGGAPLGARLGHFFRGVGVTICEGYGLTETSpAAAANLPTG----TRI--G 395
Cdd:PRK05857 269 -----TLLSKLVSElKSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETG-CTALCLPTDdgsiVKIeaG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 396 TVGRPLPGVTIRIDDD----------------GEVLIAGDIVFQGYWHNDAATAEaITTDGWFRTGDLGQLDENGYLSIT 459
Cdd:PRK05857 343 AVGRPYPGVDVYLAATdgigptapgagpsasfGTLWIKSPANMLGYWNNPERTAE-VLIDGWVNTGDLLERREDGFFYIK 421
|
490
....*....|....*..
gi 2504840381 460 GRKKEIIVTaGGKNVAP 476
Cdd:PRK05857 422 GRSSEMIIC-GGVNIAP 437
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
61-519 |
6.69e-17 |
|
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: 83.57 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 61 AQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGavavvvestaHATLVAgvrdr 140
Cdd:cd17649 26 AHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSG----------AGLLLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 141 lpdlrevwqidlgavddlvaagasvdraevETRRSLskaddvATIIYTSGTTGRPKGCVLTHRNIYSDIANAVPVLPnlF 220
Cdd:cd17649 91 ------------------------------HHPRQL------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG--L 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 221 RQGASTLLFLPL----AHA--FARLIQVGVVHARA------TMAHCADTKNLVAELQDFKPTFVlsvprvfekvyngaRQ 288
Cdd:cd17649 133 TPGDRELQFASFnfdgAHEqlLPPLICGACVVLRPdelwasADELAEMVRELGVTVLDLPPAYL--------------QQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 289 KAEaegkgkifdraekvaiawsEAQELPGGPGLGLRAQHALFDKLVYRKLRAAMGGRCRdaisggaplgarlghffrgvg 368
Cdd:cd17649 199 LAE-------------------EADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVR--------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 369 vtICEGYGLTET--SP----------AAAANLPtgtrigtVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYW 426
Cdd:cd17649 239 --LFNAYGPTEAtvTPlvwkceagaaRAGASMP-------IGRPLGGRSAYILDAdlnpvpvgvtGELYIGGEGLARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 427 HNDAATAEAITTDG-------WFRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVV---G 496
Cdd:cd17649 310 GRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDH-QVKIRGFRIELGEIEAALLEHPGVREAAVValdG 388
|
490 500
....*....|....*....|....
gi 2504840381 497 DRQP-FIAALVTIDEEALPKWLAG 519
Cdd:cd17649 389 AGGKqLVAYVVLRAAAAQPELRAQ 412
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
16-520 |
7.28e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 83.38 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 16 ANLTDPVWEN-AEVAPDTVQFVRPGagtdarEDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEwTLFDY-AIW 93
Cdd:PRK09029 2 MIFSDWPWRHwAQVRPQAIALRLND------EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPE-TLLAYlALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 94 AAGAVTVPIYETSSAEQAAwilgdsgavavvvestahatlvagvrDRLPDLREVWQIDLGAVDDLVAAGASVDRAEVETR 173
Cdd:PRK09029 75 QCGARVLPLNPQLPQPLLE--------------------------ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 174 RSLSKADDVATIIYTSGTTGRPKGCVLTHRNiysDIANAVPVLpNL--FRQGASTLLFLPLAHafarliqV---GVVH-- 246
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQA---HLASAEGVL-SLmpFTAQDSWLLSLPLFH-------VsgqGIVWrw 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 247 --ARATMaHCADTKNLVAELQDFkpTFVLSVP----RVFEkvyngarqkaeaegkgkifDRAEKVAIawseaqelpggpg 320
Cdd:PRK09029 198 lyAGATL-VVRDKQPLEQALAGC--THASLVPtqlwRLLD-------------------NRSEPLSL------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 321 lglraQHALFdklvyrklraamggrcrdaisGGAPLGARLGHFFRGVGVTICEGYGLTETSPAAAANLPTGtrIGTVGRP 400
Cdd:PRK09029 243 -----KAVLL---------------------GGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRADG--LAGVGSP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 401 LPGVTIRIDDDgEVLIAGDIVFQGYWHNDAATAeAITTDGWFRTGDLGQLDeNGYLSITGRKKEIIVTaGGKNVAPAVLE 480
Cdd:PRK09029 295 LPGREVKLVDG-EIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFS-GGEGIQPEEIE 370
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2504840381 481 DQVRAHPLISQCVVV-------GDRqPfIAALVTIDE---EALPKWLAGQ 520
Cdd:PRK09029 371 RVINQHPLVQQVFVVpvadaefGQR-P-VAVVESDSEaavVNLAEWLQDK 418
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
30-500 |
1.32e-16 |
|
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: 83.01 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 30 PDTVQFVRPGAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAE 109
Cdd:cd17634 67 GDRTAIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 110 QAAWILGDSGAVAVVvesTAHATLVAGvrdRLPDLREVwqidlgAVDDLVAAGASVDRAEVETRRSLS------------ 177
Cdd:cd17634 147 AVAGRIIDSSSRLLI---TADGGVRAG---RSVPLKKN------VDDALNPNVTSVEHVIVLKRTGSDidwqegrdlwwr 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 ---------------KADDVATIIYTSGTTGRPKGCVLTH-----------RNIY-----------SDIANAVP---VLP 217
Cdd:cd17634 215 dliakaspehqpeamNAEDPLFILYTSGTTGKPKGVLHTTggylvyaattmKYVFdygpgdiywctADVGWVTGhsyLLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 218 NLFRQGASTLLF--LPLAHAFARLIQVGVVHAratMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEgk 295
Cdd:cd17634 295 GPLACGATTLLYegVPNWPTPARMWQVVDKHG---VNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPE-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 296 gkifdraekvaiAWSEAQELPGGPGLglraqhalfdKLVYRKLRAAMGGRCRDAISGGAPLGArlGHFFR---GVGVTIC 372
Cdd:cd17634 370 ------------AYEWYWKKIGKEKC----------PVVDTWWQTETGGFMITPLPGAIELKA--GSATRpvfGVQPAVV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 373 EGYGLTEtSPAAAANLptgtrigTVGRPLPGVTIRIDDDGEVLiagdivFQGYWHndaataeaiTTDGWFRTGDLGQLDE 452
Cdd:cd17634 426 DNEGHPQ-PGGTEGNL-------VITDPWPGQTRTLFGDHERF------EQTYFS---------TFKGMYFSGDGARRDE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2504840381 453 NGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVVVGDRQP 500
Cdd:cd17634 483 DGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVGIPHA 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-519 |
4.10e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEStahatlvaGVRD 139
Cdd:PRK12316 2041 LAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR--------HLLE 2112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 RLPDLREVWQIDLGAVDDLvaAGASVDRAEVETrrslsKADDVATIIYTSGTTGRPKGCVLTHRniysdianavpvlpnl 219
Cdd:PRK12316 2113 RLPLPAGVARLPLDRDAEW--ADYPDTAPAVQL-----AGENLAYVIYTSGSTGLPKGVAVSHG---------------- 2169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 frqgastllflplahAFARLIQVGVVHARATMAHCadtknlvaELQDFKPTFVLSVPRVFEKVYNGAR---QKAEAEGKG 296
Cdd:PRK12316 2170 ---------------ALVAHCQAAGERYELSPADC--------ELQFMSFSFDGAHEQWFHPLLNGARvliRDDELWDPE 2226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 297 KIFDRAEK--VAIAwseaqELPggPG-LGLRAQHALFDKLVYRKLRAAMGGrcrDAISGGaplGARLGHffRGV-GVTIC 372
Cdd:PRK12316 2227 QLYDEMERhgVTIL-----DFP--PVyLQQLAEHAERDGRPPAVRVYCFGG---EAVPAA---SLRLAW--EALrPVYLF 2291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 373 EGYGLTETS------------PAAAANLPTGTRIGTVG--------RPLPGVTIridddGEVLIAGDIVFQGYWHNDAAT 432
Cdd:PRK12316 2292 NGYGPTEAVvtpllwkcrpqdPCGAAYVPIGRALGNRRayildadlNLLAPGMA-----GELYLGGEGLARGYLNRPGLT 2366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 433 AEAITTDGW-------FRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVV---GDRQPFI 502
Cdd:PRK12316 2367 AERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFR-IELGEIEARLQAHPAVREAVVVaqdGASGKQL 2445
|
490 500
....*....|....*....|...
gi 2504840381 503 AALV------TIDEEALPKWLAG 519
Cdd:PRK12316 2446 VAYVvpddaaEDLLAELRAWLAA 2468
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
93-496 |
4.12e-16 |
|
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: 81.27 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 93 WAAGAVTVPIY-----ETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRdrlPDLREVWQIDLGAvddlvAAGASVDR 167
Cdd:cd05929 38 GVWIADGVYIYlinsiLTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIK---AAALVCGLFTGGG-----ALDGLEDY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 168 AEVETRRSLSKADDVAT---IIYTSGTTGRPKGCV--LTHRNIYSDiANAVPVLPNLFRQGASTLLFLPLAHAfarliqv 242
Cdd:cd05929 110 EAAEGGSPETPIEDEAAgwkMLYSGGTTGRPKGIKrgLPGGPPDND-TLMAAALGFGPGADSVYLSPAPLYHA------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 243 gVVHARATMAHCA----------DTKNLVAELQDFKPTFVLSVPrvfekvyngarqkaeaegkgKIFDRAEKvaiawsea 312
Cdd:cd05929 182 -APFRWSMTALFMggtlvlmekfDPEEFLRLIERYRVTFAQFVP--------------------TMFVRLLK-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 313 qeLPggpglglRAQHALFDklvYRKLRAA--MGGRC-----RDAISGGAPLGARLGHFFRGVGVTICEGyglTE--TSPa 383
Cdd:cd05929 233 --LP-------EAVRNAYD---LSSLKRVihAAAPCppwvkEQWIDWGGPIIWEYYGGTEGQGLTIING---EEwlTHP- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 384 aaanlptgtriGTVGRPLPGVTIRIDDDGEVL---IAGDIVFQG----YWHND-AATAEAITTDGWFRTGDLGQLDENGY 455
Cdd:cd05929 297 -----------GSVGRAVLGKVHILDEDGNEVppgEIGEVYFANgpgfEYTNDpEKTAAARNEGGWSTLGDVGYLDEDGY 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2504840381 456 LSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:cd05929 366 LYLTDRRSDMIIS-GGVNIYPQEIENALIAHPKVLDAAVVG 405
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
47-560 |
7.49e-16 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 80.94 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 47 DVTCRQFRDEVVAVAQGLIAAgVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETS---SAEQAAWILGDSGAvAV 123
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPElpgHAERLDTALRDAEP-TV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VVESTAHATLVAGVRDRLPDLREVWQIDLGAVDDlvAAGASVDRAEVETrrslskaDDVATIIYTSGTTGRPKGCVLTHR 203
Cdd:PRK12476 146 VLTTTAAAEAVEGFLRNLPRLRRPRVIAIDAIPD--SAGESFVPVELDT-------DDVSHLQYTSGSTRPPVGVEITHR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 204 NIYSDIANAVPVLPNLFR--QGAStllFLPLAHAFArLIQVGVVharatmAHCADTKNLVAelqdfkPT-FVLSVPRVFE 280
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRntHGVS---WLPLYHDMG-LSMIGFP------AVYGGHSTLMS------PTaFVRRPQRWIK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 281 KVYNGARQkaeaegkGKIFDRAEKVAIAWSEAQELP-GGPGLGLRaqhalfdklvyrklRAAMggrcrdaISGGAPLG-A 358
Cdd:PRK12476 281 ALSEGSRT-------GRVVTAAPNFAYEWAAQRGLPaEGDDIDLS--------------NVVL-------IIGSEPVSiD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 359 RLGHF---FRGVGV---TICEGYGLTE-------TSPAAAAN--------LPTG--TRI-------------GTVGRPLP 402
Cdd:PRK12476 333 AVTTFnkaFAPYGLprtAFKPSYGIAEatlfvatIAPDAEPSvvyldreqLGAGraVRVaadapnavahvscGQVARSQW 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 403 GVTIRIDDD--------GEVLIAGDIVFQGYW----------------------HNDAATAEAIttdgWFRTGDLG-QLD 451
Cdd:PRK12476 413 AVIVDPDTGaelpdgevGEIWLHGDNIGRGYWgrpeetertfgaklqsrlaegsHADGAADDGT----WLRTGDLGvYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 452 enGYLSITGRKKEIIVTaGGKNVAPAVLEDQV-RAHPLIsqcvvvgdRQPFIAALVtideealpkwLAGQGRPETTSMAE 530
Cdd:PRK12476 489 --GELYITGRIADLIVI-DGRNHYPQDIEATVaEASPMV--------RRGYVTAFT----------VPAEDNERLVIVAE 547
|
570 580 590
....*....|....*....|....*....|
gi 2504840381 531 lREDAALRAEVQSAIDQANQAVSKAEAIKV 560
Cdd:PRK12476 548 -RAAGTSRADPAPAIDAIRAAVSRRHGLAV 576
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
368-470 |
1.03e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.52 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 368 GVTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIR------IDDDGEVLIAGDIVFQGYWHND---------AAT 432
Cdd:PRK08043 504 GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQGGRLQLKGPNIMNGYLRVEkpgvlevptAEN 583
|
90 100 110
....*....|....*....|....*....|....*...
gi 2504840381 433 AEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTAG 470
Cdd:PRK08043 584 ARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
347-495 |
4.22e-15 |
|
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: 77.61 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 347 RDAISGGAPLGARLGHFFRGV-GVTICEGYGLTETSpAAAANLP-TGTRIGTVGRPLPGVTIRIDD-------DGEV-LI 416
Cdd:cd05974 203 REVVGAGEPLNPEVIEQVRRAwGLTIRDGYGQTETT-ALVGNSPgQPVKAGSMGRPLPGYRVALLDpdgapatEGEVaLD 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 417 AGDI----VFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQC 492
Cdd:cd05974 282 LGDTrpvgLMKGYAGDPDKTAHAMR-GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEA 359
|
...
gi 2504840381 493 VVV 495
Cdd:cd05974 360 AVV 362
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
373-501 |
4.22e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 77.90 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 373 EGYGLTETS------PAAAANLPTgtrigTVGRPLPGVTIRI-DDDGEVLIAGDI---------VFQGYwHNDAATAEAI 436
Cdd:PRK07638 284 EFYGASELSfvtalvDEESERRPN-----SVGRPFHNVQVRIcNEAGEEVQKGEIgtvyvkspqFFMGY-IIGGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 437 TTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQPF 501
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIESVLHEHPAVDEIVVIGVPDSY 421
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
35-501 |
4.66e-15 |
|
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: 78.51 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 35 FVRPGAGTDARedVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWI 114
Cdd:cd05967 72 YDSPVTGTERT--YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 115 LGDSGAVAVVvesTAHATLVAG-VRDRLPDLRE-------------VWQ-----IDLGAV------DDLVAAGASVDRAE 169
Cdd:cd05967 150 IDDAKPKLIV---TASCGIEPGkVVPYKPLLDKalelsghkphhvlVLNrpqvpADLTKPgrdldwSELLAKAEPVDCVP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 170 VEtrrslskADDVATIIYTSGTTGRPKGCV-----------LTHRNIY-----------SDIANAV--------PVLpnl 219
Cdd:cd05967 227 VA-------ATDPLYILYTSGTTGKPKGVVrdngghavalnWSMRNIYgikpgdvwwaaSDVGWVVghsyivygPLL--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 frQGASTLLF------LPLAHAFARLIQvgvvharatmahcadtknlvaelqDFKPTFVLSVPRVFEkvyngARQKAEAE 293
Cdd:cd05967 297 --HGATTVLYegkpvgTPDPGAFWRVIE------------------------KYQVNALFTAPTAIR-----AIRKEDPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 294 GK-GKIFDraekvaiawseaqelpggpglgLRAQHALFdklvyrklraamggrcrdaiSGGAPLGARLGHFFRGV-GVTI 371
Cdd:cd05967 346 GKyIKKYD----------------------LSSLRTLF--------------------LAGERLDPPTLEWAENTlGVPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 372 CEGYGLTETSPAAAANlPTG-----TRIGTVGRPLPGVTIRI-DDDGEVLIA---GDIV---------FQGYWHNDAATA 433
Cdd:cd05967 384 IDHWWQTETGWPITAN-PVGleplpIKAGSPGKPVPGYQVQVlDEDGEPVGPnelGNIViklplppgcLLTLWKNDERFK 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 434 EAITTD--GWFRTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQCVVVGDRQPF 501
Cdd:cd05967 463 KLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHR-LSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-518 |
5.30e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.23 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 59 AVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTahatlvagVR 138
Cdd:PRK12316 548 RLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH--------LG 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 139 DRLPDLREVWQIDLGAVDDLVAAGASvdraevETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNiysdIANAVPVLPN 218
Cdd:PRK12316 620 RKLPLAAGVQVLDLDRPAAWLEGYSE------ENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA----LSNRLCWMQQ 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 219 LFRQGAS---------------TLLFLPLAHAfARLIQVGVVHARatmahcaDTKNLVAELQDFKPTFVLSVPRVFEKvy 283
Cdd:PRK12316 690 AYGLGVGdtvlqktpfsfdvsvWEFFWPLMSG-ARLVVAAPGDHR-------DPAKLVELINREGVDTLHFVPSMLQA-- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 ngarqkaeaegkgkiFDRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKL-------VYRKLRAAMGG---RCRDAISGG 353
Cdd:PRK12316 760 ---------------FLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLpqaglynLYGPTEAAIDVthwTCVEEGGDS 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 354 APLGARLGhffrGVGVTICEGYGltETSPAAAAnlptgtrigtvgrplpgvtiridddGEVLIAGDIVFQGYWHNDAATA 433
Cdd:PRK12316 825 VPIGRPIA----NLACYILDANL--EPVPVGVL-------------------------GELYLAGRGLARGYHGRPGLTA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 434 EAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVV-VGDRQPFIAALV 506
Cdd:PRK12316 874 ERFVPSPFvagermYRTGDLARYRADGVIEYAGRIDH-QVKLRGLRIELGEIEARLLEHPWVREAAVlAVDGKQLVGYVV 952
|
490
....*....|....*..
gi 2504840381 507 TIDE-----EALPKWLA 518
Cdd:PRK12316 953 LESEggdwrEALKAHLA 969
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
40-536 |
5.97e-15 |
|
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: 77.51 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 40 AGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSG 119
Cdd:cd17650 5 AVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVEStahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskaDDVATIIYTSGTTGRPKGCV 199
Cdd:cd17650 85 AKLLLTQP----------------------------------------------------EDLAYVIYTSGTTGKPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHRNIYSDIAN-----AVPVLPNLFRQGAStLLFLPLAHAFARLIQVGvvharATMAHCADtkNLVAELQDFKPTFVLS 274
Cdd:cd17650 113 VEHRNVAHAAHAwrreyELDSFPVRLLQMAS-FSFDVFAGDFARSLLNG-----GTLVICPD--EVKLDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 275 VPRVFEKVyngarqkaeaegkgkifdraekvaiawseaqelpggPGLGLRAQHALF-DKLVYRKLRAAMGGRCRDAISGG 353
Cdd:cd17650 185 RITLMEST------------------------------------PALIRPVMAYVYrNGLDLSAMRLLIVGSDGCKAQDF 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 354 APLGARLGHFFRgvgvtICEGYGLTETS------PAAAANLPTGTRIgTVGRPLPGVTIRIDDD----------GEVLIA 417
Cdd:cd17650 229 KTLAARFGQGMR-----IINSYGVTEATidstyyEEGRDPLGDSANV-PIGRPLPNTAMYVLDErlqpqpvgvaGELYIG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 418 GDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQ 491
Cdd:cd17650 303 GAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDH-QVKIRGFRIELGEIESQLARHPAIDE 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2504840381 492 CVVVgDRQpfiaalvtidEEALPKWLAGQGRP-ETTSMAELREDAA 536
Cdd:cd17650 382 AVVA-VRE----------DKGGEARLCAYVVAaATLNTAELRAFLA 416
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
71-514 |
8.40e-15 |
|
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: 77.06 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 71 PGDRVGL-MSRTryEWTLFD-YAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTahatlvagvrdrlpdlrevw 148
Cdd:cd17648 37 PDDLVGLvLDKS--ELMIIAiLAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNST-------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 149 qidlgavddlvaagasvdraevetrrslskadDVATIIYTSGTTGRPKGCVLTHRNIYSDIaNAVPVLPNLFRQGASTLL 228
Cdd:cd17648 95 --------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLR-TSLSERYFGRDNGDEAVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 229 FLPlAHAFARLIQvgvvhaRATMAHCADTKNLVAElqdfkPTFVLSVPRVFEkvYNGARQKAEAEGKGKIFDRAE----- 303
Cdd:cd17648 142 FFS-NYVFDFFVE------QMTLALLNGQKLVVPP-----DEMRFDPDRFYA--YINREKVTYLSGTPSVLQQYDlarlp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 304 --KVAIAWSEAqelpggpglglraqhalFDKLVYRKLRAAMGGRcrdaisggaplgarlghffrgvgvtICEGYGLTETS 381
Cdd:cd17648 208 hlKRVDAAGEE-----------------FTAPVFEKLRSRFAGL-------------------------IINAYGPTETT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 382 PAAAANL-PTGTRI-GTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW-------- 441
Cdd:cd17648 246 VTNHKRFfPGDQRFdKSLGRPVRNTKCYVLNDamkrvpvgavGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerar 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 442 ------FRTGDLGQLDENGYLSITGRkKEIIVTAGGKNVAPAVLEDQVRAHPLISQCVVV---------GDRQPFIAALV 506
Cdd:cd17648 326 grnarlYKTGDLVRWLPSGELEYLGR-NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasqaqSRIQKYLVGYY 404
|
....*...
gi 2504840381 507 TIDEEALP 514
Cdd:cd17648 405 LPEPGHVP 412
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
66-500 |
9.11e-15 |
|
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: 77.12 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 66 AAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVeSTAHATLVAGVRDRLPDL- 144
Cdd:cd05928 61 ACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT-SDELAPEVDSVASECPSLk 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 145 ---------REVWqidlGAVDDLVAAgASVDRAEVETrrslsKADDVATIIYTSGTTGRPK-----------GCV----- 199
Cdd:cd05928 140 tkllvseksRDGW----LNFKELLNE-ASTEHHCVET-----GSQEPMAIYFTSGTTGSPKmaehshsslglGLKvngry 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 ---LTHRNIY---SDIANAVPVLPNLFR---QGASTLlflplAHAFARLiqvgvvharatmahcaDTKNLVAELQDFKPT 270
Cdd:cd05928 210 wldLTASDIMwntSDTGWIKSAWSSLFEpwiQGACVF-----VHHLPRF----------------DPLVILKTLSSYPIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 271 FVLSVPRVFEKvyngarqkaeaegkgkifdraekvaiawseaqelpggpglglraqhalfdkLVYRKLRAAMGGRCRDAI 350
Cdd:cd05928 269 TFCGAPTVYRM---------------------------------------------------LVQQDLSSYKFPSLQHCV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 351 SGGAPLGAR-LGHFFRGVGVTICEGYGLTETSPAAAAnlPTGTRI--GTVGRPLPGVTIRI-DDDGEVL---IAGDI--- 420
Cdd:cd05928 298 TGGEPLNPEvLEKWKAQTGLDIYEGYGQTETGLICAN--FKGMKIkpGSMGKASPPYDVQIiDDNGNVLppgTEGDIgir 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 421 --------VFQGYWHNDAATAEAITTDGWFrTGDLGQLDENGYLSITGRKKEIIVTAGGKnVAPAVLEDQVRAHPLISQC 492
Cdd:cd05928 376 vkpirpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYR-IGPFEVESALIEHPAVVES 453
|
....*...
gi 2504840381 493 VVVGDRQP 500
Cdd:cd05928 454 AVVSSPDP 461
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
30-520 |
1.61e-14 |
|
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: 76.36 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 30 PDTVQFVrpgagtDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAE 109
Cdd:cd17656 2 PDAVAVV------FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 110 QAAWILGDSGAVAVVveSTAHATlvagvrDRLPDLREVWQIDlgavDDLVAAGASvdraevETRRSLSKADDVATIIYTS 189
Cdd:cd17656 76 RRIYIMLDSGVRVVL--TQRHLK------SKLSFNKSTILLE----DPSISQEDT------SNIDYINNSDDLLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 190 GTTGRPKGCVLTHRNI---------YSDIANAVPVLpnlfrQGASTLLFLPLAHAFARLIQVGVVHARATmahcaDTKNL 260
Cdd:cd17656 138 GTTGKPKGVQLEHKNMvnllhfereKTNINFSDKVL-----QFATCSFDVCYQEIFSTLLSGGTLYIIRE-----ETKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 261 VAELQDF---KPTFVLSVPRVFEKVYNGARQKAEAegkgkiFDRAEKVAIAWSEaqelpggpglglraqhalfdKLVYRK 337
Cdd:cd17656 208 VEQLFDLvkrHNIEVVFLPVAFLKFIFSEREFINR------FPTCVKHIITAGE--------------------QLVITN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 338 LRAAMggrcrdaisggaplgarlghfFRGVGVTICEGYGLTETSPAAAANLPTGTRIGT---VGRPLPGVTIRIDDD--- 411
Cdd:cd17656 262 EFKEM---------------------LHEHNVHLHNHYGPSETHVVTTYTINPEAEIPElppIGKPISNTWIYILDQeqq 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 412 -------GEVLIAGDIVFQGYWHNDAATAEAITTDGW------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAV 478
Cdd:cd17656 321 lqpqgivGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADH-QVKIRGYRIELGE 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 479 LEDQVRAHPLISQCVVVgDRQ---------PFIAALVTIDEEALPKWLAGQ 520
Cdd:cd17656 400 IEAQLLNHPGVSEAVVL-DKAddkgekylcAYFVMEQELNISQLREYLAKQ 449
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
43-205 |
2.14e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.01 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 43 DAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVA 122
Cdd:PRK10252 479 DARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 123 VVVEstahatlvAGVRDRLPDLREVwqiDLGAVDDLVAAGASVDRAevetrrsLSKADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PRK10252 559 LITT--------ADQLPRFADVPDL---TSLCYNAPLAPQGAAPLQ-------LSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
...
gi 2504840381 203 RNI 205
Cdd:PRK10252 621 TAI 623
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
171-515 |
1.19e-13 |
|
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: 73.62 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 171 ETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIYSdianAVPVLPNLFRQ--GASTLLFLPLAHAFARLI-QVGVVHA 247
Cdd:cd05937 78 GSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLV----TSNLLSHDLNLknGDRTYTCMPLYHGTAAFLgACNCLMS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 248 RATMA--HCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKaeaegkgkiFDRAEKVAIAWseaqelpggpGLGLRA 325
Cdd:cd05937 154 GGTLAlsRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSP---------YDRDHKVRVAW----------GNGLRP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 326 QhalfdklVYRKLRAamggrcRDAISggaplgarlghffrgvgvTICEGYGLTEtSPAAAANLPTGT-RIGTVGRPLP-- 402
Cdd:cd05937 215 D-------IWERFRE------RFNVP------------------EIGEFYAATE-GVFALTNHNVGDfGAGAIGHHGLir 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 403 -------GVTIRID-DDGEVLI--------------AGDIV----------FQGYWHNDAATAEAITT------DGWFRT 444
Cdd:cd05937 263 rwkfenqVVLVKMDpETDDPIRdpktgfcvrapvgePGEMLgrvpfknreaFQGYLHNEDATESKLVRdvfrkgDIYFRT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 445 GDLGQLDENGY------LSITGRKKeiivtagGKNVAPAVLEDQVRAHPLISQCVVVGDRQPFI-----AALVTIDEEAL 513
Cdd:cd05937 343 GDLLRQDADGRwyfldrLGDTFRWK-------SENVSTTEVADVLGAHPDIAEANVYGVKVPGHdgragCAAITLEESSA 415
|
..
gi 2504840381 514 PK 515
Cdd:cd05937 416 VP 417
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
181-500 |
1.48e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.51 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 181 DVATIIYTSGTTGRPKGCVLTHRNIYSDIANAV--------PVLpnlfrqgastLLFLPLAHAFARLIQVGVVhARATMA 252
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIigwemgtcPVY----------LWTLPMFHCNGWTFTWGTA-ARGGTS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 253 HC---ADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARqkaeaegkgkiFDRAEKvaiawseaqelpGGPglglraQHAL 329
Cdd:PLN03102 256 VCmrhVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNS-----------LDLSPR------------SGP------VHVL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 330 fdklvyrklraamggrcrdaiSGGAPLGARLGHFFRGVGVTICEGYGLTE-TSPAAAAN-------LP----------TG 391
Cdd:PLN03102 307 ---------------------TGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGPVLFCEwqdewnrLPenqqmelkarQG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 392 TRIGTVGR------------PLPGVTIridddGEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSIT 459
Cdd:PLN03102 366 VSILGLADvdvknketqesvPRDGKTM-----GEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIK 439
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2504840381 460 GRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQP 500
Cdd:PLN03102 440 DRSKDIIIS-GGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-512 |
1.49e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRD 139
Cdd:PRK12316 3095 LAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQV 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 RLPDlrevwqidlgavddlvaagASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRniysdianavpvlpnl 219
Cdd:PRK12316 3175 LDLD-------------------RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS---------------- 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 frqgastllflplahAFARLIQVgvvharatMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARqkAEAEGKGKIF 299
Cdd:PRK12316 3220 ---------------ALSNHLCW--------MQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGAR--VVLAGPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 300 DRAEKVAIAWSEAQELPGGPGLGLRAQHALFDKLVYRKLRAAMGGrcrdaisGGAPLGARLGHFFRGVGVTicEGYGLTE 379
Cdd:PRK12316 3275 DPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCG-------GEALPADLQQQVFAGLPLY--NLYGPTE 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 380 TSPAAAANLPTGTRIGT--VGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW------ 441
Cdd:PRK12316 3346 ATITVTHWQCVEEGKDAvpIGRPIANRACYILDGslepvpvgalGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerl 3425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 442 FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVVGDR-QPFIAALVTIDEEA 512
Cdd:PRK12316 3426 YRTGDLARYRADGVIEYIGRVDH-QVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVPEDEAG 3496
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
24-517 |
1.77e-13 |
|
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: 72.59 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVqfvrpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIY 103
Cdd:cd17645 6 EQVERTPDHV------AVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 104 ETSSAEQAAWILGDSGAVAVvvestahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrsLSKADDVA 183
Cdd:cd17645 80 PDYPGERIAYMLADSSAKIL----------------------------------------------------LTNPDDLA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 184 TIIYTSGTTGRPKGCVLTHRNiysdianavpvlpnlfrqgastllflplahafarLIQVGVVHARATMAHCADTKNLVAE 263
Cdd:cd17645 108 YVIYTSGSTGLPKGVMIEHHN----------------------------------LVNLCEWHRPYFGVTPADKSLVYAS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 264 LqdfkpTFVLSVPRVFEKVYNGA-------RQKAEAEGKGKIFDRaEKVAIAWseaqeLPggpgLGLRAQHALFDKLVYR 336
Cdd:cd17645 154 F-----SFDASAWEIFPHLTAGAalhvvpsERRLDLDALNDYFNQ-EGITISF-----LP----TGAAEQFMQLDNQSLR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 337 KLraamggrcrdaISGGAPLGArlghfFRGVGVTICEGYGLTETSPAAA--------ANLPtgtrigtVGRPLPGVTIRI 408
Cdd:cd17645 219 VL-----------LTGGDKLKK-----IERKGYKLVNNYGPTENTVVATsfeidkpyANIP-------IGKPIDNTRVYI 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 409 DDD----------GEVLIAGDIVFQGYWHNDAATAEA------ITTDGWFRTGDLGQLDENGYLSITGRKKEiIVTAGGK 472
Cdd:cd17645 276 LDEalqlqpigvaGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQ-QVKIRGY 354
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 473 NVAPAVLEDQVRAHPLISQCVVV----GDRQPFIAALVT----IDEEALPKWL 517
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLakedADGRKYLVAYVTapeeIPHEELREWL 407
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
187-495 |
7.59e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.41 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 187 YTSGTTGRPKGCVLTHRNIYSdIANAVPVLPNLfRQGASTLLFLPLAHAfarliqVGVVHARATMAHCA--------DTK 258
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYL-MALSNALIWGM-NEGAVYLWTLPMFHC------NGWCFTWTLAALCGtniclrqvTAK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 259 NLVAELQDFKPTFVLSVPRVFEKVYNGARQKAeaegkgkifdraekvaiawseAQELPggpglglRAQHALfdklvyrkl 338
Cdd:PLN02479 274 AIYSAIANYGVTHFCAAPVVLNTIVNAPKSET---------------------ILPLP-------RVVHVM--------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 339 raamggrcrdaISGGAPLGARLGHF-FRGVGVTicEGYGLTET-SPAAAA-------NLPTGTR-----------IGTVG 398
Cdd:PLN02479 317 -----------TAGAAPPPSVLFAMsEKGFRVT--HTYGLSETyGPSTVCawkpewdSLPPEEQarlnarqgvryIGLEG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 399 ---------RPLP--GVTIridddGEVLIAGDIVFQGYWHNDAATAEAITtDGWFRTGDLGQLDENGYLSITGRKKEIIV 467
Cdd:PLN02479 384 ldvvdtktmKPVPadGKTM-----GEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVKHPDGYIEIKDRSKDIII 457
|
330 340
....*....|....*....|....*...
gi 2504840381 468 TaGGKNVAPAVLEDQVRAHPLISQCVVV 495
Cdd:PLN02479 458 S-GGENISSLEVENVVYTHPAVLEASVV 484
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-496 |
5.50e-12 |
|
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: 68.15 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 46 EDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVV 125
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 126 estahatlvagvrdrlpdlrevwqidlgavddlvaagasvdraevetrrslskadDVATIIYTSGTTGRPKGCVLTHRNI 205
Cdd:cd05940 82 -------------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 206 YsdiaNAVPVLPNLFRQGASTLLF--LPLAHAFARLIQVG-VVHARATMA--HCADTKNLVAELQDFKPTFVlsvprvfe 280
Cdd:cd05940 107 W----RGGAFFAGSGGALPSDVLYtcLPLYHSTALIVGWSaCLASGATLVirKKFSASNFWDDIRKYQATIF-------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 281 kVYNGARQKAEAEGKGKIFDRAEKVAIAWseaqelpggpGLGLRAQhaLFDKLVYRklraamggrcrdaisggaplgarl 360
Cdd:cd05940 175 -QYIGELCRYLLNQPPKPTERKHKVRMIF----------GNGLRPD--IWEEFKER------------------------ 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 361 ghfFrGVGvTICEGYGLTETSpAAAANLPTgtRIGTVG-------------------------RPLPGVTIRIDDdGEV- 414
Cdd:cd05940 218 ---F-GVP-RIAEFYAATEGN-SGFINFFG--KPGAIGrnpsllrkvaplalvkydlesgepiRDAEGRCIKVPR-GEPg 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 415 LIAGDIV----FQGYWHNDAATAEAITT-----DGWFRTGDLGQLDENGYLSI------TGRKKeiivtagGKNVAPAVL 479
Cdd:cd05940 289 LLISRINplepFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFvdrlgdTFRWK-------GENVSTTEV 361
|
490
....*....|....*..
gi 2504840381 480 EDQVRAHPLISQCVVVG 496
Cdd:cd05940 362 AAVLGAFPGVEEANVYG 378
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
180-480 |
5.97e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 68.30 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 180 DDVATIIYTSGTTGRPKGCVLTHRNIysdIANAVPVL----PNlfrQGASTLLFLPLAHA--------FARLIQVGVVHA 247
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANL---LANQRACLkffsPK---EDDVMMSFLPPFHAygfnsctlFPLLSGVPVVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 248 RATMahcaDTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAegkgkiFDRAEKVAIawseaqelpGGPGLglraQH 327
Cdd:PRK06334 257 YNPL----YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESC------LPSLRFVVI---------GGDAF----KD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 328 ALFDKLvyRKLRAAmggrcrdaisggaplgarlghffrgvgVTICEGYGLTETSPAAAANLPTGTRIGT-VGRPLPGVTI 406
Cdd:PRK06334 314 SLYQEA--LKTFPH---------------------------IQLRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 407 RIDDD-----------GEVLIAGDIVFQGYWHNDAATA-EAITTDGWFRTGDLGQLDENGYLSITGRKKEiIVTAGGKNV 474
Cdd:PRK06334 365 LIVSEetkvpvssgetGLVLTRGTSLFSGYLGEDFGQGfVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMV 443
|
....*.
gi 2504840381 475 APAVLE 480
Cdd:PRK06334 444 SLEALE 449
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
45-513 |
1.37e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 67.21 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 45 REDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWtlfdYAIWAA----GAVTVPIYETSSAEQAAWILGDSGA 120
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEY----LAAWLGlaklGAVVALLNTQQRGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 121 VAVVVES-TAHAtlVAGVRDRLPDLREVWQ------IDLGAVDDLVAAGASVDRAEVETRRSLSkADDVATIIYTSGTTG 193
Cdd:PRK08279 136 KHLIVGEeLVEA--FEEARADLARPPRLWVaggdtlDDPEGYEDLAAAAAGAPTTNPASRSGVT-AKDTAFYIYTSGTTG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 194 RPKGCVLTHRNiysdIANAVPVLPNLFRQGASTLLF--LPLAHAFARLIQVG-VVHARATMAhcADTK----NLVAELQD 266
Cdd:PRK08279 213 LPKAAVMSHMR----WLKAMGGFGGLLRLTPDDVLYccLPLYHNTGGTVAWSsVLAAGATLA--LRRKfsasRFWDDVRR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 267 FKPTFVlsvprvfekVYNG------ARQKAEAEgkgkifDRAEKVAIAWseaqelpggpGLGLRAqhALFDKLVYRklra 340
Cdd:PRK08279 287 YRATAF---------QYIGelcrylLNQPPKPT------DRDHRLRLMI----------GNGLRP--DIWDEFQQR---- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 341 amggrcrdaisggaplgarlghFfrGVGvTICEGYGLTEtspaaaANlpTGT-----RIGTVGR-PLPGVT-IRI----- 408
Cdd:PRK08279 336 ----------------------F--GIP-RILEFYAASE------GN--VGFinvfnFDGTVGRvPLWLAHpYAIvkydv 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 409 -------DDDG--------EV-LIAGDIV----FQGYwHNDAATAEAITTDG------WFRTGDLGQLDENGYLSI---- 458
Cdd:PRK08279 383 dtgepvrDADGrcikvkpgEVgLLIGRITdrgpFDGY-TDPEASEKKILRDVfkkgdaWFNTGDLMRDDGFGHAQFvdrl 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 459 --TGRKKeiivtagGKNVAPAVLEDQVRAHPLISQCVVVGDRQPF------IAALVTIDEEAL 513
Cdd:PRK08279 462 gdTFRWK-------GENVATTEVENALSGFPGVEEAVVYGVEVPGtdgragMAAIVLADGAEF 517
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-483 |
3.29e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 65 IAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSA-----EQAAWILGDSGAVAVVVestahatlVAGVRD 139
Cdd:PRK05691 57 LQARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIADAEPRLLLT--------VADLRD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 RLPDLREVWQID---LGAVDDLVAAGASvdraevETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRNIysdIANAVpvl 216
Cdd:PRK05691 129 SLLQMEELAAANapeLLCVDTLDPALAE------AWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNL---VANEQ--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 217 pnLFRQGASTLL--------FLPLAHAFArliqvgvvharatmahcadtknLVAELqdFKPTF-----VLSVPRVFekvy 283
Cdd:PRK05691 197 --LIRHGFGIDLnpddvivsWLPLYHDMG----------------------LIGGL--LQPIFsgvpcVLMSPAYF---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 284 ngarqkaeaegkgkiFDRAEKVAIAWSE-AQELPGGPGLGLRAQHAlfdklvyRKLRAAMGG----RCRDAISGGAPLG- 357
Cdd:PRK05691 247 ---------------LERPLRWLEAISEyGGTISGGPDFAYRLCSE-------RVSESALERldlsRWRVAYSGSEPIRq 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 358 ---ARLGHFFRGVGVT---ICEGYGLTETS-------------------PAAAAN---LPTGTRIGTVGRPLPGVTIRID 409
Cdd:PRK05691 305 dslERFAEKFAACGFDpdsFFASYGLAEATlfvsggrrgqgipaleldaEALARNraePGTGSVLMSCGRSQPGHAVLIV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 410 DD-----------GEVLIAGDIVFQGYWHNDAATAEA-ITTDG--WFRTGDLGQLDEnGYLSITGRKKEIIVTAgGKNVA 475
Cdd:PRK05691 385 DPqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVR-GHNLY 462
|
....*...
gi 2504840381 476 PAVLEDQV 483
Cdd:PRK05691 463 PQDIEKTV 470
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
44-499 |
3.29e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.21 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 44 AREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAV 123
Cdd:PRK06060 27 AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VVESTahatlvagVRDRLPDLREVwqidlgAVDDLVAAGASVDRAEVEtrrsLSKADDVATIIYTSGTTGRPKGCVLTHR 203
Cdd:PRK06060 107 VTSDA--------LRDRFQPSRVA------EAAELMSEAARVAPGGYE----PMGGDALAYATYTSGTTGPPKAAIHRHA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 204 NIYSDI----ANAVPVLPN---------LFRQGASTLLFLPLAHAFARLIQVgvVHARATMAHCADTKnlvaelqdFKPT 270
Cdd:PRK06060 169 DPLTFVdamcRKALRLTPEdtglcsarmYFAYGLGNSVWFPLATGGSAVINS--APVTPEAAAILSAR--------FGPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 271 FVLSVPRVFEKVYNGARQKAEaegkgkifdRAEKVAIAWSEAQElpggPGLGlraqhalfdklvyrklraamggrcrdai 350
Cdd:PRK06060 239 VLYGVPNFFARVIDSCSPDSF---------RSLRCVVSAGEALE----LGLA---------------------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 351 sggaplgARLGHFFRGVgvTICEGYGLTETSPAAAANLPTGTRIGTVGRPLPGVTIRI----------DDDGEVLIAGDI 420
Cdd:PRK06060 278 -------ERLMEFFGGI--PILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVvapdgttagpGVEGDLWVRGPA 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 421 VFQGYWHNDAATaeaITTDGWFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNVAPAVLEDQVRAHPLISQCVVVGDRQ 499
Cdd:PRK06060 349 IAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLIIEDEAVAEAAVVAVRE 423
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
344-541 |
1.11e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.40 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 344 GRCRDAISGGAPLG-----------ARLGhFFRGVGVTiceGYGLTETSPAAAANLP-TGTRIGTV-------------- 397
Cdd:PRK05851 272 GALRVALNGGEPVDcdgferfatamAPFG-FDAGAAAP---SYGLAESTCAVTVPVPgIGLRVDEVttddgsgarrhavl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 398 GRPLPGVTIRI---DDD--------GEVLIAGDIVFQGYwhndaATAEAITTDGWFRTGDLGQLDENGyLSITGRKKEII 466
Cdd:PRK05851 348 GNPIPGMEVRIspgDGAagvagreiGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELI 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504840381 467 VTAgGKNVAPAVLEdQVRAHplisqcvVVGDRQPFIAALVTiDEEALpkwlagqgRPETTSMAELR--EDAALRAEV 541
Cdd:PRK05851 422 TVA-GRNIFPTEIE-RVAAQ-------VRGVREGAVVAVGT-GEGSA--------RPGLVIAAEFRgpDEAGARSEV 480
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
14-480 |
1.51e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.90 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 14 DAANLTDPVWENAEVAPDTV--QFVRPGAGTDARE-DVTCRQFRDEVVAVAQGLIAAGvSPGDRVGLMSRTRYEWTLFDY 90
Cdd:PRK07769 19 PNTNLVRHVERWAKVRGDKLayRFLDFSTERDGVArDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 91 AIWAAGAVTVPIY---ETSSAEQAAWILGDSGAVAVVVESTAHATLVAGVRDRLPDLR-EVWQIDlgAVDDLVaaGASVD 166
Cdd:PRK07769 98 GALYAGRIAVPLFdpaEPGHVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERpRVIAVD--AVPDEV--GATWV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 167 RAEVETrrslskaDDVATIIYTSGTTGRPKGCVLTHRNIYSdiaNAVPVLPNL-FRQGASTLLFLPLAHAFArLIQVgvv 245
Cdd:PRK07769 174 PPEANE-------DTIAYLQYTSGSTRIPAGVQITHLNLPT---NVLQVIDALeGQEGDRGVSWLPFFHDMG-LITV--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 246 haratmahcadtknLVAELQDFKPTFVlsVPRVF-EKVYNGARQKA-EAEGKGKIFDRAEKVAIAWSEAQELP--GGPGL 321
Cdd:PRK07769 240 --------------LLPALLGHYITFM--SPAAFvRRPGRWIRELArKPGGTGGTFSAAPNFAFEHAAARGLPkdGEPPL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 322 GLRAQHALfdklvyrklraamggrcrdaISGGAPLG-ARLGHFFRGVG------VTICEGYGLTETS------------- 381
Cdd:PRK07769 304 DLSNVKGL--------------------LNGSEPVSpASMRKFNEAFApyglppTAIKPSYGMAEATlfvsttpmdeept 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 382 -----------------PAAAANLPTGTRIGTVGRPL------PGVTIRIDDD--GEVLIAGDIVFQGYW---------- 426
Cdd:PRK07769 364 viyvdrdelnagrfvevPADAPNAVAQVSAGKVGVSEwavivdPETASELPDGqiGEIWLHGNNIGTGYWgkpeetaatf 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 427 HN------DAATAEAITTDG-WFRTGDLGQLdENGYLSITGRKKEIIVTaGGKNVAPAVLE 480
Cdd:PRK07769 444 QNilksrlSESHAEGAPDDAlWVRTGDYGVY-FDGELYITGRVKDLVII-DGRNHYPQDLE 502
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
394-513 |
1.76e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 394 IGTVGRPL-PGVTIRI-DDDGEVLIAGDI---------VFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRK 462
Cdd:PRK10946 352 FTTQGRPMsPDDEVWVaDADGNPLPQGEVgrlmtrgpyTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGRE 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2504840381 463 KEIIvTAGGKNVAPAVLEDQVRAHPLISQcvvvgdrqpfiAALVTIDEEAL 513
Cdd:PRK10946 432 KDQI-NRGGEKIAAEEIENLLLRHPAVIH-----------AALVSMEDELM 470
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
179-514 |
2.87e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 59.32 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 179 ADDVaTIIYTSGTTGRPKGCVLTHRNIYS------DIANAVPVLPNLF--RQGASTLLFL----PLAHAFARLIQVGVVH 246
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRmlmggaDFGTGEFTPSEDAhkAAAAAAGTVMfpapPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 247 ARATMAHCADTKNLVAELQDFKPTFVLSVPRVFEKVyngARQKAEAEGKGKIFDRAEKVAIAwseaqelPGGpglglraq 326
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAM---ARPLIDALRDAGPYDLSSLFAIS-------SGG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 327 hALFDKLVYRKLRAAMGGRcrdaisggaplgarlgHFFRGVGVTicEGyGLTETSPAAAANLPTGTRIgtvgRPLPGVTI 406
Cdd:cd05924 144 -ALLSPEVKQGLLELVPNI----------------TLVDAFGSS--ET-GFTGSGHSAGSGPETGPFT----RANPDTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 407 RIDDDGEVLIAGDIVFQ---------GYWHNDAATAEAI-TTDG--WFRTGDLGQLDENGYLSITGRKKEIIVTaGGKNV 474
Cdd:cd05924 200 LDDDGRVVPPGSGGVGWiarrghiplGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT-GGEKV 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2504840381 475 APAVLEDQVRAHPLISQCVVVGDRQP----FIAALVTIDEEALP 514
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVGRPDErwgqEVVAVVQLREGAGV 322
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
49-496 |
2.95e-08 |
|
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: 56.67 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILG---------DSG 119
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNhaedkvllfDPN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVESTahaTLVAGVRDRLPDLREVWQidlgaVDDLVAAGasvdRAEVETRRSLSKADDVAtIIYTSGTTGRPKGCV 199
Cdd:cd05915 106 LLPLVEAIR---GELKTVQHFVVMDEKAPE-----GYLAYEEA----LGEEADPVRVPERAACG-MAYTTGTTGLPKGVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 200 LTHRNIYSDiANAVPVLPNLFRQGASTLL-FLPLAH-----------AFARLI----QVG---------VVHARATMAHC 254
Cdd:cd05915 173 YSHRALVLH-SLAASLVDGTALSEKDVVLpVVPMFHvnawclpyaatLVGAKQvlpgPRLdpaslvelfDGEGVTFTAGV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 255 ADTKNLVAELQD-FKPTFVLSV---------PRVFEKVYN-GARQKAEAEGKGKIFDRAekVAIAW-SEAQELPGGPGLG 322
Cdd:cd05915 252 PTVWLALADYLEsTGHRLKTLRrlvvggsaaPRSLIARFErMGVEVRQGYGLTETSPVV--VQNFVkSHLESLSEEEKLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 323 LRAqhalfdklvyrklraamggrcRDAisggaplgarLGHFFRGVGVTIcegygltetspaaaanlPTgtrigTVGRPLP 402
Cdd:cd05915 330 LKA---------------------KTG----------LPIPLVRLRVAD-----------------EE-----GRPVPKD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 403 GVTIRIdddgeVLIAGDIVFQGYWHNDAATAEAITTDGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQ 482
Cdd:cd05915 357 GKALGE-----VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI-KSGGEWISSVDLENA 430
|
490
....*....|....
gi 2504840381 483 VRAHPLISQCVVVG 496
Cdd:cd05915 431 LMGHPKVKEAAVVA 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-495 |
3.47e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.10 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 65 IAAGVSPGDRVGLMsrtryewtlfdyAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVEStahatlvaGVRDRLPDL 144
Cdd:PRK05691 1186 IAAERSPQLLVGLL------------AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS--------HLLERLPQA 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 145 REVWQIDLGAVDdlvaagasVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTHRniysdianavpvlpnlfrqga 224
Cdd:PRK05691 1246 EGVSAIALDSLH--------LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHA--------------------- 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 225 stllflplahAFARLIQvgvvHARATMAHCADTknlvAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEGKGKIFDRAEK 304
Cdd:PRK05691 1297 ----------ALAERLQ----WMQATYALDDSD----VLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAE 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 305 VAIAWSEAQELPGGPGLGLRAQHALfdklvyrklrAAMGGRCRDAISGGAPLGARLGHFFRGV--GVTICEGYGLTETSP 382
Cdd:PRK05691 1359 LVQQYGVTTLHFVPPLLQLFIDEPL----------AAACTSLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAI 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 383 AAA---ANLPTGTRiGTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW-------F 442
Cdd:PRK05691 1429 NVThwqCQAEDGER-SPIGRPLGNVLCRVLDAelnllppgvaGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlY 1507
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2504840381 443 RTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVV 495
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQ-QVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
4-202 |
4.54e-08 |
|
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: 56.13 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 4 FSVPPIVTVGDAANLTDPVW---------ENA---EVAPDTVQFVRpgAGTDAREDVTCRQFRDEVVAVAQGLIAAGVSP 71
Cdd:cd05943 45 GSKPYDVVVVSGRIMPGARWfpgarlnyaENLlrhADADDPAAIYA--AEDGERTEVTWAELRRRVARLAAALRALGVKP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 72 GDRVGLMSRTRYEwTLFDY-------AIWAAGAVtvpiyetssaeqaawilgDSGAVAVV-------------VESTA-- 129
Cdd:cd05943 123 GDRVAGYLPNIPE-AVVAMlatasigAIWSSCSP------------------DFGVPGVLdrfgqiepkvlfaVDAYTyn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 130 -----HATLVAGVRDRLPDLREV---------WQIDLGAV------DDLVAAGASVDRAEVETrrslsKADDVATIIYTS 189
Cdd:cd05943 184 gkrhdVREKVAELVKGLPSLLAVvvvpytvaaGQPDLSKIakaltlEDFLATGAAGELEFEPL-----PFDHPLYILYSS 258
|
250
....*....|...
gi 2504840381 190 GTTGRPKGCVLTH 202
Cdd:cd05943 259 GTTGLPKCIVHGA 271
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
24-548 |
5.27e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.72 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 24 ENAEVAPDTVQFVRPGAGTD---AREDVTCRQFRDEVVAVAQGLIAAGvSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTV 100
Cdd:PRK05850 9 ERASLQPDDAAFTFIDYEQDpagVAETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 101 PIYET---SSAEQAAWILGDSGAVAVVVESTAhATLVAGVRDRLPDLREVWQIDLGAVDDLVAAGASVDRAEvetrrsls 177
Cdd:PRK05850 88 PLSVPqggAHDERVSAVLRDTSPSVVLTTSAV-VDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRD-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 178 kADDVATIIYTSGTTGRPKGCVLTHRNIysdIANAVPVLPNLFR-------QGASTLLFLPLAHAFArLIqVGVVharAT 250
Cdd:PRK05850 159 -LPSTAYLQYTSGSTRTPAGVMVSHRNV---IANFEQLMSDYFGdtggvppPDTTVVSWLPFYHDMG-LV-LGVC---AP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 251 M--AHCADTKNLVAELQdfKPT----FVLSVPRVFEKVYN-----GARQKAEAEGKGK-------IFDRAEKVAIA---- 308
Cdd:PRK05850 230 IlgGCPAVLTSPVAFLQ--RPArwmqLLASNPHAFSAAPNfafelAVRKTSDDDMAGLdlggvlgIISGSERVHPAtlkr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 309 ---------WSEAQELP-------------GGPGLGLRAQHalFDklvYRKLRAAMGGRCRDaiSGGAPLgarlghffrg 366
Cdd:PRK05850 308 fadrfapfnLRETAIRPsyglaeatvyvatREPGQPPESVR--FD---YEKLSAGHAKRCET--GGGTPL---------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 367 vgvticEGYGLTETS------PAAAANLPTGTRigtvgrplpgvtiridddGEVLIAGDIVFQGYWHNDAATAE------ 434
Cdd:PRK05850 371 ------VSYGSPRSPtvrivdPDTCIECPAGTV------------------GEIWVHGDNVAAGYWQKPEETERtfgatl 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 435 ----AITTDG-WFRTGDLGQLDEnGYLSITGRKKE-IIVTagGKNVAPAVLEDQVRAhplisqcvVVGDRQPFIAA---- 504
Cdd:PRK05850 427 vdpsPGTPEGpWLRTGDLGFISE-GELFIVGRIKDlLIVD--GRNHYPDDIEATIQE--------ITGGRVAAISVpddg 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2504840381 505 ---LVTIDEealpkwLAGQGRPETTSMAELRedaALRAEVQSAIDQA 548
Cdd:PRK05850 496 tekLVAIIE------LKKRGDSDEEAMDRLR---TVKREVTSAISKS 533
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-205 |
5.78e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 56.32 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 61 AQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTahatlvagVRDR 140
Cdd:PRK12467 1613 AHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH--------LQAR 1684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 141 LPDLREVWQIDLGAVDDLVAAGASVDRAevetrrSLSKADDVATIIYTSGTTGRPKGCVLTHRNI 205
Cdd:PRK12467 1685 LPLPDGLRSLVLDQEDDWLEGYSDSNPA------VNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
375-511 |
8.88e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 54.90 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 375 YGLTETSPAAAA------------NLPtgtrigtVGRPLPGVTIRIDD----------DGEVLIAGDIVFQGYWHNDAAT 432
Cdd:PRK04813 293 YGPTEATVAVTSieitdemldqykRLP-------IGYAKPDSPLLIIDeegtklpdgeQGEIVISGPSVSKGYLNNPEKT 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 433 AEAITT-DGW--FRTGDLGQLDeNGYLSITGRKKEIIVTAGGKnvapAVLED---QVRAHPLISQCVVV-----GDRQPF 501
Cdd:PRK04813 366 AEAFFTfDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYR----IELEEieqNLRQSSYVESAVVVpynkdHKVQYL 440
|
170
....*....|
gi 2504840381 502 IAALVTIDEE 511
Cdd:PRK04813 441 IAYVVPKEED 450
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
363-496 |
1.19e-06 |
|
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: 51.41 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 363 FFRGVG---VTICEGYGLTETSPAAAANLP--TGTRIGTVGRPLPGVTIRI-DDDGEVL---IAGDIVF----------- 422
Cdd:cd05966 373 YYEVIGkerCPIVDTWWQTETGGIMITPLPgaTPLKPGSATRPFFGIEPAIlDEEGNEVegeVEGYLVIkrpwpgmarti 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 423 --------QGYWHNDAataeaittdGWFRTGDLGQLDENGYLSITGRKKEIIVTAgGKNVAPAVLEDQVRAHPLISQCVV 494
Cdd:cd05966 453 ygdheryeDTYFSKFP---------GYYFTGDGARRDEDGYYWITGRVDDVINVS-GHRLGTAEVESALVAHPAVAEAAV 522
|
..
gi 2504840381 495 VG 496
Cdd:cd05966 523 VG 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
60-542 |
2.05e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 60 VAQGLIAAGVSPGDRVGLMSRTRYEWTLFDYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAVVVESTAHATLvagvrD 139
Cdd:PRK05691 2226 LARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEAL-----G 2300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 140 RLPDLREVWQIDlgavDDLvAAGASVDRAEVEtrrSLSKADDVATIIYTSGTTGRPKGCVLTHRNIysdianavpvlpnl 219
Cdd:PRK05691 2301 ELPAGVARWCLE----DDA-AALAAYSDAPLP---FLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI-------------- 2358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 220 frqgastllflplahafarliqvgVVHARATMAHcADTKNLVAELQDFKPTFVLSVPRVFEKVYNGARQKAEAEGKGKIF 299
Cdd:PRK05691 2359 ------------------------AMHCQAVIER-FGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAE 2413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 300 D-----RAEKVAIawseaqeLPGGPGLGlrAQHALFDKLVYRKLRAAMggrcrdAISGGAPL-GARL---------GHFF 364
Cdd:PRK05691 2414 EicqliREQQVSI-------LGFTPSYG--SQLAQWLAGQGEQLPVRM------CITGGEALtGEHLqrirqafapQLFF 2478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 365 rgvgvticEGYGLTETS------------PAAAANLPTGTRIGTvgrplpGVTIRIDDD---------GEVLIAGDIVFQ 423
Cdd:PRK05691 2479 --------NAYGPTETVvmplaclapeqlEEGAASVPIGRVVGA------RVAYILDADlalvpqgatGELYVGGAGLAQ 2544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 424 GYWHNDAATAEAITTDGW-------FRTGDLGQLDENGYLSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQCVVVg 496
Cdd:PRK05691 2545 GYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDH-QVKIRGFRIELGEIESRLLEHPAVREAVVL- 2622
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2504840381 497 drqpfiaALVTIDEEALPKWLAG-QGRPETTSMAELREdaALRAEVQ 542
Cdd:PRK05691 2623 -------ALDTPSGKQLAGYLVSaVAGQDDEAQAALRE--ALKAHLK 2660
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
42-202 |
2.49e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.10 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 42 TDAREDVTCRQFRDEVVAVAQGLIAAGVSPGDRVglmsrtryewtlfdyaiwaagAVTVP-IYETSSAEQAAWILG---- 116
Cdd:PRK03584 109 DGPRRELSWAELRRQVAALAAALRALGVGPGDRV---------------------AAYLPnIPETVVAMLATASLGaiws 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 117 ----DSGAVAVV-----VEST-------------AHATL--VAGVRDRLPDLREVWQID-LGAVDDLVAAGASVDRAEVe 171
Cdd:PRK03584 168 scspDFGVQGVLdrfgqIEPKvliavdgyryggkAFDRRakVAELRAALPSLEHVVVVPyLGPAAAAAALPGALLWEDF- 246
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2504840381 172 trrsLSKADDVAT------------IIYTSGTTGRPKGCVLTH 202
Cdd:PRK03584 247 ----LAPAEAAELefepvpfdhplwILYSSGTTGLPKCIVHGH 285
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
53-252 |
2.71e-05 |
|
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: 46.90 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 53 FRDEVVAVAQG-----------LIAAGVSPGDRVGLM--SRTRYEWTLFDYAiwAAGAVTVPIYETSSAEQAAWILGDSG 119
Cdd:cd05938 1 FEGETYTYRDVdrrsnqaaralLAHAGLRPGDTVALLlgNEPAFLWIWLGLA--KLGCPVAFLNTNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 120 AVAVVVEstahATLVAGVRDRLPDLRE----VWQIDLGA----VDDLVAA-GASVDRAEVETRRSLSKADDVATIIYTSG 190
Cdd:cd05938 79 AKVLVVA----PELQEAVEEVLPALRAdgvsVWYLSHTSntegVISLLDKvDAASDEPVPASLRAHVTIKSPALYIYTSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504840381 191 TTGRPKGCVLTHRNIYSDIAnavpvLPNLFRQGASTLLF--LPLAHAFARLIQ-VGVVHARATMA 252
Cdd:cd05938 155 TTGLPKAARISHLRVLQCSG-----FLSLCGVTADDVIYitLPLYHSSGFLLGiGGCIELGATCV 214
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
48-202 |
2.96e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 47.00 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLIAAGVSPGDRVGL-MSRTRYEWTLFdYAIWAAGAVTVPIYETSSAEQAAWILGDSGAVAV--- 123
Cdd:PLN03052 209 MTLSELRSQVSRVANALDALGFEKGDAIAIdMPMNVHAVIIY-LAIILAGCVVVSIADSFAPSEIATRLKISKAKAIftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 ---------------VVESTAHATLVAGVRDRLPD--LRE---VWqidlgavDDLVAAGASVDRAEvETRRSLSKADDVA 183
Cdd:PLN03052 288 dvivrggksiplysrVVEAKAPKAIVLPADGKSVRvkLREgdmSW-------DDFLARANGLRRPD-EYKAVEQPVEAFT 359
|
170
....*....|....*....
gi 2504840381 184 TIIYTSGTTGRPKGCVLTH 202
Cdd:PLN03052 360 NILFSSGTTGEPKAIPWTQ 378
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
374-496 |
3.69e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 46.66 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 374 GYGLTETSPA-----AAANLPtgtrIGTVGRPLPGVTIRI-DDDGEVLIA---GDIVFQ---------GYWHNDAATAEA 435
Cdd:PTZ00237 411 GYGQTEIGITylycyGHINIP----YNATGVPSIFIKPSIlSEDGKELNVneiGEVAFKlpmppsfatTFYKNDEKFKQL 486
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 436 ITT-DGWFRTGDLGQLDENGYLSITGRKKEIIvTAGGKNVAPAVLEDQVRAHPLISQCVVVG 496
Cdd:PTZ00237 487 FSKfPGYYNSGDLGFKDENGYYTIVSRSDDQI-KISGNKVQLNTIETSILKHPLVLECCSIG 547
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
176-533 |
1.20e-04 |
|
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: 44.73 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 176 LSKADDVATIIYTSGTTGRPKGCVLTHRNI--YSDIANAVPVLPNLFRqgasTLLFLPLA-HAFARLIQV------GVVH 246
Cdd:cd17644 102 LTQPENLAYVIYTSGSTGKPKGVMIEHQSLvnLSHGLIKEYGITSSDR----VLQFASIAfDVAAEEIYVtllsgaTLVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 247 ARATMAhcADTKNLVAELQDFKPTfVLSVPRVFekvyngarqkaeaegkgkifdraekvaiaWSE-----AQELPGGPgl 321
Cdd:cd17644 178 RPEEMR--SSLEDFVQYIQQWQLT-VLSLPPAY-----------------------------WHLlvlelLLSTIDLP-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 322 glraqHALfdKLVyrklraamggrcrdAISGGAPLGARLGHFFRGVG--VTICEGYGLTETSPAAAANLPTG------TR 393
Cdd:cd17644 224 -----SSL--RLV--------------IVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQlterniTS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 394 IgTVGRPLPGVTIRIDDD----------GEVLIAGDIVFQGYWHNDAATAEAITTDGW--------FRTGDLGQLDENGY 455
Cdd:cd17644 283 V-PIGRPIANTQVYILDEnlqpvpvgvpGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGN 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504840381 456 LSITGRKKEiIVTAGGKNVAPAVLEDQVRAHPLISQ-CVVVGDRQPFIAALVTideealpkWLAGQgRPETTSMAELRE 533
Cdd:cd17644 362 IEYLGRIDN-QVKIRGFRIELGEIEAVLSQHNDVKTaVVIVREDQPGNKRLVA--------YIVPH-YEESPSTVELRQ 430
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
91-202 |
1.32e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 91 AIWAAGAVTVPIYETSSAEQAAWILGDSGAVAV------------------VVESTAHATLVAGV--RDRLPDLREVwqi 150
Cdd:PLN03051 13 AIVLAGCVVVSVADSFSAKEIATRLDISGAKGVftqdvvlrggralplyskVVEAAPAKAIVLPAagEPVAVPLREQ--- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2504840381 151 DLGAVDDLVAAGASVDRAEVETRRSLSKADDVATIIYTSGTTGRPKGCVLTH 202
Cdd:PLN03051 90 DLSWCDFLGVAAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTH 141
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
49-243 |
3.35e-03 |
|
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: 40.10 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 49 TCRQFRDEVVAVAQGLIAAGVSPGDRVGLMSRTRYEWtlfdYAIWAA----GAVTVPIYETSSAEQAAWILGDSGAVAVV 124
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEF----VALWLGlakiGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 125 VESTAhaTLVAGVRDRLPDlrevwQIDLGAVDDLVaagasvdraevetrrslskaddvatIIYTSGTTGRPKGCVLTHRN 204
Cdd:cd05939 81 FNLLD--PLLTQSSTEPPS-----QDDVNFRDKLF-------------------------YIYTSGTTGLPKAAVIVHSR 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2504840381 205 IYSDIANAVpvlpNLFRQGASTLLF--LPLAHAFARLIQVG 243
Cdd:cd05939 129 YYRIAAGAY----YAFGMRPEDVVYdcLPLYHSAGGIMGVG 165
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
48-207 |
3.43e-03 |
|
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: 40.41 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 48 VTCRQFRDEVVAVAQGLI-AAGVSPGDRVGLMSRTRYEwtlFDYAIWA---AGAVTVPIYETSSAEQAAWILGdsgAVAV 123
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLD---FVAAFYGclyAGVVPIPIEPPDISQQLGFLLG---TCKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504840381 124 VVESTAHATLVAGVRDRLPDLREvwqidlGAVDDLVAAGASVDRAEVETRRSLSK----------ADDVATIIYTSGTTG 193
Cdd:cd05905 89 RVALTVEACLKGLPKKLLKSKTA------AEIAKKKGWPKILDFVKIPKSKRSKLkkwgphpptrDGDTAYIEYSFSSDG 162
|
170
....*....|....
gi 2504840381 194 RPKGCVLTHRNIYS 207
Cdd:cd05905 163 SLSGVAVSHSSLLA 176
|
|
| |
