|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
62-579 |
0e+00 |
|
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: 672.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEICRvlqcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLA----LGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkdRGAMIIYTSGTTGRPKGV 221
Cdd:cd05941 77 EYVITDSEPSLVL-------------------------------------------------DPALILYTSGTTGRPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWkkfLSSQAPRVSVFMA 301
Cdd:cd05941 108 VLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 302 VPTIYAKLIEYYDEHFSQPQvqdFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVR 381
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDPQ---FARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 382 VPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQmtPGLEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWF 461
Cdd:cd05941 262 RPGTVGMPLPGVQARIV-----------------DEETGE--PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 462 RTGDTAAY-HDGVYWIKGRTSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRG-EMLSVK 539
Cdd:cd05941 323 KTGDLGVVdEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLE 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1201832555 540 ELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:cd05941 403 ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-581 |
3.97e-140 |
|
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: 414.21 E-value: 3.97e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYR 134
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLA----AALR--ALGVGPgDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHPVQQLEYVIEDSQSALVIAAeeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkdrgaMIIYTSGT 214
Cdd:COG0318 82 RLTAEELAYILEDSGARALVTA--------------------------------------------------LILYTSGT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFlssQAP 294
Cdd:COG0318 112 TGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELI---ERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 RVSVFMAVPTIYAKLIEYYD---EHFSqpqvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGM 371
Cdd:COG0318 189 RVTVLFGVPTMLARLLRHPEfarYDLS--------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALS-NPL-HGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPK 449
Cdd:COG0318 255 VVTvNPEdPGERRPGSVGRPLPGVEVRIV-----------------DEDGRELPPG---EVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:COG0318 315 ATAEAF-RDGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 529 QLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:COG0318 393 VLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
57-577 |
1.27e-115 |
|
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: 351.87 E-value: 1.27e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAIIDQNGEHTYRELfcrsLRLSQEICRVLQCSsrDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:cd05936 9 ARRFPDKTALIFMGRKLTYREL----DALAEAFAAGLQNL--GVQPgDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLgshssgsaghtavEDVplassaswkdrgAMIIYTSGTT 215
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALTP-------------EDV------------AVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTHEN-------VQAVTTGLVEKwewkkEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKF 288
Cdd:cd05936 138 GVPKGAMLTHRNlvanalqIKAWLEDLLEG-----DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 lssQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE 368
Cdd:cd05936 213 ---RKHRVTIFPGVPTMYIALLNAPEFKKRDFS-----------SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 IG-MALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNR 447
Cdd:cd05936 279 TSpVVAVNPLDGPRKPGSIGIPLPGTEVKIV-----------------DDDGEELPPG---EVGELWVRGPQVMKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 448 PKETREAFTsDGWFRTGDTAaY--HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVS 525
Cdd:cd05936 339 PEETAEAFV-DGWLRTGDIG-YmdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVK 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 526 AVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05936 416 AFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
62-581 |
1.46e-106 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 329.53 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEH-TYRELFCRSLRLSqeicRVLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPL---YRKH 136
Cdd:PRK07514 17 DAPFIETPDGLRyTYGDLDAASARLA----NLLV--ALGVKPgDRVAVQVEKSPEALALYLATLRAGAVFLPLntaYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 137 pvqQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVP-VLPLGSHSSGS-----AGH-TAVEDVPLASsaswkDRGAMII 209
Cdd:PRK07514 91 ---ELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPhVETLDADGTGSlleaaAAApDDFETVPRGA-----DDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFl 289
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 290 ssqaPRVSVFMAVPTIYAKLIeyydehfsqpQVQDFVRAFCQeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEI 369
Cdd:PRK07514 242 ----PRATVMMGVPTFYTRLL----------QEPRLTREAAA-HMRLFISGSAPLLAETHREFQERTGHAILERYGMTET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 370 GMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqGDEDGTQMTPgleGQEGELLVRGSSVFREYWNRPK 449
Cdd:PRK07514 307 NMNTSNPYDGERRAGTVGFPLPGVSLRVT----------------DPETGAELPP---GEIGMIEVKGPNVFKGYWRMPE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREAFTSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:PRK07514 368 KTAEEFRADGFFITGDLGKIdERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 529 QLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK07514 447 VPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
104-579 |
6.38e-104 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 321.55 E-value: 6.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 104 RISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAeeyvgkisPSAEKLGVPVLPLGSHSSG 183
Cdd:PRK07787 47 RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP--------APDDPAGLPHVPVRLHARS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 184 saGHTAVEdvPLASSAswkdrgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKL 263
Cdd:PRK07787 119 --WHRYPE--PDPDAP------ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 264 LCPLWVGATCIMLPEFSAQMVwkkfLSSQAPRVSVFMAVPTIYAKLIEyydehfsqpqVQDFVRAFcqENIRLMVSGSAA 343
Cdd:PRK07787 189 LGPLRIGNRFVHTGRPTPEAY----AQALSEGGTLYFGVPTVWSRIAA----------DPEAARAL--RGARLLVSGSAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 344 LPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMT 423
Cdd:PRK07787 253 LPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLV-----------------DEDGGPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 424 pgLEGQE-GELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSVDIIKNGGFKISALEVERQL 501
Cdd:PRK07787 316 --HDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETAL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 502 LAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:PRK07787 394 LGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
62-579 |
5.78e-99 |
|
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: 309.63 E-value: 5.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELfcrsLRLSQEICRVLQcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPL---YRKhpv 138
Cdd:cd05926 4 PALVVPGSTPALTYADL----AELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLnpaYKK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 QQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLG-----SHSSGSAG----HTAVEDVPLASSASWKDRGAMII 209
Cdd:cd05926 76 AEFEFYLADLGSKLVLTPKGELGPASRAASKLGLAILELAldvgvLIRAPSAEslsnLLADKKNAKSEGVPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFl 289
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDV- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 290 ssQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQVQdfvrafcqenIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEI 369
Cdd:cd05926 235 --RDYNATWYTAVPTIHQILLNRPEPNPESPPPK----------LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 370 G--MAlSNPL-HGVRVPGSVGTPLpGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWN 446
Cdd:cd05926 303 AhqMT-SNPLpPGPRKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVGEICLRGPNVTRGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 447 RPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVS 525
Cdd:cd05926 361 NPEANAEAAFKDGWFRTGDLGYLdADGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVA 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 526 AVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:cd05926 440 AAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
56-574 |
2.53e-98 |
|
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: 306.07 E-value: 2.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPL 132
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLA----HAL----RALgvaKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 133 -YRKHPVQqLEYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkDRGAMIIYT 211
Cdd:cd17631 76 nFRLTPPE-VAYILADSGAKVLF------------------------------------------------DDLALLMYT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 212 SGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFlss 291
Cdd:cd17631 107 SGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI--- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 292 QAPRVSVFMAVPTIYAKLIEYydehfSQPQVQDFVRafcqenIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTEIGM 371
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH-----PRFATTDLSS------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALS--NPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPK 449
Cdd:cd17631 252 GVTflSPEDHRRKLGSAGRPVFFVEVRIV-----------------DPDGREVPPG---EVGEIVVRGPHVMAGYWNRPE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREAFtSDGWFRTGDtAAY--HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAV 527
Cdd:cd17631 312 ATAAAF-RDGWFHTGD-LGRldEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAV 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1201832555 528 VQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNK 574
Cdd:cd17631 389 VVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
206-572 |
7.36e-97 |
|
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: 298.82 E-value: 7.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVhGVINKLLCPLWVGATCIMLPEFSAQMVW 285
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKFlssQAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDFVRAfcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYG 365
Cdd:cd04433 82 ELI---EREKVTILLGVPTLLARLLK-------APESAGYDLS----SLRALVSGGAPLPPELLERFEEAPGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTEIG--MALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTqmtPGLEGQEGELLVRGSSVFRE 443
Cdd:cd04433 148 LTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIV-----------------DPDGG---ELPPGEIGELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPkETREAFTSDGWFRTGDtAAYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWG 521
Cdd:cd04433 208 YWNNP-EATAAVDEDGWYRTGD-LGRLDedGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWG 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 522 QRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKV 572
Cdd:cd04433 285 ERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-581 |
1.64e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 304.03 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 60 FGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPL-YRK 135
Cdd:PRK06187 19 HPDKEAVYFDGRRTTYAELDERVNRLA----NAL----RALgvkKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPvQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLG-----VPVLPLGSHSSGSAGHTAVEDVPLASSAS-WKDRG---- 205
Cdd:PRK06187 91 KP-EEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtvrtvIVEGDGPAAPLAPEVGEYEELLAAASDTFdFPDIDenda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTH----ENVQAVTTGLvekwEWKKEDVILHVLPLHHVHGvinkLLCP---LWVGATCIMLPE 278
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHrnlfLHSLAVCAWL----KLSRDDVYLVIVPMFHVHA----WGLPylaLMAGAKQVIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 279 FSAQMVWKKFLSSqapRVSVFMAVPTIYAKLIEYYDEHFsqpqvQDFVRafcqenIRLMVSGSAALPVPVLKKWKAITGH 358
Cdd:PRK06187 242 FDPENLLDLIETE---RVTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKFGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 359 TLLERYGMTEIGMALS-NPLH-----GVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMtPGLEGQEGE 432
Cdd:PRK06187 308 DLVQGYGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIV-----------------DDDGDEL-PPDGGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 433 LLVRGSSVFREYWNRPKETREAFTsDGWFRTGDtAAY--HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDV 510
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETID-GGWLHTGD-VGYidEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 511 AVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK06187 447 AVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
53-488 |
4.83e-89 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 281.51 E-value: 4.83e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 53 VFTRALTFGDKIAIIDQNGEH-TYRELFCRSLRLSqeicRVLQcsSRDL-KEERISFLCPNDASYVVAQWASWMSGGIAV 130
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRlTYRELDERANRLA----AGLR--ALGVgKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 131 PLYRKHPVQQLEYVIEDSQSALVIAAEE-YVGKISPSAEKLGVPVLPLGSHSSGSAGHTAV-------EDVPLASSASWK 202
Cdd:pfam00501 75 PLNPRLPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLpeeakpaDVPPPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHENV--QAVTTGLVEKWEWK--KEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPE 278
Cdd:pfam00501 155 DDLAYIIYTSGTTGKPKGVMLTHRNLvaNVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 279 FSAQMVWKKFLSSQAPRVSVFMAVPTIYAKLIEyydehfsqpqvQDFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGH 358
Cdd:pfam00501 235 FPALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 359 TLLERYGMTEIGMALSNPLHGV---RVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLV 435
Cdd:pfam00501 304 ALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIV-----------------DDETGEPVP--PGEPGELCV 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 436 RGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNG 488
Cdd:pfam00501 365 RGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDeDGYLEIVGRKK-DQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
57-572 |
5.42e-87 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 280.46 E-value: 5.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAII--DQNGEH---TYRELFCRSLRLSQeicrVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGI 128
Cdd:COG0365 19 AEGRGDKVALIweGEDGEErtlTYAELRREVNRFAN----AL----RALgvkKGDRVAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 129 AVPLYrkhP---VQQLEYVIEDSQSALVIAAEEYV--GKISPSAEKL-----GVP------VLPLGSHSSGSAGHTAVED 192
Cdd:COG0365 91 HSPVF---PgfgAEALADRIEDAEAKVLITADGGLrgGKVIDLKEKVdealeELPslehviVVGRTGADVPMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 193 VPLASSASWK------DRGAMIIYTSGTTGRPKGVLSTHEN--VQAVTTGlveKW--EWKKEDVILHVLPLHHVHGVINK 262
Cdd:COG0365 168 LLAAASAEFEpeptdaDDPLFILYTSGTTGKPKGVVHTHGGylVHAATTA---KYvlDLKPGDVFWCTADIGWATGHSYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 LLCPLWVGATCIML---PEF-SAQMVWK---KFlssqapRVSVFMAVPTIYAKLIEYYDEHfsqpqvqdfVRAFCQENIR 335
Cdd:COG0365 245 VYGPLLNGATVVLYegrPDFpDPGRLWElieKY------GVTVFFTAPTAIRALMKAGDEP---------LKKYDLSSLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 336 LMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRV-PGSVGTPLPGVEVRIAteavkgggrsytilaq 414
Cdd:COG0365 310 LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVV---------------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 415 gDEDGTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAF--TSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGG 489
Cdd:COG0365 374 -DEDGNPVPPG---EEGELVIKGPwpGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDeDGYFWILGRSD-DVINVSG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 490 FKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPR 566
Cdd:COG0365 449 HRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPK 528
|
....*.
gi 1201832555 567 NQMGKV 572
Cdd:COG0365 529 TRSGKI 534
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
57-580 |
7.09e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 273.70 E-value: 7.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcssrDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLY 133
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAA----AALA----ALgigKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 134 RKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLG----VPVLPLGSHSSGSAGHTAVEDVpLASSASWK------- 202
Cdd:PRK07656 87 TRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPalehVVICETEEDDPHTEKMKTFTDF-LAAGDPAErapevdp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQ 282
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 283 MVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYD---EHFSqpqvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITG-H 358
Cdd:PRK07656 246 EV---FRLIETERITVLPGPPTMYNSLLQHPDrsaEDLS--------------SLRLAVTGAASMPVALLERFESELGvD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 359 TLLERYGMTE-IGMALSNPLHGVR--VPGSVGTPLPGVEVRIATEavkgggrsytilaQGDEDGTqmtpgleGQEGELLV 435
Cdd:PRK07656 309 IVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIVNE-------------LGEEVPV-------GEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 436 RGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIG 514
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 515 PPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:PRK07656 448 VPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
61-581 |
9.62e-84 |
|
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: 270.39 E-value: 9.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAIIDQNGEHTYRELFCRSLRLSQEICRV-LQcssrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQ 139
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALgVK------REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 140 QLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVP----VLPLGSHSSGSAGHTAvEDVP-----LASSASWKDRGAMIIY 210
Cdd:cd05959 92 DYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTlvvlIVSGGAGPEAGALLLA-ELVAaeaeqLKPAATHADDPAFWLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 211 TSGTTGRPKGVLSTHENVQAV-------TTGLVEkwewkkEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQM 283
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTaelyarnVLGIRE------DDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VWKKFLSSQAPrvSVFMAVPTIYAKLIEyyDEhfsQPQVQDFVRafcqenIRLMVSGSAALPVPVLKKWKAITGHTLLER 363
Cdd:cd05959 245 AVFKRIRRYRP--TVFFGVPTLYAAMLA--AP---NLPSRDLSS------LRLCVSAGEALPAEVGERWKARFGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTEIG-MALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTpglEGQEGELLVRGSSVFR 442
Cdd:cd05959 312 IGSTEMLhIFLSNRPGRVR-YGTTGKPVPGYEVELR-----------------DEDGGDVA---DGEPGELYVRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 443 EYWNRPKETREAFTSdGWFRTGDTaaYH---DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVV 519
Cdd:cd05959 371 MYWNNRDKTRDTFQG-EWTRTGDK--YVrddDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 520 WGQRVSAVVQLRRGEMLSVK---ELKEWARDTMAPYAVPTELIVVEEIPRNQMGKvnkkelLQRF 581
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEAleeELKEFVKDRLAPYKYPRWIVFVDELPKTATGK------IQRF 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
65-573 |
1.59e-79 |
|
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: 258.68 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 65 AIID-QNGEH-TYRELFCRSLRLSqeicrvlqCSSRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLyrkHPVQ 139
Cdd:cd05911 1 AQIDaDTGKElTYAQLRTLSRRLA--------AGLRKLglkKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPIY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 140 Q---LEYVIEDSQSALVIAAEEYVGKISPSAEKLG--VPVLPLGSHSSGSAGHTAVEDVPLASSASW--------KDRGA 206
Cdd:cd05911 70 TadeLAHQLKISKPKVIFTDPDGLEKVKEAAKELGpkDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDlppplkdgKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 207 MIIYTSGTTGRPKGVLSTHENVQAVT--TGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQmv 284
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYG-LFTTLASLLNGATVIIMPKFDSE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 wkKFLSS-QAPRVSVFMAVPTIYAKLIEYydehfsqPQVQDFVRAfcqeNIRLMVSGSAalpvPVLKKWKA-----ITGH 358
Cdd:cd05911 227 --LFLDLiEKYKITFLYLVPPIAAALAKS-------PLLDKYDLS----SLRVILSGGA----PLSKELQEllakrFPNA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 359 TLLERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGS 438
Cdd:cd05911 290 TIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIV-----------------DDDGKDSLG--PNEPGEICVRGP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 SVFREYWNRPKETREAFTSDGWFRTGDtAAYHD--GVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPP 516
Cdd:cd05911 351 QVMKGYYNNPEATKETFDEDGWLHTGD-IGYFDedGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIP 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 517 DVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPY-----AVptelIVVEEIPRNQMGKVN 573
Cdd:cd05911 429 DEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYkqlrgGV----VFVDEIPKSASGKIL 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
53-576 |
2.21e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 255.69 E-value: 2.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 53 VFTRAL-TFGDKIAIIDQNGEHTYRELfCRSLRLSQEICRVLQCSSRDlkeeRISFLCPNDASYVVAQWASWMSGGIAV- 130
Cdd:PRK05605 37 LYDNAVaRFGDRPALDFFGATTTYAEL-GKQVRRAAAGLRALGVRPGD----RVAIVLPNCPQHIVAFYAVLRLGAVVVe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 131 --PLYRKHpvqQLEYVIEDSQSALVIAAEeyvgKISPSAEKL--GVPV---------------------LPLGS------ 179
Cdd:PRK05605 112 hnPLYTAH---ELEHPFEDHGARVAIVWD----KVAPTVERLrrTTPLetivsvnmiaampllqrlalrLPIPAlrkara 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 180 ---------------HSSGSAGHTAVEDVPLASsaswKDRGAMIIYTSGTTGRPKGVLSTHENV-------QAVTTGLVE 237
Cdd:PRK05605 185 altgpapgtvpwetlVDAAIGGDGSDVSHPRPT----PDDVALILYTSGTTGKPKGAQLTHRNLfanaaqgKAWVPGLGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 238 KWEwkkedVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVwkkfLSSQAPRVSVFM-AVPTIYAKLIEYYDEH 316
Cdd:PRK05605 261 GPE-----RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLI----LDAMKKHPPTWLpGVPPLYEKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 317 fsqpqvqdfvrAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSVGTPLPGVEV 395
Cdd:PRK05605 332 -----------GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 396 RIATEavkgggrsytilaqgdEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTsDGWFRTGDTAAYH-DGVY 474
Cdd:PRK05605 401 RIVDP----------------EDPDETMP--DGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEeDGFI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 475 WIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAV 554
Cdd:PRK05605 462 RIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKV 540
|
570 580
....*....|....*....|..
gi 1201832555 555 PTELIVVEEIPRNQMGKVNKKE 576
Cdd:PRK05605 541 PRRFYHVDELPRDQLGKVRRRE 562
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
70-577 |
1.08e-74 |
|
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: 244.12 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 70 NGEHTYRELfcrsLRLSQEICRVLQcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQ 149
Cdd:cd05934 1 GRRWTYAEL----LRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 150 SALVIAAEeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkdrgAMIIYTSGTTGRPKGVLSTHENVQ 229
Cdd:cd05934 76 AQLVVVDP------------------------------------------------ASILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 230 AVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFLSSQAPRVSVFMAVPTIYAKl 309
Cdd:cd05934 108 FAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLA- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 310 ieyydehfsQPQVQDfvrafcQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRVPGSVGTP 389
Cdd:cd05934 187 ---------QPPSPD------DRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 390 LPGVEVRIAteavkgggrsytilaqgDEDGtQMTPglEGQEGELLVR---GSSVFREYWNRPKETREAFtSDGWFRTGDT 466
Cdd:cd05934 252 APGYEVRIV-----------------DDDG-QELP--AGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 467 AaYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEW 544
Cdd:cd05934 311 G-YRDadGFFYFVDRKK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAF 388
|
490 500 510
....*....|....*....|....*....|...
gi 1201832555 545 ARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
51-577 |
4.12e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 241.02 E-value: 4.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 51 TPVF----TRALTFGDKIAIIDQNGEHTYRELFCRSLRLS---QEICRVLqcssrdlKEERISFLCPNDASYVVAQWASW 123
Cdd:PRK08314 10 TSLFhnleVSARRYPDKTAIVFYGRAISYRELLEEAERLAgylQQECGVR-------KGDRVLLYMQNSPQFVIAYYAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 124 MSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLG--------------------VPVLPLGSHSSG 183
Cdd:PRK08314 83 RANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRlrhvivaqysdylpaepeiaVPAWLRAEPPLQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 184 SAGHTAV---------EDVPLASSASWKDRgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLH 254
Cdd:PRK08314 163 ALAPGGVvawkealaaGLAPPPHTAGPDDL-AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 255 HVHGVINKLLCPLWVGATCIMLPEfsaqmvWKKFLSSQA---PRVSVFMAVPTIyakLIEYydehFSQPQVQDfvraFCQ 331
Cdd:PRK08314 242 HVTGMVHSMNAPIYAGATVVLMPR------WDREAAARLierYRVTHWTNIPTM---VVDF----LASPGLAE----RDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 332 ENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE-IGMALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsyt 410
Cdd:PRK08314 305 SSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI------------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 411 ilaqgD-EDGTQMTPgleGQEGELLVRGSSVFREYWNRPKETREAF-TSDG--WFRTGDTAAY-HDGVYWIKGRTSvDII 485
Cdd:PRK08314 372 -----DpETLEELPP---GEVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLGRMdEEGYFFITDRLK-RMI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 486 KNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLR---RGEMlSVKELKEWARDTMAPYAVPTELIVVE 562
Cdd:PRK08314 443 NASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRpeaRGKT-TEEEIIAWAREHMAAYKYPRIVEFVD 521
|
570
....*....|....*
gi 1201832555 563 EIPRNQMGKVNKKEL 577
Cdd:PRK08314 522 SLPKSGSGKILWRQL 536
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
45-581 |
1.95e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 238.68 E-value: 1.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 45 ASSHHVTPVFTR-ALTFGDKIAIIDQNGEHTYRELFcrslRLSQEICRVLqcssRDL---KEERISFLCPNDASYVVAQW 120
Cdd:PRK08316 8 ARRQTIGDILRRsARRYPDKTALVFGDRSWTYAELD----AAVNRVAAAL----LDLglkKGDRVAALGHNSDAYALLWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 121 ASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGV------PVLPLGSHSSG--------SAG 186
Cdd:PRK08316 80 ACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVdtlilsLVLGGREAPGGwldfadwaEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 187 HTAVEDVPLASsaswkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCP 266
Cdd:PRK08316 160 SVAEPDVELAD-----DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 267 LWVGATCIMLPEFSAQMVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYDehFSQPQVQDFVRAFcqenirlmvSGSAALPV 346
Cdd:PRK08316 235 LYVGATNVILDAPDPELI---LRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKGY---------YGASIMPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 347 PVLKKwkaitghtLLER---------YGMTEIGmalsnPLHGV-------RVPGSVGTPLPGVEVRIAteavkgggrsyt 410
Cdd:PRK08316 301 EVLKE--------LRERlpglrfyncYGQTEIA-----PLATVlgpeehlRRPGSAGRPVLNVETRVV------------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 411 ilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGG 489
Cdd:PRK08316 356 -----DDDGNDVAPG---EVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMdEEGYITVVDRKK-DMIKTGG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 490 FKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQM 569
Cdd:PRK08316 426 ENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPS 505
|
570
....*....|..
gi 1201832555 570 GKVNKKELLQRF 581
Cdd:PRK08316 506 GKILKRELRERY 517
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
56-577 |
1.99e-69 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 232.44 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICRVLQCSsrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVK----KGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGV-PVLPLGShSSGSAGHTAVEDVPLASSASWkdrgaMIIYTSGT 214
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVqRVISITS-LKEIEDRKIDNFVEKNESASF-----IICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPefsaqmvwKKFLSSQA- 293
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGG-IGLFAFPTLFAGGVIIVP--------RKFEPTKAl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 294 -----PRVSVFMAVPTIYAKLIEYYDehFSQPQVQdfvrafcqeNIRLMVSGSAALPVPVLKKWKAiTGHTLLERYGMTE 368
Cdd:PRK06839 232 smiekHKVTVVMGVPTIHQALINCSK--FETTNLQ---------SVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 ----IGMALSNPLHgvRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREY 444
Cdd:PRK06839 300 tsptVFMLSEEDAR--RKVGSIGKPVLFCDYELI-----------------DENKNKVEVG---EVGELLIRGPNVMKEY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 445 WNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQR 523
Cdd:PRK06839 358 WNRPDATEETI-QDGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEI 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 524 VSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK06839 436 PIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
53-581 |
1.40e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 233.07 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 53 VFTRALTFGDKIAIIDQNG----EHTYRELfcrsLRLSQEICRVLQcsSRDLK-EERISFLCPNDASYVVAQWASWMSGG 127
Cdd:COG1022 17 LRRRAARFPDRVALREKEDgiwqSLTWAEF----AERVRALAAGLL--ALGVKpGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 128 IAVPLYRKHPVQQLEYVIEDSQSALVIAA-EEYVGKISPSAEKLgvPVLPL-----GSHSSGSAGHTAVEDVpLASSASW 201
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDEL--PSLRHivvldPRGLRDDPRLLSLDEL-LALGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 202 KDRG--------------AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCpL 267
Cdd:COG1022 168 ADPAelearraavkpddlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 268 WVGATCI----------MLPEFSAQM------VWKKFLSS------QAPRV-----SVFMAVPTIYAkliEYYDEHFSQP 320
Cdd:COG1022 247 AAGATVAfaespdtlaeDLREVKPTFmlavprVWEKVYAGiqakaeEAGGLkrklfRWALAVGRRYA---RARLAGKSPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 321 QVQDFVRAFCQE------------NIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTEI-GMALSNPLHGVRvPGSVG 387
Cdd:COG1022 324 LLLRLKHALADKlvfsklrealggRLRFAVSGGAALGPELARFFRAL-GIPVLEGYGLTETsPVITVNRPGDNR-IGTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 388 TPLPGVEVRIAteavkgggrsytilaqgdedgtqmtpglegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDtA 467
Cdd:COG1022 402 PPLPGVEVKIA------------------------------EDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGD-I 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 468 AY--HDGVYWIKGRTSvDIIKN-GGFKISALEVERQLLAHPHITDVAVIGppDvvwgQR--VSAVVQLRRgEMlsvkeLK 542
Cdd:COG1022 451 GEldEDGFLRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG--D----GRpfLAALIVPDF-EA-----LG 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1201832555 543 EWARDTMAPYAVPTELI----VVEEIpRNQMGKVNKK----ELLQRF 581
Cdd:COG1022 518 EWAEENGLPYTSYAELAqdpeVRALI-QEEVDRANAGlsraEQIKRF 563
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
74-577 |
2.20e-68 |
|
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: 228.03 E-value: 2.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEIcRVLQCSSRDlkeeRISFLCPNDASYVVAQWASWMSGGIAVPL---YRKHpvqQLEYVIEDSQS 150
Cdd:cd05903 3 TYSELDTRADRLAAGL-AALGVGPGD----VVAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRAKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVIAAEEYvGKISPSAEKlgvpvlplgshssgsaghtavedvplassaswkDRGAMIIYTSGTTGRPKGVLSTHENVQA 230
Cdd:cd05903 75 KVFVVPERF-RQFDPAAMP---------------------------------DAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 VTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVwKKFLSSQapRVSVFMAVPTIYAKLI 310
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKA-LALMREH--GVTFMMGATPFLTDLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 311 ---EYYDEHFSQpqvqdfvrafcqenIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHG--VRVPGS 385
Cdd:cd05903 198 navEEAGEPLSR--------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 386 VGTPLPGVEVRIateavkgggrsytilaqGDEDGTQMTPgleGQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGD 465
Cdd:cd05903 264 DGRPLPGVEIKV-----------------VDDTGATLAP---GVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 466 TAAYHDGVYW-IKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEW 544
Cdd:cd05903 323 LARLDEDGYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY 401
|
490 500 510
....*....|....*....|....*....|....
gi 1201832555 545 -ARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05903 402 lDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
72-577 |
1.95e-67 |
|
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: 225.44 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELFCRSLRLSQEICRvlqCSSRdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSA 151
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSN---KGVR--KGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 152 LVIAaeeyvgkispsaeklgvpvlplgshssgsagHTAVEDVplassaswkdrgAMIIYTSGTTGRPKGVLSTHENVQAV 231
Cdd:cd05935 76 VAVV-------------------------------GSELDDL------------ALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 232 TTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIe 311
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLL- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 312 yydehfSQPQVQDfvraFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE-IGMALSNPLHGVRVPgSVGTPL 390
Cdd:cd05935 189 ------ATPEFKT----RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ-CLGIP* 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 391 PGVEVRIATEavkgggrsytilaqgdEDGTQMTPgleGQEGELLVRGSSVFREYWNRPKETREAFTSDG---WFRTGDTa 467
Cdd:cd05935 258 FGVDARVIDI----------------ETGRELPP---NEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDL- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 468 AYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLR---RGEmLSVKELK 542
Cdd:cd05935 318 GYMDeeGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGK-VTEEDII 395
|
490 500 510
....*....|....*....|....*....|....*
gi 1201832555 543 EWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05935 396 EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
49-582 |
6.26e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 221.40 E-value: 6.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 49 HVTPVFTRALT-FGDKIAIIDQNGEHTYRELfcrslrlSQEICRVLQC-SSRDL-KEERISFLCPNDASYVVAQWASWMS 125
Cdd:PRK06188 13 TYGHLLVSALKrYPDRPALVLGDTRLTYGQL-------ADRISRYIQAfEALGLgTGDAVALLSLNRPEVLMAIGAAQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 126 GGIAVPLyrkHPVQQLE---YVIEDSQ-SALVIAAEEYVGKISPSAEKlgVP----VLPLGSHSSG---SAGHTAVEDVP 194
Cdd:PRK06188 86 GLRRTAL---HPLGSLDdhaYVLEDAGiSTLIVDPAPFVERALALLAR--VPslkhVLTLGPVPDGvdlLAAAAKFGPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 195 LASSASWKDRgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVinKLLCPLWVGATCI 274
Cdd:PRK06188 161 LVAAALPPDI-AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 275 MLPEFSAQmvwkKFLSS-QAPRVSVFMAVPT-IYAkLIEYYDEHfsqpqVQDFvrafcqENIRLMVSGSAALPVPVLKKW 352
Cdd:PRK06188 238 VLAKFDPA----EVLRAiEEQRITATFLVPTmIYA-LLDHPDLR-----TRDL------SSLETVYYGASPMSPVRLAEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAITGHTLLERYGMTEIGMALS------NPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGl 426
Cdd:PRK06188 302 IERFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALL-----------------DEDGREVAQG- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 egQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTA-AYHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHP 505
Cdd:PRK06188 364 --EVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVArEDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHP 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 506 HITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRFY 582
Cdd:PRK06188 440 AVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW 516
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
40-580 |
7.74e-65 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 219.83 E-value: 7.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 40 QTTWTASSHHVTPvftraltfgDKIAIIDQNGEHTYRELFCRSlrlsQEICRVLQCSSRDlKEERISFLCPNDASYVVAQ 119
Cdd:PRK03640 4 MPNWLKQRAFLTP---------DRTAIEFEEKKVTFMELHEAV----VSVAGKLAALGVK-KGDRVALLMKNGMEMILVI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 120 WASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLgVPVLPLGSHSSGsaghTAVEDVPLASSA 199
Cdd:PRK03640 70 HALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVK-FAELMNGPKEEA----EIQEEFDLDEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 200 SwkdrgamIIYTSGTTGRPKGVLSTHEN--VQAVTT----GLVEKWEWkkedviLHVLPLHHVHGvINKLLCPLWVGATC 273
Cdd:PRK03640 145 T-------IMYTSGTTGKPKGVIQTYGNhwWSAVGSalnlGLTEDDCW------LAAVPIFHISG-LSILMRSVIYGMRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 274 IMLPEFSAQMVwKKFLSSQapRVSVFMAVPTIYAKLIEYYDEHfsqpqvqdfvraFCQENIRLMVSGSAALPVPVLKKWK 353
Cdd:PRK03640 211 VLVEKFDAEKI-NKLLQTG--GVTIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQCK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 354 AiTGHTLLERYGMTEIG---MALSnPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgdEDGTQMTPgleGQE 430
Cdd:PRK03640 276 E-KGIPVYQSYGMTETAsqiVTLS-PEDALTKLGSAGKPLFPCELKIE------------------KDGVVVPP---FEE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 431 GELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTaAYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHIT 508
Cdd:PRK03640 333 GEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDI-GYLDeeGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVA 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 509 DVAVIGPPDVVWGQRVSAVVqlRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:PRK03640 410 EAGVVGVPDDKWGQVPVAFV--VKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
103-575 |
2.08e-64 |
|
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: 217.85 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAaeeyvgkispsaeklgvpvlplgshss 182
Cdd:cd05907 31 DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV--------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 183 gsaghtavedvplassaSWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINK 262
Cdd:cd05907 84 -----------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 LLCPLWVGAtCIMLPEFSAQMvwkkFLSSQAPRVSVFMAVPTIYAKLieyYDEhFSQPQVQDFVRAFCQ----ENIRLMV 338
Cdd:cd05907 147 LYVPLLAGA-RIYFASSAETL----LDDLSEVRPTVFLAVPRVWEKV---YAA-IKVKAVPGLKRKLFDlavgGRLRFAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 339 SGSAALPVPVLKKWKAItGHTLLERYGMTEIGMALS-NPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgde 417
Cdd:cd05907 218 SGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTlNPPGDNR-IGTVGKPLPGVEVRIA------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 418 dgtqmtpglegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKN-GGFKISAL 495
Cdd:cd05907 277 -----------DDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDeDGFLHITGR-KKDLIITsGGKNISPE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 496 EVERQLLAHPHITDVAVIG---PpdvvwgqRVSAVVQLRRgemlsvKELKEWARDTMAPYAVPTELI----VVEEIpRNQ 568
Cdd:cd05907 345 PIENALKASPLISQAVVIGdgrP-------FLVALIVPDP------EALEAWAEEHGIAYTDVAELAanpaVRAEI-EAA 410
|
....*..
gi 1201832555 569 MGKVNKK 575
Cdd:cd05907 411 VEAANAR 417
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-577 |
1.46e-63 |
|
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: 217.10 E-value: 1.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 46 SSHHVTPVFTRAltFGDKIAIIDQ-NGEH-TYRELFCRSLRLSQEICRVLQcssrdLKEERISFLCPNDASYVVAQWASW 123
Cdd:cd05904 6 PLDSVSFLFASA--HPSRPALIDAaTGRAlTYAELERRVRRLAAGLAKRGG-----RKGDVVLLLSPNSIEFPVAFLAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 124 MSGGIAVPLyrkHP---VQQLEYVIEDSQSALVIAAEEYVGKISPsaekLGVPVLPLGSHSSGSAGH---TAVEDVPLAS 197
Cdd:cd05904 79 SLGAVVTTA---NPlstPAEIAKQVKDSGAKLAFTTAELAEKLAS----LALPVVLLDSAEFDSLSFsdlLFEADEAEPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 198 SASWK-DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKW--EWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCI 274
Cdd:cd05904 152 VVVIKqDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgsNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 275 MLPEFSAQmvwkKFLSS-QAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDFVRAfcqeNIRLMVSGSAALPVPVLKKWK 353
Cdd:cd05904 232 VMPRFDLE----ELLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKELIEAFR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 354 AITGHT-LLERYGMTE---IGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgD-EDGTQMTPgleG 428
Cdd:cd05904 297 AKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV-----------------DpETGESLPP---N 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTaAY--HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPH 506
Cdd:cd05904 357 QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDL-CYidEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPE 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 507 ITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05904 435 ILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
101-579 |
3.23e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 217.59 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 101 KEERISFLCPNDASYVVAQWASWMSGGIAV---PLYRKhpvQQLEYVIEDSQSALVIAAEEYVGKIS--PSAEKLG---- 171
Cdd:PRK06710 73 KGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTE---RELEYQLHDSGAKVILCLDLVFPRVTnvQSATKIEhviv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 172 ---VPVLPLGSH--------------SSGSAGHT-----AVE---DVPLASSASWKDRGAMIIYTSGTTGRPKGVLSTHE 226
Cdd:PRK06710 150 triADFLPFPKNllypfvqkkqsnlvVKVSESETihlwnSVEkevNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 227 NVQAVTTGLVEkWEW---KKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVwkkFLSSQAPRVSVFMAVP 303
Cdd:PRK06710 230 NLVSNTLMGVQ-WLYnckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMV---FEAIKKHKVTLFPGAP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 304 TIYAKLIeyydehfSQPQVQDFVRAfcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRV 382
Cdd:PRK06710 306 TIYIALL-------NSPLLKEYDIS----SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 383 PGSVGTPLPGVEVRIATEavkgggrsytilaqgdEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETrEAFTSDGWFR 462
Cdd:PRK06710 375 PGSIGVPWPDTEAMIMSL----------------ETGEALPPG---EIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLH 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 463 TGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKEL 541
Cdd:PRK06710 435 TGDVGYMdEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL 513
|
490 500 510
....*....|....*....|....*....|....*...
gi 1201832555 542 KEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:PRK06710 514 NQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
63-577 |
1.19e-62 |
|
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: 212.71 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 63 KIAIIDQNGEHTYRELFCRSLRLSQEICRVLQCssrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLE 142
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVS-----SGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 143 YVIEDSQSALVIAAEEYVgkispsaeklgvpvlplgshssgsaghtavedvplassASWkdrgamiIYTSGTTGRPKGVL 222
Cdd:cd05919 76 YIARDCEARLVVTSADDI--------------------------------------AYL-------LYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 223 STHENvqavTTGLVEKWE-----WKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEF-SAQMVwkkFLSSQAPRV 296
Cdd:cd05919 111 HAHRD----PLLFADAMArealgLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERV---LATLARFRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 297 SVFMAVPTIYAKLIEyydehfSQPQVQDFVRAfcqenIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSN 375
Cdd:cd05919 184 TVLYGVPTFYANLLD------SCAGSPDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 376 PLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAF 455
Cdd:cd05919 253 RPGAWR-LGSTGRPVPGYEIRLV-----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 456 tSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGE 534
Cdd:cd05919 312 -NGGWYRTGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1201832555 535 MLSVKELKEWAR---DTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05919 390 APQESLARDIHRhllERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
62-577 |
4.91e-62 |
|
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: 211.23 E-value: 4.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLA----RYLR--ERGVGpGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTTGRPKG 220
Cdd:cd05930 76 LAYILEDSGAKLVL---------------------------------TDPDDL------------AYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINkLLCPLWVGATCIMLPEfsaqMVWK------KFLSSQap 294
Cdd:cd05930 111 VMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPE----EVRKdpealaDLLAEE-- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 RVSVFMAVPTIYAKLIEYydehfsqPQVQDFvrafcqENIRLMVSGSAALPVPVLKKW-KAITGHTLLERYGMTEIGMA- 372
Cdd:cd05930 184 GITVLHLTPSLLRLLLQE-------LELAAL------PSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDa 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 373 -----LSNPLHGVRVPgsVGTPLPGVEVRIateavkgggrsytiLaqgDEDGTQMTPGLEGqegELLVRGSSVFREYWNR 447
Cdd:cd05930 251 tyyrvPPDDEEDGRVP--IGRPIPNTRVYV--------------L---DENLRPVPPGVPG---ELYIGGAGLARGYLNR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 448 PKETREAFTSDGWF------RTGDTAAY-HDG--VYwiKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDV 518
Cdd:cd05930 309 PELTAERFVPNPFGpgermyRTGDLVRWlPDGnlEF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDG 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 519 VWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05930 386 DGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
56-577 |
8.76e-62 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 212.62 E-value: 8.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAII--DQNG---EHTYRELfcrslrlSQEICRV----LQCSSRdlKEERISFLCPNDASYVVAQWASWMSG 126
Cdd:PRK08008 16 LADVYGHKTALIfeSSGGvvrRYSYLEL-------NEEINRTanlfYSLGIR--KGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 127 GIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVP---VLPLGSHSSGSAG------------HTAVE 191
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPlrhICLTRVALPADDGvssftqlkaqqpATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 192 DVPLASsaswkDRGAMIIYTSGTTGRPKGVLSTHENVQavTTGLVEKWE--WKKEDVILHVLPLHHVHGVINKLLCPLWV 269
Cdd:PRK08008 167 APPLST-----DDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQcaLRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 270 GATCIMLPEFSAQMVWKKFLSSQAprvSVFMAVPTIYAKLIeyydehfSQPQVQDfVRAFCqenIRLMVsgsAALPVPVL 349
Cdd:PRK08008 240 GATFVLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQPPSAN-DRQHC---LREVM---FYLNLSDQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 350 KKWKAIT--GHTLLERYGMTE-IGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGl 426
Cdd:PRK08008 303 EKDAFEErfGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR-----------------DDHNRPLPAG- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 egQEGELLVRG---SSVFREYWNRPKETREAFTSDGWFRTGDTAaYHD--GVYWIKGRtSVDIIKNGGFKISALEVERQL 501
Cdd:PRK08008 365 --EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTG-YVDeeGFFYFVDR-RCNMIKRGGENVSCVELENII 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 502 LAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK08008 441 ATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
74-579 |
9.66e-61 |
|
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: 206.81 E-value: 9.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLsqeiCRVLQCSSRDlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALv 153
Cdd:cd05912 3 TFAELFEEVSRL----AEHLAALGVR-KGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 iaaeeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTT 233
Cdd:cd05912 77 -------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 234 GLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQMVWKkflSSQAPRVSVFMAVPTIYAKLIEYY 313
Cdd:cd05912 108 GSALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLH---LINSGKVTIISVVPTMLQRLLEIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 314 DEHFSqpqvqdfvrafcqENIRLMVSGSAALPVPVLKKWKAiTGHTLLERYGMTEIG--MALSNPLHGVRVPGSVGTPLP 391
Cdd:cd05912 184 GEGYP-------------NNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 392 GVEVRIATEAvkgggrsytilaqgdedgtqmtpGLEGQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTaAY-- 469
Cdd:cd05912 250 PVELKIEDDG-----------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDI-GYld 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 470 HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGemLSVKELKEWARDTM 549
Cdd:cd05912 305 EEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP--ISEEELIAYCSEKL 381
|
490 500 510
....*....|....*....|....*....|
gi 1201832555 550 APYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:cd05912 382 AKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
56-581 |
1.25e-60 |
|
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: 210.00 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeiCRVLQcssRDL-KEERISFLCPNDASYVVAQWASWMSGGI---AVP 131
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLA---AGLLA---LGLrPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 132 LYRKHpvqQLEYVIEDSQSALVIAAEEYVG-----------KISPSAEklgvPVLPLGShssgSAGHTAVEDVpLASSAS 200
Cdd:COG1021 108 AHRRA---EISHFAEQSEAVAYIIPDRHRGfdyralarelqAEVPSLR----HVLVVGD----AGEFTSLDAL-LAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 201 WKDRG------AMIIYTSGTTGRPKGVLSTHE----NVQAvttgLVEKWEWKKEDVILHVLPLHH--------VHGVink 262
Cdd:COG1021 176 LSEPRpdpddvAFFQLSGGTTGLPKLIPRTHDdylySVRA----SAEICGLDADTVYLAALPAAHnfplsspgVLGV--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 llcpLWVGATCIMLPEFSAQMVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafcqENIRLMVSGSA 342
Cdd:COG1021 249 ----LYAGGTVVLAPDPSPDTA---FPLIERERVTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 343 ALPVPVLKKWKAITGHTLLERYGMTEiGM----ALSNPLHgvRVPGSVGTPL-PGVEVRIAteavkgggrsytilaqgDE 417
Cdd:COG1021 311 KLSPELARRVRPALGCTLQQVFGMAE-GLvnytRLDDPEE--VILTTQGRPIsPDDEVRIV-----------------DE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 418 DGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALE 496
Cdd:COG1021 371 DGNPVPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTpDGYLVVEGR-AKDQINRGGEKIAAEE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 497 VERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLrRGEMLSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNKK 575
Cdd:COG1021 447 VENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKK 525
|
....*.
gi 1201832555 576 ELLQRF 581
Cdd:COG1021 526 ALRAAL 531
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
57-577 |
1.90e-60 |
|
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: 208.31 E-value: 1.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICRvLQCSSRDlkeeRISFLCPNDASYVVAQWASWMSGGIAVPLYRKH 136
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAA-LGISRGD----TVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 137 PVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPlgshssgsaghTAVEDVPLAssaswkdrgamIIYTSGTTG 216
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREFEYEDLLAEGDPDFEWIP-----------PADEWDPIA-----------LNYTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 217 RPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvinklLCPLW----VGATCIMLPEFSAQMVWKkflSSQ 292
Cdd:cd12118 147 RPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYD---LIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 293 APRVSVFMAVPTIYAKLIEYYDE---HFSQPqvqdfvrafcqenIRLMVSGSAAlPVPVLKKWKAItGHTLLERYGMTEI 369
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANAPPSdarPLPHR-------------VHVMTAGAPP-PAAVLAKMEEL-GFDVTHVYGLTET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 370 -GMALSNPLHgvrvPGSVGTPLpgvEVRIATEAVKGGGrsyTILAQG----DEDGTQMTPGlEGQE-GELLVRGSSVFRE 443
Cdd:cd12118 284 yGPATVCAWK----PEWDELPT---EERARLKARQGVR---YVGLEEvdvlDPETMKPVPR-DGKTiGEIVFRGNIVMKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQ 522
Cdd:cd12118 353 YLKNPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGE 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 523 RVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTElIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12118 431 VPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKIQKFVL 484
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
72-577 |
1.90e-60 |
|
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: 209.02 E-value: 1.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELFCRSLRLSQeicrVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDS 148
Cdd:cd12119 25 RYTYAEVAERARRLAN----AL----RRLgvkPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 149 QSALVIAAEEYVGKISPSAEKL----GVPVLPLGSHSSGSAGHTAVEDVPLASSAS----WKD----RGAMIIYTSGTTG 216
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPRLptveHVVVMTDDAAMPEPAGVGVLAYEELLAAESpeydWPDfdenTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 217 RPKGVLSTHENV--------QAVTTGLVEKwewkkeDVILHVLPLHHVH--GVinkllcP---LWVGATCI-----MLPE 278
Cdd:cd12119 177 NPKGVVYSHRSLvlhamaalLTDGLGLSES------DVVLPVVPMFHVNawGL------PyaaAMVGAKLVlpgpyLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 279 FSAQMVwkkflssQAPRVSVFMAVPTIYAKLIEYYDEHFSQpqvqdfvrafcQENIRLMVSGSAALPVPVLKKWKAItGH 358
Cdd:cd12119 245 SLAELI-------EREGVTFAAGVPTVWQGLLDHLEANGRD-----------LSSLRRVVIGGSAVPRSLIEAFEER-GV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 359 TLLERYGMTE---IG-MALSNPLH-------GVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMtPGLE 427
Cdd:cd12119 306 RVIHAWGMTEtspLGtVARPPSEHsnlsedeQLALRAKQGRPVPGVELRIV-----------------DDDGREL-PWDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 428 GQEGELLVRGSSVFREYWNRPKETrEAFTSDGWFRTGDTAA-YHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPH 506
Cdd:cd12119 368 KAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATiDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 507 ITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12119 446 VAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
74-577 |
2.99e-60 |
|
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: 206.03 E-value: 2.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELfcrsLRLSQEICRVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQS 150
Cdd:cd05972 2 SFREL----KRESAKAANVL----AKLglrKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVIAAEEyvgkispsaeklgvpvlplgshssgsaghtaveDVplassaswkdrgAMIIYTSGTTGRPKGVLSTHENVQA 230
Cdd:cd05972 74 KAIVTDAE---------------------------------DP------------ALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 VTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIM--LPEFSAQmVWKKFLSSQapRVSVFMAVPTIYAK 308
Cdd:cd05972 109 HIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAE-RILELLERY--GVTSFCGPPTAYRM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 309 LIEYYDEHFsqpqvqDFVRafcqenIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNpLHGVRV-PGSVG 387
Cdd:cd05972 186 LIKQDLSSY------KFSH------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGN-FPDMPVkPGSMG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 388 TPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAFtSDGWFRTGD 465
Cdd:cd05972 253 RPTPGYDVAII-----------------DDDGRELPPG---EEGDIAIKLPppGLFLGYVGDPEKTEASI-RGDYYLTGD 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 466 TAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKEL 541
Cdd:cd05972 312 RAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelAEEL 390
|
490 500 510
....*....|....*....|....*....|....*.
gi 1201832555 542 KEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05972 391 QGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
62-577 |
2.77e-58 |
|
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: 201.32 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcSSRDLKEE-RISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAAL------ASLGLDAGdPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAAEeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswkDRGAMIIYTSGTTGRPKG 220
Cdd:cd05945 80 IREILDAAKPALLIADG---------------------------------------------DDNAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLH---HVHGvinkLLCPLWVGATCIMLPEfsAQMVWKKFLSSQAPR-- 295
Cdd:cd05945 115 VQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD----LYPALASGATLVPVPR--DATADPKQLFRFLAEhg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 296 VSVFMAVPTIYAKLIEyyDEHFSQ---PQVQDFVraFCQEnirlmvsgsaALPVPVLKKWKAIT-GHTLLERYGMTEIGM 371
Cdd:cd05945 189 ITVWVSTPSFAAMCLL--SPTFTPeslPSLRHFL--FCGE----------VLPHKTARALQQRFpDARIYNTYGPTEATV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALS------NPLHGV-RVPgsVGTPLPGVEvriateavkgggrsYTILaqgDEDGTQMTPgleGQEGELLVRGSSVFREY 444
Cdd:cd05945 255 AVTyievtpEVLDGYdRLP--IGYAKPGAK--------------LVIL---DEDGRPVPP---GEKGELVISGPSVSKGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 445 WNRPKETREAFTSD---GWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVW 520
Cdd:cd05945 313 LNNPEKTAAAFFPDegqRAYRTGDLVRLeADGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 521 GQRVSAVVQLRRG-EMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05945 392 VTELIAFVVPKPGaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
62-579 |
3.12e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 203.75 E-value: 3.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEH------TYRELFCRSLRLSQEIcrvlqcssRDLKEER---ISFLCPNDASYVVAQWASWMSGGIAVPL 132
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAALVDRVAVGL--------ARLGVGRgdvVSCQLPNWWEFTVLYLACSRIGAVLNPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 133 ---YRKHpvqQLEYVIEDSQSALVIAAEEYVG--------KISPSAEKLGVPVLPLGSHSSGSAGH---TAVEDVP---- 194
Cdd:PRK13295 111 mpiFRER---ELSFMLKHAESKVLVVPKTFRGfdhaamarRLRPELPALRHVVVVGGDGADSFEALlitPAWEQEPdapa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 195 -LASSASWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATC 273
Cdd:PRK13295 188 iLARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 274 IMlpefsaQMVW--KKFLSS-QAPRVSVFMAVPTIYAKLIEYYDEhfSQPQVQDFvRAFCqenirlmvSGSAALPVPVLK 350
Cdd:PRK13295 268 VL------QDIWdpARAAELiRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSL-RTFL--------CAGAPIPGALVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 351 KWKAITGHTLLERYGMTEIGMA----LSNPLHgvRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPgl 426
Cdd:PRK13295 331 RARAALGAKIVSAWGMTENGAVtltkLDDPDE--RASTTDGCPLPGVEVRVV-----------------DADGAPLPA-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 eGQEGELLVRGSSVFREYWNRPKETREAFtsDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHP 505
Cdd:PRK13295 390 -GQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDaDGYIRISGRSK-DVIIRGGENIPVVEIEALLYRHP 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 506 HITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNK---KELLQ 579
Cdd:PRK13295 466 AIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKfrlREMLR 543
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
74-577 |
4.42e-57 |
|
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: 198.06 E-value: 4.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEICrvlqcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALV 153
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-----AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 IAA----EEYVGKISpsAEKLGVPvlplgshssgsaghtAVEDVPLASSASwKDRGAMIIYTSGTTGRPKGVLSTHENVQ 229
Cdd:TIGR01923 76 LTDslleEKDFQADS--LDRIEAA---------------GRYETSLSASFN-MDQIATLMFTSGTTGKPKAVPHTFRNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 230 AVTTGLVEKWEWKKEDVILHVLPLHHVHGViNKLLCPLWVGATCIMLPEFSAqmvwkkFLSSQA-PRVSVFMAVPTIYAK 308
Cdd:TIGR01923 138 ASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQ------LLEMIAnERVTHISLVPTQLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 309 LIEyydehfsqpqvqdfvRAFCQENIRLMVSGSAALPVPVLKKwkAIT-GHTLLERYGMTEIG---MALSNPLHGVRvpG 384
Cdd:TIGR01923 211 LLD---------------EGGHNENLRKILLGGSAIPAPLIEE--AQQyGLPIYLSYGMTETCsqvTTATPEMLHAR--P 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 385 SVGTPLPGVEVRIATEAVKGggrsytilaqgdedgtqmtpglegqEGELLVRGSSVFREYWNrPKETREAFTSDGWFRTG 464
Cdd:TIGR01923 272 DVGRPLAGREIKIKVDNKEG-------------------------HGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 465 DTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEmlSVKELKE 543
Cdd:TIGR01923 326 DIGELdGEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI--SQAKLIA 402
|
490 500 510
....*....|....*....|....*....|....
gi 1201832555 544 WARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:TIGR01923 403 YLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
72-581 |
7.55e-57 |
|
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: 197.32 E-value: 7.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELfcrsLRLSQEICRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAV---PLYRKhpvQQLEYVIEDS 148
Cdd:cd05958 10 EWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVatmPLLRP---KELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 149 QSALVIAAEEYvgkispsaeklgvpvlplgshssgsaghTAVEDVplassASWKdrgamiiYTSGTTGRPKGVLSTHENV 228
Cdd:cd05958 83 RITVALCAHAL----------------------------TASDDI-----CILA-------FTSGTTGAPKATMHFHRDP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 229 QAVTTGL-VEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVwkkfLSSQAP-RVSVFMAVPTIY 306
Cdd:cd05958 123 LASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL----LSAIARyKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 307 AKLIEYYDehFSQPQVQdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE-IGMALSNPLHGVRvPGS 385
Cdd:cd05958 199 RAMLAHPD--AAGPDLS---------SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR-PGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 386 VGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVfreYWNRPKETREAFTSDGWFRTGD 465
Cdd:cd05958 267 TGKPVPGYEAKVV-----------------DDEGNPVPDG---TIGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 466 TAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKEL 541
Cdd:cd05958 324 TYSRDpDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlAREL 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1201832555 542 KEWARDTMAPYAVPTELIVVEEIPRNQMGKvnkkelLQRF 581
Cdd:cd05958 403 QDHAKAHIAPYKYPRAIEFVTELPRTATGK------LQRF 436
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
62-577 |
7.84e-57 |
|
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: 198.89 E-value: 7.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEH--TYRELFCRSLRLSQEICRvlqcssRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPV 138
Cdd:cd05923 16 DACAIADPARGLrlTYSELRARIEAVAARLHA------RGLRpGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 QQLEYVIEDSQSALVI---AAEEYVGKISPSAEKLGVPVLPlGSHSSGSAGhTAVEDVPLASSASwkdrgAMIIYTSGTT 215
Cdd:cd05923 90 AELAELIERGEMTAAViavDAQVMDAIFQSGVRVLALSDLV-GLGEPESAG-PLIEDPPREPEQP-----AFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTH----ENVQAVTTglVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFlss 291
Cdd:cd05923 163 GLPKGAVIPQraaeSRVLFMST--QAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLI--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 292 QAPRVSVFMAVPTIYAKLIEYydEHFSQPQVqdfvrafcqENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGM 371
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAA--AEFAGLKL---------SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALSNPlhGVRvPGSVGTPLPGVEVRIateaVKGGGRSYTILAQGDEdgtqmtpglegqeGELLVR--GSSVFREYWNRPK 449
Cdd:cd05923 307 SLYMR--DAR-TGTEMRPGFFSEVRI----VRIGGSPDEALANGEE-------------GELIVAaaADAAFTGYLNQPE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREAFtSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:cd05923 367 ATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1201832555 529 QLRRGEmLSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05923 445 VPREGT-LSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
55-577 |
2.06e-56 |
|
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: 197.16 E-value: 2.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 55 TRALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeiCRVLQCSSRdlKEERISFLCPNDASYVVAQWASWMSGGI---AVP 131
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLA---AGLRGLGIR--PGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 132 LYRKHpvqQLEYVIEDSQSALVIAAEEYvgkispsaeklgvpvlplGSHSSGSAGHTAVEDVPLAssaswkdrgAMIIYT 211
Cdd:cd05920 98 SHRRS---ELSAFCAHAEAVAYIVPDRH------------------AGFDHRALARELAESIPEV---------ALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 212 SGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHvhgviN-KLLCP-----LWVGATCIMLPEFSAQMVw 285
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDAA- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 kkFLSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYG 365
Cdd:cd05920 222 --FPLIEREGVTVTALVPALVSLWLDAAASRRADLS-----------SLRLLQVGGARLSPALARRVPPVLGCTLQQVFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTEiGM----ALSNPlhGVRVPGSVGTPL-PGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSV 440
Cdd:cd05920 289 MAE-GLlnytRLDDP--DEVIIHTQGRPMsPDDEIRVV-----------------DEEGNPVPPG---EEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 441 FREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVV 519
Cdd:cd05920 346 IRGYYRAPEHNARAFTPDGFYRTGDLVRRTpDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 520 WGQRVSAVVQLrRGEMLSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05920 425 LGERSCAFVVL-RDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-577 |
3.17e-56 |
|
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: 192.88 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENV--QAVTTGlvEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIML-PEFSAQMV 284
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnNGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 wkkFLSSQAPRVSVFMAVPTIYAKLIEyydeHFSQPQVqDFvrafcqENIRLMVSGSAALPVPVLKK-WKAITGHTLLER 363
Cdd:cd05917 85 ---LEAIEKEKCTALHGVPTMFIAELE----HPDFDKF-DL------SSLRTGIMAGAPCPPELMKRvIEVMNMKDVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTE----IGMALSNPLHGVRVpGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGSS 439
Cdd:cd05917 151 YGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIV-----------------DPEGGIVPP--VGVPGELCIRGYS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 440 VFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDV 518
Cdd:cd05917 211 VMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDeDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 519 VWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05917 290 RYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
149-577 |
8.93e-56 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 199.03 E-value: 8.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 149 QSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAGHTAVEDVPLASSASWKDRGAMIIYTSGTTGRPKGVLSTHEN- 227
Cdd:PRK07529 159 RTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNe 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 228 -VQAVTTGLVEKWewKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIML-------PEFSAQMvWKKFlssQAPRVSVF 299
Cdd:PRK07529 239 vANAWLGALLLGL--GPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgyrgPGVIANF-WKIV---ERYRINFL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 300 MAVPTIYAKLIEyydehfsQPqvqdfVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEiGMALS--NPL 377
Cdd:PRK07529 313 SGVPTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSsvNPP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 378 HGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaQGDEDGTQMTPGLEGQEGELLVRGSSVFREYWNrPKETREAFTS 457
Cdd:PRK07529 380 DGERRIGSVGLRLPYQRVRVV---------------ILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 458 DGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEML 536
Cdd:PRK07529 444 DGWLNTGDLGRIdADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASA 522
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1201832555 537 SVKELKEWARDTMA-PYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK07529 523 TEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
74-577 |
1.36e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 195.41 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFcrslRLSQEICRVLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSAL 152
Cdd:PRK09088 24 TYAELD----ALVGRLAAVLR--RRGCVDgERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 153 ViaaeeyVGKISPSAekLGVPVLPLGSHSSGSAGHTAVEDVPLAssaswKDRGAMIIYTSGTTGRPKGVLSTHENVQ--A 230
Cdd:PRK09088 98 L------LGDDAVAA--GRTDVEDLAAFIASADALEPADTPSIP-----PERVSLILFTSGTSGQPKGVMLSERNLQqtA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 VTTGLVEKWEwkKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKfLSSQAPRVSVFMAVPTIYAKLi 310
Cdd:PRK09088 165 HNFGVLGRVD--AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGR-LGDPALGITHYFCVPQMAQAF- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 311 eyydehFSQPqvqDFVRAFCQeNIRLMVSGSAALPVPVLKKWKAiTGHTLLERYGMTEIGMALSNPLHGVRVP---GSVG 387
Cdd:PRK09088 241 ------RAQP---GFDAAALR-HLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDVIRakaGAAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 388 TPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLEGqegELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTA 467
Cdd:PRK09088 310 IPTPTVQTRVV-----------------DDQGNDCPAGVPG---ELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 468 -AYHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWAR 546
Cdd:PRK09088 370 rRDADGFFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLS 448
|
490 500 510
....*....|....*....|....*....|.
gi 1201832555 547 DTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
207-574 |
3.15e-55 |
|
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: 189.79 E-value: 3.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 207 MIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQMVWK 286
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 KflsSQAPRVSVFMAVPTIYAKLIeyyDEHFSQPQVQDFVRAfcqenirlmVSGsaaLPVP-VLKKWKAITGHTLLERYG 365
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLL---DAAEKSGVDLSSLRH---------VLG---LDAPeTIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTEIGMALSnpLHGVR-VPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREY 444
Cdd:cd17637 145 QTETSGLVT--LSPYReRPGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETGEIVVRGPLVFQGY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 445 WNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSV-DIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQ 522
Cdd:cd17637 203 WNLPELTAYTF-RNGWHHTGDLGRFdEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 523 RVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNK 574
Cdd:cd17637 282 GIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
55-580 |
2.35e-54 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 193.43 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 55 TRALTFGDKIAIIDQNG-EHTYRELFCRSLRLSQEIcrvLQCSSRDLkeERISFLCPNDASYVVAQWASWMSGGIAVPLY 133
Cdd:PRK06087 31 QTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWL---LAKGIEPG--DRVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 134 RKHPVQQLEYVIEDSQSALVIAAEeYVGKISPsaEKLGVPV---LP-LG----------SHSSGSAGHTAVEDVPLASSA 199
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAPT-LFKQTRP--VDLILPLqnqLPqLQqivgvdklapATSSLSLSQIIADYEPLTTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 200 SWK-DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPE 278
Cdd:PRK06087 183 TTHgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 279 FSAQMVWkKFLSSQapRVSVFM-AVPTIY--AKLIEYYDEHFSqpqvqdfvrafcqeNIRLMVSGSAALPVPVLKK-WKA 354
Cdd:PRK06087 263 FTPDACL-ALLEQQ--RCTCMLgATPFIYdlLNLLEKQPADLS--------------ALRFFLCGGTTIPKKVAREcQQR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 355 itGHTLLERYGMTE----IGMALSNPLHgvRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLEGQE 430
Cdd:PRK06087 326 --GIKLLSVYGSTEssphAVVNLDDPLS--RFMHTDGYAAAGVEIKVV-----------------DEARKTLPPGCEGEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 431 GEllvRGSSVFREYWNRPKETREAFTSDGWFRTGDTaAYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHIT 508
Cdd:PRK06087 385 AS---RGPNVFMGYLDEPELTARALDEEGWYYSGDL-CRMDeaGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 509 DVAVIGPPDVVWGQRVSAVVQLRRGE-MLSVKELKEW-ARDTMAPYAVPTELIVVEEIPRNQMGKVNK----KELLQR 580
Cdd:PRK06087 460 DACVVAMPDERLGERSCAYVVLKAPHhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKfllrKDIMRR 537
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
103-507 |
1.03e-52 |
|
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: 186.88 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEyvgkispsaeklgvpvlplgshss 182
Cdd:cd05914 33 DRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE------------------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 183 gsaghtavEDVplassaswkdrgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINK 262
Cdd:cd05914 89 --------DDV------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 LLCPLWVGATCIMLPEFSAQM--------------------VWKKFLSSQAPRVSVFMAVPTIYAKLIeyyDEHFSQPQV 322
Cdd:cd05914 149 LLLPLLNGAHVVFLDKIPSAKiialafaqvtptlgvpvplvIEKIFKMDIIPKLTLKKFKFKLAKKIN---NRKIRKLAF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 323 QDFVRAFcQENIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTEIGMALS-NPLHGVRVpGSVGTPLPGVEVRIATea 401
Cdd:cd05914 226 KKVHEAF-GGNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISySPPNRIRL-GSAGKVIDGVEVRIDS-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 402 vkgggrsytilaqgdedgtqmtPGLEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHDGVY-WIKGRT 480
Cdd:cd05914 301 ----------------------PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRK 358
|
410 420
....*....|....*....|....*..
gi 1201832555 481 SVDIIKNGGFKISALEVERQLLAHPHI 507
Cdd:cd05914 359 KEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-577 |
1.07e-51 |
|
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: 181.14 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP----- 277
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 -EFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDFvrafcqENIRLMVSGSAALPVPVLKKWKAIT 356
Cdd:cd05944 82 nPGLFDNFWKLV---ERYRITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 357 GHTLLERYGMTEIGMALS-NPLHGVRVPGSVGTPLPGVEVRIATEavkgggrsytilaqgDEDGTQMTPGLEGQEGELLV 435
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVL---------------DGVGRLLRDCAPDEVGEICV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 436 RGSSVFREYWNRpKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIG 514
Cdd:cd05944 211 AGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLdADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVG 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 515 PPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPY-AVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05944 289 QPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
204-581 |
2.44e-51 |
|
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: 179.06 E-value: 2.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 204 RGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCIMLPEFSAQM 283
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VwkkflSSQAPRVSVFMAVPTIYAKLIeyyDEHFSQPQVqdfvrafcqENIRLMVSGSAALPVPVLKKWKAiTGHTLLER 363
Cdd:cd17630 80 E-----DLAPPGVTHVSLVPTQLQRLL---DSGQGPAAL---------KSLRAVLLGGAPIPPELLERAAD-RGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgdedgtqmtpglegQEGELLVRGSSVFRE 443
Cdd:cd17630 142 YGMTETASQVATKRPDGFGRGGVGVLLPGRELRIV------------------------------EDGEIWVGGASLAMG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPkeTREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQ 522
Cdd:cd17630 192 YLRGQ--LVPEFNEDGWFTTKDLGELHaDGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQ 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 523 RVSAVVQLRRGemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:cd17630 269 RPVAVIVGRGP--ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
64-584 |
2.45e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 183.95 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 64 IAIIDQNGEH-TYRELFCRSLRLSQEIcrvlqcSSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK08276 2 AVIMAPSGEVvTYGELEARSNRLAHGL------RALGLREgDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAGHTAVE-------DVPLASSAswkdRGAMIIYTSGT 214
Cdd:PRK08276 76 AYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEealaaqpDTPIADET----AGADMLYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQ-----AVTTGLVEKWEWKKED-VILHVLPLHHVhGVINKLLCPLWVGATCIMLPEFSAQmvwkKF 288
Cdd:PRK08276 152 TGRPKGIKRPLPGLDpdeapGMMLALLGFGMYGGPDsVYLSPAPLYHT-APLRFGMSALALGGTVVVMEKFDAE----EA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 LSS-QAPRVSVFMAVPTIYAKLIEYYDEhfsqpqvqdfVRA-FCQENIRLMVSGSAALPVPVlkKWKAIT--GHTLLERY 364
Cdd:PRK08276 227 LALiERYRVTHSQLVPTMFVRMLKLPEE----------VRArYDVSSLRVAIHAAAPCPVEV--KRAMIDwwGPIIHEYY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 365 GMTE-IGMALSNPLHGVRVPGSVGTPLPGvEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFRE 443
Cdd:PRK08276 295 ASSEgGGVTVITSEDWLAHPGSVGKAVLG-EVRIL-----------------DEDGNELPPG---EIGTVYFEMDGYPFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDGWFRTGDTAaY--HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWG 521
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVG-YldEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 522 QRVSAVVQLRRGEMLSV---KELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRFYPA 584
Cdd:PRK08276 432 ERVKAVVQPADGADAGDalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEG 497
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
62-581 |
6.21e-51 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 183.55 E-value: 6.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIidqngehTYRELfcrsLRLSQEICRVLQCSSRdLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK05852 40 DRIAI-------SYRDL----ARLVDDLAGQLTRSGL-LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAG------HTAVEDVPLASSA-SWKDRGAMIIYTSGT 214
Cdd:PRK05852 108 RVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGtlsvhlDAATEPTPATSTPeGLRPDDAMIMFTGGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATcIMLP---EFSAQMVWKKFLSS 291
Cdd:PRK05852 188 TGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 292 QAprvSVFMAVPTIYAKLIEyydehfsQPQVQDFVRAfcQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGM 371
Cdd:PRK05852 267 GA---TWYTAVPTIHQILLE-------RAATEPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATH 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALSNplhgVRVPGSVGTPLPGVEVRIATEAvkgGGRSYTILAqgdEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKET 451
Cdd:PRK05852 335 QVTT----TQIEGIGQTENPVVSTGLVGRS---TGAQIRIVG---SDGLPLPAG---AVGEVWLRGTTVVRGYLGDPTIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 452 REAFTsDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQL 530
Cdd:PRK05852 402 AANFT-DGWLRTGDLGSLSaAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVP 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 531 RRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK05852 480 RESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
48-581 |
1.89e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 182.28 E-value: 1.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 48 HHVTPVFTRALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICRvlqcssRDLK-EERISFLCPNDASYVVAQWASWMSG 126
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSR------RGVGfGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 127 GIAVPL-YRKHPvQQLEYVIEDSQSALVI---AAEEYVGKISPSAEKLGVPVLPLGSHSSGSAGH---TAVEDVPLASSA 199
Cdd:PRK07786 92 AIAVPVnFRLTP-PEIAFLVSDCGAHVVVteaALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYedlLAEAGPAHAPVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 200 SWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKE-DVILHVLPLHHVHGVINkLLCPLWVGATCIMLP- 277
Cdd:PRK07786 171 IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 -EFSA-QM--VWkkflssQAPRV-SVFMaVPTiyaklieyydehfsqpQVQdfvrAFCQE------NIRLMVSGSAALPV 346
Cdd:PRK07786 250 gAFDPgQLldVL------EAEKVtGIFL-VPA----------------QWQ----AVCAEqqarprDLALRVLSWGAAPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 347 P--VLKKWKA-ITGHTLLERYGMTEIG----MALSNplHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDG 419
Cdd:PRK07786 303 SdtLLRQMAAtFPEAQILAAFGQTEMSpvtcMLLGE--DAIRKLGSVGKVIPTVAARVV-----------------DENM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 420 TQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVE 498
Cdd:PRK07786 364 NDVPVG---EVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQdEEGYVWVVDRKK-DMIISGGENIYCAEVE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 499 RQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRG-EMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK07786 439 NVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
....
gi 1201832555 578 LQRF 581
Cdd:PRK07786 519 RERY 522
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
61-577 |
1.94e-50 |
|
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: 180.95 E-value: 1.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAIIDQNGEHTYRELFCRSLRLSqeicrvlqcssRDLKE------ERISFLCPNDASYVVAQWASWMSGGIAVPLYR 134
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLA-----------ARLRArgvgpgDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHPVQQLEYVIEDSQSALVIAAEEyvgkiSPSAEKLGVPVLPLGS---HSSGSAGHTAVEDvplassaswkDRGAMIIYT 211
Cdd:cd12116 70 DYPADRLRYILEDAEPALVLTDDA-----LPDRLPAGLPVLLLALaaaAAAPAAPRTPVSP----------DDLAYVIYT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 212 SGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVInKLLCPLWVGATCIML-------PEFSAQMV 284
Cdd:cd12116 135 SGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIApretqrdPEALARLI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 wkkflssQAPRVSVFMAVPTIYAKLIEyydehfSQPQVQDFVRAFCqenirlmvsGSAALPvPVLKKWKAITGHTLLERY 364
Cdd:cd12116 214 -------EAHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 365 GMTEIGM-ALSNPLHGVRVPGSVGTPLPGVEVRIATEavkgggrsytilaqgdedgtQMTPGLEGQEGELLVRGSSVFRE 443
Cdd:cd12116 271 GPTETTIwSTAARVTAAAGPIPIGRPLANTQVYVLDA--------------------ALRPVPPGVPGELYIGGDGVAQG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDG-------WFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVigp 515
Cdd:cd12116 331 YLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAV--- 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 516 pdVVWG----QRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12116 407 --VVREdggdRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
103-581 |
2.02e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 182.93 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVP---LYRKHpvqQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGV------- 172
Cdd:PRK06178 84 DRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH---ELSYELNDAGAEVLLALDQLAPVVEQVRAETSLrhvivts 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 173 --------PVLPL------------GSHSSGSAGHTAVEDVPLASSASwkDRGAMIIYTSGTTGRPKGVLSTHENV--QA 230
Cdd:PRK06178 161 ladvlpaePTLPLpdslraprlaaaGAIDLLPALRACTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMvyTA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 VTTGLVEKWEwKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQmvwkkflssqaprvSVFMAVP----TIY 306
Cdd:PRK06178 239 AAAYAVAVVG-GEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAV--------------AFMAAVEryrvTRT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 307 AKLIEYYDEHFSQPQVQDF-------VRAfcqenirlmVSGSAALPVPVLKKWKAITGHTLLE-RYGMTE--------IG 370
Cdd:PRK06178 304 VMLVDNAVELMDHPRFAEYdlsslrqVRV---------VSFVKKLNPDYRQRWRALTGSVLAEaAWGMTEthtcdtftAG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 MALSN-PLHGVrvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGSSVFREYWNRPK 449
Cdd:PRK06178 375 FQDDDfDLLSQ--PVFVGLPVPGTEFKIC-----------------DFETGELLP--LGAEGEIVVRTPSLLKGYWNKPE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:PRK06178 434 ATAEAL-RDGWLHTGDIGKIdEQGFLHYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFV 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 529 QLRRGEMLSVKELKEWARDTMAPYAVPtELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK06178 512 QLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALA 563
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
60-580 |
2.53e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 181.78 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 60 FGDKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcSSRDL-KEERISFLCPNDASYVVAQWASWMSGGIAVPL-YRKHP 137
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAAL------AARGVrKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 138 vQQLEYVIEDSQSALVIAAE---EYVGKISPSAEKLGVpVLPLGshssGSAGHTAVEDV-------PLASSASWKDRGAM 207
Cdd:PRK07470 94 -DEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTH-VVAIG----GARAGLDYEALvarhlgaRVANAAVDHDDPCW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENVQAVTT--------GLVEkwewkkEDVILHVLPLHHVHGVinKLLCPLWVGATCIMLP-- 277
Cdd:PRK07470 168 FFFTSGTTGRPKAAVLTHGQMAFVITnhladlmpGTTE------QDASLVVAPLSHGAGI--HQLCQVARGAATVLLPse 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 EFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYydehfsqPQVQdfvrAFCQENIRLMVSGSAALPVPVLKKWKAITG 357
Cdd:PRK07470 240 RFDPAEVWALV---ERHRVTNLFTVPTILKMLVEH-------PAVD----RYDHSSLRYVIYAGAPMYRADQKRALAKLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 358 HTLLERYGMTEIGMA---LSNPLH------GVRVpGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGleg 428
Cdd:PRK07470 306 KVLVQYFGLGEVTGNitvLPPALHdaedgpDARI-GTCGFERTGMEVQIQ-----------------DDEGRELPPG--- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAayH---DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHP 505
Cdd:PRK07470 365 ETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLG--HldaRGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHP 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 506 HITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKK----ELLQR 580
Cdd:PRK07470 441 AVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKmvreELEER 519
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
105-577 |
2.83e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 180.85 E-value: 2.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 105 ISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISpsaekLGVPVLPLGSHSSGS 184
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVA-----LETPKIVIDAAAQAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 185 AGHTAVEDVPLASSASWKDRGAM-IIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKL 263
Cdd:PRK06145 130 SRRLAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 264 LCPLWVGATCIMLPEFSAQMVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYDEHfsqpqvqdfvrAFCQENIRLMVSGSAA 343
Cdd:PRK06145 210 IAVLWVGGTLRIHREFDPEAV---LAAIERHRLTCAWMAPVMLSRVLTVPDRD-----------RFDLDSLAWCIGGGEK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 344 LPVPVLKKWKAI-TGHTLLERYGMTEI--GMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGT 420
Cdd:PRK06145 276 TPESRIRDFTRVfTRARYIDAYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIA-----------------DGAGR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 421 QMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTsDGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKISALEVER 499
Cdd:PRK06145 339 WLPPN---MKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEeGFLYLTDRKK-DMIISGGENIASSEVER 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 500 QLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
74-512 |
7.64e-50 |
|
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: 177.46 E-value: 7.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSqeicRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALV 153
Cdd:TIGR01733 1 TYRELDERANRLA----RHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 IAAEEYvgkiSPSAEKLGVPVLPLGSHSSGSAGHTAVEDVPLASSASwkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTT 233
Cdd:TIGR01733 77 LTDSAL----ASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGP--DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 234 GLVEKWEWKKEDVILHVLPLHHVHGVInKLLCPLWVGATCIMLPEfSAQMVWKKFLSS-QAPR-VSVFMAVPTIYAKLIE 311
Cdd:TIGR01733 151 WLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAALLAAlIAEHpVTVLNLTPSLLALLAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 312 yydehfsqpqvqdfVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHT-LLERYGMTEI-GMALSNPLHGVRVPG----S 385
Cdd:TIGR01733 229 --------------ALPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTETtVWSTATLVDPDDAPRespvP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 386 VGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLegqEGELLVRGSSVFREYWNRPKETREAFTSDG------ 459
Cdd:TIGR01733 295 IGRPLANTRLYVL-----------------DDDLRPVPVGV---VGELYIGGPGVARGYLNRPELTAERFVPDPfaggdg 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 460 --WFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAV 512
Cdd:TIGR01733 355 arLYRTGDLVRYlPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
208-574 |
1.42e-49 |
|
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: 174.61 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENvqavTTGLVEKW----EWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQM 283
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQ----TLRAAAAWadcaDLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VWKKFLSSqapRVSVFMAVPTIYAKLIEYydehfsqPQVQDFVRAfcqeNIRLMVSGSAALPVPVLKKWKAITG-HTLLE 362
Cdd:cd17638 81 ILEAIERE---RITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 363 RYGMTEIGMA-LSNPL-HGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgdedgtqmtpglegQEGELLVRGSSV 440
Cdd:cd17638 147 AYGLTEAGVAtMCRPGdDAETVATTCGRACPGFEVRIA------------------------------DDGEVLVRGYNV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 441 FREYWNRPKETREAFTSDGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVV 519
Cdd:cd17638 197 MQGYLDDPEATAEAIDADGWLHTGDVGELDErGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDER 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 520 WGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNK 574
Cdd:cd17638 276 MGEVGKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
60-577 |
1.61e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 177.65 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 60 FGDKIAIIDQNGEHTYRELFcrslRLSQEICRVLQcSSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAV---PLYR- 134
Cdd:PRK05677 37 FADKPAFSNLGKTLTYGELY----KLSGAFAAWLQ-QHTDLKPgDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYTa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 ---KH------------------------PVQQLEYVIEDS--------QSALVIAAEEYVGKISPS-----AEKLGvPV 174
Cdd:PRK05677 112 remEHqfndsgakalvclanmahlaekvlPKTGVKHVIVTEvadmlpplKRLLINAVVKHVKKMVPAyhlpqAVKFN-DA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 175 LPLGSHSSGSAGHTAVEDVplassaswkdrgAMIIYTSGTTGRPKGVLSTHEN-------VQAVTTGLVEKwewkKEDVI 247
Cdd:PRK05677 191 LAKGAGQPVTEANPQADDV------------AVLQYTGGTTGVAKGAMLTHRNlvanmlqCRALMGSNLNE----GCEIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 248 LHVLPLHHVHGVINKLLCPLWVGATCIMLP---EFSAqMVwkKFLSSQapRVSVFMAVPTIYAKLIEyyDEHFsqpQVQD 324
Cdd:PRK05677 255 IAPLPLYHIYAFTFHCMAMMLIGNHNILISnprDLPA-MV--KELGKW--KFSGFVGLNTLFVALCN--NEAF---RKLD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 325 FVRafcqenIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVpGSVGTPLPGVEVRIAteavk 403
Cdd:PRK05677 325 FSA------LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVI----- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 404 gggrsytilaqgDEDGTQMTpglEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGRTSv 482
Cdd:PRK05677 393 ------------DDDGNELP---LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKK- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 483 DIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVE 562
Cdd:PRK05677 457 DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRD 536
|
570
....*....|....*
gi 1201832555 563 EIPRNQMGKVNKKEL 577
Cdd:PRK05677 537 ELPTTNVGKILRREL 551
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
62-577 |
2.86e-48 |
|
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: 176.13 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcSSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLyrkHPV-- 138
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGL------RGLGLARgERVAIYLDKRLETVTAMFGAALAGGVFVPI---NPLlk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 -QQLEYVIEDSQSALVIAAEEYVGKISPSAEklGVPVLPLGSHSSGSagHTAVEDVPLASSASWK--------------- 202
Cdd:TIGR03098 86 aEQVAHILADCNVRLLVTSSERLDLLHPALP--GCHDLRTLIIVGDP--AHASEGHPGEEPASWPkllalgdadpphpvi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 -DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSA 281
Cdd:TIGR03098 162 dSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 QMVWKkflSSQAPRVSVFMAVPTIYAKLieyydehfsqpqVQDFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHT-L 360
Cdd:TIGR03098 241 RDVLK---ALEKHGITGLAAVPPLWAQL------------AQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNArL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 361 LERYGMTEIGMALSNPLHGV-RVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPgleGQEGELLVRGSS 439
Cdd:TIGR03098 306 FLMYGLTEAFRSTYLPPEEVdRRPDSIGKAIPNAEVLVL-----------------REDGSECAP---GEEGELVHRGAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 440 VFREYWNRPKETREAFTSDGWFRTG----DTAAY--------HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHI 507
Cdd:TIGR03098 366 VAMGYWNDPEKTAERFRPLPPFPGElhlpELAVWsgdtvrrdEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 508 TDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:TIGR03098 445 AEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
73-577 |
3.84e-48 |
|
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: 173.84 E-value: 3.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 73 HTYRELfcrsLRLSQEICRVLQCSSRDlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSAL 152
Cdd:cd05969 1 YTFAQL----KVLSARFANVLKSLGVG-KGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 153 VIAAEEYVGKISPsaeklgvpvlplgshssgsaghtavEDvplassaswkdrGAMIIYTSGTTGRPKGVLSTHENV--QA 230
Cdd:cd05969 76 LITTEELYERTDP-------------------------ED------------PTLLHYTSGTTGTPKGVLHVHDAMifYY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 VTTglveKW--EWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP-EFSAQMvWKKFLssQAPRVSVFMAVPTIYA 307
Cdd:cd05969 119 FTG----KYvlDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGII--ERVKVTVWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 308 KLIEYYDEhfsqpqvqdFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSV 386
Cdd:cd05969 192 MLMKEGDE---------LARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 387 GTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAFTsDGWFRTG 464
Cdd:cd05969 263 GKPLPGVKAAVV-----------------DENGNELPPG---TKGILALKPGwpSMFRGIWNDEERYKNSFI-DGWYLTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 465 DTAaYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVK--- 539
Cdd:cd05969 322 DLA-YRDedGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElke 399
|
490 500 510
....*....|....*....|....*....|....*...
gi 1201832555 540 ELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05969 400 EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
60-574 |
9.35e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 175.35 E-value: 9.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 60 FGDKIAII--DQNGEHTYRELFCRSLRLSQEICRV-LQcssrdlKEERISFLCPNDASYVVAQWASWMSGGIAV---PLY 133
Cdd:PRK12583 31 FPDREALVvrHQALRYTWRQLADAVDRLARGLLALgVQ------PGDRVGIWAPNCAEWLLTQFATARIGAILVninPAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 134 RKhpvQQLEYVIEDSQSALVIAAEEY--------VGKISPS-----AEKLGVPVLP----------------LGSHSSGS 184
Cdd:PRK12583 105 RA---SELEYALGQSGVRWVICADAFktsdyhamLQELLPGlaegqPGALACERLPelrgvvslapapppgfLAWHELQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 185 AGHT-AVEDVPLASSASWKDRGAMIIYTSGTTGRPKGVLSTHENV------QAVTTGLVEkwewkkEDVILHVLPLHHVH 257
Cdd:PRK12583 182 RGETvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIlnngyfVAESLGLTE------HDRLCVPVPLYHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 258 G-VINKLLCpLWVGAtCIMLP--EFSAQMVWKkflSSQAPRVSVFMAVPTIY-AKLieyydEHfsqPQVQDFVRAfcqeN 333
Cdd:PRK12583 256 GmVLANLGC-MTVGA-CLVYPneAFDPLATLQ---AVEEERCTALYGVPTMFiAEL-----DH---PQRGNFDLS----S 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 334 IRLMVSGSAALPVPVLKK-WKAITGHTLLERYGMTEIG-----MALSNPLHgVRVPgSVGTPLPGVEVRIAteavkgggr 407
Cdd:PRK12583 319 LRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpvslqTTAADDLE-RRVE-TVGRTQPHLEVKVV--------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 408 sytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIK 486
Cdd:PRK12583 388 --------DPDGATVPRG---EIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGR-SKDMII 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 487 NGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPR 566
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPM 535
|
....*...
gi 1201832555 567 NQMGKVNK 574
Cdd:PRK12583 536 TVTGKVQK 543
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
57-577 |
4.00e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 173.19 E-value: 4.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAIIDQNGEHTYRELfcrsLRLSQEICRVLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAEL----DEQSNALARGLL--ALGVRAgDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLG----VPVLPLGSHSSGSAGHTAVEDVPLASSAS---WKDRGAMI 208
Cdd:PRK07788 133 FSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGrlraWGGNPDDDEPSGSTDETLDDLIAGSSTAPlpkPPKPGGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 209 IYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCIMLPEFSAQMVWKkf 288
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLE-- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 lSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQVQdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE 368
Cdd:PRK07788 290 -DIAKHKATALVVVPVMLSRILDLGPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 IGMA-LSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWN- 446
Cdd:PRK07788 360 VAFAtIATPEDLAEAPGTVGRPPKGVTVKIL-----------------DENGNEVPRG---VVGRIFVGNGFPFEGYTDg 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 447 RPKETreaftSDGWFRTGDTAaYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRV 524
Cdd:PRK07788 420 RDKQI-----IDGLLSSGDVG-YFDedGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRL 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 525 SAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK07788 493 RAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
103-580 |
2.65e-46 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 171.09 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYV-VAQWASWMsGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVgkisPSAEKLGVPVLPL---- 177
Cdd:PRK06155 72 DRVALMCGNRIEFLdVFLGCAWL-GAIAVPINTALRGPQLEHILRNSGARLLVVEAALL----AALEAADPGDLPLpavw 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 178 --GSHSSGS--AGHTAVEDVPLASSASWKDRG----AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILH 249
Cdd:PRK06155 147 llDAPASVSvpAGWSTAPLPPLDAPAPAAAVQpgdtAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 250 VLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQMVWKKFLSSQAPRVSVFMAVPTIYaklieyydehFSQPQVQDfvraf 329
Cdd:PRK06155 227 TLPLFHTNA-LNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSIL----------LSQPARES----- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 330 cQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPlHGVRVPGSVGTPLPGVEVRIAteavkgggrsy 409
Cdd:PRK06155 291 -DRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVT-HGSQRPGSMGRLAPGFEARVV----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 410 tilaqgDEDGTQMTPGlegQEGELLVRGSSVF---REYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDII 485
Cdd:PRK06155 358 ------DEHDQELPDG---EPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRdADGWFRFVDRIK-DAI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 486 KNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIP 565
Cdd:PRK06155 427 RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALP 506
|
490
....*....|....*
gi 1201832555 566 RNQMGKVNKKELLQR 580
Cdd:PRK06155 507 KTENGKVQKFVLREQ 521
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
56-577 |
7.22e-46 |
|
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: 168.53 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPL 132
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRL--------RAAgvgPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 133 YRKHPVQQLEYVIEDSQSALVIAAEEYVGkispSAEKLGVPVLPLGSHSSGSAGhtavedvPLASSASwKDRGAMIIYTS 212
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAG----RAGGLEVAVVIDEALDAGPAG-------NPAVPVS-PDDLAYVMYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 213 GTTGRPKGVLSTHENVqavtTGLVEKWEW---KKEDVILHVLPL------HHVHGvinkllcPLWVGATCIMLP--EFSA 281
Cdd:cd12117 146 GSTGRPKGVAVTHRGV----VRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPkgTLLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 QMVWKKFLSSQapRVSV-FMAVPTiyaklieyydehFSQpQVQDFVRAFcqENIRLMVSGSAALPVPVLKKWKAITGH-T 359
Cdd:cd12117 215 PDALGALIAEE--GVTVlWLTAAL------------FNQ-LADEDPECF--AGLRELLTGGEVVSPPHVRRVLAACPGlR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 360 LLERYGMTE-IGMALSNPLH-GVRVPGSV--GTPLPGVEVRIAteavkgggrsytilaqgDEDGtQMTPglEGQEGELLV 435
Cdd:cd12117 278 LVNGYGPTEnTTFTTSHVVTeLDEVAGSIpiGRPIANTRVYVL-----------------DEDG-RPVP--PGVPGELYV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 436 RGSSVFREYWNRPKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHIT 508
Cdd:cd12117 338 GGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 509 DVAVIGPPDVVWGQRVSAVVQLRRGemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12117 417 EAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
62-578 |
7.70e-46 |
|
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: 174.27 E-value: 7.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:COG1020 491 DAVAVVFGDQSLTYAELNARANRLA----HHLR--ALGVGpGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAER 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAAEEYVGKISPsaekLGVPVLPLgshSSGSAGHTAVEDVPLASSAswkDRGAMIIYTSGTTGRPKG 220
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPE----LGVPVLAL---DALALAAEPATNPPVPVTP---DDLAYVIYTSGSTGRPKG 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINkLLCPLWVGATCIMLPEFSAQMV--WKKFLSSQapRVSV 298
Cdd:COG1020 635 VMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE-IFGALLSGATLVLAPPEARRDPaaLAELLARH--RVTV 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 299 FMAVPTIYAKLIEYYDEHFSQPqvqdfvrafcqeniRLMVSGSAALPVPVLKKWKAITGHT-LLERYGMTE------IGM 371
Cdd:COG1020 712 LNLTPSLLRALLDAAPEALPSL--------------RLVLVGGEALPPELVRRWRARLPGArLVNLYGPTEttvdstYYE 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALSNPLHGVRVPgsVGTPLPGVEVRIAteavkgggrsytilaqgDEDGtQMTPglEGQEGELLVRGSSVFREYWNRPKET 451
Cdd:COG1020 778 VTPPDADGGSVP--IGRPIANTRVYVL-----------------DAHL-QPVP--VGVPGELYIGGAGLARGYLNRPELT 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 452 REAFTSDG-------WFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQR 523
Cdd:COG1020 836 AERFVADPfgfpgarLYRTGDLARWLpDGNLEFLGRAD-DQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKR 914
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 524 VSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELL 578
Cdd:COG1020 915 LVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-578 |
2.15e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 166.85 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGG----IAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLG 178
Cdd:cd05922 19 ERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGTVLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 179 SHSSGSAGHTAvEDVPLAssaswKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHG 258
Cdd:cd05922 99 ADGIRAARASA-PAHEVS-----HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 259 vINKLLCPLWVGATCIMLPEFS-AQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafcqeNIRLM 337
Cdd:cd05922 173 -LSVLNTHLLRGATLVLTNDGVlDDAFWEDL---REHGATGLAGVPSTYAMLTRLGFDPAKLP------------SLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 338 VSGSAALPVPVLKKWK-AITGHTLLERYGMTEI--GMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaq 414
Cdd:cd05922 237 TQAGGRLPQETIARLReLLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEIL---------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 415 gDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKIS 493
Cdd:cd05922 301 -DDDGTPTPPG---EPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKLFGNRIS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 494 ALEVERQLLAHPHITDVAVIGPPDVVwGQRVSAVVQLRRGemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVN 573
Cdd:cd05922 376 PTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
....*
gi 1201832555 574 KKELL 578
Cdd:cd05922 453 YAALR 457
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
50-577 |
3.75e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 168.08 E-value: 3.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 50 VTPVFTRAL-TFGDKIAIIDQNGEHTYRELfcrsLRLSQEICRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGI 128
Cdd:PRK12492 26 VVEVFERSCkKFADRPAFSNLGVTLSYAEL----ERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 129 AV---PLYR----KH------------------------PVQQLEYVIE----DSQSA----LVIAAEEYVGKISPS--- 166
Cdd:PRK12492 102 VVntnPLYTaremRHqfkdsgaralvylnmfgklvqevlPDTGIEYLIEakmgDLLPAakgwLVNTVVDKVKKMVPAyhl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 167 AEKLGVP-VLPLGSHSSGSAGHTAVEDVplassaswkdrgAMIIYTSGTTGRPKGVLSTH----ENVQAVTTGLVEKWE- 240
Cdd:PRK12492 182 PQAVPFKqALRQGRGLSLKPVPVGLDDI------------AVLQYTGGTTGLAKGAMLTHgnlvANMLQVRACLSQLGPd 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 241 ----WKK-EDVILHVLPLHHVHGVINKLLCPLWVGATCIML------PEFSAQMvwKKFlssqapRVSVFMAVPTIYAKL 309
Cdd:PRK12492 250 gqplMKEgQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnprdiPGFIKEL--GKW------RFSALLGLNTLFVAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 310 IEYydehfsqPQVQ--DFvrafcqENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSV 386
Cdd:PRK12492 322 MDH-------PGFKdlDF------SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 387 GTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTpglEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDT 466
Cdd:PRK12492 389 GIPVPGTALKVI-----------------DDDGNELP---LGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 467 AAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEmLSVKELKEWA 545
Cdd:PRK12492 449 AVIDpDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYC 526
|
570 580 590
....*....|....*....|....*....|..
gi 1201832555 546 RDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12492 527 KENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
60-571 |
3.87e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 167.37 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 60 FGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPL-YRKHP 137
Cdd:PRK07798 16 VPDRVALVCGDRRLTYAELEERANRLA----HYLI--AQGLGpGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 138 vQQLEYVIEDSQSALVIAAEEY---VGKISPSAEKLGVPV-LPLGSHSSGSAGHTAVEDVpLASSASWKDRGA------M 207
Cdd:PRK07798 90 -DELRYLLDDSDAVALVYEREFaprVAEVLPRLPKLRTLVvVEDGSGNDLLPGAVDYEDA-LAAGSPERDFGErspddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENVQAVTTG---------LVEKWEWKKED------VILHVLPLHHVHGVINKLLCpLWVGAT 272
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIFRVLLGgrdfatgepIEDEEELAKRAaagpgmRRFPAPPLMHGAGQWAAFAA-LFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 273 CIMLP--EFSAQMVWKkflSSQAPRVSVFMAVPTIYAK-LIEYYDEHfsqpqvqdfvRAFCQENIRLMVSGSAALPVPVL 349
Cdd:PRK07798 247 VVLLPdvRFDADEVWR---TIEREKVNVITIVGDAMARpLLDALEAR----------GPYDLSSLFAIASGGALFSPSVK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 350 KKW-KAITGHTLLERYGMTEIGmalsNPLHGVRVPGSVGTPLPGVEVriateavkggGRSYTILaqgDEDGTQMTPGlEG 428
Cdd:PRK07798 314 EALlELLPNVVLTDSIGSSETG----FGGSGTVAKGAVHTGGPRFTI----------GPRTVVL---DEDGNPVEPG-SG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEGeLLVRGSSVFREYWNRPKETREAF-TSDG--WFRTGDTAAYH-DGVYWIKGRTSVdIIKNGGFKISALEVERQLLAH 504
Cdd:PRK07798 376 EIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEaDGTITLLGRGSV-CINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 505 PHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGK 571
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
61-577 |
4.93e-45 |
|
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: 166.30 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcSSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQ 139
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLL------RARGVGpEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 140 QLEYVIEDSQSALVIAAEEYVGKISPSAeklGVPVLPLGSHSSGSAGHTAVEDVPlassaswkDRGAMIIYTSGTTGRPK 219
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAARLPAGG---DVALLGDEALAAPPATPPLVPPRP--------DNLAYVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 220 GVLSTHEnvqavttGLVEKWEWKKE-------DVILHVLPLhhvhGV---INKLLCPLWVGATCIML-------PEFSAQ 282
Cdd:cd17646 155 GVMVTHA-------GIVNRLLWMQDeyplgpgDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 283 MVwkkflssQAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDfvrafCQeNIRLMVSGSAALPVPVLKKWKAITGHTLLE 362
Cdd:cd17646 224 LI-------REHGVTTCHFVPSMLRVFLA-------EPAAGS-----CA-SLRRVFCSGEALPPELAARFLALPGAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 363 RYGMTE--IGM---ALSNPLHGVRVPgsVGTPLPGVEVRIATEAvkgggrsytilaqgdedgtqMTPGLEGQEGELLVRG 437
Cdd:cd17646 284 LYGPTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLYVLDDA--------------------LRPVPVGVPGELYLGG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 438 SSVFREYWNRPKETREAFTSDgWF-------RTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITD 509
Cdd:cd17646 342 VQLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWrPDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTH 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 510 VAVIGPPDVVWGQRVSAVVQLRRGEM-LSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17646 420 AVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
72-579 |
9.49e-45 |
|
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: 164.53 E-value: 9.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELFCRSLRLSqeicRVLqcSSRDL-KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQS 150
Cdd:cd05971 6 KVTFKELKTASNRFA----NVL--KEIGLeKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVPlassaswkdrgAMIIYTSGTTGRPKGVLSTHE---- 226
Cdd:cd05971 80 SALV---------------------------------TDGSDDP-----------ALIIYTSGTTGPPKGALHAHRvllg 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 227 ---NVQ-----AVTTGLV----EKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVwkkFLSSQAp 294
Cdd:cd05971 116 hlpGVQfpfnlFPRDGDLywtpADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTA---FLPPTA- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 rvsvfmavptiyAKLIEYYDEHFSQPQVqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALS 374
Cdd:cd05971 192 ------------LKMMRQQGEQLKHAQV----------KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 375 N--PLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVR--GSSVFREYWNRPKE 450
Cdd:cd05971 250 NcsALFPIK-PGSMGKPIPGHRVAIV-----------------DDNGTPLPPG---EVGEIAVElpDPVAFLGYWNNPSA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 451 TREAFTSDgWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQ 529
Cdd:cd05971 309 TEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 530 LRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:cd05971 387 LNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
62-577 |
2.46e-44 |
|
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: 163.69 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLA----HRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEeyvgkispsaeklgvpvlplgshssgsaghtavedvplassaswKDRGAMIIYTSGTTGRPKGV 221
Cdd:cd17649 77 RYMLEDSGAGLLLTHH--------------------------------------------PRQLAYVIYTSGSTGTPKGV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIMLP-------EFSAQMVwkkflssQAP 294
Cdd:cd17649 113 AVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPdelwasaDELAEMV-------REL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 RVSVfMAVPTIY-AKLIEYYDEHFSQPQVQdfvrafcqenIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTE---IG 370
Cdd:cd17649 185 GVTV-LDLPPAYlQQLAEEADRTGDGRPPS----------LRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEatvTP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 MALSNPLHGVRVPGSV--GTPLPGVEVRIateavkgggrsytilaqgdeDGTQMTPGLEGQEGELLVRGSSVFREYWNRP 448
Cdd:cd17649 253 LVWKCEAGAARAGASMpiGRPLGGRSAYI--------------------LDADLNPVPVGVTGELYIGGEGLARGYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 449 KETREAFTSDG-------WFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVw 520
Cdd:cd17649 313 ELTAERFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG- 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 521 GQRVSAVVQLRRGEMLS--VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17649 391 GKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
62-577 |
6.70e-44 |
|
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: 163.28 E-value: 6.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQeicRVLQCSSRDlkEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAH---RLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPsAEKLGVPVLPLGSHSSGSAGHtaveDVPLASsaswkDRGAMIIYTSGTTGRPKGV 221
Cdd:cd17651 85 AFMLADAGPVLVLTHPALAGELAV-ELVAVTLLDQPGAAAGADAEP----DPALDA-----DDLAYVIYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKEDVILHVLPLH---HVHGVINKLLCplwvGATCIMLPE-----FSAQMVWkkfLSSQa 293
Cdd:cd17651 155 VMPHRSLANLVAWQARASSLGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPPEevrtdPPALAAW---LDEQ- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 294 pRVS-VFMavPTIYAK-LIEYYDEHFSQPQvqdfvrafcqeNIRLMVSGSAALPV-PVLKKWKA-ITGHTLLERYGMTE- 368
Cdd:cd17651 227 -RISrVFL--PTVALRaLAEHGRPLGVRLA-----------ALRYLLTGGEQLVLtEDLREFCAgLPGLRLHNHYGPTEt 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 ---IGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYW 445
Cdd:cd17651 293 hvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL-----------------DAALRPVPPG---VPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 446 NRPKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDV 518
Cdd:cd17651 353 NRPELTAERFVPDPFvpgarmYRTGDLARWLpDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 519 VWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17651 432 PGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
48-577 |
1.83e-43 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 163.51 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 48 HHVTPVF-TRALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICRVLQCSsrdlKEERISFLCPNDASYVVAQWASWMSG 126
Cdd:PRK08751 25 RTVAEVFaTSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLK----KGDRVALMMPNCLQYPIATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 127 GIAV---PLYR----KHPV---------------QQLEYVIEDSQSALVIAAE-----------------EYVGKISPSA 167
Cdd:PRK08751 101 LTVVnvnPLYTprelKHQLidsgasvlvvidnfgTTVQQVIADTPVKQVITTGlgdmlgfpkaalvnfvvKYVKKLVPEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 168 EKLGV----PVLPLGSHSSGSAGHTAVEDVplassaswkdrgAMIIYTSGTTGRPKGVLSTHENVQA---------VTTG 234
Cdd:PRK08751 181 RINGAirfrEALALGRKHSMPTLQIEPDDI------------AFLQYTGGTTGVAKGAMLTHRNLVAnmqqahqwlAGTG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 235 LVEKwewkKEDVILHVLPLHHVHGVINKLLCPLWVGAtCIMLPEFSAQMvwKKFLSS-QAPRVSVFMAVPTIYAKLIEyy 313
Cdd:PRK08751 249 KLEE----GCEVVITALPLYHIFALTANGLVFMKIGG-CNHLISNPRDM--PGFVKElKKTRFTAFTGVNTLFNGLLN-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 314 DEHFSQpqvQDFvrafcqENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSVGTPLPG 392
Cdd:PRK08751 320 TPGFDQ---IDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 393 VEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHD- 471
Cdd:PRK08751 391 TDACIK-----------------DDAGTVLAIG---EIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEq 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 472 GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVqLRRGEMLSVKELKEWARDTMAP 551
Cdd:PRK08751 451 GFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI-VKKDPALTAEDVKAHARANLTG 528
|
570 580
....*....|....*....|....*.
gi 1201832555 552 YAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK08751 529 YKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
206-577 |
2.05e-43 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 163.30 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVttglVEKWEW--------KKEDVILhVLPLHHVHGV-INKLLCpLWVGATCIM- 275
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLAN----LEQAKAaygpllhpGKELVVT-ALPLYHIFALtVNCLLF-IELGGQNLLi 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 276 -----LPEFSAQMvwKKFlssqapRVSVFMAVPTIYAKLIEyyDEHFSQpqvQDFvrafcqENIRLMVSGSAALPVPVLK 350
Cdd:PRK08974 283 tnprdIPGFVKEL--KKY------PFTAITGVNTLFNALLN--NEEFQE---LDF------SSLKLSVGGGMAVQQAVAE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 351 KWKAITGHTLLERYGMTEIGMALS-NPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPgleGQ 429
Cdd:PRK08974 344 RWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLV-----------------DDDGNEVPP---GE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 430 EGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHIT 508
Cdd:PRK08974 404 PGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEeGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVL 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 509 DVAVIGPPDVVWGQRVSAVVqLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK08974 482 EVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
105-577 |
4.15e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 162.32 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 105 ISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPsaekLGVPVLPL---GSHS 181
Cdd:PLN02574 95 VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP----LGVPVIGVpenYDFD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 182 SGSAGHTAVEDV------PLASSASWKDRGAMIIYTSGTTGRPKGVLSTHENVQAvTTGLVEKWEWKK------EDVILH 249
Cdd:PLN02574 171 SKRIEFPKFYELikedfdFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIA-MVELFVRFEASQyeypgsDNVYLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 250 VLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIeyydeHFSQPqvqdfVRAF 329
Cdd:PLN02574 250 ALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVI---DRFKVTHFPVVPPILMALT-----KKAKG-----VCGE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 330 CQENIRLMVSGSAALPVPVLKKWKAITGHT-LLERYGMTE---IGMALSNPlHGVRVPGSVGTPLPGVEVRIATEavkgg 405
Cdd:PLN02574 317 VLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEstaVGTRGFNT-EKLSKYSSVGLLAPNMQAKVVDW----- 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 406 grsytilaqgdEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDI 484
Cdd:PLN02574 391 -----------STGCLLPPG---NCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 485 IKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEI 564
Cdd:PLN02574 456 IKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSI 535
|
490
....*....|...
gi 1201832555 565 PRNQMGKVNKKEL 577
Cdd:PLN02574 536 PKSPAGKILRREL 548
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
57-577 |
4.16e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 159.59 E-value: 4.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAII--DQNGEHTYRELfcrslrlsQEICRVLQCSSRDL---KEERISFLCPNDASYVVAQWASWMSGGIAV- 130
Cdd:PRK08315 26 AARYPDREALVyrDQGLRWTYREF--------NEEVDALAKGLLALgieKGDRVGIWAPNVPEWVLTQFATAKIGAILVt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 131 --PLYRKHpvqQLEYVIEDSQSALVIAAE-----EYVGKI--------SPSAEKLGVPVLP-------LGSHSSGS---- 184
Cdd:PRK08315 98 inPAYRLS---ELEYALNQSGCKALIAADgfkdsDYVAMLyelapelaTCEPGQLQSARLPelrrvifLGDEKHPGmlnf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 185 ----AGHTAVEDVPLAssaswkDRGAM--------IIYTSGTTGRPKGVLSTHENVqaVTTGLV--EKWEWKKEDVILHV 250
Cdd:PRK08315 175 dellALGRAVDDAELA------ARQATldpddpinIQYTSGTTGFPKGATLTHRNI--LNNGYFigEAMKLTEEDRLCIP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 251 LPLHHVHG-VINKLLCpLWVGAT-CIMLPEFSAQMVwkkfLSS-QAPRVSVFMAVPTIY-AKLieyydEHfsqPqvqDFV 326
Cdd:PRK08315 247 VPLYHCFGmVLGNLAC-VTHGATmVYPGEGFDPLAT----LAAvEEERCTALYGVPTMFiAEL-----DH---P---DFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 327 RaFCQENIRLMVSGSAALPVPVLKKwkaitghtLLERYGMTEI----GM----------ALSNPLHgVRVpGSVGTPLPG 392
Cdd:PRK08315 311 R-FDLSSLRTGIMAGSPCPIEVMKR--------VIDKMHMSEVtiayGMtetspvstqtRTDDPLE-KRV-TTVGRALPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 393 VEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HD 471
Cdd:PRK08315 380 LEVKIV-----------------DPETGETVP--RGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMdEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 472 GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAP 551
Cdd:PRK08315 441 GYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAH 519
|
570 580
....*....|....*....|....*.
gi 1201832555 552 YAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK08315 520 YKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
57-580 |
1.02e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 158.19 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKIAIIDQNGEHTYRELFCRSLRLSQeicrvlQCSSRDL-KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLAS------ALARRGIgRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPL-----GSHSSGS-AGHTAVEDVpLAS---SASW---KD 203
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddPEYPGGRfIGALDYEAF-LASgdpDFAWtlpAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 204 RGAMII--YTSGTTGRPKGVLSTHEN--VQAVTTGLVekWEWKKEDVILHVLPLHHVHGvinklLCPLW----VGATCIM 275
Cdd:PRK08162 181 EWDAIAlnYTSGTTGNPKGVVYHHRGayLNALSNILA--WGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 276 LPEFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYYDEH---FSQPqvqdfvrafcqenIRLMVSGsAALPVPVLKKW 352
Cdd:PRK08162 254 LRKVDPKLIFDLI---REHGVTHYCGAPIVLSALINAPAEWragIDHP-------------VHAMVAG-AAPPAAVIAKM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAItGHTLLERYGMTEIgmalsnplHGvrvPGSVGTPLPGV-EVRIATEAVKGG--GRSYTILAQ---GDEDGTQMTPGl 426
Cdd:PRK08162 317 EEI-GFDLTHVYGLTET--------YG---PATVCAWQPEWdALPLDERAQLKArqGVRYPLQEGvtvLDPDTMQPVPA- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 EGQE-GELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLAH 504
Cdd:PRK08162 384 DGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHpDGYIKIKDR-SKDIIISGGENISSIEVEDVLYRH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 505 PHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTElIVVEEIPRNQMGKVNKKELLQR 580
Cdd:PRK08162 462 PAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVLREQ 536
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
56-572 |
1.06e-41 |
|
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: 158.17 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIA---IIDQNGE---HTYRELFCRSLRLSQEICRVLQCSsrdlkeERISFLCPNDASYVVAQWASWMSGGIA 129
Cdd:cd05931 2 RAAARPDRPAytfLDDEGGReetLTYAELDRRARAIAARLQAVGKPG------DRVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 130 VPLY---RKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLgshssgsagHTAVEDVPLASSASWKDRG- 205
Cdd:cd05931 76 VPLPpptPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---------LLVVDLLPDTSAADWPPPSp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 -----AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP--E 278
Cdd:cd05931 147 dpddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 279 FSAQ-MVWKKFLSSqapRVSVFMAVPT---------IYAKLIEYYD-----------EHFSQPQVQDFVRAFCQENIR-- 335
Cdd:cd05931 227 FLRRpLRWLRLISR---YRATISAAPNfaydlcvrrVRDEDLEGLDlsswrvalngaEPVRPATLRRFAEAFAPFGFRpe 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 336 ------------LMVSGSAALPVPVLkkwkaitghTLLERygmteigMALSNPLHGVRVPG-------SVGTPLPGVEVR 396
Cdd:cd05931 304 afrpsyglaeatLFVSGGPPGTGPVV---------LRVDR-------DALAGRAVAVAADDpaarelvSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 397 IAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAF------TSDGWFRTGDTAAYH 470
Cdd:cd05931 368 IV-----------------DPETGRELP--DGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 471 DGVYWIKGRTSvDIIKNGGFKISALEVERQL-LAHPHI--TDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARD 547
Cdd:cd05931 429 DGELYITGRLK-DLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRA 507
|
570 580
....*....|....*....|....*....
gi 1201832555 548 TMA-PYAV-PTELIVVE--EIPRNQMGKV 572
Cdd:cd05931 508 AVArEHGVaPADVVLVRpgSIPRTSSGKI 536
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
5-577 |
2.31e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 156.70 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 5 LLFPPASWSARCLLRDLHRWGlrgqnragcprrgvqttwtasSHHVTPVFTRALTFGDKIAIIDQNGEHTYRELFCRSLR 84
Cdd:PRK13383 14 LLNPPSPRAVLRLLREASRGG---------------------TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 85 LSQEICRVLQCSSRdlkeeRISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKIS 164
Cdd:PRK13383 73 LARRLTRDGVAPGR-----AVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 165 PSAEKLGVpVLPLGSHSSGSAGHTAVedvplASSaswkdrGAMIIYTSGTTGRPKGVLSTHENVQA--VTTGLVEKWEWK 242
Cdd:PRK13383 148 GADDAVAV-IDPATAGAEESGGRPAV-----AAP------GRIVLLTSGTTGKPKGVPRAPQLRSAvgVWVTILDRTRLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 243 KEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQMVWKKflsSQAPRVSVFMAVPTIYAKLIEYYDEhfsqpqv 322
Cdd:PRK13383 216 TGSRISVAMPMFHGLG-LGMLMLTIALGGTVLTHRHFDAEAALAQ---ASLHRADAFTAVPVVLARILELPPR------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 323 qdfVRAfcqEN----IRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGM-ALSNPLHGVRVPGSVGTPLPGVEVRI 397
Cdd:PRK13383 285 ---VRA---RNplpqLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 398 ATEAVKGGGRSYT--ILAQGDEDGTQMTPGlegqegellvRGSSVFreywnrpketreaftsDGWFRTGDTaAYHD--GV 473
Cdd:PRK13383 359 LDRNNRPVGPRVTgrIFVGGELAGTRYTDG----------GGKAVV----------------DGMTSTGDM-GYLDnaGR 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 474 YWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYA 553
Cdd:PRK13383 412 LFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFE 490
|
570 580
....*....|....*....|....
gi 1201832555 554 VPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
62-580 |
2.35e-41 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 156.84 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEICRvLQCSSRDlkeeRISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQA-LPIGEPR----VVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYvgkiSPSAEKlGVPVLPLGSHS------SGSAGHTAVEDVPLASSASWKDR-GAMIIYTSGT 214
Cdd:PRK13382 133 AEVVTREGVDTVIYDEEF----SATVDR-ALADCPQATRIvawtdeDHDLTVEVLIAAHAGQRPEPTGRkGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIML----PEFSAQMVwkkfls 290
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRrrfdPEATLDLI------ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 291 sQAPRVSVFMAVPTIYAKLIEYYDEHFSQpqvqdfvraFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG 370
Cdd:PRK13382 281 -DRHRATGLAVVPVMFDRIMDLPAEVRNR---------YSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 M-ALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPgleGQEGELLVRGSSVFREYwnRPK 449
Cdd:PRK13382 351 MiATATPADLRAAPDTAGRPAEGTEIRIL-----------------DQDFREVPT---GEVGTIFVRNDTQFDGY--TSG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETREafTSDGWFRTGDTAAYHD-GVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:PRK13382 409 STKD--FHDGFMASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 529 QLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:PRK13382 486 VLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
62-577 |
5.68e-41 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 155.18 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLKEERI-SFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLA----RTLR--EKGVGPDTIvGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAAEEyvgkispsaeklgvpvLPLGSHSSGSAG--------HTAVEDVPLASSAswkDRGAMIIYTS 212
Cdd:cd17655 86 IQYILEDSGADILLTQSH----------------LQPPIAFIGLIDlldedtiyHEESENLEPVSKS---DDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 213 GTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLH---HVHGVINKLLCplwvGATCIMLP--EFSAQMVWKK 287
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASLLS----GNTLYIVRkeTVLDGQALTQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 288 FLSSQapRVSVFMAVPTiYAKLIEYydehfsqpqvqdfVRAFCQENIRLMVSGSAALPVPVLKKWKAITGH--TLLERYG 365
Cdd:cd17655 223 YIRQN--RITIIDLTPA-HLKLLDA-------------ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTE------IGMALSNPLHGVRVPgsVGTPLPGVEVRIATEavkgggrsytilaqgdedgtQMTPGLEGQEGELLVRGSS 439
Cdd:cd17655 287 PTEttvdasIYQYEPETDQQVSVP--IGKPLGNTRIYILDQ--------------------YGRPQPVGVAGELYIGGEG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 440 VFREYWNRPKETREAFTSDGW------FRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAV 512
Cdd:cd17655 345 VARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 513 IGPPDVVWGQRVSA-VVQLRRgemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17655 424 IARKDEQGQNYLCAyIVSEKE---LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
59-577 |
6.82e-41 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 155.95 E-value: 6.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 59 TFGDKIAIIDQNGEHTYRELFcrslRLSQEICRVLQcsSRDL-KEERISFLCPNDASYVVAQWASWMSGGIAV---PLYR 134
Cdd:PRK07059 35 QYADRPAFICMGKAITYGELD----ELSRALAAWLQ--SRGLaKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHpvqQLEYVIEDSQS-ALVI------AAEEYVGKIS-------PSAEKLG----------------VPVLPLGSHSSGS 184
Cdd:PRK07059 109 PR---ELEHQLKDSGAeAIVVlenfatTVQQVLAKTAvkhvvvaSMGDLLGfkghivnfvvrrvkkmVPAWSLPGHVRFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 185 AGHTAVEDVPLASSASWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLvEKW-----EWKKED---VILHVLPLHHV 256
Cdd:PRK07059 186 DALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQM-EAWlqpafEKKPRPdqlNFVCALPLYHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 257 HGVINKLLCPLWVGATCIMLPE------FSAQMvwKKFlssqapRVSVFMAVPTIYAKLIEYYDehFSQpqvQDFvrafc 330
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILIPNprdipgFIKEL--KKY------QVHIFPAVNTLYNALLNNPD--FDK---LDF----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 331 qENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsy 409
Cdd:PRK07059 327 -SKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIR----------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 410 tilaqgDEDGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTaayhdGVYWIKGRTSV-----DI 484
Cdd:PRK07059 395 ------DDDGNDLPLG---EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDV-----GVMDERGYTKIvdrkkDM 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 485 IKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVqLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEI 564
Cdd:PRK07059 461 ILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTEL 539
|
570
....*....|...
gi 1201832555 565 PRNQMGKVNKKEL 577
Cdd:PRK07059 540 PKTNVGKILRREL 552
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
53-577 |
8.67e-41 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 155.52 E-value: 8.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 53 VFTRALTFGDKIAIID-QNGE-HTYRELfcrslrlsQEICRVLQCSSRDL---KEERISFLCPNDASYVVAQWASWMSGG 127
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADV--------ELLSRRVAAGLHKLgirQGDVVMLLLPNCPEFVLAFLGASRRGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 128 I---AVPLYRKHpvqQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSG----SAGHTAVEDVPLASSAS 200
Cdd:PLN02246 101 VtttANPFYTPA---EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGclhfSELTQADENELPEVEIS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 201 WKDRGAMIiYTSGTTGRPKGVLSTHENVqaVTT------GLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCI 274
Cdd:PLN02246 178 PDDVVALP-YSSGTTGLPKGVMLTHKGL--VTSvaqqvdGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 275 MLPEFSA----QMVwkkflssQAPRVSVFMAVPTIYAKLIEyydehfsqpqvQDFVRAFCQENIRLMVSGSAALPVPVLK 350
Cdd:PLN02246 255 IMPKFEIgallELI-------QRHKVTIAPFVPPIVLAIAK-----------SPVVEKYDLSSIRMVLSGAAPLGKELED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 351 KWKA-ITGHTLLERYGMTEIGMALSNPLHGVRVP-----GSVGTPLPGVEVRIAteavkgggrsytilaqgDEDgTQMTP 424
Cdd:PLN02246 317 AFRAkLPNAVLGQGYGMTEAGPVLAMCLAFAKEPfpvksGSCGTVVRNAELKIV-----------------DPE-TGASL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 425 GlEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTaAYHDG------VYWIKgrtsvDIIKNGGFKISALEVE 498
Cdd:PLN02246 379 P-RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDI-GYIDDddelfiVDRLK-----ELIKYKGFQVAPAELE 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 499 RQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PLN02246 452 ALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
74-514 |
9.41e-41 |
|
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: 154.05 E-value: 9.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSqeicrvlqCSSRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQS 150
Cdd:cd17640 7 TYKDLYQEILDFA--------AGLRSLgvkAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVIaaeeyvgkispsaeklgvpvlplgshssgsaghtaVEDVPlassaswkDRGAMIIYTSGTTGRPKGVLSTHENVqa 230
Cdd:cd17640 79 VALV-----------------------------------VENDS--------DDLATIIYTSGTTGNPKGVMLTHANL-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 231 vTTGLVEKWEW---KKEDVILHVLPLHHVHGVINKLLCPLWvGATCImlpeFSAQMVWKKFLSSQAPrvSVFMAVPTIYA 307
Cdd:cd17640 114 -LHQIRSLSDIvppQPGDRFLSILPIWHSYERSAEYFIFAC-GCSQA----YTSIRTLKDDLKRVKP--HYIVSVPRLWE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 308 KLIE-YYDEHFSQPQVQDFVRAFCQ--ENIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTEIGMALSNPLHGVRVPG 384
Cdd:cd17640 186 SLYSgIQKQVSKSSPIKQFLFLFFLsgGIFKFGISGGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 385 SVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTG 464
Cdd:cd17640 265 SVGRPLPGTEIKIV-----------------DPEGNVVLP--PGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTG 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 465 DTAAY-HDGVYWIKGRTSVDIIKNGGFKISALEVERQLLAHPHITDVAVIG 514
Cdd:cd17640 326 DLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
126-580 |
9.97e-41 |
|
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: 155.35 E-value: 9.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 126 GGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYV--GKISPSAEKLGVPVLPLGSHSSGSAG----HTAVEDV------ 193
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNipEEIEKAAPECPSKPKLVWVGDPVPEGwidfRKLIKNAspdfer 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 194 PLASSASWKDRGAMIIYTSGTTGRPKGVlsTHENVQAVTTGLVEK-WEWKKEDVI-LHVLPLHHVHGVINKLLCPlWVGA 271
Cdd:cd05970 176 PTANSYPCGEDILLVYFSSGTTGMPKMV--EHDFTYPLGHIVTAKyWQNVREGGLhLTVADTGWGKAVWGKIYGQ-WIAG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 272 TCIMLPEFSaQMVWKKFLSS-QAPRVSVFMAVPTIYAKLIEYYDEHFsqpqvqDFvrafcqENIRLMVSGSAALPVPVLK 350
Cdd:cd05970 253 AAVFVYDYD-KFDPKALLEKlSKYGVTTFCAPPTIYRFLIREDLSRY------DL------SSLRYCTTAGEALNPEVFN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 351 KWKAITGHTLLERYGMTEIGMALSNpLHGVRV-PGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQ 429
Cdd:cd05970 320 TFKEKTGIKLMEGFGQTETTLTIAT-FPWMEPkPGSMGKPAPGYEIDLI-----------------DREGRSCEAG---E 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 430 EGELLVRGSS-----VFREYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLA 503
Cdd:cd05970 379 EGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQ 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 504 HPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:cd05970 457 HPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSeelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
61-572 |
1.11e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 155.44 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAI--IDQNGEH--TYRELfcrsLRLSQEICRVLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLY 133
Cdd:PRK04319 58 KDKVALryLDASRKEkyTYKEL----KELSNKFANVL----KELgveKGDRVFIFMPRIPELYFALLGALKNGAIVGPLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 134 ---RKHPVQQLeyvIEDSQSALVIAAEEYVGKIS----PSAEKlgvpVLPLGSHSSGSAGHTAVEdvPLASSAS------ 200
Cdd:PRK04319 130 eafMEEAVRDR---LEDSEAKVLITTPALLERKPaddlPSLKH----VLLVGEDVEEGPGTLDFN--ALMEQASdefdie 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 201 WKDR--GAMIIYTSGTTGRPKGVLSTHENV-QAVTTGlveKWewkkedvilhVLPLHH----------------VHGVIN 261
Cdd:PRK04319 201 WTDRedGAILHYTSGSTGKPKGVLHVHNAMlQHYQTG---KY----------VLDLHEddvywctadpgwvtgtSYGIFA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 262 KLLCplwvGATCIML-PEFSAQMvWKKFLSSQapRVSVFMAVPTIYAKLIEYYDEHFSQpqvqdfvraFCQENIRLMVSG 340
Cdd:PRK04319 268 PWLN----GATNVIDgGRFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGDDLVKK---------YDLSSLRHILSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 341 SAALPVPVLKKWKAITGHTLLERYGMTEIG--MALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDED 418
Cdd:PRK04319 332 GEPLNPEVVRWGMKVFGLPIHDNWWMTETGgiMIANYPAMDIK-PGSMGKPLPGIEAAIV-----------------DDQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 419 GTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISAL 495
Cdd:PRK04319 394 GNELPPN---RMGNLAIKKGwpSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMdEDGYFWFQGRVD-DVIKTSGERVGPF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 496 EVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRG----EMLSvKELKEWARDTMAPYAVPTELIVVEEIPRNQMGK 571
Cdd:PRK04319 469 EVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGyepsEELK-EEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
.
gi 1201832555 572 V 572
Cdd:PRK04319 548 I 548
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
68-580 |
1.44e-40 |
|
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: 154.03 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 68 DQNG-EHTYRELFCRSLRLSQEICRVLQcssrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIE 146
Cdd:cd05909 2 DTLGtSLTYRKLLTGAIALARKLAKMTK------EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 147 DSQSALVIAAEEYVgkispsaEKLGvpvLPLGSHSSGSAGHTAVEDV------------------PLASSASWK------ 202
Cdd:cd05909 76 LAGIKTVLTSKQFI-------EKLK---LHHLFDVEYDARIVYLEDLrakiskadkckaflagkfPPKWLLRIFgvapvq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 -DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP---- 277
Cdd:cd05909 146 pDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPnpld 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 -EFSAQMVWKKflssqapRVSVFMAVPT---IYAKLIEYYDehFSqpqvqdfvrafcqeNIRLMVSGSAALPVPVLKKWK 353
Cdd:cd05909 226 yKKIPELIYDK-------KATILLGTPTflrGYARAAHPED--FS--------------SLRLVVAGAEKLKDTLRQEFQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 354 AITGHTLLERYGMTEIG--MALSNPLHGvRVPGSVGTPLPGVEVRIatEAVKGGgrsytilaqgdedgtqmTPGLEGQEG 431
Cdd:cd05909 283 EKFGIRILEGYGTTECSpvISVNTPQSP-NKEGTVGRPLPGMEVKI--VSVETH-----------------EEVPIGEGG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 432 ELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAH-PHITD 509
Cdd:cd05909 343 LLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIdGEGFLTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNE 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 510 VAVIGPPDVVWGQRVSAVVQlrrGEMLSVKELKEWARDTMAP-YAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:cd05909 421 VAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
104-578 |
2.27e-40 |
|
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: 152.92 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 104 RISFLCPNDASYVVAQWASWmsggiavplyrkhpvqqleyVIEDSQSALVIAAE--EYVGKISPSAEKLGVPVLPLGSHS 181
Cdd:cd05929 44 GVYIYLINSILTVFAAAAAW--------------------KCGACPAYKSSRAPraEACAIIEIKAAALVCGLFTGGGAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 182 SGSAGHTAVE---DVPLASSASwkdRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVE---KWEWKKEDVILHVLPLHH 255
Cdd:cd05929 104 DGLEDYEAAEggsPETPIEDEA---AGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAaalGFGPGADSVYLSPAPLYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 256 VHGVINKLLCpLWVGATCIMLPEFSAQmvwkKFLSS-QAPRVSVFMAVPTIYAKLIEYYDEhfsQPQVQDFvrafcqENI 334
Cdd:cd05929 181 AAPFRWSMTA-LFMGGTLVLMEKFDPE----EFLRLiERYRVTFAQFVPTMFVRLLKLPEA---VRNAYDL------SSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 335 RLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE-IGMALSNPLHGVRVPGSVGTPLPGvEVRIAteavkgggrsytila 413
Cdd:cd05929 247 KRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRAVLG-KVHIL--------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 414 qgDEDGTQMTPGlegQEGELLVRGSSVFrEYWNRPKETREAFTSDGWFRTGDTA-AYHDGVYWIKGRTSvDIIKNGGFKI 492
Cdd:cd05929 311 --DEDGNEVPPG---EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGyLDEDGYLYLTDRRS-DMIISGGVNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 493 SALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSV---KELKEWARDTMAPYAVPTELIVVEEIPRNQM 569
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTalaEELIAFLRDRLSRYKCPRSIEFVAELPRDDT 463
|
....*....
gi 1201832555 570 GKVNKKELL 578
Cdd:cd05929 464 GKLYRRLLR 472
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
62-577 |
3.03e-40 |
|
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: 152.08 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPV 138
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTL--------RAEgvgPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 QQLEYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTTGRP 218
Cdd:cd17643 74 ERIAFILADSGPSLLL---------------------------------TDPDDL------------AYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 219 KGVLSTHENVQAVTTGLVEKWEWKKEDVilhVLPLHH---------VHGVINK----LLCPLWVGATcimlPEFSAQMVW 285
Cdd:cd17643 109 KGVVVSHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWGALLHggrlVVVPYEVARS----PEDFARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKflssqapRVSVFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafcqENIRLMVSGSAALPVPVLKKWKAITGH---TLLE 362
Cdd:cd17643 182 DE-------GVTVLNQTPSAFYQLVEAADRDGRDP-----------LALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 363 RYGMTEIGMALS-NPLHGVRVPGS----VGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRG 437
Cdd:cd17643 244 MYGITETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVL-----------------DADGRPVPPG---VVGELYVSG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 438 SSVFREYWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITD 509
Cdd:cd17643 304 AGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRD 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 510 VAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17643 383 AAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
203-580 |
6.51e-40 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 153.42 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQ 282
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGG-LSSALAMLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 283 MVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafCQENIRLMVSGSAALPVPVLKKWKAITGHT-LL 361
Cdd:PLN02860 251 AA---LQAIKQHNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 362 ERYGMTEIGMALS---------------------------NPLHGVrvpgSVGTPLPGVEVRIATeavkgggrsytilaq 414
Cdd:PLN02860 319 SAYGMTEACSSLTfmtlhdptlespkqtlqtvnqtksssvHQPQGV----CVGKPAPHVELKIGL--------------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 415 gDEDGTqmtpglegqEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKIS 493
Cdd:PLN02860 380 -DESSR---------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 494 ALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLR-------------RGEM-LSVKELKEWARD-TMAPYAVPTEL 558
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRdgwiwsdnekenaKKNLtLSSETLRHHCREkNLSRFKIPKLF 528
|
410 420
....*....|....*....|...
gi 1201832555 559 IVVEE-IPRNQMGKVnKKELLQR 580
Cdd:PLN02860 529 VQWRKpFPLTTTGKI-RRDEVRR 550
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
56-579 |
1.03e-39 |
|
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: 152.30 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIID-QNG-EHTYRELFCRSLRLSQEICRVlqcssrDLKEERISFLCP-NDASYVVAQWASWMSGGIAVPL 132
Cdd:cd17642 26 RYASVPGTIAFTDaHTGvNYSYAEYLEMSVRLAEALKKY------GLKQNDRIAVCSeNSLQFFLPVIAGLFIGVGVAPT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 133 YRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKL----GVPVLPLGSHSSG------------SAGHTAVEDVPla 196
Cdd:cd17642 100 NDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiikTIIILDSKEDYKGyqclytfitqnlPPGFNEYDFKP-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 197 SSASWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEK---WEWKKEDVILHVLPLHHVHGVINkLLCPLWVGATC 273
Cdd:cd17642 178 PSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 274 IMLPEFSAQMvwkkFLSS-QAPRVSVFMAVPTIYA-----KLIEYYDehfsqpqvqdfvrafcQENIRLMVSGSAalpvP 347
Cdd:cd17642 257 VLMYKFEEEL----FLRSlQDYKVQSALLVPTLFAffaksTLVDKYD----------------LSNLHEIASGGA----P 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 348 VLKKwkaiTGHTLLER---------YGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDED 418
Cdd:cd17642 313 LSKE----VGEAVAKRfklpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVV-----------------DLD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 419 gTQMTPGLEgQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEV 497
Cdd:cd17642 372 -TGKTLGPN-ERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAEL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 498 ERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYA-VPTELIVVEEIPRNQMGKVNKKE 576
Cdd:cd17642 449 ESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRK 528
|
...
gi 1201832555 577 LLQ 579
Cdd:cd17642 529 IRE 531
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-514 |
1.13e-39 |
|
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: 151.85 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 104 RISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIaaeeyVGKISP-SAEKLGVP----VLPLG 178
Cdd:cd05932 33 KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF-----VGKLDDwKAMAPGVPegliSISLP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 179 SHSSGS---------AGHTAVEDVPLASSaswkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILH 249
Cdd:cd05932 108 PPSAANcqyqwddliAQHPPLEERPTRFP----EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 250 VLPLHHVHGVINKLLCPLWVGATcIMLPE----FSAQMvwkkflssQAPRVSVFMAVPTIYAKL---------IEYYDEH 316
Cdd:cd05932 184 YLPLAHVTERVFVEGGSLYGGVL-VAFAEsldtFVEDV--------QRARPTLFFSVPRLWTKFqqgvqdkipQQKLNLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 317 FSQPQVQDFVR-----AFCQENIRLMVSGSAALPvPVLKKWKAITGHTLLERYGMTEiGMALSN---PlhGVRVPGSVGT 388
Cdd:cd05932 255 LKIPVVNSLVKrkvlkGLGLDQCRLAGCGSAPVP-PALLEWYRSLGLNILEAYGMTE-NFAYSHlnyP--GRDKIGTVGN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 389 PLPGVEVRIateavkgggrsytilaqgdedgtqmtpgleGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAA 468
Cdd:cd05932 331 AGPGVEVRI------------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1201832555 469 Y-HDGVYWIKGRTSvDIIKNGGFK-ISALEVERQLLAHPHITDVAVIG 514
Cdd:cd05932 381 LdADGNLTITGRVK-DIFKTSKGKyVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
62-577 |
1.49e-39 |
|
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: 150.16 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcRVLQCssrdLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARL-RAAGV----GPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTTGRPKGV 221
Cdd:cd12115 89 RFILEDAQARLVL---------------------------------TDPDDL------------AYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTtglvekwEWKKedvilHVLPLHHVHGV-----------INKLLCPLWVGATCIMlpefsAQMVWKKFLS 290
Cdd:cd12115 124 AIEHRNAAAFL-------QWAA-----AAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVL-----ADNVLALPDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 291 SQAPRVSVFMAVPTIYAKLIEyydeHFSQPQVqdfVRAFCqenirlmVSGSAALPVPVLKKWKAITGHTLLERYGMTE-- 368
Cdd:cd12115 187 PAAAEVTLINTVPSAAAELLR----HDALPAS---VRVVN-------LAGEPLPRDLVQRLYARLQVERVVNLYGPSEdt 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 -IGMALSNPLHGVRVPgSVGTPLPGVEVRIATEAvkgggrsytilaqgdedgtqMTPGLEGQEGELLVRGSSVFREYWNR 447
Cdd:cd12115 253 tYSTVAPVPPGASGEV-SIGRPLANTQAYVLDRA--------------------LQPVPLGVPGELYIGGAGVARGYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 448 PKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVW 520
Cdd:cd12115 312 PGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 521 GQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-574 |
2.58e-39 |
|
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: 147.02 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLV-EKWEWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCIMLPEFSAQMV 284
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 WKKFLSSQAprVSVFMAVPTIYAKLIEYYDEhfsqpqvqdfVRAFCqENIRLMVSGSaALPVPVLKKWKAITGHT-LLER 363
Cdd:cd17635 83 LFKILTTNA--VTTTCLVPTLLSKLVSELKS----------ANATV-PSLRLIGYGG-SRAIAADVRFIEATGLTnTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTEIGMALSNPLH-GVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQmtpGLEGQEGELLVRGSSVFR 442
Cdd:cd17635 149 YGLSETGTALCLPTDdDSIEINAVGRPYPGVDVYLA-----------------ATDGIA---GPSASFGTIWIKSPANML 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 443 EYWNRPKETREAFTsDGWFRTGDTA-AYHDGVYWIKGRTSVDIIKnGGFKISALEVERQLLAHPHITDVAVIGPPDVVWG 521
Cdd:cd17635 209 GYWNNPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 522 QRV-SAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNK 574
Cdd:cd17635 287 ELVgLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
62-577 |
8.35e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 148.77 E-value: 8.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFcrslrlsQEICRVLQ-CSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWF-------ESVCKVANwLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAAEEYVGKISPsaeklgvpvlplgshssgsaghtavEDVPLASSASWK-------DRGAMII---- 209
Cdd:PRK07638 89 LKERLAISNADMIVTERYKLNDLPD-------------------------EEGRVIEIDEWKrmiekylPTYAPIEnvqn 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 ------YTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVH---GVINKLlcplWVGATCIMLPEFS 280
Cdd:PRK07638 144 apfymgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 281 AQMVWKKFLSSQaprVSVFMAVPTIYAKLIEyydehfsqpqvqdfVRAFCQENIRLMVSGsAALPVPVLKKWKAITGH-T 359
Cdd:PRK07638 220 PNQVLDKLETEN---ISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 360 LLERYGMTEIG-MALSNPLHGVRVPGSVGTPLPGVEVRIATEAvkgggrsytilaqgdedGTQMTPGlegQEGELLVRGS 438
Cdd:PRK07638 282 LYEFYGASELSfVTALVDEESERRPNSVGRPFHNVQVRICNEA-----------------GEEVQKG---EIGTVYVKSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 SVFREYWNRPKETREaFTSDGWFRTGDTAaYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPP 516
Cdd:PRK07638 342 QFFMGYIIGGVLARE-LNADGWMTVRDVG-YEDeeGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVP 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 517 DVVWGQRVSAVVQLRRgemlSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK07638 419 DSYWGEKPVAIIKGSA----TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
62-577 |
4.09e-38 |
|
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: 145.86 E-value: 4.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLKEERISFLC-PNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLA----RLLA--ARGVGPERLVALAlPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAaeeyvgkispsaeklgvpvlplgshssgSAGHTAvedvplassaswkdrgaMIIYTSGTTGRPKG 220
Cdd:cd17652 76 IAYMLADARPALLLT----------------------------TPDNLA-----------------YVIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHhVHGVINKLLCPLWVGATCIMLPEFSAQmvwkkflssqaprvsvfm 300
Cdd:cd17652 111 VVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPAEELL------------------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 301 AVPTIYAKLIEYYDEHFSQ-PQVQDFVRAFCQENIRLMVSGSAALPVPVLKKWKaiTGHTLLERYGMTE--IGMALSNPL 377
Cdd:cd17652 172 PGEPLADLLREHRITHVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTEttVCATMAGPL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 378 HGVRVPgSVGTPLPGVEVRIAteavkgggrsytilaqgdEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTS 457
Cdd:cd17652 250 PGGGVP-PIGRPVPGTRVYVL------------------DARLRPVP--PGVPGELYIAGAGLARGYLNRPGLTAERFVA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 458 DGW-------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQ 529
Cdd:cd17652 309 DPFgapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1201832555 530 LRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17652 388 PAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
74-582 |
4.72e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 147.15 E-value: 4.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSqeicRVLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSAL 152
Cdd:PRK13391 26 TYRELDERSNRLA----HLFR--SLGLKRgDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 153 VIAAEEYvGKISPSAEKLgVP------VLPLGSHSSGSAGH-TAVEDVPLASSASwKDRGAMIIYTSGTTGRPKGVLS-- 223
Cdd:PRK13391 100 LITSAAK-LDVARALLKQ-CPgvrhrlVLDGDGELEGFVGYaEAVAGLPATPIAD-ESLGTDMLYSSGTTGRPKGIKRpl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 224 THENVQAVT--TGLVEK-WEWKKEDVILHVLPLHHVH-----GVINKLlcplwvGATCIMLPEFSAQmvwkKFLSS-QAP 294
Cdd:PRK13391 177 PEQPPDTPLplTAFLQRlWGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHFDAE----QYLALiEEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 RVSVFMAVPTIYAKLIEYYDEHFSQPQVQDfvrafcqenirLMVSGSAALPVPVLKKWKAIT--GHTLLERYGMTE-IGM 371
Cdd:PRK13391 247 GVTHTQLVPTMFSRMLKLPEEVRDKYDLSS-----------LEVAIHAAAPCPPQVKEQMIDwwGPIIHEYYAATEgLGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALSNPLHGVRVPGSVGTPLPGVeVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGSSVFrEYWNRPKET 451
Cdd:PRK13391 316 TACDSEEWLAHPGTVGRAMFGD-LHIL-----------------DDDGAELPPG---EPGTIWFEGGRPF-EYLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 452 REAFTSDG-WFRTGDTAaY--HDGVYWIKGRTSVDIIkNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:PRK13391 374 AEARHPDGtWSTVGDIG-YvdEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 529 QLRRGEMLSV---KELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRFY 582
Cdd:PRK13391 452 QPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYW 508
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
207-566 |
6.50e-38 |
|
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: 142.83 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 207 MIIYTSGTTGRPKGVLSTHENV--QAVTTGLVEKWEwkKEDVILHVLPLHHVhGVINKLLCPLWVGATCIMLPEFSAQMV 284
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALlaQALVLAVLQAID--EGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 WKKFlssQAPRVS-VFMAVPTIyaklieyydehfsqPQVQDFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLEr 363
Cdd:cd17636 81 LELI---EAERCThAFLLPPTI--------------DQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIateavkgggrsytilaqGDEDGTQMTPGlegQEGELLVRGSSVFRE 443
Cdd:cd17636 143 YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRI-----------------LDEDGREVPDG---EVGEIVARGPTVMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTsDGWFRTGDTaayhdgvywikGRTSVD-----------IIKNGGFKISALEVERQLLAHPHITDVAV 512
Cdd:cd17636 203 YWNRPEVNARRTR-GGWHHTNDL-----------GRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 513 IGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPR 566
Cdd:cd17636 271 IGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
207-572 |
7.53e-38 |
|
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: 142.16 E-value: 7.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 207 MIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvINKLLCPLWVGATCIMLPEFSAQMVWK 286
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLF-LYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 KFlssQAPRVSVFMAVPTIYAKLIEYYDEHFSqpqvqdfvrafcqenIRLMVSGSAALPVPVLKKWKAITGHT-LLERYG 365
Cdd:cd17633 83 KI---NQYNATVIYLVPTMLQALARTLEPESK---------------IKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGtqmtpgleGQEGELLVRGSSVFREYW 445
Cdd:cd17633 145 TSELSFITYNFNQESRPPNSVGRPFPNVEIEIR-----------------NADG--------GEIGKIFVKSEMVFSGYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 446 nrpkeTREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRV 524
Cdd:cd17633 200 -----RGGFSNPDGWMSVGDIGYVdEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1201832555 525 SAVVQlrrGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKV 572
Cdd:cd17633 274 VALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-573 |
1.55e-37 |
|
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: 142.52 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHE-------NVQAVTTGLVEKWEW------KKED-VILHVLPLHHVHGVINKLLCPLWVGATC 273
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEdifrmlmGGADFGTGEFTPSEDahkaaaAAAGtVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 274 IMLPEFSAQMVWKkflSSQAPRVSVFMAVPTIYAK-LIEYYDEhfsqpqvqdfVRAFCQENIRLMVSGSAALPVPVLKKW 352
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----------AGPYDLSSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAITGH-TLLERYGMTEIGMAlsnplhgvrvpGSVGTPLPGVEVRIATEAVKGggrsyTILAqgDEDGTQMTPGlEGQEG 431
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFT-----------GSGHSAGSGPETGPFTRANPD-----TVVL--DDDGRVVPPG-SGGVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 432 ELLVRGSsVFREYWNRPKETREAF-TSDG--WFRTGDTAAYH-DGVYWIKGRTSVdIIKNGGFKISALEVERQLLAHPHI 507
Cdd:cd05924 216 WIARRGH-IPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEaDGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 508 TDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVN 573
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
62-577 |
1.66e-37 |
|
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: 145.11 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVA----GALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLGshssgsaghtAVEDVPLASSASwkDRGAMIIYTSGTTGRPKGV 221
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALA----------APAPPPPVDVAP--DDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINkLLCPLWVGATCIMLPEFSAQMV--WKKFLssQAPRVSVF 299
Cdd:cd12114 145 MISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEARRRDPahWAELI--ERHGVTLW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 300 MAVPTIYAKLIEYYdehfsqPQVQDFVRafcqeNIRL-MVSGSaALPVPVLKKWKAITGH-TLLERYGMTEiGMALSNpL 377
Cdd:cd12114 222 NSVPALLEMLLDVL------EAAQALLP-----SLRLvLLSGD-WIPLDLPARLRALAPDaRLISLGGATE-ASIWSI-Y 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 378 HGVRVP----GSV--GTPLPgvevriateavkggGRSYTILAQGDEDGTQMTPglegqeGELLVRGSSVFREYWNRPKET 451
Cdd:cd12114 288 HPIDEVppdwRSIpyGRPLA--------------NQRYRVLDPRGRDCPDWVP------GELWIGGRGVALGYLGDPELT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 452 REAFTSDG----WFRTGDTAAY-HDGVYWIKGRtsVDI-IKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVS 525
Cdd:cd12114 348 AARFVTHPdgerLYRTGDLGRYrPDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 526 AVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd12114 426 FVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
206-581 |
2.88e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 141.72 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKW----EWkkedviLHVLPLHHVHGvINKLLCPLWVGATCIMLPefsa 281
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLggpgQW------LLALPAHHIAG-LQVLVRSVIAGSEPVELD---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 qmVWKKFLSSQAPRVSVFMAVPTIYAKLIEY-YDEHFSQPQVQDFVRAFcqeniRLMVSGSAALPVPVLKKWKAItGHTL 360
Cdd:PRK07824 107 --VSAGFDPTALPRAVAELGGGRRYTSLVPMqLAKALDDPAATAALAEL-----DAVLVGGGPAPAPVLDAAAAA-GINV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 361 LERYGMTEIGmalsnplhgvrvPGSV--GTPLPGVEVRIATEAVKGGGrsyTILAQGdedgtqmtpglegqegellvrgs 438
Cdd:PRK07824 179 VRTYGMSETS------------GGCVydGVPLDGVRVRVEDGRIALGG---PTLAKG----------------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 svfreYWNRPKEtrEAFTSDGWFRTGDTAAYHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDV 518
Cdd:PRK07824 221 -----YRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 519 VWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK07824 293 RLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
182-577 |
3.11e-37 |
|
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: 145.30 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 182 SGSAGHTAVEDvplassaswKDRGAMIIY-TSGTTGRPKGVLSTHENVQAVTTGLVEKW-EWKKEDVILHVLPLHHVHGV 259
Cdd:cd05928 161 EASTEHHCVET---------GSQEPMAIYfTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 260 INKLLCPlWVGATCIM---LPEFSAQMVWKKFlsSQAPrVSVFMAVPTIYAKLIEyydehfsqpqvQDFVRaFCQENIRL 336
Cdd:cd05928 232 WSSLFEP-WIQGACVFvhhLPRFDPLVILKTL--SSYP-ITTFCGAPTVYRMLVQ-----------QDLSS-YKFPSLQH 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 337 MVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPlHGVRV-PGSVGTPLPGVEVRIAteavkgggrsytilaqg 415
Cdd:cd05928 296 CVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANF-KGMKIkPGSMGKASPPYDVQII----------------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 416 DEDGTQMTPGLEGQEGELL--VRGSSVFREYWNRPKETREAFTSDGWFrTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKI 492
Cdd:cd05928 358 DDNGNVLPPGTEGDIGIRVkpIRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 493 SALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQL------RRGEMLsVKELKEWARDTMAPYAVPTELIVVEEIPR 566
Cdd:cd05928 436 GPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflsHDPEQL-TKELQQHVKSVTAPYKYPRKVEFVQELPK 514
|
410
....*....|.
gi 1201832555 567 NQMGKVNKKEL 577
Cdd:cd05928 515 TVTGKIQRNEL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
62-577 |
4.55e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 148.18 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPV 138
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRL--------RARgvgPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 QQLEYVIEDSQSALVIAAEEYVGKISPSAeklGVPVLPLGSHSSGSAGHTAVEDVPLASsaswkDRGAMIIYTSGTTGRP 218
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRHLLERLPLPA---GVARLPLDRDAEWADYPDTAPAVQLAG-----ENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 219 KGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIM------LPE-FSAQMVwkkflsS 291
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGARVLIrddelwDPEqLYDEME------R 2234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 292 QAPRVSVFMAVptiyaklieyydehFSQPQVQDFVRAFCQENIRLMVSGSAALPVPVLKK-WKAITGHTLLERYGMTEig 370
Cdd:PRK12316 2235 HGVTILDFPPV--------------YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTE-- 2298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 mALSNPLH---GVRVPGS-----VGTPLpgvevriateavkgGGRSYTILaqgDEDGTQMTPGLegqEGELLVRGSSVFR 442
Cdd:PRK12316 2299 -AVVTPLLwkcRPQDPCGaayvpIGRAL--------------GNRRAYIL---DADLNLLAPGM---AGELYLGGEGLAR 2357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 443 EYWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRtsVD-IIKNGGFKISALEVERQLLAHPHITDVAVI 513
Cdd:PRK12316 2358 GYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVREAVVV 2435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 514 GpPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12316 2436 A-QDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
111-582 |
7.68e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 143.69 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 111 NDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIA----AEEYVGKISPSAEKLGVPVLP--------LG 178
Cdd:PRK12406 45 NDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhadlLHGLASALPAGVTVLSVPTPPeiaaayriSP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 179 SHSSGSAGHTAVEDVpLASSASW-----KDRGAMIiYTSGTTGRPKGV---LSTHENVQAVTTGLVEKWEWKKEDVILHV 250
Cdd:PRK12406 125 ALLTPPAGAIDWEGW-LAQQEPYdgppvPQPQSMI-YTSGTTGHPKGVrraAPTPEQAAAAEQMRALIYGLKPGIRALLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 251 LPLHH----VHGvinklLCPLWVGATCIMLPEFSAQmvwkKFLSS-QAPRVSVFMAVPTIYAKLIEYYDEhfsqpqvqdf 325
Cdd:PRK12406 203 GPLYHsapnAYG-----LRAGRLGGVLVLQPRFDPE----ELLQLiERHRITHMHMVPTMFIRLLKLPEE---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 326 VRA-FCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIG-MALSNPLHGVRVPGSVGTPLPGVEVRIAteavk 403
Cdd:PRK12406 264 VRAkYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGaVTFATSEDALSHPGTVGKAAPGAELRFV----- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 404 gggrsytilaqgDEDGTQMTPGlegQEGELLVR--GSSVFrEYWNRPkETREAFTSDGWFRTGDTAAYH-DGVYWIKGRT 480
Cdd:PRK12406 339 ------------DEDGRPLPQG---EIGEIYSRiaGNPDF-TYHNKP-EKRAEIDRGGFITSGDVGYLDaDGYLFLCDRK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 481 SvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIV 560
Cdd:PRK12406 402 R-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEI 480
|
490 500
....*....|....*....|..
gi 1201832555 561 VEEIPRNQMGKVNKKELLQRFY 582
Cdd:PRK12406 481 MAELPREDSGKIFKRRLRDPYW 502
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
61-572 |
1.34e-36 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 144.31 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAII---DQNGEH---TYRELFcrslrlsQEICR---VLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGI 128
Cdd:TIGR02188 71 PDKVAIIwegDEPGEVrkiTYRELH-------REVCRfanVL----KSLgvkKGDRVAIYMPMIPEAAIAMLACARIGAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 129 avplyrkHPV-------QQLEYVIEDSQSALVIAAEEYV--GKISP--------------SAEK------LGVPVLPLgS 179
Cdd:TIGR02188 140 -------HSVvfggfsaEALADRINDAGAKLVITADEGLrgGKVIPlkaivdealekcpvSVEHvlvvrrTGNPVVPW-V 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 180 HSSGSAGHTAVEDVPLASSASWKDRGAM--IIYTSGTTGRPKGVLSTHE--NVQAVTTGlveKW--EWKKEDVILHVLPL 253
Cdd:TIGR02188 212 EGRDVWWHDLMAKASAYCEPEPMDSEDPlfILYTSGSTGKPKGVLHTTGgyLLYAAMTM---KYvfDIKDGDIFWCTADV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 254 HHVHGVINKLLCPLWVGATCIML------PEFS--AQMVWKKflssqapRVSVFMAVPTIYAKLIEYYDEHfsqpqvqdf 325
Cdd:TIGR02188 289 GWITGHSYIVYGPLANGATTVMFegvptyPDPGrfWEIIEKH-------KVTIFYTAPTAIRALMRLGDEW--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 326 VRAFCQENIRLMvsGSAALPV-PVLKKW--KAITGH--TLLERYGMTEIGMALSNPLHGV--RVPGSVGTPLPGVEVRIA 398
Cdd:TIGR02188 353 VKKHDLSSLRLL--GSVGEPInPEAWMWyyKVVGKErcPIVDTWWQTETGGIMITPLPGAtpTKPGSATLPFFGIEPAVV 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 399 teavkgggrsytilaqgDEDGTQMTPglEGQEGELLVRGS--SVFREYWNRPKETREAFTSD--GWFRTGDTAAY-HDGV 473
Cdd:TIGR02188 431 -----------------DEEGNPVEG--PGEGGYLVIKQPwpGMLRTIYGDHERFVDTYFSPfpGYYFTGDGARRdKDGY 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 474 YWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMA 550
Cdd:TIGR02188 492 IWITGRVD-DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDdelRKELRKHVRKEIG 570
|
570 580
....*....|....*....|..
gi 1201832555 551 PYAVPTELIVVEEIPRNQMGKV 572
Cdd:TIGR02188 571 PIAKPDKIRFVPGLPKTRSGKI 592
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
74-581 |
2.17e-35 |
|
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: 140.11 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSqeicRVLQcSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPL-------YRKHPVQQLEYVIE 146
Cdd:cd05906 41 SYQDLLEDARRLA----AGLR-QLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 147 DSQSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAgHTAVEDVPLASSaswkDRGAMIIYTSGTTGRPKGVLSTHE 226
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLD-TAADHDLPQSRP----DDLALLMLTSGSTGFPKAVPLTHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 227 NVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP--EFSAQ-MVWKKFLssQAPRVSVFMAVP 303
Cdd:cd05906 191 NILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPteEILADpLRWLDLI--DRYRVTITWAPN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 304 TIYAKLIEYYDEhfSQPQVQDFvrafcqENIRLMVSGSAALPVPVLKKWKaitghTLLERY-----------GMTEI--G 370
Cdd:cd05906 269 FAFALLNDLLEE--IEDGTWDL------SSLRYLVNAGEAVVAKTIRRLL-----RLLEPYglppdairpafGMTETcsG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 MALSNPLHGVRVPG-----SVGTPLPGVEVRIAteavkgggrsytilaqgDEDGtQMTPglEGQEGELLVRGSSVFREYW 445
Cdd:cd05906 336 VIYSRSFPTYDHSQalefvSLGRPIPGVSMRIV-----------------DDEG-QLLP--EGEVGRLQVRGPVVTKGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 446 NRPKETREAFTSDGWFRTGDTAAYHDGVYWIKGRTSVDIIKNgGFKISALEVERQL-----------LAHPH-----ITD 509
Cdd:cd05906 396 NNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVN-GVNYYSHEIEAAVeevpgvepsftAAFAVrdpgaETE 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 510 VAVI--GPPDVVWGQRVSAVVQLRRGEMLSVkelkewardTMAP-YAVPTELivvEEIPRNQMGKVNKKELLQRF 581
Cdd:cd05906 475 ELAIffVPEYDLQDALSETLRAIRSVVSREV---------GVSPaYLIPLPK---EEIPKTSLGKIQRSKLKAAF 537
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
56-579 |
5.23e-35 |
|
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: 137.06 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICRVLQCSSrdlkeERISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPG-----DVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTT 215
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTT-------------------------------DSPDDL------------AYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTHENvqavttglvekwewkkedvILHVLP-----LHHVHGVINKLLCPL------WVGATCIMlpeFSAQMV 284
Cdd:cd17653 118 GIPKGVMVPHRG-------------------VLNYVSqpparLDVGPGSRVAQVLSIafdaciGEIFSTLC---NGGTLV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 WK---KFLSSQAPRVSVFMAVPTIYAKLieyydehfsqpQVQDFvrafcqENIRLMVSGSAALPVPVLKKWKAitGHTLL 361
Cdd:cd17653 176 LAdpsDPFAHVARTVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLY 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 362 ERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTqmtPGLEGQEGELLVRGSSVF 441
Cdd:cd17653 237 NAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYIL-----------------DADLQ---PVPEGVVGEICISGVQVA 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 442 REYWNRPKETREAFTSDGW------FRTGDTAAY-HDGVYWIKGRTSVDIiKNGGFKISALEVERQLLA-HPHITDVAVI 513
Cdd:cd17653 297 RGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAI 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 514 gppdVVWGQRVSAVVQlrrgEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:cd17653 376 ----VVNGRLVAFVTP----ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
74-465 |
5.45e-35 |
|
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: 138.89 E-value: 5.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEICRVLQCSSrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALV 153
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPA---PASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 IAAEeyvgkispsaeklGVPV------LPLGSHssgsaghtAVEDVPLASsaswKDRGAMIIYTSGTTGRPKGVLSTHEN 227
Cdd:cd05927 84 FCDA-------------GVKVysleefEKLGKK--------NKVPPPPPK----PEDLATICYTSGTTGNPKGVMLTHGN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 228 VQAVTTGLVEKWE----WKKEDVILHVLPLHHV--HGVINKLLCplwVGAtCImlpefsaqmvwkKFLSS---------Q 292
Cdd:cd05927 139 IVSNVAGVFKILEilnkINPTDVYISYLPLAHIfeRVVEALFLY---HGA-KI------------GFYSGdirlllddiK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 293 APRVSVFMAVPTIYAKLieyYDEHFSQPQVQDFVRAFC-------------------------------QE----NIRLM 337
Cdd:cd05927 203 ALKPTVFPGVPRVLNRI---YDKIFNKVQAKGPLKRKLfnfalnyklaelrsgvvraspfwdklvfnkiKQalggNVRLM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 338 VSGSAALPVPVLKKWKAITGHTLLERYGMTEI--GMALSNPlhGVRVPGSVGTPLPGVEVRIateavkgggrsytilaqg 415
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKL------------------ 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 416 dEDGTQM--TPGLEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGD 465
Cdd:cd05927 340 -VDVPEMnyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
62-579 |
1.19e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 137.95 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEICRVLQCssrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK06164 25 DAVALIDEDRPLSRAELRALVDRLAAWLAAQGVR-----RGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVG--------KISPSAEK-------------------LGVPVLPLGSHssGSAGHTAvedvp 194
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGidfaailaAVPPDALPplraiavvddaadatpapaPGARVQLFALP--DPAPPAA----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 195 LASSASWKDRGAMIIYTSGTTGRPKGV------LSTHENVQAVTTGLvekwewKKEDVILHVLPLHHVHGvINKLLCPLW 268
Cdd:PRK06164 173 AGERAADPDAGALLFTTSGTTSGPKLVlhrqatLLRHARAIARAYGY------DPGAVLLAALPFCGVFG-FSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 269 VGATCIMLPEFSAQMVWKKFLSSqapRVSVFMAVPTIYAKLieyydeHFSQPQVQDFVRAfcqeniRLMVSGSAALPVPV 348
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRH---RVTHTFGNDEMLRRI------LDTAGERADFPSA------RLFGFASFAPALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 349 LKKWKAITGHTLLERYGMTEI-----GMALSNPLHGVRVPGsvGTPL-PGVEVRIAteavkgggrsytilaqgDEDGTQM 422
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEVqalvaLQPATDPVSVRIEGG--GRPAsPEARVRAR-----------------DPQDGAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 423 TPglEGQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTA-AYHDGVYWIKGRTSvDIIKNGGFKISALEVERQL 501
Cdd:PRK06164 372 LP--DGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGyTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 502 LAHPHITDVAVIGPpdVVWGQ-RVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMG---KVNKKEL 577
Cdd:PRK06164 449 EALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
..
gi 1201832555 578 LQ 579
Cdd:PRK06164 527 RE 528
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
210-577 |
3.27e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 137.07 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvinkllcplWV--------GATCIMLPEFSA 281
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwgtaarGGTSVCMRHVTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 QMVWKKFlssQAPRVSVFMAVPTIYAKLIE--YYDEHFSQPQVQdfvrafcqenirlMVSGSAALPVPVLKKWKAItGHT 359
Cdd:PLN03102 264 PEIYKNI---EMHNVTHMCCVPTVFNILLKgnSLDLSPRSGPVH-------------VLTGGSPPPAALVKKVQRL-GFQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 360 LLERYGMTE-IGMAL---------SNPLH---------GVRVPGsvgtpLPGVEVRiATEAVKGGGRsytilaqgdeDGT 420
Cdd:PLN03102 327 VMHAYGLTEaTGPVLfcewqdewnRLPENqqmelkarqGVSILG-----LADVDVK-NKETQESVPR----------DGK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 421 QMtpglegqeGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVER 499
Cdd:PLN03102 391 TM--------GEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDR-SKDIIISGGENISSVEVEN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 500 QLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGE----------MLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQM 569
Cdd:PLN03102 461 VLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGEttkedrvdklVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGN 540
|
....*...
gi 1201832555 570 GKVNKKEL 577
Cdd:PLN03102 541 GKILKPKL 548
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-581 |
1.89e-33 |
|
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: 132.64 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKIspsaeklgvpvlplgshss 182
Cdd:cd05973 26 DVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAANRHKL------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 183 gsaghtavEDVPLassaswkdrgaMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINK 262
Cdd:cd05973 87 --------DSDPF-----------VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 LLCPLWVGATCIMLP-EFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQVqdfvrafcqeniRLMVSGS 341
Cdd:cd05973 148 ITGPLALGHPTILLEgGFSVESTWRVI---ERLGVTNLAGSPTAYRLLMAAGAEVPARPKG------------RLRRVSS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 342 AALPV-PVLKKW-KAITGHTLLERYGMTEIGMALSN---PLHGVRVpGSVGTPLPGVEVriateavkgggrsyTILaqgD 416
Cdd:cd05973 213 AGEPLtPEVIRWfDAALGVPIHDHYGQTELGMVLANhhaLEHPVHA-GSAGRAMPGWRV--------------AVL---D 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 417 EDGTQMTPGLEGQEGeLLVRGSSV--FREYWNRPKETreafTSDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKIS 493
Cdd:cd05973 275 DDGDELGPGEPGRLA-IDIANSPLmwFRGYQLPDTPA----IDGGYYLTGDTVEFDpDGSFSFIGRAD-DVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 494 ALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQMG 570
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
490
....*....|.
gi 1201832555 571 KVnkkellQRF 581
Cdd:cd05973 429 KI------QRF 433
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
74-581 |
3.28e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 133.72 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEICRvlqcssRDLKE-ERISFLCPNDASYVVAqWASWMsgGIAVPLY----RKHPvQQLEYVIEDS 148
Cdd:PRK06018 41 TYAQIHDRALKVSQALDR------DGIKLgDRVATIAWNTWRHLEA-WYGIM--GIGAICHtvnpRLFP-EQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 149 QSALVIAAEEYVGKISPSAEKL----GVPVLPLGSHSSGSAGHTAV--EDVPLASSAS--WKD----RGAMIIYTSGTTG 216
Cdd:PRK06018 111 EDRVVITDLTFVPILEKIADKLpsveRYVVLTDAAHMPQTTLKNAVayEEWIAEADGDfaWKTfdenTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 217 RPKGVLSTHE-NV-QAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLwVGATCIMlPefSAQM----VWKkFLS 290
Cdd:PRK06018 191 DPKGVLYSHRsNVlHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVM-P--GAKLdgasVYE-LLD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 291 SQapRVSVFMAVPTIYAKLIEYYDEHFSQ-PqvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAItGHTLLERYGMTEI 369
Cdd:PRK06018 266 TE--KVTFTAGVPTVWLMLLQYMEKEGLKlP------------HLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 370 gmalsNPLhgvrvpGSVGTPLPGVEvriateAVKGGGRSYTILAQG-----------DEDGTQMTpgLEGQE-GELLVRG 437
Cdd:PRK06018 331 -----SPL------GTLAALKPPFS------KLPGDARLDVLQKQGyppfgvemkitDDAGKELP--WDGKTfGRLKVRG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 438 SSVFREYWnrpKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPP 516
Cdd:PRK06018 392 PAVAAAYY---RVDGEILDDDGFFDTGDVATIdAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 517 DVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK06018 468 HPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
126-577 |
4.69e-33 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 133.21 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 126 GGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEyvGKISPSAEKLGVPVLPLGSHSSGS----AGHTAVEDVPLASSASW 201
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFCQITDPAAALVAPG--SKMASSAVPEALHSIPVIAVDIAAvtreSEHSLDAASLAGNADQG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 202 KDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEK---W-EWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCIMLP 277
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnWvTWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 EFSAQMvwKKFLSSQAprVSVFMAVPTIYAKLIeyYDEHFSQPQVqdfvrafcqENIRLMV-SGSAALPVPVlkKWKAIT 356
Cdd:PRK05857 247 ENTTSL--LEILTTNA--VATTCLVPTLLSKLV--SELKSANATV---------PSLRLVGyGGSRAIAADV--RFIEAT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 357 GHTLLERYGMTEIG-MALSNPLHGVRVP----GSVGTPLPGVEVRIATEavkGGGrsytilaqgdeDGTQMTPGLEGQEG 431
Cdd:PRK05857 310 GVRTAQVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAAT---DGI-----------GPTAPGAGPSASFG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 432 ELLVRGSSVFREYWNRPKETREAFTsDGWFRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDV 510
Cdd:PRK05857 376 TLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREA 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 511 AVIGPPDVVWGQRVS-AVVQLRRGEMLSVKELKE-----WARDTMApYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK05857 454 ACYEIPDEEFGALVGlAVVASAELDESAARALKHtiaarFRRESEP-MARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
202-581 |
9.19e-33 |
|
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: 131.95 E-value: 9.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 202 KDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEK-WEWKKE-DVILHVLPLHHVHGVINKLLCPLWVGATC------ 273
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvPELLGPdDRYLAYLPLAHIFELAAENVCLYRGGTIGygsprt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 274 ----IM------LPEFsaqmvwKKFLSSQAPRV--SVFMAV-------PTI--------YAKLIEYYDEHFSQPQVQDFV 326
Cdd:cd17639 167 ltdkSKrgckgdLTEF------KPTLMVGVPAIwdTIRKGVlaklnpmGGLkrtlfwtaYQSKLKALKEGPGTPLLDELV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 327 ----RAFCQENIRLMVSGSAALPvPVLKKWKAITGHTLLERYGMTEI--GMALSNPLHgvRVPGSVGTPLPGVEVRIATe 400
Cdd:cd17639 241 fkkvRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDPGD--LETGRVGPPLPCCEIKLVD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 401 aVKGGGRSYtilaqgDEDGTQmtpglegqeGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGR 479
Cdd:cd17639 317 -WEEGGYST------DKPPPR---------GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHpDGTLKIIDR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 480 TSvDIIKNGGFKISALE-VERQLLAHPHITDVAVIGPPDVVwgqRVSAVVqlrrgeMLSVKELKEWARDTMAPYAVPTEL 558
Cdd:cd17639 381 KK-DLVKLQNGEYIALEkLESIYRSNPLVNNICVYADPDKS---YPVAIV------VPNEKHLTKLAEKHGVINSEWEEL 450
|
410 420
....*....|....*....|....*.
gi 1201832555 559 I---VVEEIPRNQMGKVNKKELLQRF 581
Cdd:cd17639 451 CedkKLQKAVLKSLAETARAAGLEKF 476
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
171-577 |
1.84e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 131.34 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 171 GVPVLPLGS--HSSGSAGHTAVEdvPLASSASWKDRgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVIL 248
Cdd:PRK07867 121 GVRVINVDSpaWADELAAHRDAE--PPFRVADPDDL-FMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 249 HVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQmvwkKFLssqaPRVSVFMAVPTIY-AKLIEYYdehFSQPQVQDFvr 327
Cdd:PRK07867 198 VSMPLFHSNAVMAGWAVALAAGASIALRRKFSAS----GFL----PDVRRYGATYANYvGKPLSYV---LATPERPDD-- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 328 afcQENIRLMVSGSAALPVPVlKKWKAITGHTLLERYGMTEIGMALS----NPlhgvrvPGSVGTPLPGVEVR-IATEAV 402
Cdd:PRK07867 265 ---ADNPLRIVYGNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAITrtpdTP------PGALGPLPPGVAIVdPDTGTE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 403 KGGGRsytILAQGDEDGTQMTpglegqeGELL-VRGSSVFREYWNRPKETREAFtSDGWFRTGDTAaYHD--GVYWIKGR 479
Cdd:PRK07867 335 CPPAE---DADGRLLNADEAI-------GELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLA-YRDadGYAYFAGR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 480 TSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEW--ARDTMAPYAVPTE 557
Cdd:PRK07867 403 LG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSY 481
|
410 420
....*....|....*....|
gi 1201832555 558 LIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK07867 482 VRVCAELPRTATFKVLKRQL 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-584 |
2.05e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.93 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICrvlqcsSRDLKEE-RISFLCPNDASYVVAQWASWMSGGIAVPLYR 134
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALI------ARGVGPEvLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHPVQQLEYVIEDSQSALVIAAEEYVGKIsPSAEKLGVPVLPLGSHSSGSAGHTAveDVPLASsaswkDRGAMIIYTSGT 214
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLLTQSHLLQRL-PIPDGLASLALDRDEDWEGFPAHDP--AVRLHP-----DNLAYVIYTSGS 4705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIM------LPEFSAQMVWKKf 288
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLYAEIHEH- 4783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 lssqapRVSVFMAVPTIYaklieyydehfsQPQVQDFVRAFCQENIRLMVSGSAALPVPVLKK-WKAITGHTLLERYGMT 367
Cdd:PRK12316 4784 ------RVTVLVFPPVYL------------QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPT 4845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 368 EigmALSNPLH----GVRVPGSVGTPLPGVEvriateavkgGGRSYTILaqgdeDGtQMTPGLEGQEGELLVRGSSVFRE 443
Cdd:PRK12316 4846 E---TTVTVLLwkarDGDACGAAYMPIGTPL----------GNRSGYVL-----DG-QLNPLPVGVAGELYLGGEGVARG 4906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRtsVD-IIKNGGFKISALEVERQLLAHPHITDVAVIG 514
Cdd:PRK12316 4907 YLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVIA 4984
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 515 PPDVVWGQRVSAVV---------QLRRGEMlsVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL-------L 578
Cdd:PRK12316 4985 QEGAVGKQLVGYVVpqdpaladaDEAQAEL--RDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALpqpdaslL 5062
|
....*.
gi 1201832555 579 QRFYPA 584
Cdd:PRK12316 5063 QQAYVA 5068
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
61-572 |
2.85e-32 |
|
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: 131.53 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAII------DQNGEHTYRELFcrslrlsQEICR---VLqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGI 128
Cdd:cd05966 67 GDKVAIIwegdepDQSRTITYRELL-------REVCRfanVL----KSLgvkKGDRVAIYMPMIPELVIAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 129 avplyrkHPV-------QQLEYVIEDSQSALVIAAEEYV--GKI-------------SPSAEKlgVPVLP-LGSHSSGSA 185
Cdd:cd05966 136 -------HSVvfagfsaESLADRINDAQCKLVITADGGYrgGKViplkeivdealekCPSVEK--VLVVKrTGGEVPMTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 186 G-----HTAVEDVPLASSASWKDRGAM--IIYTSGTTGRPKGVLSTHE--NVQAVTTGlveKW--EWKKEDV-------- 246
Cdd:cd05966 207 GrdlwwHDLMAKQSPECEPEWMDSEDPlfILYTSGSTGKPKGVVHTTGgyLLYAATTF---KYvfDYHPDDIywctadig 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 247 -------IlhvlplhhVHGvinkllcPLWVGATCIML------PEFSA--QMVWKKflssqapRVSVFMAVPTIYAKLIE 311
Cdd:cd05966 284 witghsyI--------VYG-------PLANGATTVMFegtptyPDPGRywDIVEKH-------KVTIFYTAPTAIRALMK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 312 YYDEHfsqpqvqdfVRAFCQENIRLMvsGSAALPV-PVLKKW--KAItGH---TLLERYGMTEIGMALSNPLHGVR--VP 383
Cdd:cd05966 342 FGDEW---------VKKHDLSSLRVL--GSVGEPInPEAWMWyyEVI-GKercPIVDTWWQTETGGIMITPLPGATplKP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 384 GSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAFTSD--G 459
Cdd:cd05966 410 GSATRPFFGIEPAIL-----------------DEEGNEVEGE---VEGYLVIKRPwpGMARTIYGDHERYEDTYFSKfpG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 460 WFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS- 537
Cdd:cd05966 470 YYFTGDGARRdEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSd 548
|
570 580 590
....*....|....*....|....*....|....*..
gi 1201832555 538 --VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKV 572
Cdd:cd05966 549 elRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
55-577 |
2.91e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 130.51 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 55 TRALTFGDKIAII-DQNGEH-TYRELFCRSLRLSqeicRVLQCSSrdLKE-ERISFLCPNDASYVVAQWASWMSGGIAVP 131
Cdd:PRK13390 5 THAQIAPDRPAVIvAETGEQvSYRQLDDDSAALA----RVLYDAG--LRTgDVVALLSDNSPEALVVLWAALRSGLYITA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 132 LYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISpsaeKLGVPV---LPLGSHSSGSAGHTAV---EDVPLASSASwkdrG 205
Cdd:PRK13390 79 INHHLTAPEADYIVGDSGARVLVASAALDGLAA----KVGADLplrLSFGGEIDGFGSFEAAlagAGPRLTEQPC----G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKG---------VLSTHENVQAVTTGLvekWEWKKEDVILHVLPLHHVhgvinkllCPL-W------V 269
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIYHA--------APLrWcsmvhaL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 270 GATCIMLPEFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQVqdfvrafcqENIRLMVSGSAALPVPVL 349
Cdd:PRK13390 220 GGTVVLAKRFDAQATLGHV---ERYRITVTQMVPTMFVRLLKLDADVRTRYDV---------SSLRAVIHAAAPCPVDVK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 350 KKWKAITGHTLLERYGMTEI-GMALSNPLHGVRVPGSVGTPLPGVevriateavkgggrsytiLAQGDEDGTQMTPGLEG 428
Cdd:PRK13390 288 HAMIDWLGPIVYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLGD------------------LHICDDDGNELPAGRIG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEgeLLVRGSSVFReYWNRPKETREAF--TSDGWFRTGDTAAY-HDGVYWIKGRTSVDIIkNGGFKISALEVERQLLAHP 505
Cdd:PRK13390 350 TV--YFERDRLPFR-YLNDPEKTAAAQhpAHPFWTTVGDLGSVdEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHP 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 506 HITDVAVIGPPDVVWGQRVSAVVQLRRG----EMLSvKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK13390 426 AVHDVAVIGVPDPEMGEQVKAVIQLVEGirgsDELA-RELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
57-584 |
3.09e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.36 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKiaiidqngEHTYRELFCRSLRLSQEICrvlqcsSRDLKEE-RISFLCPNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:PRK12467 1592 ALVFGEQ--------ELTYGELNRRANRLAHRLI------ALGVGPEvLVGIAVERSLEMVVGLLAILKAGGAYVPLDPE 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAAEEYVGKIsPSAEklGVPVLPLGSHSSGSAGHTaveDVPLASSASwKDRGAMIIYTSGTT 215
Cdd:PRK12467 1658 YPRERLAYMIEDSGIELLLTQSHLQARL-PLPD--GLRSLVLDQEDDWLEGYS---DSNPAVNLA-PQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPlHHVHGVINKLLCPLWVGATCIMLPeFSAQMVWKKFLSS-QAP 294
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQLIQLiERQ 1808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 295 RVSVFMAVPTIYAKLIEyYDEHFSQPQvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHT-LLERYGMTEIGM-- 371
Cdd:PRK12467 1809 QVTTLHFVPSMLQQLLQ-MDEQVEHPL-----------SLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVdv 1876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 -----ALSNPLHGVRVPgsVGTPLPgvevriateavkggGRSYTILaqgDEdgtQMTPGLEGQEGELLVRGSSVFREYWN 446
Cdd:PRK12467 1877 thwtcRRKDLEGRDSVP--IGQPIA--------------NLSTYIL---DA---SLNPVPIGVAGELYLGGVGLARGYLN 1934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 447 RPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRtsVD-IIKNGGFKISALEVERQLLAHPHITDVAVIgPPD 517
Cdd:PRK12467 1935 RPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQGGVREAVVI-AQD 2011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 518 VVWGQRVSAVVQLRRGEML--------SVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL-------LQRFY 582
Cdd:PRK12467 2012 GANGKQLVAYVVPTDPGLVdddeaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALpapdaseLQQAY 2091
|
..
gi 1201832555 583 PA 584
Cdd:PRK12467 2092 VA 2093
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
206-581 |
7.04e-32 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 129.90 E-value: 7.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENV--QAVTTGLVEKWEWKKEDVILHVLPLHHV--HGVinkllcPL--WVGATCIMLP-- 277
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLylQSLSLRTTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 EFSAQMVwKKFLSSQAPRVSvfMAVPTIYAKLIEYYDEHfsQPQvqdfvRAFCQEnirLMVSGSAALPVpVLKKWKAITG 357
Cdd:PRK05620 258 DLSAPTL-AKIIATAMPRVA--HGVPTLWIQLMVHYLKN--PPE-----RMSLQE---IYVGGSAVPPI-LIKAWEERYG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 358 HTLLERYGMTEIGMAlsnplhgvrvpGSVGTPLPGV--EVRIATEAVKG---GGRSYTILaqgdEDGTQMTpGLEGQEGE 432
Cdd:PRK05620 324 VDVVHVWGMTETSPV-----------GTVARPPSGVsgEARWAYRVSQGrfpASLEYRIV----NDGQVME-STDRNEGE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 433 LLVRGSSVFREYWNRPKET----------------REAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISAL 495
Cdd:PRK05620 388 IQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVtRDGFLTIHDRAR-DVIRSGGEWIYSA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 496 EVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRG---EMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKV 572
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*....
gi 1201832555 573 NKKELLQRF 581
Cdd:PRK05620 547 DKKDLRQHL 555
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
62-577 |
7.27e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 128.35 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLKEERISFLCPNDASY-VVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLA----RTLR--GLGVAPGSVVGVCADRSLDaIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTTGRPKG 220
Cdd:cd17650 76 LQYMLEDSGAKLLL---------------------------------TQPEDL------------AYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPE---FSAQMVWKKFLSSqapRVS 297
Cdd:cd17650 111 VMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDevkLDPAALYDLILKS---RIT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 298 VFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafcqENIRLMVSGSAALPVpvlkKWKAitghTLLER----------YGMT 367
Cdd:cd17650 188 LMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDFK----TLAARfgqgmriinsYGVT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 368 EIGMALS------NPLHGVR-VPgsVGTPLPGVEVRIATEavkgggrsytilaqgdedgtQMTPGLEGQEGELLVRGSSV 440
Cdd:cd17650 249 EATIDSTyyeegrDPLGDSAnVP--IGRPLPNTAMYVLDE--------------------RLQPQPVGVAGELYIGGAGV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 441 FREYWNRPKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVI 513
Cdd:cd17650 307 ARGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVA 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 514 GPPDVvwGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17650 386 VREDK--GGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
62-577 |
9.33e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.82 E-value: 9.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQeicrVLQCSSRdLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAH----VLIAAGV-GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAeklGVPVLPL---GSHSSGSAGHTAveDVPLASsaswkDRGAMIIYTSGTTGRP 218
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQLPVPA---GLRSLCLdepADLLCGYSGHNP--EVALDP-----DNLAYVIYTSGSTGQP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 219 KGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVInKLLCPLWVGATCIMLP--------EFSAQMVwkkfls 290
Cdd:PRK12467 672 KGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT-ELFGALASGATLHLLPpdcardaeAFAALMA------ 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 291 sqAPRVSVFMAVPTIYAKLIeyydehfsqpqvQDFVRAFCQENIRLMVSGSaALPVPVLKKWKAIT-GHTLLERYGMTEI 369
Cdd:PRK12467 745 --DQGVTVLKIVPSHLQALL------------QASRVALPRPQRALVCGGE-ALQVDLLARVRALGpGARLINHYGPTET 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 370 GMALS------NPLHGVRVPgsVGTPLPGVEVRIAteavkgggrsytilaqgdeDGtQMTPGLEGQEGELLVRGSSVFRE 443
Cdd:PRK12467 810 TVGVStyelsdEERDFGNVP--IGQPLANLGLYIL-------------------DH-YLNPVPVGVVGELYIGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGP 515
Cdd:PRK12467 868 YHRRPALTAERFVPDPFgadggrlYRTGDLARYRaDGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 516 PDVVWGQRVSAVVQLRRGE----MLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12467 947 PGDAGLQLVAYLVPAAVADgaehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
48-581 |
1.41e-31 |
|
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: 128.04 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 48 HHVtpVFTRALTFGDKIAIIDQNGEHTYRELFCRSLRLSQEICrvlqcsSRDLKEERISFLCPnDAS--YVVAQWASWMS 125
Cdd:cd05918 2 HDL--IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLR------SLGVGPGVFVPLCF-EKSkwAVVAMLAVLKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 126 GGIAVPLYRKHPVQQLEYVIEDSQSALVIAaeeyvgkispsaeklgvpvlplgsHSSGSAghtavedvplassaswkdrg 205
Cdd:cd05918 73 GGAFVPLDPSHPLQRLQEILQDTGAKVVLT------------------------SSPSDA-------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHenvQAVTTGlvekwewkkedvILHVLPLHHVHGV--------------INKLLCPLWVGA 271
Cdd:cd05918 109 AYVIFTSGSTGKPKGVVIEH---RALSTS------------ALAHGRALGLTSEsrvlqfasytfdvsILEIFTTLAAGG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 272 T-CIM--------LPEFSAQMvwkkflssqapRVSVFMAVPTIyAKLIeyydehfsQPQvqDFVrafcqeNIRLMVSGSA 342
Cdd:cd05918 174 ClCIPseedrlndLAGFINRL-----------RVTWAFLTPSV-ARLL--------DPE--DVP------SLRTLVLGGE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 343 ALPVPVLKKWkaITGHTLLERYGMTE--IGMALSNPLHGVRvPGSVGTPLpgvevriateavkgGGRSYtILAQGDEDgt 420
Cdd:cd05918 226 ALTQSDVDTW--ADRVRLINAYGPAEctIAATVSPVVPSTD-PRNIGRPL--------------GATCW-VVDPDNHD-- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 421 QMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTSD-GW------------FRTGDTAAY-HDG-VYWIkGRTSvDII 485
Cdd:cd05918 286 RLVP--IGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYnPDGsLEYV-GRKD-TQV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 486 KNGGFKISALEVERQLLAHPHITD---VAVIGPPDVVWGQRVSAVVQLRRGEMLS-----------------VKELKEWA 545
Cdd:cd05918 362 KIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralVAELRSKL 441
|
570 580 590
....*....|....*....|....*....|....*.
gi 1201832555 546 RDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:cd05918 442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
63-575 |
1.46e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 130.81 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 63 KIAIIDQNG-EHTYRELFCRSLRLSQEICRVLQcssrdlKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:PRK08633 631 RLAVADSTGgELSYGKALTGALALARLLKRELK------DEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAAL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLP-------LGSHSSGSAGHTAVEDVPLASSASWK---------DRG 205
Cdd:PRK08633 705 KSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVkviyledLKAKISKVDKLTALLAARLLPARLLKrlygptfkpDDT 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP-----EFS 280
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdptdaLGI 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 281 AQMVWKKflssqapRVSVFMAVPT---IYAKLIEYYDEHFsqpqvqdfvrafcqENIRLMVSGSAALPVPVLKKWKAITG 357
Cdd:PRK08633 865 AKLVAKH-------RATILLGTPTflrLYLRNKKLHPLMF--------------ASLRLVVAGAEKLKPEVADAFEEKFG 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 358 HTLLERYGMTE-----------IGMALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgdeDGTQMTPGL 426
Cdd:PRK08633 924 IRILEGYGATEtspvasvnlpdVLAADFKRQTGSK-EGSVGMPLPGVAVRIV-------------------DPETFEELP 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 EGQEGELLVRGSSVFREYWNRPKETREAFT---SDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLL 502
Cdd:PRK08633 984 PGEDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLdEDGFLTITDRYS-RFAKIGGEMVPLGAVEEELA 1062
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 503 A--HPHITDVAVIGPPDVVWGQRVsaVVQLRRGEMlSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNKK 575
Cdd:PRK08633 1063 KalGGEEVVFAVTAVPDEKKGEKL--VVLHTCGAE-DVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
53-580 |
2.89e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.79 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 53 VFTRALTFGDKIAIID--QNGEHTYRELFCRSLRLSQEIcrvlqcSSRDLKEERISFLC-PNDASYVVAQWASWMSGGIA 129
Cdd:PLN02330 34 VLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKAL------RSLGLRKGQVVVVVlPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 130 VPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKIspsaEKLGVPVLPLGSHSSGSA-------------GHTAVEDVPLA 196
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDTNYGKV----KGLGLPVIVLGEEKIEGAvnwkelleaadraGDTSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 197 SsaswkDRGAMIiYTSGTTGRPKGVLSTHENVQA--VTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCI 274
Cdd:PLN02330 184 T-----DLCALP-FSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 275 MLPEFSAQMVWKKFLSSQaprVSVFMAVPTIYAKLIEyydehfsQPQVQDFvrAFCQENIRLMVSGSAALPVPVLKKWKA 354
Cdd:PLN02330 258 VMSRFELRTFLNALITQE---VSFAPIVPPIILNLVK-------NPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 355 -ITGHTLLERYGMTE---IGMALSNPL--HGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglEG 428
Cdd:PLN02330 326 kFPGVQVQEAYGLTEhscITLTHGDPEkgHGIAKKNSVGFILPNLEVKFI-----------------DPDTGRSLP--KN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHI 507
Cdd:PLN02330 387 TPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIdDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 508 TDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQR 580
Cdd:PLN02330 466 EDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
61-572 |
8.22e-31 |
|
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: 126.92 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAIIDQNGE------HTYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVP 131
Cdd:cd17634 67 GDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTL--------LDLgvkKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 132 LYRKHPVQQLEYVIEDSQSALVIAAEEYV--GKISP----SAEKLGVPVLPL---------GSHSSGSAG-----HTAVE 191
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLITADGGVraGRSVPlkknVDDALNPNVTSVehvivlkrtGSDIDWQEGrdlwwRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 192 DVPLASSASWKDRG--AMIIYTSGTTGRPKGVLSTHEN-VQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLW 268
Cdd:cd17634 219 KASPEHQPEAMNAEdpLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 269 VGATCIML--------PEFSAQMVWKKflssqapRVSVFMAVPTIYAKLieyydehfsQPQVQDFVRAFCQENIRLMVS- 339
Cdd:cd17634 299 CGATTLLYegvpnwptPARMWQVVDKH-------GVNILYTAPTAIRAL---------MAAGDDAIEGTDRSSLRILGSv 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 340 GSAALPVPVLKKWKAITGH--TLLERYGMTEIGMALSNPLHGVR--VPGSVGTPLPGVEVRIAteavkgggrsytilaqg 415
Cdd:cd17634 363 GEPINPEAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVV----------------- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 416 DEDGtQMTPGleGQEGELLVRGS--SVFREYWNRPKETREAF--TSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGF 490
Cdd:cd17634 426 DNEG-HPQPG--GTEGNLVITDPwpGQTRTLFGDHERFEQTYfsTFKGMYFSGDGARRdEDGYYWITGR-SDDVINVAGH 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 491 KISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRN 567
Cdd:cd17634 502 RLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKT 581
|
....*
gi 1201832555 568 QMGKV 572
Cdd:cd17634 582 RSGKI 586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-577 |
3.47e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.00 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 116 VVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAGHTAVEDVpl 195
Cdd:PRK12316 3121 VVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENL-- 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 196 assaswkdrgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIM 275
Cdd:PRK12316 3199 ----------AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVL 3267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 276 LPEFSAQMVWKKFLSSQAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDFVrafcqeNIRLMVSGSAALPVPVLKKWKAi 355
Cdd:PRK12316 3268 AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE-------EEDAHRCT------SLKRIVCGGEALPADLQQQVFA- 3333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 356 tGHTLLERYGMTEigmALSNPLHGVRVPGSVGTPLPGVEVriateavkgGGRSYTILAQGdedgtqMTPGLEGQEGELLV 435
Cdd:PRK12316 3334 -GLPLYNLYGPTE---ATITVTHWQCVEEGKDAVPIGRPI---------ANRACYILDGS------LEPVPVGALGELYL 3394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 436 RGSSVFREYWNRPKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRTSVDiIKNGGFKISALEVERQLLAHPHIT 508
Cdd:PRK12316 3395 GGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEARLLEHPWVR 3473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 509 DVAVIGppdvVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12316 3474 EAVVLA----VDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
62-579 |
8.41e-30 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 123.08 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcSSRDLKEER-------------ISFLcpndasyvvaqwASWMSGGI 128
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFI------DSLKLPDKSpiivfghmspemlATFL------------GAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 129 AVPLYRKHPVQQLEYVIEDSQSALVIAAEEYvgkispSAEKLGVPVLPLGSHSSGSAGHTAVEdvplASSASWKDRGAMI 208
Cdd:PRK04813 79 YIPVDVSSPAERIEMIIEVAKPSLIIATEEL------PLEILGIPVITLDELKDIFATGNPYD----FDHAVKGDDNYYI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 209 IYTSGTTGRPKGVLSTHENvqavttgLVEKWEWKKED--------------------VI-----------LHVLPlhhvH 257
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDN-------LVSFTNWMLEDfalpegpqflnqapysfdlsVMdlyptlasggtLVALP----K 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 258 GVIN--KLL------CPL--WVgAT------CIMLPEFSAQmvwkkflssQAPRVSVFMavptiyaklieyydehfsqpq 321
Cdd:PRK04813 218 DMTAnfKQLfetlpqLPInvWV-STpsfadmCLLDPSFNEE---------HLPNLTHFL--------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 322 vqdfvraFCQEnirlmvsgsaALPVPVLKKwkaitghtLLER---------YGMTEIGMALSnplhGVRVPGSV---GTP 389
Cdd:PRK04813 267 -------FCGE----------ELPHKTAKK--------LLERfpsatiyntYGPTEATVAVT----SIEITDEMldqYKR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 390 LP-GVevriateaVKGGGRSYTIlaqgDEDGTqmtPGLEGQEGELLVRGSSVFREYWNRPKETREAF-TSDGW--FRTGD 465
Cdd:PRK04813 318 LPiGY--------AKPDSPLLII----DEEGT---KLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGD 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 466 TAAYHDGVYWIKGRtsVDI-IKNGGFKISALEVERQLLAHPHItDVAVIGP--PD--VVwgQRVSAVV---QLRRGEMLS 537
Cdd:PRK04813 383 AGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQSSYV-ESAVVVPynKDhkVQ--YLIAYVVpkeEDFEREFEL 457
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1201832555 538 VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:PRK04813 458 TKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
62-577 |
2.42e-29 |
|
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: 121.43 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQCSSRdLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLA----RFLREKGV-KKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAEEYVGKISPSAEKLgVPVLPLGSHSSGSAGHTAVEDvplassaswkDRGAMIIYTSGTTGRPKGV 221
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKSKLSFNKSTI-LLEDPSISQEDTSNIDYINNS----------DDLLYIIYTSGTTGKPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKEDVILH-VLPLHHV--HGVINKLLcplwVGATCIMLPEFSAQMVWKKF-LSSQAPRVS 297
Cdd:cd17656 147 QLEHKNMVNLLHFEREKTNINFSDKVLQfATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFdLVKRHNIEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 298 VFMavPTIYAKLIeyYDEHFSQPQVQDFVRAFCQENIRLMVSGsaaLPVPVLKKwkaiTGHTLLERYGMTEIGMALSNPL 377
Cdd:cd17656 223 VFL--PVAFLKFI--FSEREFINRFPTCVKHIITAGEQLVITN---EFKEMLHE----HNVHLHNHYGPSETHVVTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 378 -HGVRVP--GSVGTPLPGVEVRIATEAvkgggrsytilaqgdedgTQMTPglEGQEGELLVRGSSVFREYWNRPKETREA 454
Cdd:cd17656 292 nPEAEIPelPPIGKPISNTWIYILDQE------------------QQLQP--QGIVGELYISGASVARGYLNRQELTAEK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 455 FTSDGW------FRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSA- 526
Cdd:cd17656 352 FFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAy 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 527 VVQLRRgemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17656 431 FVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
73-581 |
4.11e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 121.35 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 73 HTYRELFCRSLRLSQEICRvLQCSSRDlkeeRISFLCPNDASYVVAQWAswMSGGIAV-----PlyRKHPvQQLEYVIED 147
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAA-LGVEPGD----RVGTLAWNGYRHLEAYYG--VSGSGAVchtinP--RLFP-EQIAYIVNH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 148 SQSALVIAAEEY---VGKISP------------SAEKLGVPVLPLGSHSSGSAGHTAVEDVPL-----ASSaswkdrgam 207
Cdd:PRK07008 110 AEDRYVLFDLTFlplVDALAPqcpnvkgwvamtDAAHLPAGSTPLLCYETLVGAQDGDYDWPRfdenqASS--------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHEN--VQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLwVGATCIML-PEFSAQMV 284
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 WKKFlssQAPRVSVFMAVPTIYAKLIEYYDE---HFSqpqvqdfvrafcqeNIRLMVSGSAALPVPVLKKWKAITGHTLL 361
Cdd:PRK07008 260 YELI---EAERVTFSAGVPTVWLGLLNHMREaglRFS--------------TLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 362 ERYGMTEIgmalsNPL---------HGVRVPGSV-------GTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMtPG 425
Cdd:PRK07008 323 HAWGMTEM-----SPLgtlcklkwkHSQLPLDEQrkllekqGRVIYGVDMKIV-----------------GDDGREL-PW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 426 LEGQEGELLVRGSSVFREYWNRpketREAFTSDGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAH 504
Cdd:PRK07008 380 DGKAFGDLQVRGPWVIDRYFRG----DASPLVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAH 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 505 PHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQRF 581
Cdd:PRK07008 455 PAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
62-577 |
4.59e-29 |
|
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: 120.23 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQeicrVLQcsSRDLKEERISFLC-PNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAH----YLQ--SLGVKSESLVGICvERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAAEEYVgkispsaeklgvpvlplgshssgsaghtavedvplassaswkdrgAMIIYTSGTTGRPKG 220
Cdd:cd17644 89 LTYILEDAQISVLLTQPENL---------------------------------------------AYVIYTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhhVHGVINKLLCPLWV-GATCIMLPE---FSAQMVWKKflsSQAPRV 296
Cdd:cd17644 124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTLLsGATLVLRPEemrSSLEDFVQY---IQQWQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 297 SVFmAVPTIYAKLIeyydehfsqpqVQDFVRAFCQ--ENIRLMVSGSAALPVPVLKKWKAITGH--TLLERYGMTEIGMA 372
Cdd:cd17644 199 TVL-SLPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 373 -----LSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLEGqegELLVRGSSVFREYWNR 447
Cdd:cd17644 267 atvcrLTQLTERNITSVPIGRPIANTQVYIL-----------------DENLQPVPVGVPG---ELHIGGVGLARGYLNR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 448 PKETREAFTSDGW--------FRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDV 518
Cdd:cd17644 327 PELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 519 VWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17644 406 PGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
207-577 |
7.33e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 120.52 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 207 MIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQmvwk 286
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSAS---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 KFLssqaPRVSVFMAVPTIY-AKLIEYYdehFSQPQVQD-----FVRAFcqenirlmvsGSAALPvpvlkkwKAIT---- 356
Cdd:PRK13388 230 GFL----DDVRRYGATYFNYvGKPLAYI---LATPERPDdadnpLRVAF----------GNEASP-------RDIAefsr 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 357 --GHTLLERYGMTEIGMALsnplhgVRVP----GSVGTPLPGVEVriateaVKGGGRSYTILAQGDEDGTQMTPglEGQE 430
Cdd:PRK13388 286 rfGCQVEDGYGSSEGAVIV------VREPgtppGSIGRGAPGVAI------YNPETLTECAVARFDAHGALLNA--DEAI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 431 GELLVR-GSSVFREYWNRPKETREAFtSDGWFRTGDTAaYHDGVYWI--KGRTSvDIIKNGGFKISALEVERQLLAHPHI 507
Cdd:PRK13388 352 GELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLA-YRDADGWIyfAGRTA-DWMRVDGENLSAAPIERILLRHPAI 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 508 TDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEW--ARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK13388 429 NRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
210-577 |
1.23e-28 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 120.33 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHEN--VQAVTTGLVekWEWKKEDVILHVLPLHHVHGvinklLCPLWVGA----TCIMLPEFSAQM 283
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGayLMALSNALI--WGMNEGAVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VWKKFLSSQaprVSVFMAVPTIYAKLIEYYDEHFSQPqvqdfvrafCQENIRLMVSGSAalPVPVLKKWKAITGHTLLER 363
Cdd:PLN02479 275 IYSAIANYG---VTHFCAAPVVLNTIVNAPKSETILP---------LPRVVHVMTAGAA--PPPSVLFAMSEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 YGMTE-------------------IGMALSNPLHGVRVPGsvgtpLPGVEVrIATEAVKgggrsyTILAqgdeDGTQMtp 424
Cdd:PLN02479 341 YGLSEtygpstvcawkpewdslppEEQARLNARQGVRYIG-----LEGLDV-VDTKTMK------PVPA----DGKTM-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 425 glegqeGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLA 503
Cdd:PLN02479 403 ------GEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHpDGYIEIKDR-SKDIIISGGENISSLEVENVVYT 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 504 HPHITDVAVIGPPDVVWGQRVSAVVQLRRG-----EMLSVKELKEWARDTMAPYAVPTElIVVEEIPRNQMGKVNKKEL 577
Cdd:PLN02479 475 HPAVLEASVVARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-577 |
3.06e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.83 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKiaiidqngEHTYRELFCRSLRLSQEIcrvlqcSSRDLKEERISFLC-PNDASYVVAQWASWMSGGIAVPLYRK 135
Cdd:PRK12316 529 ALAFGEE--------TLDYAELNRRANRLAHAL------IERGVGPDVLVGVAmERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 136 HPVQQLEYVIEDSQSALVIAaEEYVGKISPSAEklGVPVLPLGSHSSGSAGHTaveDVPLASSASwKDRGAMIIYTSGTT 215
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLLS-QSHLGRKLPLAA--GVQVLDLDRPAAWLEGYS---EENPGTELN-PENLAYVIYTSGST 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVInKLLCPLWVGATCIMLPEFSAQMVWKKFLSSQAPR 295
Cdd:PRK12316 668 GKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPGDHRDPAKLVELINREG 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 296 VSVFMAVPTIYAKLIeyydeHFSQPQVQDfvrafcqeNIRLMVSGSAALPVPVLKK--WKAITGHtLLERYGMTEIGMAL 373
Cdd:PRK12316 747 VDTLHFVPSMLQAFL-----QDEDVASCT--------SLRRIVCSGEALPADAQEQvfAKLPQAG-LYNLYGPTEAAIDV 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 374 SnplHGVRVPGSVGTPLPGVEVriateavkGGGRSYTILAQGDedgtqmtPGLEGQEGELLVRGSSVFREYWNRPKETRE 453
Cdd:PRK12316 813 T---HWTCVEEGGDSVPIGRPI--------ANLACYILDANLE-------PVPVGVLGELYLAGRGLARGYHGRPGLTAE 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 454 AFTSDGW------FRTGDTAAYH-DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIgppdVVWGQRVSA 526
Cdd:PRK12316 875 RFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVG 949
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1201832555 527 VVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12316 950 YVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
61-571 |
3.34e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 116.39 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 61 GDKIAII---DQNGEH---TYRELFcrslrlsQEICR---VLQcsSRDLKE-ERISFLCPNDASYVVAQWASWMSGGIav 130
Cdd:PRK00174 81 GDKVAIIwegDDPGDSrkiTYRELH-------REVCRfanALK--SLGVKKgDRVAIYMPMIPEAAVAMLACARIGAV-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 131 plyrkHPV-------QQLEYVIEDSQSALVIAAEEYV--GKISP-------------SAEKlgVPVLP-LGSHSSGSAG- 186
Cdd:PRK00174 150 -----HSVvfggfsaEALADRIIDAGAKLVITADEGVrgGKPIPlkanvdealancpSVEK--VIVVRrTGGDVDWVEGr 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 187 ----HTAVEDVPLASSASWKDrgA----MIIYTSGTTGRPKGVLSTHE--NVQAVTTglvEKW--EWKKEDV-------- 246
Cdd:PRK00174 223 dlwwHELVAGASDECEPEPMD--AedplFILYTSGSTGKPKGVLHTTGgyLVYAAMT---MKYvfDYKDGDVywctadvg 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 247 -------IlhvlplhhVHGvinkllcPLWVGATCIML---PEFS-----AQMVWKKflssqapRVSVFMAVPTIYAKLIE 311
Cdd:PRK00174 298 wvtghsyI--------VYG-------PLANGATTLMFegvPNYPdpgrfWEVIDKH-------KVTIFYTAPTAIRALMK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 312 YYDEHfsqpqvqdfVRAFCQENIRLMvsGSAALPV-PVLKKW--KAITGhtllER------YGMTEIGMALSNPLHGVR- 381
Cdd:PRK00174 356 EGDEH---------PKKYDLSSLRLL--GSVGEPInPEAWEWyyKVVGG----ERcpivdtWWQTETGGIMITPLPGATp 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 382 -VPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGS--SVFREYWNRPKETREAFTSD 458
Cdd:PRK00174 421 lKPGSATRPLPGIQPAVV-----------------DEEGNPLEGG---EGGNLVIKDPwpGMMRTIYGDHERFVKTYFST 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 459 --GWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEM 535
Cdd:PRK00174 481 fkGMYFTGDGARRdEDGYYWITGRVD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE 559
|
570 580 590
....*....|....*....|....*....|....*....
gi 1201832555 536 LS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGK 571
Cdd:PRK00174 560 PSdelRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
62-577 |
3.36e-27 |
|
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: 114.80 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLA----HYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIaaeeyvgkispsaeklgvpvlplgshssgsaghTAVEDVplassaswkdrgAMIIYTSGTTGRPKGV 221
Cdd:cd17648 78 QFILEDTGARVVI---------------------------------TNSTDL------------AYAIYTSGTTGKPKGV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 222 LSTHENVQAVTTGLVEKWEWKKED--VIL----HVLPlHHVHgvinKLLCPLWVGATCIMLPEfsaQMVWKK---FLSSQ 292
Cdd:cd17648 113 LVEHGSVVNLRTSLSERYFGRDNGdeAVLffsnYVFD-FFVE----QMTLALLNGQKLVVPPD---EMRFDPdrfYAYIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 293 APRVSVFMAVPtiyaklieyydehfSQPQVQDFVRAfcqENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGM- 371
Cdd:cd17648 185 REKVTYLSGTP--------------SVLQQYDLARL---PHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVt 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 372 ALSNPLHGV-RVPGSVGTPLPGVevriateavkgggRSYTIlaqgdEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKE 450
Cdd:cd17648 248 NHKRFFPGDqRFDKSLGRPVRNT-------------KCYVL-----NDAMKRVP--VGAVGELYLGGDGVARGYLNRPEL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 451 TREAFTSDGW--------------FRTGDTAAY-HDGVYWIKGRTSVDIiKNGGFKISALEVERQLLAHPHITDVAVIGP 515
Cdd:cd17648 308 TAERFLPNPFqteqerargrnarlYKTGDLVRWlPSGELEYLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 516 --PDVVWGQRVSAVV--QLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17648 387 edASQAQSRIQKYLVgyYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
57-577 |
1.60e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.64 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGDKiaiidqngEHTYRELFCRSLRLSQEI------CRVLqcssrdlkeerISFLCPNDASYVVAQWASWMSGGIAV 130
Cdd:PRK12467 3113 ALVFGDQ--------QLSYAELNRRANRLAHRLiaigvgPDVL-----------VGVAVERSVEMIVALLAVLKAGGAYV 3173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 131 PLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKIsPSAEKLGVPVLPLGSHSSGSaghtavEDVPLASSASwkDRGAMIIY 210
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQL-PAPAGDTALTLDRLDLNGYS------ENNPSTRVMG--ENLAYVIY 3244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 211 TSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIMLP--EFSAQMVWKKF 288
Cdd:PRK12467 3245 TSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVVRDndLWDPEELWQAI 3323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 LssqAPRVSVFMAVPTIYAKLIEYYDehfsqpqVQDFVRafcqenIRLMVSGSAALPVPVLKKWKA-ITGHTLLERYGMT 367
Cdd:PRK12467 3324 H---AHRISIACFPPAYLQQFAEDAG-------GADCAS------LDIYVFGGEAVPPAAFEQVKRkLKPRGLTNGYGPT 3387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 368 EigmALSNPLH----GVRVPGSVGTPLpGVEVriateavkgGGRSYTILaqgdeDGtQMTPGLEGQEGELLVRGSSVFRE 443
Cdd:PRK12467 3388 E---AVVTVTLwkcgGDAVCEAPYAPI-GRPV---------AGRSIYVL-----DG-QLNPVPVGVAGELYIGGVGLARG 3448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRtsVD-IIKNGGFKISALEVERQLLAHPHITDVAVIG 514
Cdd:PRK12467 3449 YHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLLQHPSVREAVVLA 3526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 515 PPDVVWGQRVSAVV-QLRRGEMLsvKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK12467 3527 RDGAGGKQLVAYVVpADPQGDWR--ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
205-577 |
2.26e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 111.67 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 205 GAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIML----PEFS 280
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIItnknPKFA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 281 AQMVwkkflssQAPRVSVFMAVPTIYAKLIEyydehFSQPQVQDFvrafcqeniRLMVSGsAALPVPVLKKWKAITGHtL 360
Cdd:PRK08308 183 LNIL-------RNTPQHILYAVPLMLHILGR-----LLPGTFQFH---------AVMTSG-TPLPEAWFYKLRERTTY-M 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 361 LERYGMTEIG-MALSnplHGVRVPGSVGTPLPGVEVRIateavkGGGrsytilaqgdedgtqmtpglEGQEGELLVRGSs 439
Cdd:PRK08308 240 MQQYGCSEAGcVSIC---PDMKSHLDLGNPLPHVSVSA------GSD--------------------ENAPEEIVVKMG- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 440 vfreywnrpkeTREAFTSDGWFRTgdtaayHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVV 519
Cdd:PRK08308 290 -----------DKEIFTKDLGYKS------ERGTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPV 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 520 WGQRVSAVVQLRrgEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK08308 352 AGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
62-577 |
2.75e-26 |
|
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: 111.88 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQ 140
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLA----RHLR--GKGVKpDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 141 LEYVIEDSQSALVIAaeeyvgkispSAEKLgvpvlplgshssgsaghtavedvplassaswkdrgAMIIYTSGTTGRPKG 220
Cdd:cd17645 87 IAYMLADSSAKILLT----------NPDDL-----------------------------------AYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 221 VLSTHENvqavttgLVEKWEWKK-------EDVILhVLPLHHVHGVINKLLCPLWVGATCIMLPefsaqmvwkkflssQA 293
Cdd:cd17645 122 VMIEHHN-------LVNLCEWHRpyfgvtpADKSL-VYASFSFDASAWEIFPHLTAGAALHVVP--------------SE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 294 PRVSVfmavptiyAKLIEYYDEH-----FSQPQVQDFVRAFCQENIRLMVSGSAALPVPVLKkwkaitGHTLLERYGMTE 368
Cdd:cd17645 180 RRLDL--------DALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK------GYKLVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 369 IG-MALSNPLHGVRVPGSVGTPLPGVEVRIATEavkgggrsytilaqgdedGTQMTPglEGQEGELLVRGSSVFREYWNR 447
Cdd:cd17645 246 NTvVATSFEIDKPYANIPIGKPIDNTRVYILDE------------------ALQLQP--IGVAGELCIAGEGLARGYLNR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 448 PKETREAFTSDGW------FRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVvw 520
Cdd:cd17645 306 PELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA-- 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 521 GQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17645 383 DGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
62-577 |
4.34e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.11 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEHTYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPV 138
Cdd:PRK05691 1146 ERIALVWDGGSLDYAELHAQANRLAHYL--------RDKgvgPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPA 1217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 139 QQLEYVIEDSQSALVIAAEEYVGKIsPSAEklGVPVLPLGS-HSSGSAGHTAVEDVPlassaswKDRGAMIIYTSGTTGR 217
Cdd:PRK05691 1218 ERLAYMLADSGVELLLTQSHLLERL-PQAE--GVSAIALDSlHLDSWPSQAPGLHLH-------GDNLAYVIYTSGSTGQ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 218 PKGVLSTHenvqavtTGLVEKWEWKK-------EDVILHVLPLHHVHGVINKLLcPLWVGATCIML-------PEFSAQM 283
Cdd:PRK05691 1288 PKGVGNTH-------AALAERLQWMQatyalddSDVLMQKAPISFDVSVWECFW-PLITGCRLVLAgpgehrdPQRIAEL 1359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VwkkflssQAPRVSVFMAVPTIYAKLIEyydehfsQPQVQDfvrafCQeNIRLMVSGSAALPVP----VLKKWKAITGHT 359
Cdd:PRK05691 1360 V-------QQYGVTTLHFVPPLLQLFID-------EPLAAA-----CT-SLRRLFSGGEALPAElrnrVLQRLPQVQLHN 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 360 lleRYGMTEIGMalsNPLH-------GVRVPgsVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLegqEGE 432
Cdd:PRK05691 1420 ---RYGPTETAI---NVTHwqcqaedGERSP--IGRPLGNVLCRVL-----------------DAELNLLPPGV---AGE 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 433 LLVRGSSVFREYWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRTSVDiIKNGGFKISALEVERQLLAH 504
Cdd:PRK05691 1472 LCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQ 1550
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 505 PHITDVAVIGPPDVVwGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK05691 1551 PGVAQAAVLVREGAA-GAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
166-580 |
4.78e-26 |
|
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: 111.12 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 166 SAEKLGVPVLPLGSHSS----------GSAGHTAVEDVPLAssaswkDRGAMIIYTSGTTGRPKGVLSTHENVQAvttGL 235
Cdd:cd05974 44 AAMKLGAVVIPATTLLTpddlrdrvdrGGAVYAAVDENTHA------DDPMLLYFTSGTTSKPKLVEHTHRSYPV---GH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 236 VEKWEW---KKEDVILHVLPLHHVHGVINKLLCPLWVGATCIML--PEFSAQMVWKKFLSSqapRVSVFMAVPTIYAKLI 310
Cdd:cd05974 115 LSTMYWiglKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAALVRY---GVTTLCAPPTVWRMLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 311 EyydehfsqpqvQDFVRAfcQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRVPGSVGTPL 390
Cdd:cd05974 192 Q-----------QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 391 PGVEVRIAteavkgggrsytilaqgDEDGTqmtpglEGQEGELLV-----RGSSVFREYWNRPKETREAFtSDGWFRTGD 465
Cdd:cd05974 259 PGYRVALL-----------------DPDGA------PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 466 TAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKEL 541
Cdd:cd05974 315 IAMRdEDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpetALEI 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1201832555 542 KEWARDTMAPYAVPTELIVVeEIPRNQMGKVNKKELLQR 580
Cdd:cd05974 394 FRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
147-577 |
1.47e-25 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 111.66 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 147 DSQSALVIAAEEYVGKISPSaeklgvpvlplgshssgsaghTAVEDVPLASSASWK----------DRGAMIIYTSGTTG 216
Cdd:PRK06060 100 NTEPALVVTSDALRDRFQPS---------------------RVAEAAELMSEAARVapggyepmggDALAYATYTSGTTG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 217 RPKGVLSTHENVQAVTTGLVEK-WEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP----EFSAQMVWKKFlss 291
Cdd:PRK06060 159 PPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSapvtPEAAAILSARF--- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 292 qapRVSVFMAVPTIYAKLIeyydehfsqpqvqDFVRAFCQENIRLMVSGSAALPVPVLKKWKAITGHT-LLERYGMTEIG 370
Cdd:PRK06060 236 ---GPSVLYGVPNFFARVI-------------DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 371 MA-LSNPLHGVRvPGSVGTPLPGVEVRIATEavkgggrsytilaqgdeDGTQMTPGLEGqegELLVRGSSVFREYWNRPK 449
Cdd:PRK06060 300 QTfVSNRVDEWR-LGTLGRVLPPYEIRVVAP-----------------DGTTAGPGVEG---DLWVRGPAIAKGYWNRPD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 450 ETreaFTSDGWFRTGDTAAYhDGVYWIK-GRTSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVV 528
Cdd:PRK06060 359 SP---VANEGWLDTRDRVCI-DSDGWVTyRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 529 QLRRGEMLSVKELKEWAR---DTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK06060 435 VATSGATIDGSVMRDLHRgllNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
103-581 |
5.21e-25 |
|
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: 109.05 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAA-EEYVGKISPSAEKlgVPVL------ 175
Cdd:cd17641 37 DVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEdEEQVDKLLEIADR--IPSVryviyc 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 176 -PLG----SHS----------SGSAGHTAVEDVPLASSASWK-DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKW 239
Cdd:cd17641 115 dPRGmrkyDDPrlisfedvvaLGRALDRRDPGLYEREVAAGKgEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAAD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 240 EWKKEDVILHVLPLHHVHGVINKLLCPLWVGaTCIMLPE-----------------FSAQMVWKKFLS------SQAPRV 296
Cdd:cd17641 195 PLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreigptfvLLPPRVWEGIAAdvrarmMDATPF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 297 SVFMAvpTIYAKL-IEYYDEHFSQPQVQDFVR---AFCQE-------------NIRLMVSGSAALPVPVLKKWKAItGHT 359
Cdd:cd17641 274 KRFMF--ELGMKLgLRALDRGKRGRPVSLWLRlasWLADAllfrplrdrlgfsRLRSAATGGAALGPDTFRFFHAI-GVP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 360 LLERYGMTEI-GMALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgdedgtqmtpglegQEGELLVRGS 438
Cdd:cd17641 351 LKQLYGQTELaGAYTVHRDGDVD-PDTVGVPFPGTEVRID------------------------------EVGEILVRSP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 SVFREYWNRPKETREAFTSDGWFRTGDtAAY--HDGVYWIKGRTSvDIIK-NGGFKISALEVERQLLAHPHITDVAVIG- 514
Cdd:cd17641 400 GVFVGYYKNPEATAEDFDEDGWLHTGD-AGYfkENGHLVVIDRAK-DVGTtSDGTRFSPQFIENKLKFSPYIAEAVVLGa 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 515 --PpdvvwgqRVSAVVQLRrgemlsVKELKEWARDTMAPYAVPTELIV---VEEIPRNQMGKVNK----KELLQRF 581
Cdd:cd17641 478 grP-------YLTAFICID------YAIVGKWAEQRGIAFTTYTDLASrpeVYELIRKEVEKVNAslpeAQRIRRF 540
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
63-581 |
1.06e-24 |
|
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: 107.57 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 63 KIAIIDQNGEH---TYRELFCRSLRLSQEicrvLQCSSRDLKEErISFLCPNDASYVVAQWASWMSGGIAVPLYrkhpvq 139
Cdd:cd05908 3 GIIFILGDKKEkfvSYRHLREEALGYLGA----LQELGIKPGQE-VVFQITHNNKFLYLFWACLLGGMIAVPVS------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 140 qleyviedsqsalVIAAEEYVGKISPSAEKLGVPVLplgshssgsaghtavedvpLASSASW---KDRGAMIIYTSGTTG 216
Cdd:cd05908 72 -------------IGSNEEHKLKLNKVWNTLKNPYL-------------------ITEEEVLcelADELAFIQFSSGSTG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 217 RPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPefsaqmvwkkflssqaprV 296
Cdd:cd05908 120 DPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP------------------T 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 297 SVFMAVPTIYAKLIeyyDEH---------FSQPQVQDFVRAFCQEN-----IRLMVSGSAALPVPVLKKW-KAITGHTL- 360
Cdd:cd05908 182 RLFIRRPILWLKKA---SEHkativsspnFGYKYFLKTLKPEKANDwdlssIRMILNGAEPIDYELCHEFlDHMSKYGLk 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 361 ----LERYGMTEIGMALSNP----------------LHGVRVPG------------SVGTPLPGVEVRIATEAvkgggrs 408
Cdd:cd05908 259 rnaiLPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDETDIRICDED------- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 409 ytilAQGDEDGTQmtpglegqeGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHDGVYWIKGRTSVDIIKNG 488
Cdd:cd05908 332 ----NKILPDGYI---------GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNG 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 489 ------GFKISALEVERQLLAHphitdVAVIGPPD-----------VVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAP 551
Cdd:cd05908 399 qnvyphDIERIAEELEGVELGR-----VVACGVNNsntrneeifcfIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLP 473
|
570 580 590
....*....|....*....|....*....|
gi 1201832555 552 yavptelivVEEIPRNQMGKVNKKELLQRF 581
Cdd:cd05908 474 ---------IRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
57-577 |
1.77e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 109.10 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 57 ALTFGdkiaiidqnGEH-TYRELFCRSLRLSqeicRVLQcsSRDLKEE-RISFLCPNDASYVVAQWASWMSGGIAVPLYR 134
Cdd:PRK05691 2206 ALTFA---------GQTlSYAELDARANRLA----RALR--ERGVGPQvRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHPVQQLEYVIEDSQSALVIAAEEYVgkispsaEKLGVpvLPLG----SHSSGSAGHTAVEDVPLASsASWKDRGAMIIY 210
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALF-------EALGE--LPAGvarwCLEDDAAALAAYSDAPLPF-LSLPQHQAYLIY 2340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 211 TSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLhHVHGVINKLLCPLWVGATCIMlpefSAQMVWK---- 286
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL----RAQGQWGaeei 2415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 -KFLSSQapRVSVFMAVPTIYAKLIEYYDehfSQPQvqdfvrafcQENIRLMVSGSAALPVPVLKKWK-AITGHTLLERY 364
Cdd:PRK05691 2416 cQLIREQ--QVSILGFTPSYGSQLAQWLA---GQGE---------QLPVRMCITGGEALTGEHLQRIRqAFAPQLFFNAY 2481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 365 GMTE-IGMALSNPLHGVRVPGSVGTPLPGVEvriateavkgGGRSYTILaqgDEDgtqMTPGLEGQEGELLVRGSSVFRE 443
Cdd:PRK05691 2482 GPTEtVVMPLACLAPEQLEEGAASVPIGRVV----------GARVAYIL---DAD---LALVPQGATGELYVGGAGLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRTSVDiIKNGGFKISALEVERQLLAHPHITDVAVI-- 513
Cdd:PRK05691 2546 YHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQ-VKIRGFRIELGEIESRLLEHPAVREAVVLal 2624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 514 ---GPPDVVwGQRVSAVVQLRRGEMLSVKE-LKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK05691 2625 dtpSGKQLA-GYLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
185-572 |
1.53e-23 |
|
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: 105.09 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 185 AGHTAVEDVPLASsaswkDRGAMIIYTSGTTGRPKGVLS-----------THENVQAVTTGLVekWeWKKEDVILHVLPL 253
Cdd:cd05967 217 AKAEPVDCVPVAA-----TDPLYILYTSGTTGKPKGVVRdngghavalnwSMRNIYGIKPGDV--W-WAASDVGWVVGHS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 254 HHVHGvinkllcPLWVGATCIML-------PEFSAqmvWKKFLSSQapRVSVFMAVPT-IYAklIEYYDEHfsqpqvQDF 325
Cdd:cd05967 289 YIVYG-------PLLHGATTVLYegkpvgtPDPGA---FWRVIEKY--QVNALFTAPTaIRA--IRKEDPD------GKY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 326 VRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRV----PGSVGTPLPGVEVRIAtea 401
Cdd:cd05967 349 IKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPlpikAGSPGKPVPGYQVQVL--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 402 vkgggrsytilaqgDEDGTQMTPGlegQEGELLVRGS---SVFREYWNRPKETREAF--TSDGWFRTGDtAAYHD--GVY 474
Cdd:cd05967 426 --------------DEDGEPVGPN---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGD-AGYKDedGYL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 475 WIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS----VKELKEWARDTMA 550
Cdd:cd05967 488 FIMGRTD-DVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIG 566
|
410 420
....*....|....*....|..
gi 1201832555 551 PYAVPTELIVVEEIPRNQMGKV 572
Cdd:cd05967 567 PVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
206-465 |
1.64e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 104.80 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCimlpEFSAQMVW 285
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKFLSSQAPRVSVFMAVP----TIYAKLIEYYDE------------HFSQPQ---------------VQDFVRAFCQENI 334
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPrlynRIYDGITNAVKEsgglkerlfnaaYNAKKQalengknpspmwdrlVFNKIKAKLGGRV 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 335 RLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIA--TEAvkgggrSYTil 412
Cdd:PLN02736 379 RFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvPEM------NYT-- 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 413 aqgDEDgtQMTPglegqEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGD 465
Cdd:PLN02736 451 ---SED--QPYP-----RGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
65-577 |
2.39e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 105.13 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 65 AIIDQNGEHTYRELFCRSLRLSQeicrvlQCSSRDLKEERISFLC-PNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEY 143
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALAN------LLRERGVKPGDSVAVAlPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKM 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 144 VIEDSQSALVIAAEEYVGKISpsaeklGVPVLPLGSHSSGSAghtAVEDVPLASSASwkDRGAMIIYTSGTTGRPKGVLS 223
Cdd:PRK10252 550 MLEDARPSLLITTADQLPRFA------DVPDLTSLCYNAPLA---PQGAAPLQLSQP--HHTAYIIFTSGSTGRPKGVMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 224 THenvqavtTGLVEKWEWKKE-------DVILHVLPLHHVHGVInKLLCPLWVGATCIMLPefsaqmvwkkflsSQAPRv 296
Cdd:PRK10252 619 GQ-------TAIVNRLLWMQNhypltadDVVLQKTPCSFDVSVW-EFFWPFIAGAKLVMAE-------------PEAHR- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 297 svfmaVPTIYAKLIEYY---DEHFSQPQVQDFVRAFCQENI--------RLMVSGSaALPVPVLKKWKAITGHTLLERYG 365
Cdd:PRK10252 677 -----DPLAMQQFFAEYgvtTTHFVPSMLAAFVASLTPEGArqscaslrQVFCSGE-ALPADLCREWQQLTGAPLHNLYG 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 366 MTEIGMALSN-PLHGVRVPGSVGTPLP-GVEV-----RIATEAvkgggrsytilaqgdedgtqMTPGLEGQEGELLVRGS 438
Cdd:PRK10252 751 PTEAAVDVSWyPAFGEELAAVRGSSVPiGYPVwntglRILDAR--------------------MRPVPPGVAGDLYLTGI 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 SVFREYWNRPKETREAFTSDGW------FRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPhitDVA 511
Cdd:PRK10252 811 QLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALP---DVE 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 512 VIGPPDVVWGQRVSAVVQLRR---------GEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:PRK10252 887 QAVTHACVINQAAATGGDARQlvgylvsqsGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
74-572 |
6.61e-23 |
|
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: 102.95 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEIcrvlqcssRDL---KEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQS 150
Cdd:cd05968 93 TYGELLYEVKRLANGL--------RALgvgKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVIAAEEYV--GKI-------------SPSAEK------LGVPVLPLGSHSSGSAGHTAVEDVPLASSASwkDRGAMII 209
Cdd:cd05968 165 KALITADGFTrrGREvnlkeeadkacaqCPTVEKvvvvrhLGNDFTPAKGRDLSYDEEKETAGDGAERTES--EDPLMII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHEN--VQAVTTgLVEKWEWKKEDVILHVLPLHHVHGVInKLLCPLWVGATCIM---LPEF-SAQM 283
Cdd:cd05968 243 YTSGTTGKPKGTVHVHAGfpLKAAQD-MYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHpKADR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 284 VWKkflSSQAPRVSVFMAVPTIYAKLIeyydehfsqPQVQDFVRAFCQENIRLMVS-GSAALPVPvlkkWKAITGHTLLE 362
Cdd:cd05968 321 LWR---MVEDHEITHLGLSPTLIRALK---------PRGDAPVNAHDLSSLRVLGStGEPWNPEP----WNWLFETVGKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 363 RY------GMTEI--GMALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPglegQEGELL 434
Cdd:cd05968 385 RNpiinysGGTEIsgGILGNVLIKPIK-PSSFNGPVPGMKADVL-----------------DESGKPARP----EVGELV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 435 VRGS--SVFREYWNRPKETREAFTS--DGWFRTGDTAAY-HDGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITD 509
Cdd:cd05968 443 LLAPwpGMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYdEEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 510 VAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKV 572
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
209-579 |
8.65e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 101.61 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 209 IYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILhVLPLHHVHGVInKLLCPLWVGATCIMLPefsaqmvWKKF 288
Cdd:PRK07445 126 IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQVNSFC-VLPLYHVSGLM-QFMRSFLTGGKLVILP-------YKRL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 LSSQAPRVSV---FMA-VPTiyaKLieyydEHFSQPQVQdFVRAFcqeNIRLmVSGSAALPvpvlkkwkaitghTLLER- 363
Cdd:PRK07445 197 KSGQELPPNPsdfFLSlVPT---QL-----QRLLQLRPQ-WLAQF---RTIL-LGGAPAWP-------------SLLEQa 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 364 ----------YGMTEIG--MALSNP---LHGVRvpgSVGTPLPGVEVRIAteavkgggrsytilaqgdedgtqmtpglEG 428
Cdd:PRK07445 251 rqlqlrlaptYGMTETAsqIATLKPddfLAGNN---SSGQVLPHAQITIP----------------------------AN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 429 QEGELLVRGSSVFREYWNRPKETREAFTSD--GWFRtgdtaayHDGVYWIKGRTSVDIIkNGGFKISALEVERQLLAHPH 506
Cdd:PRK07445 300 QTGNITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGL 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 507 ITDVAVIGPPDVVWGQRVSAVVQLRRGEmLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKELLQ 579
Cdd:PRK07445 372 VQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
140-471 |
5.95e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 99.95 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 140 QLEYVIEDSQSALVIA--AEEYVGKISpSAEKLGVPVLPLGSHSSGSAGH--------TAVEDVPLASSASWKDRGAMII 209
Cdd:PRK08180 137 KLRHVLELLTPGLVFAddGAAFARALA-AVVPADVEVVAVRGAVPGRAATpfaallatPPTAAVDAAHAAVGPDTIAKFL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 210 YTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKED--VILHVLPLHHVHGVINKLLCPLWVGATCIM-----LPEFSAQ 282
Cdd:PRK08180 216 FTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPGGFDE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 283 MVwkKFLSSQAPrvSVFMAVPTIYAKLIEYYDEHfsqpqvQDFVRAFCqENIRLMVSGSAALPVPVLKKWKAITGHTLLE 362
Cdd:PRK08180 296 TL--RNLREISP--TVYFNVPKGWEMLVPALERD------AALRRRFF-SRLKLLFYAGAALSQDVWDRLDRVAEATCGE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 363 R------YGMTEIGMALSNpLHGVRV-PGSVGTPLPGVEVRIateaVKGGGRSytilaqgdedgtqmtpglegqegELLV 435
Cdd:PRK08180 365 RirmmtgLGMTETAPSATF-TTGPLSrAGNIGLPAPGCEVKL----VPVGGKL-----------------------EVRV 416
|
330 340 350
....*....|....*....|....*....|....*.
gi 1201832555 436 RGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHD 471
Cdd:PRK08180 417 KGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
111-514 |
1.79e-21 |
|
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: 98.58 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 111 NDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSA-LVIAAEEYVGKISPSAEKLgvPVL--------PLGSHS 181
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANiLVVENQKQLQKILQIQDKL--PHLkaiiqykePLKEKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 182 SG--------SAGHTAVEDVPLASSASWK-DRGAMIIYTSGTTGRPKGVLSTHEN----VQAVTTGLVEKWEWKKEDVIL 248
Cdd:cd05933 120 PNlyswdefmELGRSIPDEQLDAIISSQKpNQCCTLIYTSGTTGMPKGVMLSHDNitwtAKAASQHMDLRPATVGQESVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 249 HVLPLHHVHGVINKLLCPLWVGAtCIMLPEFSAqMVWKKFLSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQP---QVQDF 325
Cdd:cd05933 200 SYLPLSHIAAQILDIWLPIKVGG-QVYFAQPDA-LKGTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSgtlKRKIA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 326 VRAF---CQENIRLMVSGSaalPVP---------VLKKWKAITG----HTLL----------------------ERYGMT 367
Cdd:cd05933 278 SWAKgvgLETNLKLMGGES---PSPlfyrlakklVFKKVRKALGldrcQKFFtgaapisretlefflslnipimELYGMS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 368 EigmalSNPLHGVRVPG-----SVGTPLPGVEVRIATEavkgggrsytilaqgDEDGtqmtpglegqEGELLVRGSSVFR 442
Cdd:cd05933 355 E-----TSGPHTISNPQayrllSCGKALPGCKTKIHNP---------------DADG----------IGEICFWGRHVFM 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201832555 443 EYWNRPKETREAFTSDGWFRTGDtAAYHD--GVYWIKGRTSVDIIKNGGFKISALEVERQLLAH-PHITDVAVIG 514
Cdd:cd05933 405 GYLNMEDKTEEAIDEDGWLHSGD-LGKLDedGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
62-550 |
2.81e-21 |
|
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: 97.50 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 62 DKIAIIDQNGEH-----TYRELFCRSLRLSQEICrvlqcsSRDLKEER-ISFLCPNDASYVVAQWASwMSGGIAV----P 131
Cdd:cd05921 10 DRTWLAEREGNGgwrrvTYAEALRQVRAIAQGLL------DLGLSAERpLLILSGNSIEHALMALAA-MYAGVPAapvsP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 132 LY--RKHPVQQLEYVIEDSQSALVIA--AEEYVGKISpSAEKLGVPVLPLGSHSSGS--------AGHTAVEDVPLASSA 199
Cdd:cd05921 83 AYslMSQDLAKLKHLFELLKPGLVFAqdAAPFARALA-AIFPLGTPLVVSRNAVAGRgaisfaelAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 200 SWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKED--VILHVLPLHHVHGVINKLLCPLWVGATCIM-- 275
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIdd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 276 ---LPEFSAQMVwkKFLSSQAPrvSVFMAVPTIYAKLIEYYDEhfsqpqvQDFVRAFCQENIRLMVSGSAALPVPVLKKW 352
Cdd:cd05921 242 gkpMPGGFEETL--RNLREISP--TVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDVWDRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAI----TGH--TLLERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIateaVKGGGRSytilaqgdedgtqmtpgl 426
Cdd:cd05921 311 QALavatVGEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL----VPSGGKY------------------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 egqegELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHD------GVYWiKGRTSVDIIKNGGFKISALEVERQ 500
Cdd:cd05921 369 -----EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADpddpakGLVF-DGRVAEDFKLASGTWVSVGPLRAR 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 501 LLAH--PHITDVAVIGP----------PDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMA 550
Cdd:cd05921 443 AVAAcaPLVHDAVVAGEdraevgalvfPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLA 504
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
51-580 |
5.31e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 96.60 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 51 TPVFTRALTfGDKIAIIDQNGEHTYRELFCRSLRLSQEICRV-LQCSSRDLKEerisflCPNDASYVVAQWAsWMSGGIA 129
Cdd:PRK10946 28 TDILTRHAA-SDAIAVICGERQFSYRELNQASDNLACSLRRQgIKPGDTALVQ------LGNVAEFYITFFA-LLKLGVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 130 vplyrkhPV------QQLE---Y--------VIEDSQSALvIAAEEYVGKISpsAEKLGVPVLPLGSHSSGSAGHTAVED 192
Cdd:PRK10946 100 -------PVnalfshQRSElnaYasqiepalLIADRQHAL-FSDDDFLNTLV--AEHSSLRVVLLLNDDGEHSLDDAINH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 193 --VPLASSASWKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHH--------VHGVink 262
Cdd:PRK10946 170 paEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmsspgALGV--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 263 llcpLWVGATCIMLPEFSAQMVwkkFLSSQAPRVSVFMAVPTIYAKLIEYYDEHFSQPQVQdfvrafcqeNIRLMVSGSA 342
Cdd:PRK10946 247 ----FLAGGTVVLAPDPSATLC---FPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLA---------SLKLLQVGGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 343 ALPVPVLKKWKAITGHTLLERYGMTEiGM----ALSNPlhGVRVPGSVGTPL-PGVEVRIAteavkgggrsytilaqgDE 417
Cdd:PRK10946 311 RLSETLARRIPAELGCQLQQVFGMAE-GLvnytRLDDS--DERIFTTQGRPMsPDDEVWVA-----------------DA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 418 DGTQMTPGlegQEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALE 496
Cdd:PRK10946 371 DGNPLPQG---EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREK-DQINRGGEKIAAEE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 497 VERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRrgEMLSVKELKEWARDT-MAPYAVPTELIVVEEIPRNQMGKVNKK 575
Cdd:PRK10946 447 IENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK--EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKK 524
|
....*
gi 1201832555 576 ELLQR 580
Cdd:PRK10946 525 QLRQW 529
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
74-514 |
1.17e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 96.06 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEIcrvlqcSSRDLKE-ERISFLCPNDASYVVAQWASwMSGGIA-VPLYRKHPVQQLEYVIEDSQSA 151
Cdd:PLN02861 79 TYKEVYDAAIRIGSAI------RSRGVNPgDRCGIYGSNCPEWIIAMEAC-NSQGITyVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 152 LVIAAEEYVGKISPSAEKLGVPVLPLGSHSSGSAGHTAVEDVPLASSASWKDRGAM-----------------IIYTSGT 214
Cdd:PLN02861 152 IAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMgsldcelppkqktdictIMYTSGT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 215 TGRPKGVLSTHENVQA---VTTGLVEKWE--WKKEDVILHVLPLHHVHGVINKLLCpLWVGATCimlpefsaqMVWK--- 286
Cdd:PLN02861 232 TGEPKGVILTNRAIIAevlSTDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI---------GFWQgdi 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 KFL--SSQAPRVSVFMAVPTIYAKL--------------------------IEYYDEHFSQPQVQDFVRAFCQENI---- 334
Cdd:PLN02861 302 RYLmeDVQALKPTIFCGVPRVYDRIytgimqkissggmlrkklfdfaynykLGNLRKGLKQEEASPRLDRLVFDKIkegl 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 335 ----RLMVSGSAALPVPVLKKWKAITGHTLLERYGMTE-IGMALSNPLHGVRVPGSVGTPLPGVEVRIatEAVKGGGRsy 409
Cdd:PLN02861 382 ggrvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARL--ESVPEMGY-- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 410 tilaqgdeDGTQMTPglegqEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRtsvdiiKNG 488
Cdd:PLN02861 458 --------DALSDVP-----RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQpNGAMKIIDR------KKN 517
|
490 500 510
....*....|....*....|....*....|..
gi 1201832555 489 GFKIS-----ALEV-ERQLLAHPHITDVAVIG 514
Cdd:PLN02861 518 IFKLSqgeyvAVENlENTYSRCPLIASIWVYG 549
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
103-488 |
2.02e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 95.18 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 103 ERISFLCPNDASYVVAQWASWMSGGIAVPLYR-KHP--VQQLEYVIEDSQSALVI---AAEEYVGKI---SPSAEKLGVp 173
Cdd:PRK07769 80 DRVAILAPQNLDYLIAFFGALYAGRIAVPLFDpAEPghVGRLHAVLDDCTPSAILtttDSAEGVRKFfraRPAKERPRV- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 174 vlplgshssgsaghTAVEDVPLASSASW------KDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVI 247
Cdd:PRK07769 159 --------------IAVDAVPDEVGATWvppeanEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 248 LHVLPLHHVHGVINKLLCPLWVGATCIMLPefsAQMV-----WKKFLSSQAP-RVSVFMAVPTiyaklieYYDEHFSQPQ 321
Cdd:PRK07769 225 VSWLPFFHDMGLITVLLPALLGHYITFMSP---AAFVrrpgrWIRELARKPGgTGGTFSAAPN-------FAFEHAAARG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 322 V-QDFVRAFCQENIRLMVSGSAALPVPVLKKW-KAITGHTLLER-----YGMTEIGMALS------------------NP 376
Cdd:PRK07769 295 LpKDGEPPLDLSNVKGLLNGSEPVSPASMRKFnEAFAPYGLPPTaikpsYGMAEATLFVSttpmdeeptviyvdrdelNA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 377 LHGVRVPGSVGTPLPGV---EVRIATEAVKGGGRSYTILAqgdedgtqmtpglEGQEGELLVRGSSVFREYWNRPKETRE 453
Cdd:PRK07769 375 GRFVEVPADAPNAVAQVsagKVGVSEWAVIVDPETASELP-------------DGQIGEIWLHGNNIGTGYWGKPEETAA 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 454 AF---------------TSDG--WFRTGDTAAYHDGVYWIKGRTSVDIIKNG 488
Cdd:PRK07769 442 TFqnilksrlseshaegAPDDalWVRTGDYGVYFDGELYITGRVKDLVIIDG 493
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
74-496 |
3.44e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 94.70 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEIcrvLQCSSRDlkEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALV 153
Cdd:PLN02614 81 TYQEVYDIVIKLGNSL---RSVGVKD--EAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 IAAEEYVG---KISPSAEKLGVPVLPLG---------SHSSGSAGHTAVEDVPLASSASW------KDRGAMIIYTSGTT 215
Cdd:PLN02614 156 FVEEKKISelfKTCPNSTEYMKTVVSFGgvsreqkeeAETFGLVIYAWDEFLKLGEGKQYdlpikkKSDICTIMYTSGTT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 216 GRPKGVLSTHENVQAVTTGLVE-----KWEWKKEDVILHVLPLHHVHG-VINKllCPLWVGATcIMLPEFSAQMVWKKfL 289
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDrVIEE--CFIQHGAA-IGFWRGDVKLLIED-L 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 290 SSQAPrvSVFMAVPTI----YAKLIE-----------YYDEHFS-----QPQVQDFVRA--FCQE------------NIR 335
Cdd:PLN02614 312 GELKP--TIFCAVPRVldrvYSGLQKklsdggflkkfVFDSAFSykfgnMKKGQSHVEAspLCDKlvfnkvkqglggNVR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 336 LMVSGSAALPVPVLKKWKAITGHTLLERYGMTE--IGMALSNPlHGVRVPGSVGTPLPGVEVRIATeavkgggrsytiLA 413
Cdd:PLN02614 390 IILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLP-DELDMLGTVGPPVPNVDIRLES------------VP 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 414 QGDEDGTQMTPglegqEGELLVRGSSVFREYWNRPKETREAFTsDGWFRTGDTAAYH-DGVYWIKGRtsvdiiKNGGFKI 492
Cdd:PLN02614 457 EMEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQpNGSMKIIDR------KKNIFKL 524
|
....
gi 1201832555 493 SALE 496
Cdd:PLN02614 525 SQGE 528
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
206-471 |
3.46e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 94.34 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHE---NVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGViNKLLCP-LWVGATCIM-----L 276
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGG-NANFNGlLWGGGTLYIddgkpL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 277 PEFSAQMVwkKFLSSQAPrvSVFMAVPTIYAKLIEYYDehfsqpQVQDFVRAFCQeNIRLMVSGSAALPVPVLKKWKA-- 354
Cdd:PRK12582 302 PGMFEETI--RNLREISP--TVYGNVPAGYAMLAEAME------KDDALRRSFFK-NLRLMAYGGATLSDDLYERMQAla 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 355 --ITGH--TLLERYGMTEIGMALSNPLHGVRVPGSVGTPLPGVEVRIAteavkgggrsytilaqgdedgtqmtPglEGQE 430
Cdd:PRK12582 371 vrTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLA-------------------------P--VGDK 423
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1201832555 431 GELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAYHD 471
Cdd:PRK12582 424 YEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVD 464
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
186-479 |
5.56e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 93.89 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 186 GHTAVEDVPLASSASwKDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKW-----EWKKEDVILHVLPLHHVhgvi 260
Cdd:PTZ00216 248 GHSAGSHHPLNIPEN-NDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCSYLPLAHI---- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 261 nkllcpLWVGATCIMLpefsAQMVWKKFLSsqaPRV-----------------SVFMAVPTIY--------AKL------ 309
Cdd:PTZ00216 323 ------MEFGVTNIFL----ARGALIGFGS---PRTltdtfarphgdltefrpVFLIGVPRIFdtikkaveAKLppvgsl 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 310 ---------------------IEYYDEH-FSQPqvqdfvRAFCQENIRLMVSGSAALPVPVlKKWKAITGHTLLERYGMT 367
Cdd:PTZ00216 390 krrvfdhayqsrlralkegkdTPYWNEKvFSAP------RAVLGGRVRAMLSGGGPLSAAT-QEFVNVVFGMVIQGWGLT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 368 EI----GMALSNPLHgvrvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTPGLEGQeGELLVRGSSVFRE 443
Cdd:PTZ00216 463 ETvccgGIQRTGDLE----PNAVGQLLKGVEMKLL-----------------DTEEYKHTDTPEPR-GEILLRGPFLFKG 520
|
330 340 350
....*....|....*....|....*....|....*..
gi 1201832555 444 YWNRPKETREAFTSDGWFRTGDTAAYH-DGVYWIKGR 479
Cdd:PTZ00216 521 YYKQEELTREVLDEDGWFHTGDVGSIAaNGTLRIIGR 557
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
187-533 |
1.87e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 91.88 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 187 HTAVEDVPLASSASwkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvinkLLCp 266
Cdd:PRK09274 160 DGAAAPFPMADLAP--DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFG----PAL- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 267 lwvGATCImLPEFSAQ---MVWKKFLSSQAPR--VSVFMAVPTIYAKLIEYYDEHFSQpqvqdfvrafcQENIRLMVSGS 341
Cdd:PRK09274 233 ---GMTSV-IPDMDPTrpaTVDPAKLFAAIERygVTNLFGSPALLERLGRYGEANGIK-----------LPSLRRVISAG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 342 AALPVPVLKKWKAITGHT--LLERYGMTE------IGMalSNPLHGVRV-----PGS-VGTPLPGVEVRIateavkgggr 407
Cdd:PRK09274 298 APVPIAVIERFRAMLPPDaeILTPYGATEalpissIES--REILFATRAatdngAGIcVGRPVDGVEVRI---------- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 408 sytiLAQGDEDGTQMTPGLE---GQEGELLVRGSSVFREYWNRPKETREAFTSDG----WFRTGDtAAYHD--GVYWIKG 478
Cdd:PRK09274 366 ----IAISDAPIPEWDDALRlatGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGD-LGYLDaqGRLWFCG 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 479 RTSVDIIKNGG--FKIsalEVERQLLAHPHITDVAVIGPPDVVwGQRVSAVVQLRRG 533
Cdd:PRK09274 441 RKAHRVETAGGtlYTI---PCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPG 493
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
56-564 |
3.46e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 91.09 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAIIDQNGEHTYRELFCRSLRLSqeicRVLQcsSRDLKE-ERISFLCPNDASYVVAqWASWMSGGIAVPLYR 134
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNARANRYA----HWAA--ARGVGKgDVVALLMENRPEYLAA-WLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 135 KHPVQQ-LEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVL-----------PLGSHSSGSAGHTAVEDVPLASSASWK 202
Cdd:PRK08279 119 TQQRGAvLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRlwvaggdtlddPEGYEDLAAAAAGAPTTNPASRSGVTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQ 282
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 283 MVWKKFlssQAPRVSVFMAVptiyAKLIEYYDEHFSQPQVQDfvrafcqENIRLMVsgSAALPVPVLKKWKAITG-HTLL 361
Cdd:PRK08279 279 RFWDDV---RRYRATAFQYI----GELCRYLLNQPPKPTDRD-------HRLRLMI--GNGLRPDIWDEFQQRFGiPRIL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 362 ERYGMTEIGMALSNpLHGV-----RVPGSVGTPLPGVEVRIATEAVKgggRsytilaqgDEDGtQMTPGLEGQEGELL-- 434
Cdd:PRK08279 343 EFYAASEGNVGFIN-VFNFdgtvgRVPLWLAHPYAIVKYDVDTGEPV---R--------DADG-RCIKVKPGEVGLLIgr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 435 VRGSSVFREYwNRPKET-----REAFT-SDGWFRTGDTAAYHDGVY------------WiKGrtsvdiiKNggfkISALE 496
Cdd:PRK08279 410 ITDRGPFDGY-TDPEASekkilRDVFKkGDAWFNTGDLMRDDGFGHaqfvdrlgdtfrW-KG-------EN----VATTE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 497 VERQLLAHPHITDVavigppdVVWGQRVS--------AVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEI 564
Cdd:PRK08279 477 VENALSGFPGVEEA-------VVYGVEVPgtdgragmAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
74-563 |
4.68e-19 |
|
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: 90.98 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSlrlsQEICRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSALV 153
Cdd:cd17632 69 TYAELWERV----GAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 154 IAAEEYVG-KISPSAEKLGVPVL-------PLGSHSSGSAG--------------HTAV----EDVPLAS---SASWKDR 204
Cdd:cd17632 145 AVSAEHLDlAVEAVLEGGTPPRLvvfdhrpEVDAHRAALESarerlaavgipvttLTLIavrgRDLPPAPlfrPEPDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 205 GAMIIYTSGTTGRPKGVLSTHENVqaVTTGLVEKWE---WKKEDVILHVLPLHHVHGViNKLLCPLWVGATcimlpefsA 281
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTERLV--ATFWLKVSSIqdiRPPASITLNFMPMSHIAGR-ISLYGTLARGGT--------A 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 QMVWKKFLSS-----QAPRVSVFMAVPTIYAKLIEYY--------DEHFSQPQVQDFVRAFCQENI---RLM--VSGSAA 343
Cdd:cd17632 294 YFAAASDMSTlfddlALVRPTELFLVPRVCDMLFQRYqaeldrrsVAGADAETLAERVKAELRERVlggRLLaaVCGSAP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 344 LPvPVLKKWKAIT-GHTLLERYGMTEIGMALSNplhgvrvpgsvgtplpGVEVRIATEAVKgggrsytiLAQGDEDGTQM 422
Cdd:cd17632 374 LS-AEMKAFMESLlDLDLHDGYGSTEAGAVILD----------------GVIVRPPVLDYK--------LVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 423 T----PglegqEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGDTAAY--HDGVYWIKGRTSVDIIKNGGF-KISAL 495
Cdd:cd17632 429 TdrphP-----RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAElgPDRLVYVDRRNNVLKLSQGEFvTVARL 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201832555 496 E-------VERQLLAHPHITD---VAVIGPPDVVWGQRVSAVVQLRRGEmlsvkELKEWARDT-MAPYAVPTELIVVEE 563
Cdd:cd17632 504 EavfaaspLVRQIFVYGNSERaylLAVVVPTQDALAGEDTARLRAALAE-----SLQRIAREAgLQSYEIPRDFLIETE 577
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
56-479 |
1.35e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 56 RALTFGDKIAI---IDQNGEH---TYRELFCRSlrlsQEICRVLQcsSRDLKEERISFLCPNDASYVVAQWASWMSGGIA 129
Cdd:PRK05691 18 RAAQTPDRLALrflADDPGEGvvlSYRDLDLRA----RTIAAALQ--ARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 130 VPLY-----RKHPVQQLEYVIEDSQSALVIaaeeyvgkispSAEKLGVPVLPLGSHSSGSA-GHTAVEDVPLASSASWK- 202
Cdd:PRK05691 92 VPAYppesaRRHHQERLLSIIADAEPRLLL-----------TVADLRDSLLQMEELAAANApELLCVDTLDPALAEAWQe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 -----DRGAMIIYTSGTTGRPKGVLSTHENVQAVttglvekwEW----------KKEDVILHVLPLHHVHGVINKLLCPL 267
Cdd:PRK05691 161 palqpDDIAFLQYTSGSTALPKGVQVSHGNLVAN--------EQlirhgfgidlNPDDVIVSWLPLYHDMGLIGGLLQPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 268 WVGATCI-MLPEFsaqmvwkkflssqaprvsvFMAVPTIYAKLIEYYDEHFS-QPqvqDFVRAFCQENI----------- 334
Cdd:PRK05691 233 FSGVPCVlMSPAY-------------------FLERPLRWLEAISEYGGTISgGP---DFAYRLCSERVsesalerldls 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 335 --RLMVSGSAALPVPVLKKWK------AITGHTLLERYGMTEIGMALSNPLHGVRVP------------------GSV-- 386
Cdd:PRK05691 291 rwRVAYSGSEPIRQDSLERFAekfaacGFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtGSVlm 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 387 --GTPLPGVEVRIAtEAVKGGGRSytilaqgdedgtqmtpglEGQEGELLVRGSSVFREYWNRPKETREAFTS-DG--WF 461
Cdd:PRK05691 371 scGRSQPGHAVLIV-DPQSLEVLG------------------DNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWL 431
|
490
....*....|....*...
gi 1201832555 462 RTGDTAAYHDGVYWIKGR 479
Cdd:PRK05691 432 RTGDLGFLRDGELFVTGR 449
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
496-571 |
1.51e-18 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 80.28 E-value: 1.51e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201832555 496 EVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGK 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
206-573 |
2.14e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 89.64 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPefSA---- 281
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP--SPlhyr 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 ---QMVWK----------KFLSSqaprvsvfmavptiYAKLIEYYDehfsqpqvqdFVRafcqenIRLMVSGSAALPVPV 348
Cdd:PRK06814 874 iipELIYDtnatilfgtdTFLNG--------------YARYAHPYD----------FRS------LRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 349 LKKWKAITGHTLLERYGMTEIG--MALSNPLHGVrvPGSVGTPLPGVEVRIatEAVKG---GGRsytilaqgdedgtqmt 423
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRL--EPVPGideGGR---------------- 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 424 pglegqegeLLVRGSSVFREYW--NRPKETREAftSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVErQ 500
Cdd:PRK06814 984 ---------LFVRGPNVMLGYLraENPGVLEPP--ADGWYDTGDIVTIdEEGFITIKGRAK-RFAKIAGEMISLAAVE-E 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 501 LLAHphitdvavigppdvVWGQRVSAVVQL---RRGEML---------SVKELKEWARDTMAP-YAVPTELIVVEEIPRN 567
Cdd:PRK06814 1051 LAAE--------------LWPDALHAAVSIpdaRKGERIillttasdaTRAAFLAHAKAAGASeLMVPAEIITIDEIPLL 1116
|
....*.
gi 1201832555 568 QMGKVN 573
Cdd:PRK06814 1117 GTGKID 1122
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-552 |
3.07e-18 |
|
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: 87.52 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 193 VPLAssaswkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHhvhgvinKLLCPLwVGAT 272
Cdd:cd05910 81 IPKA------DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPA-LGLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 273 CImLPEFSAqmvwkkflsSQAPRVSvfmavPtiyAKLIEYYDEH-----FSQPQVQDFVRAFCQEN------IRLMVSGS 341
Cdd:cd05910 147 SV-IPDMDP---------TRPARAD-----P---QKLVGAIRQYgvsivFGSPALLERVARYCAQHgitlpsLRRVLSAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 342 AALPVPVLKKWKAITGHT--LLERYGMTE---IGMALSNPLHGVRVPGS-------VGTPLPGVEVRIaTEAVKGGGRSY 409
Cdd:cd05910 209 APVPIALAARLRKMLSDEaeILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRI-IEIDDEPIAEW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 410 tilaqgdeDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAFTSDG----WFRTGDTAAYHD-GVYWIKGRTSVDI 484
Cdd:cd05910 288 --------DDTLELP--RGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRV 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 485 IKNGGfKISALEVERQLLAHPHITDVAVIGPPDVVwGQRVSAVVQLRRGEMLSVKELKEWARDTMAPY 552
Cdd:cd05910 358 ITTGG-TLYTEPVERVFNTHPGVRRSALVGVGKPG-CQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
72-577 |
7.49e-18 |
|
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: 86.72 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELFCRSLRLSQEICRvLQCSSRDLkeerISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDSQSA 151
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRA-LGVGVGDR----VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 152 LVIAAEEYvgkISPSAEKLGVpVLPLGSHSSGSAGHTAVEDVPLASSASWK-----DRGAMII--YTSGTTGRPKGVLST 224
Cdd:cd05915 99 VLLFDPNL---LPLVEAIRGE-LKTVQHFVVMDEKAPEGYLAYEEALGEEAdpvrvPERAACGmaYTTGTTGLPKGVVYS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 225 HEN--VQAVTTGLVEKWEWKKEDVILHVLPLHHVHGvinklLCPLWV----GATCIMLPEFSAQMVWkkFLSSQAPRVSV 298
Cdd:cd05915 175 HRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGPRLDPASL--VELFDGEGVTF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 299 FMAVPTIYAKLieyydehfsqPQVQDFVRAFCQENIRLMVSGSAalPVPVLKKWKAITGHTLLERYGMTEIgmalsnplH 378
Cdd:cd05915 248 TAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRSLIARFERMGVEVRQGYGLTET--------S 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 379 GVrvpGSVGTPLPGVEVRIATEAVKGGGR---SYTILAQGDEDGTQMTPGLEGQEGELL-VRGSSVFREYWNRPKETREA 454
Cdd:cd05915 308 PV---VVQNFVKSHLESLSEEEKLTLKAKtglPIPLVRLRVADEEGRPVPKDGKALGEVqLKGPWITGGYYGNEEATRSA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 455 FTSDGWFRTGDTAAYH-DGVYWIKGRtSVDIIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRG 533
Cdd:cd05915 385 LTPDGFFRTGDIAVWDeEGYVEIKDR-LKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1201832555 534 EMLSvKELKEWARDTMAPYA-VPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05915 464 KPTP-EELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
74-547 |
3.45e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 85.25 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFcrslrlsQEicrVLQCSS--RDLKEE---RISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEYVIEDS 148
Cdd:PLN02430 78 TYKEVY-------EE---VLQIGSalRASGAEpgsRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 149 QSALVIAAEEYV-GKISP---SAEKLG--VPVLPLGSHSSGSAGHTAVEdvplasSASWKDRGAM--------------- 207
Cdd:PLN02430 148 EIDFVFVQDKKIkELLEPdckSAKRLKaiVSFTSVTEEESDKASQIGVK------TYSWIDFLHMgkenpsetnppkpld 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 ---IIYTSGTTGRPKGVLSTHENVQAVTTGL---VEKWEWK--KEDVILHVLPLHHV-------------------HGVI 260
Cdd:PLN02430 222 ictIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFEDKmtHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 261 NKL------LCPLWVGATCIMLPEFSAQMvwKKFLSSQAP-RVSVFMAvptIYAKLIEYYDEHFSQPQVQDF-------- 325
Cdd:PLN02430 302 NALrddlmeLKPTLLAGVPRVFERIHEGI--QKALQELNPrRRLIFNA---LYKYKLAWMNRGYSHKKASPMadflafrk 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 326 VRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEI--GMALSNPLHGVRVpGSVGTPLPGVEVRIateavk 403
Cdd:PLN02430 377 VKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFPDEMCML-GTVGAPAVYNELRL------ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 404 gggrsytilaqgdEDGTQM--TPGLEGQEGELLVRGSSVFREYWNRPKETREAFtSDGWFRTGDTAAYH-DGVYWIKGRT 480
Cdd:PLN02430 450 -------------EEVPEMgyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILpNGVLKIIDRK 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201832555 481 SvDIIKNGGFKISALE-VERQLLAHPHITDVAVIGppDVVWGQRVSAVVqlrrgemLSVKELKEWARD 547
Cdd:PLN02430 516 K-NLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG--DSFKSMLVAVVV-------PNEENTNKWAKD 573
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
190-577 |
3.75e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 84.95 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 190 VEDVPLASSASWKDRG--AMIIYTSGTTGRPKGVLSTHENVQAVT-TGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCP 266
Cdd:PLN02654 260 VPNYPTKCEVEWVDAEdpLFLLYTSGSTGKPKGVLHTTGGYMVYTaTTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 267 LWVGATCIML---PEF-SAQMVWK---KFlssqapRVSVFMAVPTIYAKLIEYYDEhfsqpqvqdFVRAFCQENIRLMvs 339
Cdd:PLN02654 340 MLNGATVLVFegaPNYpDSGRCWDivdKY------KVTIFYTAPTLVRSLMRDGDE---------YVTRHSRKSLRVL-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 340 GSAALPV-PVLKKW-KAITGHT---LLERYGMTEIGMALSNPLHGV--RVPGSVGTPLPGVEVRIAteavkgggrsytil 412
Cdd:PLN02654 403 GSVGEPInPSAWRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIV-------------- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 413 aqgDEDGTQMtpglEGQ-EGELLVRGS--SVFREYWNRPK--ETREAFTSDGWFRTGDTAAY-HDGVYWIKGRTSvDIIK 486
Cdd:PLN02654 469 ---DEKGKEI----EGEcSGYLCVKKSwpGAFRTLYGDHEryETTYFKPFAGYYFSGDGCSRdKDGYYWLTGRVD-DVIN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 487 NGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLSV---KELKEWARDTMAPYAVPTELIVVEE 563
Cdd:PLN02654 541 VSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEelrKSLILTVRNQIGAFAAPDKIHWAPG 620
|
410
....*....|....
gi 1201832555 564 IPRNQMGKVNKKEL 577
Cdd:PLN02654 621 LPKTRSGKIMRRIL 634
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
190-558 |
9.51e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 83.00 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 190 VEDVPLASSASWK-DRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGV-InkllcpL 267
Cdd:PRK09029 121 LQLVEGAHAVAWQpQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQgI------V 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 268 W----VGATcIMLPEFS--AQMVwkkflsSQAPRVSVfmaVPTIYAKLIEYYDEHFSQPQVqdfvrafcqenirLMvsGS 341
Cdd:PRK09029 195 WrwlyAGAT-LVVRDKQplEQAL------AGCTHASL---VPTQLWRLLDNRSEPLSLKAV-------------LL--GG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 342 AALPvpvlkkwkaitgHTLLER-----------YGMTEigMAlsNPLHGVRVPGS--VGTPLPGVEVRIAteavkgggrs 408
Cdd:PRK09029 250 AAIP------------VELTEQaeqqgircwcgYGLTE--MA--STVCAKRADGLagVGSPLPGREVKLV---------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 409 ytilaqgdedgtqmtpglegqEGELLVRGSSVFREYWnRPKETREAFTSDGWFRTGDTAAYHDGVYWIKGRtsvdiIKN- 487
Cdd:PRK09029 304 ---------------------DGEIWLRGASLALGYW-RQGQLVPLVNDEGWFATRDRGEWQNGELTILGR-----LDNl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 488 ---GGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEmlSVKELKEWARDTMA----P---YAVPTE 557
Cdd:PRK09029 357 ffsGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEA--AVVNLAEWLQDKLArfqqPvayYLLPPE 434
|
.
gi 1201832555 558 L 558
Cdd:PRK09029 435 L 435
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
150-555 |
1.05e-16 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 83.11 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 150 SALVIAAE--EYVGKISPSAEKLGVPVLPLGSHSS-------GSAGHTAVED-VP--LASSASWKDRgAMIIYTSGTTGR 217
Cdd:cd05938 80 KVLVVAPElqEAVEEVLPALRADGVSVWYLSHTSNtegvislLDKVDAASDEpVPasLRAHVTIKSP-ALYIYTSGTTGL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 218 PKGVLSTHENVQAVTtGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKkflSSQAPRVS 297
Cdd:cd05938 159 PKAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD---DCRKHNVT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 298 VFMAVptiyAKLIEYYdehFSQPQ-VQDfvrafCQENIRLMVsGSaALPVPVLKKWKAITGHT-LLERYGMTEIGMALSN 375
Cdd:cd05938 235 VIQYI----GELLRYL---CNQPQsPND-----RDHKVRLAI-GN-GLRADVWREFLRRFGPIrIREFYGSTEGNIGFFN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 376 PlhgVRVPGSVG---------TPLPGVEVRIAT-EAVKgggrsytilaqgDEDGTQMTPGLeGQEGELL--VRGSSVFRE 443
Cdd:cd05938 301 Y---TGKIGAVGrvsylykllFPFELIKFDVEKeEPVR------------DAQGFCIPVAK-GEPGLLVakITQQSPFLG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 444 YWNRPKET-----REAFTS-DGWFRTGDT-AAYHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPP 516
Cdd:cd05938 365 YAGDKEQTekkllRDVFKKgDVYFNTGDLlVQDQQNFLYFHDRVG-DTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1201832555 517 dvVWGQ--RVS-AVVQLRRGEMLSVKELKEWARDTMAPYAVP 555
Cdd:cd05938 444 --VPGHegRIGmAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
75-531 |
5.58e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 81.20 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 75 YRELFCRSLRLSqeiCRVLqcsSRDLK-EERISFLCPNDASYVVAQWASWMSGGIAVPLY-------RKHPVQQLEYVIE 146
Cdd:PRK09192 52 YQTLRARAEAGA---RRLL---ALGLKpGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 147 DSQSALVIAAEEYVGKISPSAEklGVPVLPLGSHSSGSAGHTAVEDVPLASsaswKDRGAMIIYTSGTTGRPKGVLSTHE 226
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEATH--GNPLLHVLSHAWFKALPEADVALPRPT----PDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 227 ----NVQAVT-TGLvekwEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP--EFSAQ-MVWKKFLSSQAPRVSV 298
Cdd:PRK09192 200 almaNLRAIShDGL----KVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFARRpLQWLDLISRNRGTISY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 299 fmaVPTIYAKL---------IEYYD-----------EHFSQPQVQDFVRAFCQENIR---LMVS---GSAALPVPVLKKW 352
Cdd:PRK09192 276 ---SPPFGYELcarrvnskdLAELDlscwrvagigaDMIRPDVLHQFAEAFAPAGFDdkaFMPSyglAEATLAVSFSPLG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAITGHTLlERYGMTEIGMALSNPLHGVRVPGSV--GTPLPGVEVRIAteavkgggrsytilaqgDEDGTQMTpglEGQE 430
Cdd:PRK09192 353 SGIVVEEV-DRDRLEYQGKAVAPGAETRRVRTFVncGKALPGHEIEIR-----------------NEAGMPLP---ERVV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 431 GELLVRGSSVFREYWNRPkETREAFTSDGWFRTGDTAAYHDGVYWIKGRTSVDIIKNGGfKISALEVERQLLAHP--HIT 508
Cdd:PRK09192 412 GHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIINGR-NIWPQDIEWIAEQEPelRSG 489
|
490 500
....*....|....*....|...
gi 1201832555 509 DVAVIGPPDVVwGQRVSAVVQLR 531
Cdd:PRK09192 490 DAAAFSIAQEN-GEKIVLLVQCR 511
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
72-488 |
6.87e-16 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 80.94 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 72 EHTYRELfcrSLRLSQEICRVLQCSSRDlkeERISFLCPNDASYVVAQWASWMSGGIAVPLYRK----HpVQQLEYVIED 147
Cdd:PRK12476 68 ELTWTQL---GVRLRAVGARLQQVAGPG---DRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgH-AERLDTALRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 148 SQSALVI---AAEEYVGKISPSAEKLGVPVLplgshssgsaghTAVEDVPLASSASWK------DRGAMIIYTSGTTGRP 218
Cdd:PRK12476 141 AEPTVVLtttAAAEAVEGFLRNLPRLRRPRV------------IAIDAIPDSAGESFVpveldtDDVSHLQYTSGSTRPP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 219 KGVLSTHenvQAVTTGLVEkwewkkedVILHV------------LPLHHVHGVINKLLCPLWVGATCIMLPefsAQMV-- 284
Cdd:PRK12476 209 VGVEITH---RAVGTNLVQ--------MILSIdlldrnthgvswLPLYHDMGLSMIGFPAVYGGHSTLMSP---TAFVrr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 285 ---WKKFLSSQAPRVSVFMAVPTiYAklIEYYDEHFSQPQvqdfvrafcQENIRL----MVSGSAALPVPVLKKWKAITG 357
Cdd:PRK12476 275 pqrWIKALSEGSRTGRVVTAAPN-FA--YEWAAQRGLPAE---------GDDIDLsnvvLIIGSEPVSIDAVTTFNKAFA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 358 HTLLER------YGMTEIGMALSNPL------------------HGVRVPGsvGTPLPGVEVRIATEAvkgggRS-YTIL 412
Cdd:PRK12476 343 PYGLPRtafkpsYGIAEATLFVATIApdaepsvvyldreqlgagRAVRVAA--DAPNAVAHVSCGQVA-----RSqWAVI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 413 AqgDEDGTQMTPglEGQEGELLVRGSSVFREYWNRPKETREAF------------------TSDGWFRTGDTAAYHDGVY 474
Cdd:PRK12476 416 V--DPDTGAELP--DGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLDGEL 491
|
490
....*....|....
gi 1201832555 475 WIKGRTSVDIIKNG 488
Cdd:PRK12476 492 YITGRIADLIVIDG 505
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
203-577 |
1.77e-15 |
|
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: 79.01 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGV-LSTHENVqaVTTGLVEKW-EWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFS 280
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAaISWRRTL--VTSNLLSHDlNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 281 AQMVWKKFLSSQAPRV-------SVFMAVPtiyaklIEYYDEhfsqpqvqdfvrafcQENIRlMVSGSAALPvpvlKKWK 353
Cdd:cd05937 165 ASQFWKDVRDSGATIIqyvgelcRYLLSTP------PSPYDR---------------DHKVR-VAWGNGLRP----DIWE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 354 AITghtllERYGMTEIGmalsnplhgvrvpgsvgtplpgvEVRIATEAV-------KGG------GRSYTILA---QGDE 417
Cdd:cd05937 219 RFR-----ERFNVPEIG-----------------------EFYAATEGVfaltnhnVGDfgagaiGHHGLIRRwkfENQV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 418 DGTQMTPGLE----------------GQEGELLVR----GSSVFREYWNRPKET-----REAF-TSDGWFRTGDTA-AYH 470
Cdd:cd05937 271 VLVKMDPETDdpirdpktgfcvrapvGEPGEMLGRvpfkNREAFQGYLHNEDATesklvRDVFrKGDIYFRTGDLLrQDA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 471 DGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIG---PPDVvwGQRVSAVVQLRRGEMLSV----KELKE 543
Cdd:cd05937 351 DGRWYFLDRLG-DTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHD--GRAGCAAITLEESSAVPTeftkSLLAS 427
|
410 420 430
....*....|....*....|....*....|....
gi 1201832555 544 WARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05937 428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
122-577 |
3.48e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.44 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 122 SWMSGGIAVPLYRKHPVQQLEYVIEDSQSALVIAAEEYVGKISPSAEKLGVPVLPL-----GSHSSGSAGHTavedvPLA 196
Cdd:PRK05691 3790 SFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCANRPRllvweEVQAGEVASHN-----PGI 3864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 197 SSASwkDRGAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWvGATCIML 276
Cdd:PRK05691 3865 YSGP--DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIV 3941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 277 PEFSAQMVWKKFLSSQAPRVSVFMAVPTIYAKLIEyydehfSQPQVQDfvrafcqeNIRLMVSGSAALPVPVLKKWkait 356
Cdd:PRK05691 3942 PNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLA------EDRQALD--------GLRWMLPTGEAMPPELARQW---- 4003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 357 ghtlLERYgmTEIGMA-------LSNPLHGVRV--PGSVGTPLPgvevrIATEAvkGGGRSYTIlaqgdEDGTQMTPglE 427
Cdd:PRK05691 4004 ----LQRY--PQIGLVnaygpaeCSDDVAFFRVdlASTRGSYLP-----IGSPT--DNNRLYLL-----DEALELVP--L 4063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 428 GQEGELLVRGSSVFREYWNRPKETREAFTSDGW-------FRTGDTAAYH-DGVYWIKGRtsVD-IIKNGGFKISALEVE 498
Cdd:PRK05691 4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRsDGVLEYVGR--IDhQVKIRGYRIELGEIE 4141
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 499 RQLLAHPHITDVAVI---GPP-DVVWGQRVSAVVQLRRGEMLsvKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNK 574
Cdd:PRK05691 4142 ARLHEQAEVREAAVAvqeGVNgKHLVGYLVPHQTVLAQGALL--ERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219
|
...
gi 1201832555 575 KEL 577
Cdd:PRK05691 4220 KAL 4222
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
206-577 |
2.29e-14 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 75.59 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCpLWVGATCIMLPEfSAQMVW 285
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKFLSS--QAPRVSVFMAVPTIYaklieyydEHFSQPQVQDFVRAfCQENIRLMVSGSAALPVPV-LKKWKAITGHT-LL 361
Cdd:cd17654 199 SKLADIlfKRHRITVLQATPTLF--------RRFGSQSIKSTVLS-ATSSLRVLALGGEPFPSLViLSSWRGKGNRTrIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 362 ERYGMTEIGM-ALSNPLHGVRVPGSVGTPLPGVEVRIATEAvkgggrsytilaqgdedgtqmtpGLEGQeGELLVRGSS- 439
Cdd:cd17654 270 NIYGITEVSCwALAYKVPEEDSPVQLGSPLLGTVIEVRDQN-----------------------GSEGT-GQVFLGGLNr 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 440 --VFREYWNRPKETreaftsdgWFRTGDTAAYHDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAvigppd 517
Cdd:cd17654 326 vcILDDEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCA------ 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 518 vVWGQRVSAVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd17654 391 -VTLSDQQRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
206-577 |
7.13e-14 |
|
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: 73.93 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVW 285
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFW 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKFLSSQAprvSVFMAVptiyAKLIEYYdehFSQPQVQDfVRAfcqENIRlMVSGSAALPvPVLKKWKAITG-HTLLERY 364
Cdd:cd05940 164 DDIRKYQA---TIFQYI----GELCRYL---LNQPPKPT-ERK---HKVR-MIFGNGLRP-DIWEEFKERFGvPRIAEFY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 365 GMTEIGMALSNPLhgvRVPGSVGTPLPGVEVRIATEAVKGGGRSYTILAqgDEDGtQMTPGLEGQEGELLVRGSSV--FR 442
Cdd:cd05940 228 AATEGNSGFINFF---GKPGAIGRNPSLLRKVAPLALVKYDLESGEPIR--DAEG-RCIKVPRGEPGLLISRINPLepFD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 443 EYWNRPKET----REAFTS-DGWFRTGDTAAYHDGVYW-IKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAVIGPP 516
Cdd:cd05940 302 GYTDPAATEkkilRDVFKKgDAWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201832555 517 DVVWGQRVS-AVVQLRRGEMLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05940 381 VPGTDGRAGmAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDL 442
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
203-565 |
2.49e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.82 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 203 DRGAMIIYTSGTTGRPKGVLSTHE----NVQAVTTGLvekwEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLP- 277
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKsllaNVEQIKTIA----DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPs 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 ----EFSAQMVWKKflssqapRVSVFMAVPTI---YAKlieyydehFSQPqvQDFVRafcqenIRLMVSGSAALPVPVLK 350
Cdd:PRK08043 441 plhyRIVPELVYDR-------NCTVLFGTSTFlgnYAR--------FANP--YDFAR------LRYVVAGAEKLQESTKQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 351 KWKAITGHTLLERYGMTEIGmalsnPLHGVRVP-----GSVGTPLPGVEVRIATeavkgggrsytilaqgdedgtqmTPG 425
Cdd:PRK08043 498 LWQDKFGLRILEGYGVTECA-----PVVSINVPmaakpGTVGRILPGMDARLLS-----------------------VPG 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 426 LEgQEGELLVRGSSVFREYW--NRP-------KETREAFTSDGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKISaL 495
Cdd:PRK08043 550 IE-QGGRLQLKGPNIMNGYLrvEKPgvlevptAENARGEMERGWYDTGDIVRFDEqGFVQIQGRAK-RFAKIAGEMVS-L 626
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201832555 496 EVERQL--LAHPHITDVAVIGPPdvvwGQRVSAVVQLRRGEMLSVKELKEWARDTMAP-YAVPTELIVVEEIP 565
Cdd:PRK08043 627 EMVEQLalGVSPDKQHATAIKSD----ASKGEALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
206-516 |
6.51e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.39 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVinkllcplwvgATCIMLPEFSAQMVw 285
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGF-----------NSCTLFPLLSGVPV- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 kkflssqaprvsVFMAVPTIYAKLIEYYDEHF-----SQPQVQDFV------RAFCQENIRLMVSGSAALPVPVLKKWKA 354
Cdd:PRK06334 254 ------------VFAYNPLYPKKIVEMIDEAKvtflgSTPVFFDYIlktakkQESCLPSLRFVVIGGDAFKDSLYQEALK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 355 ITGH-TLLERYGMTEIGMALS-NPLHGVRVPGSVGTPLPGVEVRIATEAVKgggrsytilaqgdedgtqmTPGLEGQEGE 432
Cdd:PRK06334 322 TFPHiQLRQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEETK-------------------VPVSSGETGL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 433 LLVRGSSVFREYW-NRPKETREAFTSDGWFRTGDTaAYHD--GVYWIKGRTSvDIIKNGGFKISALEVERQLLAH----- 504
Cdd:PRK06334 383 VLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDL-GYVDrhGELFLKGRLS-RFVKIGAEMVSLEALESILMEGfgqna 460
|
330
....*....|...
gi 1201832555 505 -PHITDVAVIGPP 516
Cdd:PRK06334 461 aDHAGPLVVCGLP 473
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
206-581 |
1.75e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.15 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 206 AMIIYTSGTTGRPKGVLSTHENVQAVTTG---LVEKWEwkKEDVILHVLPLHHVHGVINKLLCpLWVGA-----TCIMLP 277
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGvmtVVPKLG--KNDVYLAYLPLAHILELAAESVM-AAVGAaigygSPLTLT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 278 EFSAQMvwKKFLSSQAP--RVSVFMAVPTIY------------------AKLIEY-YDEHFS------------QPQVQD 324
Cdd:PLN02387 330 DTSNKI--KKGTKGDASalKPTLMTAVPAILdrvrdgvrkkvdakgglaKKLFDIaYKRRLAaiegswfgawglEKLLWD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 325 F-----VRAFCQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEI--GMALSNPlHGVRVpGSVGTPLPgvevri 397
Cdd:PLN02387 408 AlvfkkIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETcaGATFSEW-DDTSV-GRVGPPLP------ 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 398 ateavkgggRSYTILAQGDEDGTQMT----PglegqEGELLVRGSSVFREYWNRPKETREAFTSDG----WFRTGDTAAY 469
Cdd:PLN02387 480 ---------CCYVKLVSWEEGGYLISdkpmP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQF 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 470 H-DGVYWIKGRTSvDIIK-NGGFKISALEVERQLLAHPHITDVAVIGPPdvVWGQRVSAVVQlrrgemlSVKELKEWARD 547
Cdd:PLN02387 546 HpDGCLEIIDRKK-DIVKlQHGEYVSLGKVEAALSVSPYVDNIMVHADP--FHSYCVALVVP-------SQQALEKWAKK 615
|
410 420 430
....*....|....*....|....*....|....*...
gi 1201832555 548 TMAPYAVPTELI----VVEEIpRNQMGKVNKKELLQRF 581
Cdd:PLN02387 616 AGIDYSNFAELCekeeAVKEV-QQSLSKAAKAARLEKF 652
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
55-499 |
8.92e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 67.71 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 55 TRALTFGDkiaiIDQNGEHTYRELFCRSLRLSqeicrvlqcssRDLKEERISflcPNDASYVVA----------QwASWM 124
Cdd:PRK07768 16 PRGMVTGE----PDAPVRHTWGEVHERARRIA-----------GGLAAAGVG---PGDAVAVLAgapveiaptaQ-GLWM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 125 SGGIAVPLYRKHPVQQLEYVIEDS-------QSALVIAAEEYVGkISPSAEKLGVPVLPLGShssgSAGHTAVEDVPLAS 197
Cdd:PRK07768 77 RGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAKAVVVGEPFLA-AAPVLEEKGIRVLTVAD----LLAADPIDPVETGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 198 SASwkdrgAMIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKE-DVILHVLPLHHVHGVINKLLCPLWVGAT--CI 274
Cdd:PRK07768 152 DDL-----ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAElvKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 275 MLPEFSAQ-MVWKKFLSSQapRVSVfMAVP----TIYAKLIEYYDEHFS-------------QPQVQDFVRAFCQENIRL 336
Cdd:PRK07768 227 TPMDFLRDpLLWAELISKY--RGTM-TAAPnfayALLARRLRRQAKPGAfdlsslrfalngaEPIDPADVEDLLDAGARF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 337 MVSGSAALPVpvlkkwkaitghtllerYGMTEIGMALS-----NPL------------HGVRVPG---------SVGTPL 390
Cdd:PRK07768 304 GLRPEAILPA-----------------YGMAEATLAVSfspcgAGLvvdevdadllaaLRRAVPAtkgntrrlaTLGPPL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 391 PGVEVRIAteavkgggrsytilaqgDEDGTQMTPgleGQEGELLVRGSSVFREYW--NRPKETREAftsDGWFRTGDTaA 468
Cdd:PRK07768 367 PGLEVRVV-----------------DEDGQVLPP---RGVGVIELRGESVTPGYLtmDGFIPAQDA---DGWLDTGDL-G 422
|
490 500 510
....*....|....*....|....*....|...
gi 1201832555 469 Y--HDGVYWIKGRTSvDIIKNGGFKISALEVER 499
Cdd:PRK07768 423 YltEEGEVVVCGRVK-DVIIMAGRNIYPTDIER 454
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
74-479 |
1.04e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 61.11 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 74 TYRELFCRSLRLSQEICRVlqCSSRDlkeeRISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQLEY---VIEDSQS 150
Cdd:PRK05850 37 TWSQLYRRTLNVAEELRRH--GSTGD----RAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERvsaVLRDTSP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 151 ALVI---AAEEYVGKispsaeklgvpvlpLGSHSSGSAGHTAVE------DVPLASSASWKDR--GAMIIYTSGTTGRPK 219
Cdd:PRK05850 111 SVVLttsAVVDDVTE--------------YVAPQPGQSAPPVIEvdlldlDSPRGSDARPRDLpsTAYLQYTSGSTRTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 220 GVLSTHENVQAVTTGLVEKWEWKKEDV------ILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFS--------AQMVW 285
Cdd:PRK05850 177 GVMVSHRNVIANFEQLMSDYFGDTGGVpppdttVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAflqrparwMQLLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 286 KKFLS-SQAPRVSVFMAVPTIYAKLIEYYD-----------EHFSQPQVQDFVRAFCQENIR-LMVSGSAALPVPVLKKW 352
Cdd:PRK05850 257 SNPHAfSAAPNFAFELAVRKTSDDDMAGLDlggvlgiisgsERVHPATLKRFADRFAPFNLReTAIRPSYGLAEATVYVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 353 KAITGHTLLERYGMTEigmALSNPlHGVRVPGSVGTPLP--GV----EVRIAteavkgggrsytilaqgdeDGTQMTPGL 426
Cdd:PRK05850 337 TREPGQPPESVRFDYE---KLSAG-HAKRCETGGGTPLVsyGSprspTVRIV-------------------DPDTCIECP 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201832555 427 EGQEGELLVRGSSVFREYWNRPKETREAF----------TSDG-WFRTGDTAAYHDGVYWIKGR 479
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
211-499 |
6.13e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 58.62 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 211 TSGTTGRPKGVLSTHENVQAVTTGLVEKWEW-KKEDVILHVLPLHHVHGVINkLLCPLWVGATCIMLPE--FSAQ-MVWK 286
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLdAATDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTtaFSASpFRWL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 287 KFLS-SQAprvsVFMAVPTIYAKLIEYYDEHFS--------------QPQVQDFVRAFCQENIRLMVSGSAALPvpvlkk 351
Cdd:PRK05851 239 SWLSdSRA----TLTAAPNFAYNLIGKYARRVSdvdlgalrvalnggEPVDCDGFERFATAMAPFGFDAGAAAP------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 352 wkaitghtlleRYGMTEIGMALSNPLHGV---------------RVPGSVGTPLPGVEVRIATeavkgggrsytilaqGD 416
Cdd:PRK05851 309 -----------SYGLAESTCAVTVPVPGIglrvdevttddgsgaRRHAVLGNPIPGMEVRISP---------------GD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 417 EDgtqmtPGLEGQE-GELLVRGSSVFREYWNRPketreAFTSDGWFRTGDTAAYHDGVYWIKGRTSvDIIKNGGFKISAL 495
Cdd:PRK05851 363 GA-----AGVAGREiGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPT 431
|
....
gi 1201832555 496 EVER 499
Cdd:PRK05851 432 EIER 435
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
209-577 |
1.35e-08 |
|
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: 57.43 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 209 IYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPEFSAQMVWKKF 288
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDC 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 289 LSSQAprvsvfmavpTIyaklIEYYDEHFSQPQVQDFVRAFCQENIRLMVsGSAALPvpvlKKWKAITGH----TLLERY 364
Cdd:cd05939 190 VKYNC----------TI----VQYIGEICRYLLAQPPSEEEQKHNVRLAV-GNGLRP----QIWEQFVRRfgipQIGEFY 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 365 GMTEIGMALSNPLHGVRVPGSVGTPLPGV-EVRIateaVKGGgrSYTILAQGDEDGTqMTPGLEGQEGELLVR-----GS 438
Cdd:cd05939 251 GATEGNSSLVNIDNHVGACGFNSRILPSVyPIRL----IKVD--EDTGELIRDSDGL-CIPCQPGEPGLLVGKiiqndPL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 439 SVFREYWNR----PKETREAFTS-DGWFRTGDTAAYHD-GVYWIKGRTSvDIIKNGGFKISALEVERQLLAHPHITDVAV 512
Cdd:cd05939 324 RRFDGYVNEgatnKKIARDVFKKgDSAFLSGDVLVMDElGYLYFKDRTG-DTFRWKGENVSTTEVEGILSNVLGLEDVVV 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 513 IGP--PDVVWGQRVSAVVQLRRGemLSVKELKEWARDTMAPYAVPTELIVVEEIPRNQMGKVNKKEL 577
Cdd:cd05939 403 YGVevPGVEGRAGMAAIVDPERK--VDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
208-465 |
9.90e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 51.64 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHV--LPLHHVHGVINKLLCPL-------W---------- 268
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLsyLPISHIYERVIAYLSFMlggtiniWskdinyfskd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 269 ---------VGA--------TCIM-----LPEFSAQMVwKKFLSSqapRVSVFMAVptiYAKLIEYYdEHFSQpQVQDFV 326
Cdd:PTZ00342 389 iynskgnilAGVpkvfnriyTNIMteinnLPPLKRFLV-KKILSL---RKSNNNGG---FSKFLEGI-THISS-KIKDKV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 327 rafcQENIRLMVSGSAALPVPVLKKWKAITGHTLLERYGMTEIGMALSNPLHGVRVPGSVGTPL-PGVEVRIateavkgg 405
Cdd:PTZ00342 460 ----NPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV-------- 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 406 gRSYTILaqgdeDGTQMTPglegqEGELLVRGSSVFREYWNRPKETREAFTSDGWFRTGD 465
Cdd:PTZ00342 528 -RTWETY-----KATDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGD 576
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
208-571 |
1.23e-06 |
|
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: 51.50 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVLSTHENVqavttgLVEKWewkKEdvilhvlplHHVHGVI-----------------NKLLCPLWVG 270
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGGT------LLQHL---KE---------HILHCDLrpgdrlfyyttcgwmmwNWLVSGLAVG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 271 ATCIML---PEFSAQMV-WKkfLSSQApRVSVFMAVPTIYAKLIEYYdehfsqpqvQDFVRAFCQENIRLMVSGSAALPv 346
Cdd:cd05943 316 ATIVLYdgsPFYPDTNAlWD--LADEE-GITVFGTSAKYLDALEKAG---------LKPAETHDLSSLRTILSTGSPLK- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 347 PVLKKW--KAITGHTLLERY-GMTEI--GMALSNPLHGVRvPGSVGTPLPGVEVRIAteavkgggrsytilaqgDEDGTQ 421
Cdd:cd05943 383 PESFDYvyDHIKPDVLLASIsGGTDIisCFVGGNPLLPVY-RGEIQCRGLGMAVEAF-----------------DEEGKP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 422 MTpgleGQEGELLVR----GSSVFreYWNRPKETR--EAF--TSDGWFRTGDTA-AYHDGVYWIKGRtSVDIIKNGGFKI 492
Cdd:cd05943 445 VW----GEKGELVCTkpfpSMPVG--FWNDPDGSRyrAAYfaKYPGVWAHGDWIeITPRGGVVILGR-SDGTLNPGGVRI 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 493 SALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIVVEEIPRNQM 569
Cdd:cd05943 518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLS 597
|
..
gi 1201832555 570 GK 571
Cdd:cd05943 598 GK 599
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
427-577 |
1.54e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 50.98 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 427 EGQEGELLVRGSSVFREYWNRPKetreaftsDGWFRTGDTAAY-HDGVYWIKGRTSvDIIKNGGFKISALEVERQLLAHP 505
Cdd:cd17647 348 PDHWNYLDKDNNEPWRQFWLGPR--------DRLYRTGDLGRYlPNGDCECCGRAD-DQVKIRGFRIELGEIDTHISQHP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 506 HI---------------TDVAVIGPPDVVWGQRVSA------------VVQLRRGEMLSVKELKEWARDTMAPYAVPTEL 558
Cdd:cd17647 419 LVrenitlvrrdkdeepTLVSYIVPRFDKPDDESFAqedvpkevstdpIVKGLIGYRKLIKDIREFLKKRLASYAIPSLI 498
|
170
....*....|....*....
gi 1201832555 559 IVVEEIPRNQMGKVNKKEL 577
Cdd:cd17647 499 VVLDKLPLNPNGKVDKPKL 517
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
208-572 |
2.82e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 50.33 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 208 IIYTSGTTGRPKGVL-STHENVQAVTTGLVEKWEWKKEDVILHVLPLHHV--HGVInkLLCPLWVGATCIM---LPEFSA 281
Cdd:PRK10524 238 ILYTSGTTGKPKGVQrDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVvgHSYI--VYAPLLAGMATIMyegLPTRPD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 282 QMVWKKFLssQAPRVSVFMAVPTIyAKLIEYYDEhfsqpqvqDFVRAFCQENIR-LMVSG-----------SAALPVPVL 349
Cdd:PRK10524 316 AGIWWRIV--EKYKVNRMFSAPTA-IRVLKKQDP--------ALLRKHDLSSLRaLFLAGepldeptaswiSEALGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 350 kkwkaitghtllERYGMTEIGMALSNPLHGVRV----PGSVGTPLPGVEVRIATEAvkgggrsytilaqgdeDGTQMTPG 425
Cdd:PRK10524 385 ------------DNYWQTETGWPILAIARGVEDrptrLGSPGVPMYGYNVKLLNEV----------------TGEPCGPN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 426 legQEGELLVRG-------SSVFRE-------YWNRPKetREAFTSDGWFRTGDtaayhDGVYWIKGRTSvDIIKNGGFK 491
Cdd:PRK10524 437 ---EKGVLVIEGplppgcmQTVWGDddrfvktYWSLFG--RQVYSTFDWGIRDA-----DGYYFILGRTD-DVINVAGHR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 492 ISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS--------VKELKEWARDTMAPYAVPTELIVVEE 563
Cdd:PRK10524 506 LGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSA 585
|
....*....
gi 1201832555 564 IPRNQMGKV 572
Cdd:PRK10524 586 LPKTRSGKL 594
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
191-572 |
9.67e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.58 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 191 EDVPLASSASwkdrgAMIIYTSGTTGRPKGVL-STHENVqavtTGLVEKWEWKKEDVILHVLPLHH------VHGVINKL 263
Cdd:PTZ00237 247 EYVPVESSHP-----LYILYTSGTTGNSKAVVrSNGPHL----VGLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 264 LCplwVGATCIML------PEFSAQMVWKKFlssQAPRVSVFMAVPTIYAKLIEYydehfsQPQVQDFVRAFCQENIRLM 337
Cdd:PTZ00237 318 LS---LGNTFVMFeggiikNKHIEDDLWNTI---EKHKVTHTLTLPKTIRYLIKT------DPEATIIRSKYDLSNLKEI 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 338 VSGSA----ALPVPVLKKWKAITGHTllerYGMTEIGMALSNPLHGVRVP-GSVGTPLPGVEVRIATEavkgggrsytil 412
Cdd:PTZ00237 386 WCGGEvieeSIPEYIENKLKIKSSRG----YGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSE------------ 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 413 aqgdeDGTQMTpglEGQEGEL---LVRGSSVFREYWNRPKETREAFTS-DGWFRTGDTAaYHD--GVYWIKGRtSVDIIK 486
Cdd:PTZ00237 450 -----DGKELN---VNEIGEVafkLPMPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLG-FKDenGYYTIVSR-SDDQIK 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 487 NGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGE------MLSVK-ELKEWARDTMAPYAVPTELI 559
Cdd:PTZ00237 520 ISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQsnqsidLNKLKnEINNIITQDIESLAVLRKII 599
|
410
....*....|...
gi 1201832555 560 VVEEIPRNQMGKV 572
Cdd:PTZ00237 600 IVNQLPKTKTGKI 612
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
416-577 |
1.58e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.32 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 416 DEDGTQmtpgLEGQEGELLVRGS----SVFreYWNRP--KETREAF--TSDGWFRTGD----TAayHDGVYwIKGRtSVD 483
Cdd:PRK03584 453 DEDGRP----VVGEVGELVCTKPfpsmPLG--FWNDPdgSRYRDAYfdTFPGVWRHGDwieiTE--HGGVV-IYGR-SDA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 484 IIKNGGFKISALEVERQLLAHPHITDVAVIGPPDVVWGQRVSAVVQLRRGEMLS---VKELKEWARDTMAPYAVPTELIV 560
Cdd:PRK03584 523 TLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDdalRARIRTTIRTNLSPRHVPDKIIA 602
|
170
....*....|....*..
gi 1201832555 561 VEEIPRNQMGKvnKKEL 577
Cdd:PRK03584 603 VPDIPRTLSGK--KVEL 617
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
66-278 |
8.90e-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: 38.87 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 66 IIDQNG----EHTYRELFCRSLRlsqeICRVLQCSSRDLKEERISFLCPNDASYVVAQWASWMSGGIAVPLYRKHPVQQL 141
Cdd:cd05905 4 LLDSKGkeatTLTWGKLLSRAEK----IAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201832555 142 EYVIEDSQSALVIAAE----------EYVGKISPSAEKLGVPVL--------PLGSHSSGSAGH--TAVEDVPLassasw 201
Cdd:cd05905 80 GFLLGTCKVRVALTVEaclkglpkklLKSKTAAEIAKKKGWPKIldfvkipkSKRSKLKKWGPHppTRDGDTAY------ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201832555 202 kdrgamIIYTSGTTGRPKGVLSTHENVQAVTTGLVEKWEWKKEDVILHVLPLHHVHGVINKLLCPLWVGATCIMLPE 278
Cdd:cd05905 154 ------IEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPP 224
|
|
| |
