|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
17-510 |
1.41e-124 |
|
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: 371.84 E-value: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 17 MAKHVLRAGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAG 96
Cdd:COG0318 1 LADLLRRAAARHPDRPALV-------FGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 97 GLVPIPASPDLTARELGFLLDDSDAAAIVLddtlphgdfapglavvteaaliaaidsgpegafadtaaddpAFLIYTSGT 176
Cdd:COG0318 73 GAVVVPLNPRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 177 TANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGeRHPSIWPGLIRAFDV 256
Cdd:COG0318 112 TGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 257 TIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPD--FPRKPGT 334
Cdd:COG0318 191 TVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEdpGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 335 VGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhRSdPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRAS 414
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRE--LPPGEVGEIVV-RG-PNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 415 DLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVE 494
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVD 426
|
490
....*....|....*.
gi 503186189 495 RLPKTPNGKLKRSDLK 510
Cdd:COG0318 427 ELPRTASGKIDRRALR 442
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
11-510 |
5.74e-116 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 353.65 E-value: 5.74e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 11 PPRNLNMAKHVL-RAGAAAGDKTALvvIHDPAGREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALA 89
Cdd:COG0365 4 VGGRLNIAYNCLdRHAEGRGDKVAL--IWEGEDGEERTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 90 FFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD-TLPHGDFAPGLAVVTEA----------------------- 145
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgGLRGGKVIDLKEKVDEAleelpslehvivvgrtgadvpme 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 146 ------ALIAAidSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMY-RGWYGITAADRLMHSGVINWT 218
Cdd:COG0365 161 gdldwdELLAA--ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTaKYVLDLKPGDVFWCTADIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 219 YAMGTGLSDPLANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQ--ASGDRLDLARLRHGLTAGDTL 293
Cdd:COG0365 239 TGHSYIVYGPLLNGATVVLYEGRpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 294 -PDALEAeWSERTGTRLYEGFGQTE-LSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRSDP 371
Cdd:COG0365 319 nPEVWEW-WYEAVGVPIVDGWGQTEtGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDG--NPVPPGEEGELVIKGPWP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 372 GLMLGYWQrpDEER------EMFRGEWFTgGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVI 445
Cdd:COG0365 396 GMFRGYWN--DPERyretyfGRFPGWYRT-GDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503186189 446 DVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGvepSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-510 |
2.16e-101 |
|
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: 312.96 E-value: 2.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAA-GDKTALVViHDpagreaETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGL 98
Cdd:cd05936 3 DLLEEAARRfPDKTALIF-MG------RKLTYRELDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 99 VPIPASPDLTARELGFLLDDSDAAAIVLDDTLPHGdFAPGLAVVTEAALiaaidsgpegafadtAADDPAFLIYTSGTTA 178
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDL-LAAGAPLGERVAL---------------TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 179 NPKGVLHAHRSVWGRRPMYRGWYG--ITAADRLM------HsgvinwTYAMGTGLSDPLANGATALLytgerHPSIWP-- 248
Cdd:cd05936 139 VPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVLaalplfH------VFGLTVALLLPLALGATIVL-----IPRFRPig 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 249 --GLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAP 326
Cdd:cd05936 208 vlKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 327 -DFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDG 405
Cdd:cd05936 288 lDGPRKPGSIGIPLPGTEVKIVDDDG--EELPPGEVGELWV--RGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 406 AIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYK 485
Cdd:cd05936 364 YFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYK 443
|
490 500
....*....|....*....|....*
gi 503186189 486 RPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05936 444 VPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
20-510 |
3.74e-93 |
|
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: 292.74 E-value: 3.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAAGDKTALVvihDPAGreaeTWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLV 99
Cdd:cd05959 9 VDLNLNEGRGDKTAFI---DDAG----SLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 100 PIPASPDLTARELGFLLDDSDA-AAIVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEGAF----------------ADT 162
Cdd:cd05959 81 PVPVNTLLTPDDYAYYLEDSRArVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGAlllaelvaaeaeqlkpAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 163 AADDPAFLIYTSGTTANPKGVLHAHRSV-WGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGE 241
Cdd:cd05959 161 HADDPAFWLYSSGSTGRPKGVVHLHADIyWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 242 RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTE-LST 320
Cdd:cd05959 241 PTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEmLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 321 YLSSAPDfPRKPGTVGRAQPGRCVAILPEDGGDTslPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGEWFTGGDLGC 400
Cdd:cd05959 321 FLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDV--ADGEPGELYVR--GPSSATMYWNNRDKTRDTFQGEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 401 IDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGAD---LSAELAARA 477
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDseaLEEELKEFV 475
|
490 500 510
....*....|....*....|....*....|...
gi 503186189 478 EASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05959 476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
49-510 |
2.78e-92 |
|
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: 288.21 E-value: 2.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDd 128
Cdd:cd05919 12 TYGQLHDGANRLGSALR-NLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 tlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHR-SVWGRRPMYRGWYGITAAD 207
Cdd:cd05919 90 -----------------------------------ADDIAYLLYSSGTTGPPKGVMHAHRdPLLFADAMAREALGLTPGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 208 RLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGL 287
Cdd:cd05919 135 RVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 288 TAGDTLPDALEAEWSERTGTRLYEGFGQTE-LSTYLSSAPDFPRkPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAV 366
Cdd:cd05919 215 SAGEALPRGLGERWMEHFGGPILDGIGATEvGHIFLSNRPGAWR-LGSTGRPVPGYEIRLVDEEG--HTIPPGEEGDLLV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 367 hRSdPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVID 446
Cdd:cd05919 292 -RG-PSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVA 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 447 VPQPHGGTAITAFVVAREGGAD---LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05919 370 VPESTGLSRLTAFVVLKSPAAPqesLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
48-510 |
2.31e-89 |
|
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: 280.38 E-value: 2.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 48 WTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 dtlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAAD 207
Cdd:cd05972 80 ------------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 208 rlMHSGVINWTYAMGT--GLSDPLANGATALLYTGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQaSGDRLDLARLR 284
Cdd:cd05972 124 --IHWNIADPGWAKGAwsSFFGPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYRMLIKQ-DLSSYKFSHLR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 285 HGLTAGDTL-PDALEAeWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGM 363
Cdd:cd05972 201 LVVSAGEPLnPEVIEW-WRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG--RELPPGEEGD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 364 IAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAG 443
Cdd:cd05972 278 IAIKLPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 444 VIDVPQPHGGTAITAFVVAREGGAD---LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05972 358 VVGSPDPVRGEVVKAFVVLTSGYEPseeLAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
23-504 |
3.76e-87 |
|
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: 274.87 E-value: 3.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:cd17631 3 RRARRHPDRTALVF-------GGRSLTYAELDERVNRLAHALRA-LGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVlddtlphgdfapglavvteaaliaaidsgpegafadtaaDDPAFLIYTSGTTANPKG 182
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 183 VLHAHRSVWGrrpMYRGW---YGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIWpGLIRAFDVTIF 259
Cdd:cd17631 116 AMLTHRNLLW---NAVNAlaaLDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVL-DLIERHRVTSF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 260 AGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERtGTRLYEGFGQTELS---TYLSSApDFPRKPGTVG 336
Cdd:cd17631 192 FLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpgvTFLSPE-DHRRKLGSAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 337 RAQPGRCVAILPEDGGDtsLPPGEAGMIaVHRSdPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDL 416
Cdd:cd17631 270 RPVFFVEVRIVDPDGRE--VPPGEVGEI-VVRG-PHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 417 MNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERL 496
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
....*...
gi 503186189 497 PKTPNGKL 504
Cdd:cd17631 426 PRNATGKI 433
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
166-505 |
6.54e-85 |
|
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: 265.69 E-value: 6.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTyAMGTGLSDPLANGATALLYTGERHPS 245
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 246 IWPgLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSS- 324
Cdd:cd04433 80 ALE-LIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 325 -APDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDE 403
Cdd:cd04433 159 pPDDDARKPGSVGRPVPGVEVRIVDPDGGE--LPPGEIGELVVR--GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 404 DGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAA 483
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 503186189 484 YKRPRHYVFVERLPKTPNGKLK 505
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
19-510 |
2.32e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 259.73 E-value: 2.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 19 KHVLRAGAAA-GDKTALVvihdpagREAETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGG 97
Cdd:PRK06187 9 GRILRHGARKhPDKEAVY-------FDGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 98 LVPIPASPDLTARELGFLLDDSDAAAIVLD-----------DTLPH---------GDFAPGLAVVTE-AALIAAIDSGPE 156
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDsefvpllaailPQLPTvrtvivegdGPAAPLAPEVGEyEELLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 157 gaFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLM------HSGVINWTYAmgtglsdPLA 230
Cdd:PRK06187 161 --FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpmfHVHAWGLPYL-------ALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 231 NGATaLLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLY 310
Cdd:PRK06187 232 AGAK-QVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTELSTYLSSAP------DFPRKPGTVGRAQPGRCVAILPEDGGDtsLPP--GEAGMIAVhRSdPGLMLGYWQRPD 382
Cdd:PRK06187 311 QGYGMTETSPVVSVLPpedqlpGQWTKRRSAGRPLPGVEARIVDDDGDE--LPPdgGEVGEIIV-RG-PWLMQGYWNRPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 383 EEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVA 462
Cdd:PRK06187 387 ATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503186189 463 REgGADLSA-ELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK06187 467 KP-GATLDAkELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
45-510 |
7.81e-77 |
|
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: 248.16 E-value: 7.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 45 AETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAI 124
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 125 VLDDTLphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANPKGVLHAHRSV------WGRRPMyr 198
Cdd:cd05958 88 LCAHAL-------------------------------TASDDICILAFTSGTTGAPKATMHFHRDPlasadrYAVNVL-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 199 gwyGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTgERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRL 278
Cdd:cd05958 135 ---RLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE-EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 DLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTE-LSTYLSSAPDFPRkPGTVGRAQPGRCVAILPEDGGDtsLP 357
Cdd:cd05958 211 DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR-PGATGKPVPGYEAKVVDDEGNP--VP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 358 PGEAGMIAVHRSDpglmlGYWQRPDE-EREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREH 436
Cdd:cd05958 288 DGTIGRLAVRGPT-----GCRYLADKrQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQH 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 437 PLVAEAGVIDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05958 363 PAVAECAVVGHPDESRGVVVKAFVVLRPGvipGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-507 |
3.82e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 249.08 E-value: 3.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:PRK08316 19 RSARRYPDKTALVF-------GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTL-PHGDFAPGLA-VVTEAALIAAIDSGPEGAFADTAA---------------- 164
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDPALaPTAEAALALLpVDTLILSLVLGGREAPGGWLDFADwaeagsvaepdvelad 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGRrpmyrgwY-------GITAADRLMHSGVINWTYAMGTGLSDPLANGATALL 237
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRALIAE-------YvscivagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 238 YTGERHPSIWPgLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQT 316
Cdd:PRK08316 244 LDAPDPELILR-TIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 317 E---LSTYLSsAPDFPRKPGTVGRaqPGRCV--AILPEDGGDtsLPPGEAGMIaVHRSdPGLMLGYWQRPDEEREMFRGE 391
Cdd:PRK08316 323 EiapLATVLG-PEEHLRRPGSAGR--PVLNVetRVVDDDGND--VAPGEVGEI-VHRS-PQLMLGYWDDPEKTAEAFRGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSA 471
Cdd:PRK08316 396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVERLPKTPNGK-LKRS 507
Cdd:PRK08316 476 ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKiLKRE 512
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
45-510 |
1.07e-75 |
|
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: 245.42 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 45 AETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAI 124
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 125 VLDdtlphgdfapglavvteaaliaaidsgpegafadtAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGIT 204
Cdd:cd05971 83 VTD-----------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 205 AADRLMHSGVINWTY--AMGTGLSDPLANGATALLYTGERHPsiwPGliRAFDVTIFAGV-----PGLYHQIMRQAsGDR 277
Cdd:cd05971 128 PRDGDLYWTPADWAWigGLLDVLLPSLYFGVPVLAHRMTKFD---PK--AALDLMSRYGVttaflPPTALKMMRQQ-GEQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 278 LDLA--RLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPD-FPRKPGTVGRAQPGRCVAILPEDGgdT 354
Cdd:cd05971 202 LKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVDDNG--T 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 355 SLPPGEAGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLR 434
Cdd:cd05971 280 PLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 435 EHPLVAEAGVIDVPQPHGGTAITAFVVAREG--GAD-LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05971 360 KHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGetPSDaLAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
30-510 |
5.77e-75 |
|
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: 243.35 E-value: 5.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVIHDpagreaeTWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:cd05941 1 DRIAIVDDGD-------SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVlddtlphgdfapglavvteaaliaaidsgpegafadtaadDPAFLIYTSGTTANPKGVLHAHRS 189
Cdd:cd05941 74 AELEYVITDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHAN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 190 VWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATaLLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQI 269
Cdd:cd05941 114 LAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGAS-VEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 270 M----RQASGDRLDLARLRHGL---TAGDT-LPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPG 341
Cdd:cd05941 193 LqyyeAHFTDPQFARAAAAERLrlmVSGSAaLPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 RCVAILPEDGGDtSLPPGEAGMIAVhRSdPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRAS-DLMNA 419
Cdd:cd05941 273 VQARIVDEETGE-PLPRGEVGEIQV-RG-PSVFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGYYWILGRSSvDIIKS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 420 GGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAE-LAARAEASLAAYKRPRHYVFVERLPK 498
Cdd:cd05941 350 GGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEeLKEWAKQRLAPYKRPRRLILVDELPR 429
|
490
....*....|..
gi 503186189 499 TPNGKLKRSDLK 510
Cdd:cd05941 430 NAMGKVNKKELR 441
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
13-510 |
8.50e-75 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 245.13 E-value: 8.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 13 RNLNMAKHVLRAGAAA--GDKTALVvihDPAGReaetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAF 90
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgrGGKTAFI---DDISS----LSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 91 FGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTL-----------PH-------GDFAPGlaVVTEAALIAaiD 152
Cdd:TIGR02262 73 LGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALlpvikaalgksPHlehrvvvGRPEAG--EVQLAELLA--T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 153 SGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMY-RGWYGITAADRLMHSGVINWTYAMGTGLSDPLAN 231
Cdd:TIGR02262 149 ESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYaRNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 232 GATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYE 311
Cdd:TIGR02262 229 GATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 312 GFGQTE-LSTYLSSAPDFPRKpGTVGRAQPGRCVAILPEDGGDTSlpPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRG 390
Cdd:TIGR02262 309 GIGSTEmLHIFLSNLPGDVRY-GTSGKPVPGYRLRLVGDGGQDVA--DGEPGELLIS--GPSSATMYWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLS 470
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALE 463
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 503186189 471 AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:TIGR02262 464 TELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-420 |
5.05e-74 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 240.29 E-value: 5.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:pfam00501 3 RQAARTPDKTALEV------GEGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEGAF-----------------ADTAAD 165
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEeplpeeakpadvpppppPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRS----VWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGE 241
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 242 --RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELS 319
Cdd:pfam00501 236 paLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 320 TYLSSAPDFP---RKPGTVGRAQPGRCVAILPEDGGDTsLPPGEAGMIAVHRsdPGLMLGYWQRPDEERE-MFRGEWFTG 395
Cdd:pfam00501 316 GVVTTPLPLDedlRSLGSVGRPLPGTEVKIVDDETGEP-VPPGEPGELCVRG--PGVMKGYLNDPELTAEaFDEDGWYRT 392
|
410 420
....*....|....*....|....*
gi 503186189 396 GDLGCIDEDGAIAHLGRASDLMNAG 420
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
30-506 |
5.51e-74 |
|
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: 242.60 E-value: 5.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdPAGREAetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:cd05926 2 DAPALVV---PGSTPA--LTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLDD--TLPHGDFAP--GLAVVtEAALIAAI-------DSGPEGAFADTAA--------DDPAFL 170
Cdd:cd05926 76 AEFEFYLADLGSKLVLTPKgeLGPASRAASklGLAIL-ELALDVGVlirapsaESLSNLLADKKNAksegvplpDDLALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 171 IYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR------LMH-SGVInwtyamgTGLSDPLANGATALLYTGERH 243
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvvmpLFHvHGLV-------ASLLSTLAAGGSVVLPPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 244 PSIWPgLIRAFDVTIFAGVPGLyHQIM--RQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTY 321
Cdd:cd05926 228 STFWP-DVRDYNATWYTAVPTI-HQILlnRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 322 LSSAP--DFPRKPGTVGRAQpGRCVAILPEDGGdtSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREM-FRGEWFTGGDL 398
Cdd:cd05926 306 MTSNPlpPGPRKPGSVGKPV-GVEVRILDEDGE--ILPPGVVGEICL--RGPNVTRGYLNNPEANAEAaFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 399 GCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAE 478
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR 460
|
490 500
....*....|....*....|....*...
gi 503186189 479 ASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd05926 461 KHLAAFKVPKKVYFVDELPKTATGKIQR 488
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
162-510 |
6.71e-70 |
|
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: 230.47 E-value: 6.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 162 TAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGE 241
Cdd:cd05969 86 TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 242 RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRqaSGDRL----DLARLRHGLTAGDTL-PDALEaeWSERT-GTRLYEGFGQ 315
Cdd:cd05969 166 FDAESWYGIIERVKVTVWYTAPTAIRMLMK--EGDELarkyDLSSLRFIHSVGEPLnPEAIR--WGMEVfGVPIHDTWWQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 316 TELSTYL-SSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFT 394
Cdd:cd05969 242 TETGSIMiANYPCMPIKPGSMGKPLPGVKAAVVDENG--NELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFIDGWYL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 395 GGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG---GADLSA 471
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepSDELKE 399
|
330 340 350
....*....|....*....|....*....|....*....
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05969 400 EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
12-510 |
3.67e-69 |
|
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: 230.82 E-value: 3.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNMAKHVLRAGA---AAGDKTAlvvihDPA-----GREAET-WTYRALESAALRVAFELRSNRSLAPRTRVLIRLRN 82
Cdd:cd05928 2 PEYFNFASDVLDQWAdkeKAGKRPP-----NPAlwwvnGKGDEVkWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 83 RTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLphgdfAPGLAVVT------EAALIAAIDS--- 153
Cdd:cd05928 77 VPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDEL-----APEVDSVAsecpslKTKLLVSEKSrdg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 154 -----------GPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSV-WGRRPMYRGWYGITAADRLMHSGVINWTYAM 221
Cdd:cd05928 152 wlnfkellneaSTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 222 GTGLSDPLANGATALLYTGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQasgdrlDLAR-----LRHGLTAGDTL-P 294
Cdd:cd05928 232 WSSLFEPWIQGACVFVHHLPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ------DLSSykfpsLQHCVTGGEPLnP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 295 DALEaEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhRSDP--- 371
Cdd:cd05928 306 EVLE-KWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNG--NVLPPGTEGDIGI-RVKPirp 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 372 -GLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQP 450
Cdd:cd05928 382 fGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 451 HGGTAITAFVV--AREGGAD---LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05928 462 IRGEVVKAFVVlaPQFLSHDpeqLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-510 |
6.59e-69 |
|
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: 227.17 E-value: 6.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 48 WTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:cd05934 4 WTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 dtlphgdfapglavvteaaliaaidsgpegafadtaaddPAFLIYTSGTTANPKGVL--HAHRSVWGRrpMYRGWYGITA 205
Cdd:cd05934 83 ---------------------------------------PASILYTSGTTGPPKGVVitHANLTFAGY--YSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADRLMHSGVINWTYAMGTGLSDPLANGATALLytGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLR 284
Cdd:cd05934 122 DDVYLTVLPLFHINAQAVSVLAALSVGATLVL--LPRfSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 285 hgLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMI 364
Cdd:cd05934 200 --AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE--LPAGEPGEL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 365 AVHRSDP-GLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAG 443
Cdd:cd05934 276 VIRGLRGwGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAA 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 444 VIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05934 356 VVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
21-510 |
1.39e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 228.64 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 21 VLRAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:PRK07656 11 LARAARRFGDKEAYVF-------GDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDA-AAIVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPE--------------GAFADTAA- 164
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAkALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPhtekmktftdflaaGDPAERAPe 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 ---DDPAFLIYTSGTTANPKGVLHAHRSVWGrrpMYRGW---YGITAADRLMhsgVIN---WTYAMGTGLSDPLANGATA 235
Cdd:PRK07656 163 vdpDDVADILFTSGTTGRPKGAMLTHRQLLS---NAADWaeyLGLTEGDRYL---AANpffHVFGYKAGVNAPLMRGATI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 236 LLytgerHPSIWPG----LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDAL----EAEWSERTgt 307
Cdd:PRK07656 237 LP-----LPVFDPDevfrLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALlerfESELGVDI-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 308 rLYEGFGQTELS--TYLSSaPDFPRK--PGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDE 383
Cdd:PRK07656 310 -VLTGYGLSEASgvTTFNR-LDDDRKtvAGTIGTAIAGVENKIVNELGEE--VPVGEVGELLVR--GPNVMKGYYDDPEA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 384 EREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVA 462
Cdd:PRK07656 384 TAAAIDADgWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 503186189 463 REGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07656 464 KPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
30-509 |
3.78e-65 |
|
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: 217.78 E-value: 3.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpagrEAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLrNRTAYAL-AFFGAIAGGLVPIPASPDLT 108
Cdd:cd05930 2 DAVAVVD-------GDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLL-ERSLEMVvAILAVLKAGAAYVPLDPSYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 109 ARELGFLLDDSDAAAIVlddtlphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANPKGVLHAHR 188
Cdd:cd05930 73 AERLAYILEDSGAKLVL------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 189 SV-----WGRRPmyrgwYGITAADRLMHSGVINWTyAMGTGLSDPLANGATALLYTGERH--PSIWPGLIRAFDVTIFAG 261
Cdd:cd05930 117 GLvnlllWMQEA-----YPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPEEVRkdPEALADLLAEEGITVLHL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 262 VPGLYHQIMrqASGDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTELS----TYLSSAPDFPRKPGTVG 336
Cdd:cd05930 191 TPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATvdatYYRVPPDDEEDGRVPIG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 337 RAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG-------GDLGCIDEDGAIAH 409
Cdd:cd05930 269 RPIPNTRVYVL--DENLRPVPPGVPGELYI--GGAGLARGYLNRPELTAERFVPNPFGPgermyrtGDLVRWLPDGNLEF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 410 LGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRH 489
Cdd:cd05930 345 LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSA 424
|
490 500
....*....|....*....|
gi 503186189 490 YVFVERLPKTPNGKLKRSDL 509
Cdd:cd05930 425 FVVLDALPLTPNGKVDRKAL 444
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
12-510 |
1.49e-62 |
|
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: 213.51 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNMAKHVLRAGAA-AGDKTALVVIHDPAgrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAY---- 86
Cdd:cd05970 13 PENFNFAYDVVDAMAKeYPDKLALVWCDDAG--EERIFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFwysl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 87 -ALAFFGAIAgglvpIPASPDLTARELGFLLDDSDAAAIVLD--DTLPH--GDFAPGLAVVTEAALIAaiDSGPEG---- 157
Cdd:cd05970 90 lALHKLGAIA-----IPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEeiEKAAPECPSKPKLVWVG--DPVPEGwidf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 158 ---------------AFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMG 222
Cdd:cd05970 163 rkliknaspdferptANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 223 TGLSDPLANGATALLYTGERH-PSIWPGLIRAFDVTIFAGVPGLYHQIMRqASGDRLDLARLRHGLTAGDTLPDALEAEW 301
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFdPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 302 SERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRSD--P-GLMLGYW 378
Cdd:cd05970 322 KEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREG--RSCEAGEEGEIVIRTSKgkPvGLFGGYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 379 QRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITA 458
Cdd:cd05970 400 KDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 459 FVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05970 480 TIVLAKGyepSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-504 |
1.91e-62 |
|
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: 211.69 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 37 IHDPAGREaetWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLL 116
Cdd:cd05911 3 IDADTGKE---LTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 117 DDSDAAAIVLD-DTLP--------------------HGDFAPGLAVVTEAALIAAIDSGPEgaFADTAADDPAFLIYTSG 175
Cdd:cd05911 79 KISKPKVIFTDpDGLEkvkeaakelgpkdkiivlddKPDGVLSIEDLLSPTLGEEDEDLPP--PLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 176 TTANPKGVLHAHR-------SVWGRRPmyrgwYGITAADRLMHSGVINWTYAMGTGLSDPLaNGATalLYTGER-HPSIW 247
Cdd:cd05911 157 TTGLPKGVCLSHRnlianlsQVQTFLY-----GNDGSNDVILGFLPLYHIYGLFTTLASLL-NGAT--VIIMPKfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 248 PGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTELSTYLSSAP 326
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATIKQGYGMTETGGILTVNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 327 DFPRKPGTVGRAQPGRCVAILPEDGGDtSLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMF-RGEWFTGGDLGCIDEDG 405
Cdd:cd05911 309 DGDDKPGSVGRLLPNVEAKIVDDDGKD-SLGPNEPGEICVR--GPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 406 AIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYK 485
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK 465
|
490 500
....*....|....*....|
gi 503186189 486 RPR-HYVFVERLPKTPNGKL 504
Cdd:cd05911 466 QLRgGVVFVDEIPKSASGKI 485
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-509 |
7.93e-60 |
|
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: 203.48 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:cd05935 3 TYLELLEVVKKLASFL-SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TLphgdfapglavvteaaliaaidsgpegafadtaaDDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR 208
Cdd:cd05935 82 EL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 209 LMHSGVINWTYAMGTGLSDPLANGATALLYtgerhpSIW-----PGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARL 283
Cdd:cd05935 128 ILACLPLFHVTGFVGSLNTAVYVGGTYVLM------ARWdretaLELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPG-RCVAILPEDGGDtsLPPGEAG 362
Cdd:cd05935 202 KVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGvDARVIDIETGRE--LPPNEVG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 363 MIAVHrsDPGLMLGYWQRPDEEREMF---RG-EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPL 438
Cdd:cd05935 280 EIVVR--GPQIFKGYWNRPEETEESFieiKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 439 VAEAGVIDVPQPHGGTAITAFVVAREG--GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd05935 358 I*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
30-509 |
7.46e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 202.40 E-value: 7.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpagrEAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:PRK06839 17 DRIAIIT-------EEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLDDTlphgdFAPGLAVVTEAALIAAI----------DSGPEGaFADTAADDPAFLIYTSGTTAN 179
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEKT-----FQNMALSMQKVSYVQRVisitslkeieDRKIDN-FVEKNESASFIICYTSGTTGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 180 PKGvlhahrSVWGRRPMYrgWYGI--------TAADR------LMHSGVINwTYAMGTglsdPLANGAtaLLYTGERHPS 245
Cdd:PRK06839 164 PKG------AVLTQENMF--WNALnntfaidlTMHDRsivllpLFHIGGIG-LFAFPT----LFAGGV--IIVPRKFEPT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 246 IWPGLIRAFDVTIFAGVPGLyHQIMRQASgDRL--DLARLRHGLTAGDTLPDALEAEWSERtGTRLYEGFGQTELS--TY 321
Cdd:PRK06839 229 KALSMIEKHKVTVVMGVPTI-HQALINCS-KFEttNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSptVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 322 LSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCI 401
Cdd:PRK06839 306 MLSEEDARRKVGSIGKPVLFCDYELIDENKNK--VEVGEVGELLIR--GPNVMKEYWNRPDATEETIQDGWLCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 402 DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASL 481
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFL 461
|
490 500
....*....|....*....|....*...
gi 503186189 482 AAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-510 |
2.96e-58 |
|
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: 201.55 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAAGDKTALVVIHdpAGReaeTWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLV 99
Cdd:TIGR03098 3 HHLLEDAAARLPDATALVH--HDR---TLTYAALSERVLALASGLRG-LGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 100 PIPASPDLTARELGFLLDDSDAAAIV--------LDDTLPH----------GDFA------PGLAVVTEAALIAAidsGP 155
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVRLLVtsserldlLHPALPGchdlrtliivGDPAhaseghPGEEPASWPKLLAL---GD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 156 EGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTgLSDPLANGATA 235
Cdd:TIGR03098 154 ADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQ-LTTAFYVGATV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 236 LLytgerHPSIWP-GLIRAFD---VTIFAGVPGLYHQIMRQASGDRlDLARLRHGLTAGDTLPDALEAEWSER-TGTRLY 310
Cdd:TIGR03098 233 VL-----HDYLLPrDVLKALEkhgITGLAAVPPLWAQLAQLDWPES-AAPSLRYLTNSGGAMPRATLSRLRSFlPNARLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTEL--STYLSSApDFPRKPGTVGRAQPGRCVAILPEDGGDTSlpPGEAGMIaVHRSdPGLMLGYWQRPDEEREMF 388
Cdd:TIGR03098 307 LMYGLTEAfrSTYLPPE-EVDRRPDSIGKAIPNAEVLVLREDGSECA--PGEEGEL-VHRG-ALVAMGYWNDPEKTAERF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 389 R------------GEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAI 456
Cdd:TIGR03098 382 RplppfpgelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAI 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 503186189 457 TAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:TIGR03098 462 VLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALA 515
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
30-504 |
3.04e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 202.11 E-value: 3.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVIhdpaGREAetwTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:PRK08314 25 DKTAIVFY----GRAI---SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDA-AAIVLDDTLP-----HGDFA----------------PGLAV---VTEAALIAAIDSGPEGAFADTAA 164
Cdd:PRK08314 98 EELAHYVTDSGArVAIVGSELAPkvapaVGNLRlrhvivaqysdylpaePEIAVpawLRAEPPLQALAPGGVVAWKEALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 ------------DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR------LMH-SGVINwtyamgtGL 225
Cdd:PRK08314 178 aglappphtagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVvlavlpLFHvTGMVH-------SM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 226 SDPLANGATALLYTgerhpsIW-----PGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAE 300
Cdd:PRK08314 251 NAPIYAGATVVLMP------RWdreaaARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 301 WSERTGTRLYEGFGQTE-LSTYLSSAPDFPRKpgtvgraqpgRCVAIlPEDGGD---------TSLPPGEAGMIAVHrsD 370
Cdd:PRK08314 325 LKELTGLDYVEGYGLTEtMAQTHSNPPDRPKL----------QCLGI-PTFGVDarvidpetlEELPPGEVGEIVVH--G 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 371 PGLMLGYWQRPDEEREMF---RG-EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVID 446
Cdd:PRK08314 392 PQVFKGYWNRPEATAEAFieiDGkRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 447 VPQPHGGTAITAFVVAREG--GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKL 504
Cdd:PRK08314 472 TPDPRRGETVKAVVVLRPEarGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
23-509 |
4.30e-58 |
|
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: 200.19 E-value: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:cd17646 6 EQAARTPDAPAVV-------DEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTLPHGdfAPGLAVVTEAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKG 182
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAAR--LPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 183 VLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSdPLANGATALLYT--GERHPSIWPGLIRAFDVTIFA 260
Cdd:cd17646 156 VMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFW-PLVAGARLVVARpgGHRDPAYLAALIREHGVTTCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 261 GVPGLYHQIMRQASGDRLdlARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELS---TYLSSAPDFPRKPGTVGR 337
Cdd:cd17646 235 FVPSMLRVFLAEPAAGSC--ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAidvTHWPVRGPAETPSVPIGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 338 AQPGRCVAILPEDGgdTSLPPGEAGMIavHRSDPGLMLGYWQRPDEEREMFRGEWF-TG------GDLGCIDEDGAIAHL 410
Cdd:cd17646 313 PVPNTRLYVLDDAL--RPVPVGVPGEL--YLGGVQLARGYLGRPALTAERFVPDPFgPGsrmyrtGDLARWRPDGALEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 411 GRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLS-AELAARAEASLAAYKRPRH 489
Cdd:cd17646 389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDtAALRAHLAERLPEYMVPAA 468
|
490 500
....*....|....*....|
gi 503186189 490 YVFVERLPKTPNGKLKRSDL 509
Cdd:cd17646 469 FVVLDALPLTANGKLDRAAL 488
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
22-503 |
3.42e-57 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 198.18 E-value: 3.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 22 LRAGAAAGDKTAlvvIHDPAGReaeTWTYRALESAALRVAFELRSnRSLAPRTRVLIRLrNRTAYALAFFGA-IAGGLVP 100
Cdd:PRK07514 9 LRAAFADRDAPF---IETPDGL---RYTYGDLDAASARLANLLVA-LGVKPGDRVAVQV-EKSPEALALYLAtLRAGAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVLDDTLphgdfAPGLAVVTEAA----------------LIAAIDSGPEGAFADTAA 164
Cdd:PRK07514 81 LPLNTAYTLAELDYFIGDAEPALVVCDPAN-----FAWLSKIAAAAgaphvetldadgtgslLEAAAAAPDDFETVPRGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHP 244
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 245 SIWPGLIRAfdvTIFAGVPGLYHQIMRQASGDRLDLARLRhgLTAGDTLPDALE--AEWSERTGTRLYEGFGQTElSTYL 322
Cdd:PRK07514 236 AVLALMPRA---TVMMGVPTFYTRLLQEPRLTREAAAHMR--LFISGSAPLLAEthREFQERTGHAILERYGMTE-TNMN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 323 SSAP-DFPRKPGTVGRAQPGRCVAIL-PEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE-WFTGGDLG 399
Cdd:PRK07514 310 TSNPyDGERRAGTVGFPLPGVSLRVTdPETG--AELPPGEIGMIEV--KGPNVFKGYWRMPEKTAEEFRADgFFITGDLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 400 CIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEA 479
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKG 465
|
490 500
....*....|....*....|....
gi 503186189 480 SLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:PRK07514 466 RLARFKQPKRVFFVDELPRNTMGK 489
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-506 |
2.17e-56 |
|
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: 194.27 E-value: 2.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 141 VVTEAALIAAIDSgpegafadtaadDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYA 220
Cdd:cd05973 76 VVTDAANRHKLDS------------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 221 MGTGLSDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMrqASGDRLDLA---RLRHGLTAGDTL-PDA 296
Cdd:cd05973 144 LYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLM--AAGAEVPARpkgRLRRVSSAGEPLtPEV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 297 LEaeWSE-RTGTRLYEGFGQTELSTYLSS--APDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRSDPGL 373
Cdd:cd05973 222 IR--WFDaALGVPIHDHYGQTELGMVLANhhALEHPVHAGSAGRAMPGWRVAVLDDDG--DELGPGEPGRLAIDIANSPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 374 ML--GYWQRPDEEremFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPH 451
Cdd:cd05973 298 MWfrGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPE 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 503186189 452 GGTAITAFVVAR---EGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd05973 375 RTEVVKAFVVLRgghEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
47-510 |
6.49e-56 |
|
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: 192.98 E-value: 6.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVL 126
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 127 DDTLPHGDFAPglavvteaaliaaidsgpegafadtAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAA 206
Cdd:cd05903 80 PERFRQFDPAA-------------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 DRLMHSGVINWTYAMGTGLSDPLANGATALLYtgerhpSIWPG-----LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLA 281
Cdd:cd05903 135 DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ------DIWDPdkalaLMREHGVTFMMGATPFLTDLLNAVEEAGEPLS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 282 RLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFP--RKPGTVGRAQPGRCVAILPEDGgdTSLPPG 359
Cdd:cd05903 209 RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGRPLPGVEIKVVDDTG--ATLAPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 360 EAGMIAVhRSdPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLV 439
Cdd:cd05903 287 VEGELLS-RG-PSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503186189 440 AEAGVIDVPQPHGGTAITAFVVAREGGA-DLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05903 365 IEAAVVALPDERLGERACAVVVTKSGALlTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
10-510 |
1.24e-55 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 195.50 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 10 LPPRNLNMA-----KHvlrAGAAAGDKTALVVIhdpAGREAETWTYRALESAALRVAFELRS------NR--SLAPRTRV 76
Cdd:PRK04319 37 LETGKVNIAyeaidRH---ADGGRKDKVALRYL---DASRKEKYTYKELKELSNKFANVLKElgvekgDRvfIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 77 LirlrnrtaYAlAFFGAIAGGLVpipASPDLTArelgFL-------LDDSDAAAIVLDDTLPHGDFAPGLAVVtEAALIA 149
Cdd:PRK04319 111 L--------YF-ALLGALKNGAI---VGPLFEA----FMeeavrdrLEDSEAKVLITTPALLERKPADDLPSL-KHVLLV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 150 AIDSGPEGAFAD----------------TAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRpmyrgwygITAADRL-MHS 212
Cdd:PRK04319 174 GEDVEEGPGTLDfnalmeqasdefdiewTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHY--------QTGKYVLdLHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 213 GVINWTYA-----MGT--GLSDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARL 283
Cdd:PRK04319 246 DDVYWCTAdpgwvTGTsyGIFAPWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDlvKKYDLSSL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTL-PDALEaeWSERT-GTRLYEGFGQTELSTYL-SSAPDFPRKPGTVGRAQPGRCVAILpEDGGDtSLPPGE 360
Cdd:PRK04319 326 RHILSVGEPLnPEVVR--WGMKVfGLPIHDNWWMTETGGIMiANYPAMDIKPGSMGKPLPGIEAAIV-DDQGN-ELPPNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVA 440
Cdd:PRK04319 402 MGNLAIKKGWPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 441 EAGVIDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK04319 482 EAGVIGKPDPVRGEIIKAFVALRPGyepSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
20-510 |
1.44e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 195.60 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAA-GDKTALvvihDPAGReaeTWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGGL 98
Cdd:PRK05605 36 DLYDNAVARfGDRPAL----DFFGA---TTTYAELGKQVRRAAAGLRAL-GVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 99 VPIPASPDLTARELGFLLDDSDAA-AIVLDDTLPHGD------------------------------------------- 134
Cdd:PRK05605 108 VVVEHNPLYTAHELEHPFEDHGARvAIVWDKVAPTVErlrrttpletivsvnmiaampllqrlalrlpipalrkaraalt 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 135 -FAPGlAVVTEAALIAAIdsGPEGAFAD---TAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYG-------- 202
Cdd:PRK05605 188 gPAPG-TVPWETLVDAAI--GGDGSDVShprPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPglgdgper 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 203 ITAADRLMHSgvinwtYAMGTGLSDPLANGATALLYtgerhPSIWPGLI----RAFDVTIFAGVPGLYHQIMRQASGDRL 278
Cdd:PRK05605 265 VLAALPMFHA------YGLTLCLTLAVSIGGELVLL-----PAPDIDLIldamKKHPPTWLPGVPPLYEKIAEAAEERGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 DLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFP-RKPGTVGRAQPGRCVAIL-PEDGGDTsL 356
Cdd:PRK05605 334 DLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDdRRPGYVGVPFPDTEVRIVdPEDPDET-M 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 357 PPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREH 436
Cdd:PRK05605 413 PDGEEGELLV--RGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 437 PLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSAE-LAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK05605 491 PGVEDAAVVGLPREDGSEEVVAAVVLEP-GAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
11-509 |
1.98e-55 |
|
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: 193.61 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 11 PPRNLNMAKHVLRAGAAAGDKTALVvihDPA-GReaeTWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALA 89
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALI---DAAtGR---ALTYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 90 FFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVT----EAALIAAIDSGPEGAFADTAA- 164
Cdd:cd05904 74 FLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLldsaEFDSLSFSDLLFEADEAEPPVv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 ----DDPAFLIYTSGTTANPKGVLHAHRS--------VWGRRPMYRGwygitaADRLM------HSgvinwtYAMGTGLS 226
Cdd:cd05904 154 vikqDDVAALLYSSGTTGRSKGVMLTHRNliamvaqfVAGEGSNSDS------EDVFLcvlpmfHI------YGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 227 DPLANGATALLYTGERHPSIWpGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTG 306
Cdd:cd05904 222 GLLRLGATVVVMPRFDLEELL-AAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 307 T-RLYEGFGQTELSTYLSSAPDF---PRKPGTVGRAQPGRCVAIL-PEDGGdtSLPPGEAGMIAVHrsDPGLMLGYWQRP 381
Cdd:cd05904 301 NvDLGQGYGMTESTGVVAMCFAPekdRAKYGSVGRLVPNVEAKIVdPETGE--SLPPNQTGELWIR--GPSIMKGYLNNP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 382 DEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFV 460
Cdd:cd05904 377 EATAATIDKEgWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503186189 461 VaREGGADLS-AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd05904 457 V-RKPGSSLTeDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
49-444 |
4.36e-54 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 187.47 E-value: 4.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSNRSLAPRTRVLIRLrNRTAYALAFFGAI--AGG-LVPI-PASPdlTAReLGFLLDDSDAAAI 124
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLL-ERSAELVVAILAVlkAGAaYVPLdPAYP--AER-LAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 125 VLDDTLPH--GDFAPGLAVVTEAALIAAIDSGPEG-AFADTAADDPAFLIYTSGTTANPKGVLHAHRSV-----WGRRPm 196
Cdd:TIGR01733 77 LTDSALASrlAGLVLPVILLDPLELAALDDAPAPPpPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLvnllaWLARR- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 197 yrgwYGITAADRLMHSGvinwTYAMGTGLSD---PLANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGVPGLYHQIM 270
Cdd:TIGR01733 156 ----YGLDPDDRVLQFA----SLSFDASVEEifgALLAGATLVVPPEDeerDDAALLAALIAEHPVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 271 RQasgDRLDLARLRHGLTAGDTLPDALEAEWSERTG-TRLYEGFGQTELSTY-----LSSAPDFPRKPGTVGRAQPGRCV 344
Cdd:TIGR01733 228 AA---LPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWstatlVDPDDAPRESPVPIGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 345 AILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG---------GDLGCIDEDGAIAHLGRASD 415
Cdd:TIGR01733 305 YVL--DDDLRPVPVGVVGELYI--GGPGVARGYLNRPELTAERFVPDPFAGgdgarlyrtGDLVRYLPDGNLEFLGRIDD 380
|
410 420
....*....|....*....|....*....
gi 503186189 416 LMNAGGYRVSPVEVEAVLREHPLVAEAGV 444
Cdd:TIGR01733 381 QVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-510 |
3.07e-53 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 185.85 E-value: 3.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:cd05974 2 SFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TlphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANPKGVLHAHRS--VWGRRPMYrgWYGITAA 206
Cdd:cd05974 81 N--------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMY--WIGLKPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 DRLMHSGVINWTYAMGTGLSDPLANGATALLYTGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQasgdrlDLARLRH 285
Cdd:cd05974 127 DVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ------DLASFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 286 GL----TAGDTL-PDALE---AEWsertGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGdtslp 357
Cdd:cd05974 201 KLrevvGAGEPLnPEVIEqvrRAW----GLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA----- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 358 PGEAGMIAVHRSDP---GLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLR 434
Cdd:cd05974 272 PATEGEVALDLGDTrpvGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLI 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 435 EHPLVAEAGVIDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVErLPKTPNGKLKRSDLK 510
Cdd:cd05974 352 EHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELR 429
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
49-510 |
3.09e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 188.69 E-value: 3.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAI---- 124
Cdd:PRK07059 50 TYGELDELSRALAAWLQS-RGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIvvle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 125 --------VLDDT-LPH------GDF------------------APGLAVVTEAALIAAIDSGPEGAF--ADTAADDPAF 169
Cdd:PRK07059 129 nfattvqqVLAKTaVKHvvvasmGDLlgfkghivnfvvrrvkkmVPAWSLPGHVRFNDALAEGARQTFkpVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 170 LIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGiTAADRLMHSGVINWTYAMgtglsdPL--------------ANGATA 235
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQ-PAFEKKPRPDQLNFVCAL------PLyhifaltvcgllgmRTGGRN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 236 LLYTgerHPSIWPGLIRA---FDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEG 312
Cdd:PRK07059 282 ILIP---NPRDIPGFIKElkkYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 313 FGQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhrSDPGLMLGYWQRPDE-EREMFRG 390
Cdd:PRK07059 359 YGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRDDDGND--LPLGEPGEICI--RGPQVMAGYWNRPDEtAKVMTAD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREggADLS 470
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD--PALT 512
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 503186189 471 -AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07059 513 eEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
23-509 |
3.14e-53 |
|
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: 187.02 E-value: 3.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRnRTAYALAFFGAI--AGG-LV 99
Cdd:cd12117 5 EQAARTPDAVAVV-------YGDRSLTYAELNERANRLARRLRA-AGVGPGDVVGVLAE-RSPELVVALLAVlkAGAaYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 100 PIPasPDLTARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEGAFAdtaADDPAFLIYTSGTTAN 179
Cdd:cd12117 76 PLD--PELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS---PDDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 180 PKGVLHAHRSVwGRRPMYRGWYGITAADRLMHSGVINW---TYAMGTglsdPLANGATALLYtgERHPSIWPGLIRAF-- 254
Cdd:cd12117 151 PKGVAVTHRGV-VRLVKNTNYVTLGPDDRVLQTSPLAFdasTFEIWG----ALLNGARLVLA--PKGTLLDPDALGALia 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 255 --DVTIFAGVPGLYHQIMRQASGDrldLARLRHGLTAGDTLPDALEAEWSERT-GTRLYEGFGQTE---LSTYLSSAPDF 328
Cdd:cd12117 224 eeGVTVLWLTAALFNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEnttFTTSHVVTELD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 329 PRkPGTV--GRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF-------RGEWFTGGDLG 399
Cdd:cd12117 301 EV-AGSIpiGRPIANTRVYVLDEDG--RPVPPGVPGELYV--GGDGLALGYLNRPALTAERFvadpfgpGERLYRTGDLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 400 CIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADlsAELAARAEA 479
Cdd:cd12117 376 RWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA--AELRAFLRE 453
|
490 500 510
....*....|....*....|....*....|
gi 503186189 480 SLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd12117 454 RLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
47-510 |
1.23e-52 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 187.34 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV- 125
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVy 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 -----------LDDT-------LPHGDFAPGL-----------------------AVVTEAALIAAIDSGPEGAfaDTAA 164
Cdd:PRK12492 129 lnmfgklvqevLPDTgieylieAKMGDLLPAAkgwlvntvvdkvkkmvpayhlpqAVPFKQALRQGRGLSLKPV--PVGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAAD--RLMHSGV--------INWTYAMGTGLSDPLANGAT 234
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqPLMKEGQevmiaplpLYHIYAFTANCMCMMVSGNH 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 235 ALLYTgerHPSIWPGLIRA---FDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYE 311
Cdd:PRK12492 287 NVLIT---NPRDIPGFIKElgkWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 312 GFGQTELSTYLSSAPDFPR-KPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRG 390
Cdd:PRK12492 364 GYGLTETSPVASTNPYGELaRLGTVGIPVPGTALKVIDDDG--NELPLGERGELCI--KGPQVMKGYWQQPEATAEALDA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 E-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADL 469
Cdd:PRK12492 440 EgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSV 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 503186189 470 SaELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK12492 520 E-ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
49-509 |
1.48e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 187.17 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:PRK06178 60 TYAELDELSDRFAALLRQ-RGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TL---------------------------------PHGDFAPGLAVVTEAALIAAIDSGPEGAFADTAA-DDPAFLIYTS 174
Cdd:PRK06178 139 QLapvveqvraetslrhvivtsladvlpaeptlplPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPAlDALAALNYTG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 175 GTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGV-INWTYAMGTGLSDPLANGATALLYTgERHPSIWPGLIRA 253
Cdd:PRK06178 219 GTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLpEFWIAGENFGLLFPLFSGATLVLLA-RWDAVAFMAAVER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 254 FDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAG--DTLPDALEAEWSERTGTRLYEG-FGQTELSTY--------- 321
Cdd:PRK06178 298 YRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCdtftagfqd 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 322 ----LSSAPDFprkpgtVGRAQPGRCVAILPEDGGDTsLPPGEAGMIAVhRSdPGLMLGYWQRPDEEREMFRGEWFTGGD 397
Cdd:PRK06178 378 ddfdLLSQPVF------VGLPVPGTEFKICDFETGEL-LPLGAEGEIVV-RT-PSLLKGYWNKPEATAEALRDGWLHTGD 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 398 LGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARA 477
Cdd:PRK06178 449 IGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWC 528
|
490 500 510
....*....|....*....|....*....|..
gi 503186189 478 EASLAAYKRPRHYVfVERLPKTPNGKLKRSDL 509
Cdd:PRK06178 529 RENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
75-510 |
9.16e-52 |
|
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: 182.64 E-value: 9.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 75 RVLIRLRNRTAYALAFFGAIAGG----LVPIPASPDLTARELGFLLDDSDAAAIVLDDTLpHGDFAPGLAVVTEAALIAA 150
Cdd:cd05922 20 RVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGA-ADRLRDALPASPDPGTVLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 151 IDsGPEGAFADTAA-----DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTgL 225
Cdd:cd05922 99 AD-GIRAARASAPAhevshEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSV-L 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 226 SDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYhQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSER- 304
Cdd:cd05922 177 NTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELl 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 305 TGTRLYEGFGQTELSTYLSSAP--DFPRKPGTVGRAQPGRCVAILPEDGGDTslPPGEAGMIAVHRsdPGLMLGYWQRPD 382
Cdd:cd05922 256 PGAQVYVMYGQTEATRRMTYLPpeRILEKPGSIGLAIPGGEFEILDDDGTPT--PPGEPGEIVHRG--PNVMKGYWNDPP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 383 EEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVV 461
Cdd:cd05922 332 YRRKEGRGGgVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVT 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 503186189 462 AREGGADlsAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05922 411 APDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
13-515 |
1.02e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 184.09 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 13 RNLNMAKHVLRAGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFG 92
Cdd:PRK07470 5 RVMNLAHFLRQAARRFPDRIALV-------WGDRSWTWREIDARVDALAAALAA-RGVRKGDRILVHSRNCNQMFESMFA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 93 AIAGGLVPIPASPDLTARELGFLLDDSDAAAIvlddtLPHGDFAPGLAVVTEAAL-------------------IAAIDS 153
Cdd:PRK07470 77 AFRLGAVWVPTNFRQTPDEVAYLAEASGARAM-----ICHADFPEHAAAVRAASPdlthvvaiggaragldyeaLVARHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 154 GPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHrsvwGRR------------PmyrgwyGITAADRLMhsGVINWTYAM 221
Cdd:PRK07470 152 GARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTH----GQMafvitnhladlmP------GTTEQDASL--VVAPLSHGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 222 GTGLSDPLANGATALLYTGERH--PSIWpGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEA 299
Cdd:PRK07470 220 GIHQLCQVARGAATVLLPSERFdpAEVW-ALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 300 EWSERTGTRLYEGFGQTE-------LSTYLSSAPDFPR-KPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhrSDP 371
Cdd:PRK07470 299 RALAKLGKVLVQYFGLGEvtgnitvLPPALHDAEDGPDaRIGTCGFERTGMEVQIQDDEGRE--LPPGETGEICV--IGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 372 GLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPH 451
Cdd:PRK07470 375 AVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503186189 452 GGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK----------LKRSDLKIPQPP 515
Cdd:PRK07470 455 WGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKitkkmvreelEERGLLDLERAP 528
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
47-510 |
1.21e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 184.58 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV- 125
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVc 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 -------LDDTLPH-----------GDFAPGLAVVTEAALI-------------------AAIDSGPEGAF--ADTAADD 166
Cdd:PRK05677 129 lanmahlAEKVLPKtgvkhvivtevADMLPPLKRLLINAVVkhvkkmvpayhlpqavkfnDALAKGAGQPVteANPQADD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 167 PAFLIYTSGTTANPKGVLHAHRSVWGR----RPMYRGWYG-----ITAADRLMHsgvinwTYAMGTGLSDPLANGATALL 237
Cdd:PRK05677 209 VAVLQYTGGTTGVAKGAMLTHRNLVANmlqcRALMGSNLNegceiLIAPLPLYH------IYAFTFHCMAMMLIGNHNIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 238 YTgerHPSIWPGLIRAFDVTIFAGVPG---LYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFG 314
Cdd:PRK05677 283 IS---NPRDLPAMVKELGKWKFSGFVGlntLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 315 QTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE-WF 393
Cdd:PRK05677 360 MTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNE--LPLGEVGELCV--KGPQVMKGYWQRPEATDEILDSDgWL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 394 TGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAEL 473
Cdd:PRK05677 436 KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQV 515
|
490 500 510
....*....|....*....|....*....|....*..
gi 503186189 474 AARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK05677 516 MEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
21-509 |
1.32e-51 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 183.09 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 21 VLRAGAAAGDKTALVvihDPAGreAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:cd05923 7 LRRAASRAPDACAIA---DPAR--GLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVL-DDTLP-HGDFAPGLAVVTEAALI---AAIDSGPEGAFADTAADDPAFLIYTSG 175
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIaVDAQVmDAIFQSGVRVLALSDLVglgEPESAGPLIEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 176 TTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMG--TGLSDPLANGATALLYTgERHPSIWPGLIRA 253
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGffAVLVAALALDGTYVVVE-EFDPADALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 254 FDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTEL--STYLSSApdfprK 331
Cdd:cd05923 240 ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAmnSLYMRDA-----R 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 332 PGTVGRAQPGRCVAILPEDGG-DTSLPPGEAGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHL 410
Cdd:cd05923 315 TGTEMRPGFFSEVRIVRIGGSpDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRIL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 411 GRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHY 490
Cdd:cd05923 395 GRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRASELADFKRPRRY 474
|
490
....*....|....*....
gi 503186189 491 VFVERLPKTPNGKLKRSDL 509
Cdd:cd05923 475 FFLDELPKNAMNKVLRRQL 493
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-506 |
2.77e-51 |
|
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: 177.85 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR------LMHSGvinwtyAMGTGLSDPLANGATALLyt 239
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVylnmlpLFHIA------GLNLALATFHAGGANVVM-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 gERH-PSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRH--GLTAGDTLpdaleAEWSERTGTRLYEGFGQT 316
Cdd:cd17637 73 -EKFdPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHvlGLDAPETI-----QRFEETTGATFWSLYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 317 ELSTYLSSAPDFPRkPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhRSdPGLMLGYWQRPDEEREMFRGEWFTGG 396
Cdd:cd17637 147 ETSGLVTLSPYRER-PGSAGRPGPLVRVRIVDDNDRP--VPAGETGEIVV-RG-PLVFQGYWNLPELTAYTFRNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 397 DLGCIDEDGAIAHLGR--ASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELA 474
Cdd:cd17637 222 DLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 503186189 475 ARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
29-509 |
6.36e-51 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 180.56 E-value: 6.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 29 GDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLT 108
Cdd:cd12116 1 PDATAVR-------DDDRSLSYAELDERANRLAARLRA-RGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 109 ARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVvteAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHR 188
Cdd:cd12116 73 ADRLRYILEDAEPALVLTDDALPDRLPAGLPVL---LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 189 SV------WGRRPmyrgwyGITAADRLMHSGvinwTYAMGTGLSD---PLANGATALLYTGE--RHPSIWPGLIRAFDVT 257
Cdd:cd12116 150 NLvnflhsMRERL------GLGPGDRLLAVT----TYAFDISLLElllPLLAGARVVIAPREtqRDPEALARLIEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 258 IFAGVPGLYHqiMRQASGDRlDLARLRhGLTAGDTLPDALEAEWSERTGtRLYEGFGQTElSTYLSSAPDF--PRKPGTV 335
Cdd:cd12116 220 VMQATPATWR--MLLDAGWQ-GRAGLT-ALCGGEALPPDLAARLLSRVG-SLWNLYGPTE-TTIWSTAARVtaAAGPIPI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 336 GRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFR--------GEWFTGGDLGCIDEDGAI 407
Cdd:cd12116 294 GRPLANTQVYVLDAAL--RPVPPGVPGELYI--GGDGVAQGYLGRPALTAERFVpdpfagpgSRLYRTGDLVRRRADGRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 408 AHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVVAREGGADLSAELAARAEASLAAYKRP 487
Cdd:cd12116 370 EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVP 448
|
490 500
....*....|....*....|..
gi 503186189 488 RHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd12116 449 SAFVRLDALPLTANGKLDRKAL 470
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
26-506 |
1.29e-50 |
|
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: 179.37 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 26 AAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASP 105
Cdd:cd05945 2 AANPDRPAVVE-------GGRTLTYRELKERADALAAALAS-LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 106 DLTARELGFLLDDSDAAAIVLDDtlphgdfapglavvteaaliaaidsgpegafadtaaDDPAFLIYTSGTTANPKGVLH 185
Cdd:cd05945 74 SSPAERIREILDAAKPALLIADG------------------------------------DDNAYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 186 AHRSVwgrrPMYRGW----YGITAADRLMHS-------GVINWTYAmgtglsdpLANGATALLYTGE--RHPSIWPGLIR 252
Cdd:cd05945 118 SHDNL----VSFTNWmlsdFPLGPGDVFLNQapfsfdlSVMDLYPA--------LASGATLVPVPRDatADPKQLFRFLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 253 AFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERT-GTRLYEGFGQTElSTYLSSAPDFPRK 331
Cdd:cd05945 186 EHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTE-ATVAVTYIEVTPE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 332 PGT------VGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE----WFTGGDLGCI 401
Cdd:cd05945 265 VLDgydrlpIGYAKPGAKLVILDEDG--RPVPPGEKGELVI--SGPSVSKGYLNNPEKTAAAFFPDegqrAYRTGDLVRL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 402 DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGAD-LSAELAARAEAS 480
Cdd:cd05945 341 EADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgLTKAIKAELAER 420
|
490 500
....*....|....*....|....*.
gi 503186189 481 LAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd05945 421 LPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
17-510 |
2.40e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 179.03 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 17 MAKHVLRAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnrslAPRTRVLIRLRNRTAyaLAFFGAIAG 96
Cdd:PRK07787 2 ASLNPAAVAAAADIADAVRI-------GGRVLSRSDLAGAATAVAERVAG----ARRVAVLATPTLATV--LAVVGALIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 97 GLVPIPASPDLTARELGFLLDDSDAAAiVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEGAfadtaaddPAFLIYTSGT 176
Cdd:PRK07787 69 GVPVVPVPPDSGVAERRHILADSGAQA-WLGPAPDDPAGLPHVPVRLHARSWHRYPEPDPDA--------PALIVYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 177 TANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATaLLYTGERHPSiwpGLIRAFDV 256
Cdd:PRK07787 140 TGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNR-FVHTGRPTPE---AYAQALSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 257 --TIFAGVPGLYHQIMR-QASGDRLDLARLrhgLTAGDT-LPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKP 332
Cdd:PRK07787 216 ggTLYFGVPTVWSRIAAdPEAARALRGARL---LVSGSAaLPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 333 GTVGRAQPGRCVAILPEDGGDTSLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLG 411
Cdd:PRK07787 293 GWVGLPLAGVETRLVDEDGGPVPHDGETVGELQVR--GPTLFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 412 RAS-DLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADlsAELAARAEASLAAYKRPRHY 490
Cdd:PRK07787 371 REStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA--DELIDFVAQQLSVHKRPREV 448
|
490 500
....*....|....*....|
gi 503186189 491 VFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07787 449 RFVDALPRNAMGKVLKKQLL 468
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
13-511 |
2.75e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 180.36 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 13 RNLNMAKHVLRAGAAAGDKTALVVIhdpagreAETWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFG 92
Cdd:PRK07786 15 RRQNWVNQLARHALMQPDAPALRFL-------GNTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 93 AIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLPH-----GDFAPGLAVV------TEAALIAAID----SGPEG 157
Cdd:PRK07786 87 ANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPvatavRDIVPLLSTVvvaggsSDDSVLGYEDllaeAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 158 AFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMY-RGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATAL 236
Cdd:PRK07786 167 APVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTClRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 237 LYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIM--RQASGDRLDLARLRHGLT-AGDTLPDALEAEWSertGTRLYEGF 313
Cdd:PRK07786 247 YPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCaeQQARPRDLALRVLSWGAApASDTLLRQMAATFP---EAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTELS--TYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIaVHRSdPGLMLGYWQRPDEEREMFRGE 391
Cdd:PRK07786 324 GQTEMSpvTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMND--VPVGEVGEI-VYRA-PTLMSGYWNNPEATAEAFAGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLS- 470
Cdd:PRK07786 400 WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTl 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 503186189 471 AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKI 511
Cdd:PRK07786 480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
75-509 |
4.75e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 180.23 E-value: 4.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 75 RVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV-LDDTLPH------------------GDF 135
Cdd:PRK06710 76 RVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcLDLVFPRvtnvqsatkiehvivtriADF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 136 AP---------------GLAV-VTEAALIAAIDSGPEGAfaDTAAD---DP----AFLIYTSGTTANPKGVLHAHRSVWG 192
Cdd:PRK06710 156 LPfpknllypfvqkkqsNLVVkVSESETIHLWNSVEKEV--NTGVEvpcDPendlALLQYTGGTTGFPKGVMLTHKNLVS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 193 RRPMYRGW-YGITAADRLMhSGVINW--TYAMGTGLSDPLANGATALLYTGERHPSIWPGlIRAFDVTIFAGVPGLYHQI 269
Cdd:PRK06710 234 NTLMGVQWlYNCKEGEEVV-LGVLPFfhVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEA-IKKHKVTLFPGAPTIYIAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 270 MRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSapDF---PRKPGTVGRAQPGRCVAI 346
Cdd:PRK06710 312 LNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHS--NFlweKRVPGSIGVPWPDTEAMI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 347 LPEDGGDtSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSP 426
Cdd:PRK06710 390 MSLETGE-ALPPGEIGEIVV--KGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYP 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 427 VEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK06710 467 REVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
|
...
gi 503186189 507 SDL 509
Cdd:PRK06710 547 RVL 549
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
23-503 |
2.10e-49 |
|
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: 176.72 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTAlvvIHDPAGReaetWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:cd12118 12 RAAAVYPDRTS---IVYGDRR----YTWRQTYDRCRRLASAL-AALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTLPHGDFapglavvteaalIAAIDSGPEgafADTAAD--DPAFLIYTSGTTANP 180
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLFVDREFEYEDL------------LAEGDPDFE---WIPPADewDPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 181 KGVLHAHRSVwgrrpmYRGWYGITAADRLMHSGVINWTYAM----G-TGLSDPLANGATALLYTGERHPSIWpGLIRAFD 255
Cdd:cd12118 149 KGVVYHHRGA------YLNALANILEWEMKQHPVYLWTLPMfhcnGwCFPWTVAAVGGTNVCLRKVDAKAIY-DLIEKHK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 256 VTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEwSERTGTRLYEGFGQTElsTYlssapdfprKPGTV 335
Cdd:cd12118 222 VTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTE--TY---------GPATV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 336 GRAQPG------------------RCVAILPEDGGDT----SLP-PGE-AGMIAVHRSDpgLMLGYWQRPDEEREMFRGE 391
Cdd:cd12118 290 CAWKPEwdelpteerarlkarqgvRYVGLEEVDVLDPetmkPVPrDGKtIGEIVFRGNI--VMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSA 471
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510
....*....|....*....|....*....|..
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVErLPKTPNGK 503
Cdd:cd12118 448 EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
21-510 |
2.12e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 177.87 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 21 VLRAGAAAGDKTALVvihDPAGReaetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:PRK06188 18 LVSALKRYPDRPALV---LGDTR----LTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVLDDT------LPHGDFAPGL-------AVVTEAALIAAIDS-GPEGAFADTAADD 166
Cdd:PRK06188 90 TALHPLGSLDDHAYVLEDAGISTLIVDPApfveraLALLARVPSLkhvltlgPVPDGVDLLAAAAKfGPAPLVAAALPPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 167 PAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRlmhsgvinwtYAMGTglsdPLANGATALLYtgerhPSI 246
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPR----------FLMCT----PLSHAGGAFFL-----PTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 247 WPG----LIRAFD------------VTIFAGVPGLYHQIMRQASGDRLDLARLR---HGltAGDTLPDALeAEWSERTGT 307
Cdd:PRK06188 231 LRGgtviVLAKFDpaevlraieeqrITATFLVPTMIYALLDHPDLRTRDLSSLEtvyYG--ASPMSPVRL-AEAIERFGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 308 RLYEGFGQTELS---TYLSSA---PDFPRKPGTVGRAQPGRCVAILPEDGGDTslPPGEAGMIAVhrSDPGLMLGYWQRP 381
Cdd:PRK06188 308 IFAQYYGQTEAPmviTYLRKRdhdPDDPKRLTSCGRPTPGLRVALLDEDGREV--AQGEVGEICV--RGPLVMDGYWNRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 382 DEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVV 461
Cdd:PRK06188 384 EETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVV 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503186189 462 AREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK06188 464 LRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
10-510 |
2.81e-49 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 177.64 E-value: 2.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 10 LPPRNLNMAKHVLRAGAAAGDKTaLVVIHDpagreaETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALA 89
Cdd:PRK06155 16 LPPSERTLPAMLARQAERYPDRP-LLVFGG------TRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 90 FFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD-------DTLPHGDFAPGLAVVTEAALIAAIDSG------PE 156
Cdd:PRK06155 88 FLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEaallaalEAADPGDLPLPAVWLLDAPASVSVPAGwstaplPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 157 GAFADTAAD----DPAFLIYTSGTTANPKGVL--HAHRSVWGRrpMYRGWYGITAADRLMHSGVINWTYAMGTgLSDPLA 230
Cdd:PRK06155 168 LDAPAPAAAvqpgDTAAILYTSGTTGPSKGVCcpHAQFYWWGR--NSAEDLEIGADDVLYTTLPLFHTNALNA-FFQALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 231 NGATALLytGERHPS--IWPGLiRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGdtLPDALEAEWSERTGTR 308
Cdd:PRK06155 245 AGATYVL--EPRFSAsgFWPAV-RRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERFGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 309 LYEGFGQTELSTYLSSAPDFPRkPGTVGRAQPGRCVAILPEDggDTSLPPGEAGMIAVHRSDPG-LMLGYWQRPDEEREM 387
Cdd:PRK06155 320 LLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVVDEH--DQELPDGEPGELLLRADEPFaFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 388 FRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGA 467
Cdd:PRK06155 397 WRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 503186189 468 DLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK06155 477 LEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
23-509 |
7.86e-49 |
|
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: 175.61 E-value: 7.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:cd17651 3 RQAARTPDAPALVA-------EGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTLPHgDFAPGLAVVTEAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKG 182
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLTHPALAG-ELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 183 VLHAHRSV-----WGRRpmyrgWYGITAADRLMHSGVINWTYAMGTGLSdPLANGATALLYTGE--RHPSIWPGLIRAFD 255
Cdd:cd17651 154 VVMPHRSLanlvaWQAR-----ASSLGPGARTLQFAGLGFDVSVQEIFS-TLCAGATLVLPPEEvrTDPPALAAWLDEQR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 256 VTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLP-DALEAEW-SERTGTRLYEGFGQTE--LSTY--LSSAPDFP 329
Cdd:cd17651 228 ISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFcAGLPGLRLHNHYGPTEthVVTAlsLPGDPAAW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 330 RKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG-------GDLGCID 402
Cdd:cd17651 308 PAPPPIGRPIDNTRVYVL--DAALRPVPPGVPGELYI--GGAGLARGYLNRPELTAERFVPDPFVPgarmyrtGDLARWL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 403 EDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLA 482
Cdd:cd17651 384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLP 463
|
490 500
....*....|....*....|....*..
gi 503186189 483 AYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd17651 464 EYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
30-510 |
4.07e-48 |
|
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: 172.55 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpagrEAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:cd17649 2 DAVALVF-------GDQSLSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSdAAAIVLDDtlpHGDfapglavvteaaliaaidsgpegafadtaadDPAFLIYTSGTTANPKGVLHAHRS 189
Cdd:cd17649 74 ERLRYMLEDS-GAGLLLTH---HPR-------------------------------QLAYVIYTSGSTGTPKGVAVSHGP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 190 VWGRRPMYRGWYGITAADRLMHSGVINWTYAMgTGLSDPLANGATALLytgeRHPSIWPG------LIRAFDVTIFAGVP 263
Cdd:cd17649 119 LAAHCQATAERYGLTPGDRELQFASFNFDGAH-EQLLPPLICGACVVL----RPDELWASadelaeMVRELGVTVLDLPP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 264 GLYHQIMRQA--SGDRlDLARLRHGLTAGDTLPDALEAEWsERTGTRLYEGFGQTE---LSTYLSSAPDFPRKPGTV--G 336
Cdd:cd17649 194 AYLQQLAEEAdrTGDG-RPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEatvTPLVWKCEAGAARAGASMpiG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 337 RAQPGRCVAILPEDGGdtSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF--------RGEWFTGGDLGCIDEDGAIA 408
Cdd:cd17649 272 RPLGGRSAYILDADLN--PVPVGVTGELYI--GGEGLARGYLGRPELTAERFvpdpfgapGSRLYRTGDLARWRDDGVIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 409 HLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVVAREG--GADLSAELAARAEASLAAYKR 486
Cdd:cd17649 348 YLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAaaQPELRAQLRTALRASLPDYMV 426
|
490 500
....*....|....*....|....
gi 503186189 487 PRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd17649 427 PAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
13-514 |
4.49e-48 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 177.15 E-value: 4.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 13 RNLNMAKHVLRAGAAAG--DKtalvvihdPAGREAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAF 90
Cdd:PRK06060 2 RNGNLAGLLAEQASEAGwyDR--------PAFYAADVVTHGQIHDGAARLGEVLR-NRGLSSGDRVLLCLPDSPDLVQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 91 FGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLpHGDFAPGLAVVTEAALIAAIDSGPEGaFADTAADDPAFL 170
Cdd:PRK06060 73 LACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL-RDRFQPSRVAEAAELMSEAARVAPGG-YEPMGGDALAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 171 IYTSGTTANPKGVLHAHRSVWG-RRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIWPG 249
Cdd:PRK06060 151 TYTSGTTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 250 LIRAFDVTIFAGVPGLYHQIMRQASGDrlDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTEL-STYLSSAPD 327
Cdd:PRK06060 231 LSARFGPSVLYGVPNFFARVIDSCSPD--SFRSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTEVgQTFVSNRVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 328 FPRkPGTVGRAQPGRCVAILPEDGGDTSlpPGEAGMIAVHrsDPGLMLGYWQRPDEEREmfRGEWFTGGDLGCIDEDGAI 407
Cdd:PRK06060 309 EWR-LGTLGRVLPPYEIRVVAPDGTTAG--PGVEGDLWVR--GPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 408 AHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG-GADLSA--ELAARAEASLAAY 484
Cdd:PRK06060 382 TYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGaTIDGSVmrDLHRGLLNRLSAF 461
|
490 500 510
....*....|....*....|....*....|
gi 503186189 485 KRPRHYVFVERLPKTPNGKLKRSDLKIPQP 514
Cdd:PRK06060 462 KVPHRFAVVDRLPRTPNGKLVRGALRKQSP 491
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
26-515 |
4.66e-48 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 179.28 E-value: 4.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 26 AAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAI-AGG-LVPI-P 102
Cdd:COG1020 487 ARTPDAVAVVF-------GDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEMVVALLAVLkAGAaYVPLdP 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDltAReLGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVT--EAALIAAIDSGPEgafADTAADDPAFLIYTSGTTANP 180
Cdd:COG1020 559 AYPA--ER-LAYMLEDAGARLVLTQSALAARLPELGVPVLAldALALAAEPATNPP---VPVTPDDLAYVIYTSGSTGRP 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 181 KGVLHAHRSVWGRRPMYRGWYGITAADRLMHSgvinwtyamgTGLS-D--------PLANGATALLYTGE--RHPSIWPG 249
Cdd:COG1020 633 KGVMVEHRALVNLLAWMQRRYGLGPGDRVLQF----------ASLSfDasvweifgALLSGATLVLAPPEarRDPAALAE 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 250 LIRAFDVTIFAGVPGLYHQIMRQASGDrldLARLRHGLTAGDTLPDALEAEWSERT-GTRLYEGFGQTE----LSTYLSS 324
Cdd:COG1020 703 LLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTEttvdSTYYEVT 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 325 APDFPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPD--EER-----EMFRGE-WFTGG 396
Cdd:COG1020 780 PPDADGGSVPIGRPIANTRVYVL--DAHLQPVPVGVPGELYI--GGAGLARGYLNRPEltAERfvadpFGFPGArLYRTG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 397 DLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAAR 476
Cdd:COG1020 856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA 935
|
490 500 510
....*....|....*....|....*....|....*....
gi 503186189 477 AEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKIPQPP 515
Cdd:COG1020 936 LALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAA 974
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
47-445 |
5.08e-48 |
|
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: 172.39 E-value: 5.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVL 126
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 127 DDtlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRSVwgrrpmyrgWYGITAA 206
Cdd:cd05907 84 ED-----------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNI---------LSNALAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 DRLMHSGVIN---------WTYAMGTGLSDPLANGATalLYTGERHPSIWPGLiRAFDVTIFAGVP----GLYHQIMRQA 273
Cdd:cd05907 120 AERLPATEGDrhlsflplaHVFERRAGLYVPLLAGAR--IYFASSAETLLDDL-SEVRPTVFLAVPrvweKVYAAIKVKA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 274 SG-------DRLDLARLRHGLTAGDTLPDALeAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAI 346
Cdd:cd05907 197 VPglkrklfDLAVGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 347 lpedggdtslppGEAGMIAVHrsDPGLMLGYWQRPDEERE-MFRGEWFTGGDLGCIDEDGAIAHLGRASDLM-NAGGYRV 424
Cdd:cd05907 276 ------------ADDGEILVR--GPNVMLGYYKNPEATAEaLDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNI 341
|
410 420
....*....|....*....|.
gi 503186189 425 SPVEVEAVLREHPLVAEAGVI 445
Cdd:cd05907 342 SPEPIENALKASPLISQAVVI 362
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
46-510 |
5.12e-48 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 174.47 E-value: 5.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:PRK08974 47 EVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 LDDTLPH-------------------GD---FAPGLAV----------VTEAALIAAI---DSGPEGAF-----ADTAAD 165
Cdd:PRK08974 127 IVSNFAHtlekvvfktpvkhviltrmGDqlsTAKGTLVnfvvkyikrlVPKYHLPDAIsfrSALHKGRRmqyvkPELVPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSV--------WGRRPMYR-GWYGITAADRLMHsgvinwTYAMGTGLSDPLANGATAL 236
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNMlanleqakAAYGPLLHpGKELVVTALPLYH------IFALTVNCLLFIELGGQNL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 237 LYTgerHPSIWPGLI---RAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGF 313
Cdd:PRK08974 281 LIT---NPRDIPGFVkelKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGEW 392
Cdd:PRK08974 358 GLTECSPLVSVNPyDLDYYSGSIGLPVPSTEIKLVDDDGNE--VPPGEPGELWVK--GPQVMLGYWQRPEATDEVIKDGW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 393 FTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREggADLSA- 471
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEe 511
|
490 500 510
....*....|....*....|....*....|....*....
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK08974 512 ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
44-509 |
7.53e-48 |
|
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: 171.72 E-value: 7.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 44 EAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLrNRTAYALAFFGAI--AGG-LVPI-PASPDltAReLGFLLDDS 119
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRA-EGVGPGDRVALAL-PRSAELIVALLAIlkAGGaYVPIdPAYPV--ER-IAFILADS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 120 DAAAIVlddtlphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANPKGVLHAHRSV----WGRRP 195
Cdd:cd17643 84 GPSLLL------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVlalfAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 196 myrgWYGITAADR--LMHSGVIN---WTyamgtgLSDPLANGATALL--YTGERHPSIWPGLIRAFDVTIFAGVPGLYHQ 268
Cdd:cd17643 128 ----WFGFNEDDVwtLFHSYAFDfsvWE------IWGALLHGGRLVVvpYEVARSPEDFARLLRDEGVTVLNQTPSAFYQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 269 IMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTG---TRLYEGFGQTE---LSTY--LSSAPDFPRKPGTVGRAQP 340
Cdd:cd17643 198 LVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGldrPQLVNMYGITEttvHVTFrpLDAADLPAAAASPIGRPLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 341 GRCVAILPEDGGDtsLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG--------GDLGCIDEDGAIAHLGR 412
Cdd:cd17643 278 GLRVYVLDADGRP--VPPGVVGELYV--SGAGVARGYLGRPELTAERFVANPFGGpgsrmyrtGDLARRLPDGELEYLGR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 413 ASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVF 492
Cdd:cd17643 354 ADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVP 433
|
490
....*....|....*..
gi 503186189 493 VERLPKTPNGKLKRSDL 509
Cdd:cd17643 434 LDALPLTVNGKLDRAAL 450
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
30-510 |
9.78e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 172.45 E-value: 9.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpagrEAETWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTA-----YALAFFGAIAGGLvpipaS 104
Cdd:PRK03640 17 DRTAIEF-------EEKKVTFMELHEAVVSVAGKL-AALGVKKGDRVALLMKNGMEmilviHALQQLGAVAVLL-----N 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 105 PDLTARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEGAFADtaaDDPAFLIYTSGTTANPKGVL 184
Cdd:PRK03640 84 TRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDL---DEVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 185 HAHRSVWgrrpmyrgW--------YGITAADR------LMH-SG-------VInwtYAMGTGLSDPL-ANGATALLYTGE 241
Cdd:PRK03640 161 QTYGNHW--------WsavgsalnLGLTEDDCwlaavpIFHiSGlsilmrsVI---YGMRVVLVEKFdAEKINKLLQTGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 242 rhpsiwpglirafdVTIFAGVPGLYHQIMRQASGDRLDlARLRHGLTAGDTLPDALEAEWSERtGTRLYEGFGQTELSTY 321
Cdd:PRK03640 230 --------------VTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETASQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 322 LSS-APDFPR-KPGTVGraQPGRCVAILPEDGGdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLG 399
Cdd:PRK03640 294 IVTlSPEDALtKLGSAG--KPLFPCELKIEKDG-VVVPPFEEGEIVV--KGPNVTKGYLNREDATRETFQDGWFKTGDIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 400 CIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVArEGGADlSAELAARAEA 479
Cdd:PRK03640 369 YLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-SGEVT-EEELRHFCEE 446
|
490 500 510
....*....|....*....|....*....|.
gi 503186189 480 SLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK03640 447 KLAKYKVPKRFYFVEELPRNASGKLLRHELK 477
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
29-504 |
1.28e-47 |
|
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: 173.92 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 29 GDKTAlvVIHDPA-GREAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDL 107
Cdd:cd17634 67 GDRTA--IIYEGDdTSQSRTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 108 TARELGFLLDDSDAAAIVL-DDTLPHGDFAPGLAVVTEAALIAAI------------------------------DSGPE 156
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITaDGGVRAGRSVPLKKNVDDALNPNVTsvehvivlkrtgsdidwqegrdlwwrdliaKASPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 157 GAFADTAADDPAFLIYTSGTTANPKGVLHAHrsvwGRRPMYRGW-----YGITAADRLMHSGVINWTYAMGTGLSDPLAN 231
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTT----GGYLVYAATtmkyvFDYGPGDIYWCTADVGWVTGHSYLLYGPLAC 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 232 GATALLYTGErhpSIWPGLIRAFDVTIFAGVPGLYH-----QIMRQASGD---RLDLARLRHGLTAGDTL-PDALEAEWS 302
Cdd:cd17634 300 GATTLLYEGV---PNWPTPARMWQVVDKHGVNILYTaptaiRALMAAGDDaieGTDRSSLRILGSVGEPInPEAYEWYWK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 303 ERTGTR--LYEGFGQTELSTYLSS--APDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRSDPGLMLGYW 378
Cdd:cd17634 377 KIGKEKcpVVDTWWQTETGGFMITplPGAIELKAGSATRPVFGVQPAVVDNEG--HPQPGGTEGNLVITDPWPGQTRTLF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 379 QRPDEEREM----FRGEWFTGgDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGT 454
Cdd:cd17634 455 GDHERFEQTyfstFKGMYFSG-DGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503186189 455 AITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKL 504
Cdd:cd17634 534 APYAYVVLNHGvepSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
49-510 |
2.43e-47 |
|
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: 171.36 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSNRslAPRTRVLIRLRNRTAYALAFFGAIAGGLVPI----PASPD--------------LTAR 110
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVmlnyTAGLRelraciklagiktvLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 111 EL-------GFLLDDSDAAAIVLDDTLPHGDFAPGLAVVTeAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGV 183
Cdd:cd05909 87 QFieklklhHLFDVEYDARIVYLEDLRAKISKADKCKAFL-AGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 184 LHAHRSVWGRRPMYRGWYGITAADRLM------HSgvinwtYAMGTGLSDPLANGATALLYTGERHPSIWPGLIRAFDVT 257
Cdd:cd05909 166 VLSHKNLLANVEQITAIFDPNPEDVVFgalpffHS------FGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 258 IFAGVPGLYHQIMRQASGDrlDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLS-SAPDFPRKPGTVG 336
Cdd:cd05909 240 ILLGTPTFLRGYARAAHPE--DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISvNTPQSPNKEGTVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 337 RAQPGRCVAILPEDGGdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDL 416
Cdd:cd05909 318 RPLPGMEVKIVSVETH-EEVPIGEGGLLLV--RGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 417 MNAGGYRVSPVEVEAVLREH-PLVAEAGVIDVPQPHGGTAITAFVVAREGGAD-LSAELAARAEASLAaykRPRHYVFVE 494
Cdd:cd05909 395 AKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSsLNDILKNAGISNLA---KPSYIHQVE 471
|
490
....*....|....*.
gi 503186189 495 RLPKTPNGKLKRSDLK 510
Cdd:cd05909 472 EIPLLGTGKPDYVTLK 487
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
30-509 |
1.06e-46 |
|
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: 169.37 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:cd12114 2 DATAVI-------CGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVteaALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRS 189
Cdd:cd12114 74 ARREAILADAGARLVLTDGPDAQLDVAVFDVLI---LDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 190 VW------GRRpmyrgwYGITAADRLMhsgvinwtyamgtGLSD------------PLANGATALLYTGE--RHPSIWPG 249
Cdd:cd12114 151 ALntildiNRR------FAVGPDDRVL-------------ALSSlsfdlsvydifgALSAGATLVLPDEArrRDPAHWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 250 LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGD----TLPDALEAEWSertGTRLYEGFGQTEL---STYL 322
Cdd:cd12114 212 LIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDwiplDLPARLRALAP---DARLISLGGATEAsiwSIYH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 323 SSAPDFPR-KPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIavHRSDPGLMLGYWQRPDEEREMF-----RGEWFTGG 396
Cdd:cd12114 289 PIDEVPPDwRSIPYGRPLANQRYRVLDPRGRD--CPDWVPGEL--WIGGRGVALGYLGDPELTAARFvthpdGERLYRTG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 397 DLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVVAREGGA-DLSAELAA 475
Cdd:cd12114 365 DLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTpIAPDALRA 443
|
490 500 510
....*....|....*....|....*....|....
gi 503186189 476 RAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd12114 444 FLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
20-510 |
2.47e-46 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 169.85 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAAGDKTALVVIHDPAGrEAETWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNR-----TAYALAFFGAI 94
Cdd:PRK13295 29 DLDACVASCPDKTAVTAVRLGTG-APRRFTYRELAALVDRVAVGL-ARLGVGRGDVVSCQLPNWweftvLYLACSRIGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 95 AGGLVPIpaspdLTARELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVVTEA--AL--IAAIDSGPEGAFAD--------- 161
Cdd:PRK13295 107 LNPLMPI-----FRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPElpALrhVVVVGGDGADSFEAllitpaweq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 162 ------------TAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAAD-RLMHSGVINWTYAMgTGLSDP 228
Cdd:PRK13295 182 epdapailarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDvILMASPMAHQTGFM-YGLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 LANGATALLYtgerhpSIWP-----GLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSE 303
Cdd:PRK13295 261 VMLGATAVLQ------DIWDparaaELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 304 RTGTRLYEGFGQTE---LSTYLSSAPDfPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhRSdPGLMLGYWQR 380
Cdd:PRK13295 335 ALGAKIVSAWGMTEngaVTLTKLDDPD-ERASTTDGCPLPGVEVRVV--DADGAPLPAGQIGRLQV-RG-CSNFGGYLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 381 PDEEREMFRGeWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFV 460
Cdd:PRK13295 410 PQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 503186189 461 VAREG-GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK13295 489 VPRPGqSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
23-510 |
2.78e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 170.91 E-value: 2.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVIHDPAG-REAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVpI 101
Cdd:PRK07529 33 RAAARHPDAPALSFLLDADPlDRPETWTYAELLADVTRTANLLHS-LGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-N 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 102 PASPDLTARELGFLLDDSDAAAIVL----------DDTLPHGDFAPGLAVVTEAALI----------------------- 148
Cdd:PRK07529 111 PINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwQKVAEVLAALPELRTVVEVDLArylpgpkrlavplirrkaharil 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 149 ---AAIDSGP-EGAFADTA--ADDPAFLIYTSGTTANPKGVLHAHRSVwgrrpMYRGWYGITAADR-----------LMH 211
Cdd:PRK07529 191 dfdAELARQPgDRLFSGRPigPDDVAAYFHTGGTTGMPKLAQHTHGNE-----VANAWLGALLLGLgpgdtvfcglpLFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 212 SGVinwtyAMGTGLSdPLANGATALLYT--GERHPS----IWpGLIRAFDVTIFAGVPGLYHQIMRQASGDRlDLARLRH 285
Cdd:PRK07529 266 VNA-----LLVTGLA-PLARGAHVVLATpqGYRGPGvianFW-KIVERYRINFLSGVPTVYAALLQVPVDGH-DISSLRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 286 GLTAGDTLPDALEAEWSERTGTRLYEGFGQTElSTYLSSA--PDFPRKPGTVGRAQPGRCVAILPEDGGDTSL---PPGE 360
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSSVnpPDGERRIGSVGLRLPYQRVRVVILDDAGRYLrdcAVDE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVA 440
Cdd:PRK07529 417 VGVLCI--AGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVA 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 441 EAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAayKR---PRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07529 495 LAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIA--ERaavPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
48-511 |
3.33e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 168.06 E-value: 3.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 48 WTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRR-RGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 DTLPHGdfapGLAVVTEAALIAAIDsGPEGAFADTA-ADDPAFLIYTSGTTANPKGVLHAHR---------SVWGRrpmy 197
Cdd:PRK09088 102 DAVAAG----RTDVEDLAAFIASAD-ALEPADTPSIpPERVSLILFTSGTSGQPKGVMLSERnlqqtahnfGVLGR---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 198 rgwygITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTG-ERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGD 276
Cdd:PRK09088 173 -----VDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGfEPKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGFD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 277 RLDLARLRHGLTAGDTLPDALEAEWSERtGTRLYEGFGQTELSTYLSSAPDFPR---KPGTVGRAQPGRCVAILPEDGGD 353
Cdd:PRK09088 248 AAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIPTPTVQTRVVDDQGND 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 354 tsLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAV 432
Cdd:PRK09088 327 --CPAGVPGELLL--RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 433 LREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKI 511
Cdd:PRK09088 403 LADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
35-506 |
5.54e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 167.77 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 35 VVIHDPAGreaETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGF 114
Cdd:PRK08276 2 AVIMAPSG---EVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 115 LLDDSDAAAIVLddtlpHGDFAPGLAVVTEAA-----LIAAIDSGPEG---------AFADTAADDPAF---LIYTSGTT 177
Cdd:PRK08276 78 IVDDSGAKVLIV-----SAALADTAAELAAELpagvpLLLVVAGPVPGfrsyeealaAQPDTPIADETAgadMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 178 ANPKGVLhahRSVWGRRPMYRG---------WYGITAADR------LMHSGVINW---TYAMGtGLS------DPLanGA 233
Cdd:PRK08276 153 GRPKGIK---RPLPGLDPDEAPgmmlallgfGMYGGPDSVylspapLYHTAPLRFgmsALALG-GTVvvmekfDAE--EA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 234 TALLytgERHpsiwpglirafDVTIFAGVPGLYHQIMR--QASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYE 311
Cdd:PRK08276 227 LALI---ERY-----------RVTHSQLVPTMFVRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 312 GFGQTEL--STYLSSApDFPRKPGTVGRAQPGRcVAILPEDGGDtsLPPGEAGMIAVHRsdPGLMLGYWQRPDEEREMFR 389
Cdd:PRK08276 293 YYASSEGggVTVITSE-DWLAHPGSVGKAVLGE-VRILDEDGNE--LPPGEIGTVYFEM--DGYPFEYHNDPEKTAAARN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 390 GE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG--- 465
Cdd:PRK08276 367 PHgWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGada 446
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 503186189 466 GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKL-KR 506
Cdd:PRK08276 447 GDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLyKR 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-514 |
7.77e-46 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 172.83 E-value: 7.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 20 HVLRAGAAAGDKTALVVIHDpagreAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLV 99
Cdd:PRK12316 4554 HQLVAERARMTPDAVAVVFD-----EEKLTYAELNRRANRLAHALIA-RGVGPEVLVGIAMERSAEMMVGLLAVLKAGGA 4627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 100 PIPASPDLTARELGFLLDDSDAAAIvlddtLPHGDFAPGLAVvteAALIAAIDSGPEGAFADTAADDP---------AFL 170
Cdd:PRK12316 4628 YVPLDPEYPRERLAYMMEDSGAALL-----LTQSHLLQRLPI---PDGLASLALDRDEDWEGFPAHDPavrlhpdnlAYV 4699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 171 IYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAmGTGLSDPLANGATALLytgeRHPSIWP-- 248
Cdd:PRK12316 4700 IYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGS-HEGLYHPLINGASVVI----RDDSLWDpe 4774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 249 ---GLIRAFDVTIFAGVPGLYHQIMRQASGDRlDLARLRHGLTAGDTL-PDALEAEWSERTGTRLYEGFGQTE---LSTY 321
Cdd:PRK12316 4775 rlyAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVaQASYDLAWRALKPVYLFNGYGPTEttvTVLL 4853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 322 LSSAPDFPRKPGTV--GRAQPGRCVAILpeDGGDTSLPPGEAGmiAVHRSDPGLMLGYWQRPDEEREMF--------RGE 391
Cdd:PRK12316 4854 WKARDGDACGAAYMpiGTPLGNRSGYVL--DGQLNPLPVGVAG--ELYLGGEGVARGYLERPALTAERFvpdpfgapGGR 4929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHgGTAITAFVV--------AR 463
Cdd:PRK12316 4930 LYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVpqdpaladAD 5008
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 503186189 464 EGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLkiPQP 514
Cdd:PRK12316 5009 EAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL--PQP 5057
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
11-445 |
1.40e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 165.66 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 11 PPRNLNMAKHVLRAGAAAGDKTALvviHDPAGREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAF 90
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL---REKEDGIWQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 91 FGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDT------LPHGDFAPGL---------------AVVTEAALIA 149
Cdd:COG1022 83 LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldklLEVRDELPSLrhivvldprglrddpRLLSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 150 A-IDSGPEGAFADTAA----DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLM------HSGVINWT 218
Cdd:COG1022 163 LgREVADPAELEARRAavkpDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplaHVFERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 219 YAMgtglsdpLANGATalLYTGERHPSIWPGLiRAFDVTIFAGVPGLYHQI-------MRQASGDR-------LDLA-RL 283
Cdd:COG1022 243 YYA-------LAAGAT--VAFAESPDTLAEDL-REVKPTFMLAVPRVWEKVyagiqakAEEAGGLKrklfrwaLAVGrRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTLPDALEAEWS-----------ERTGTRL-------------------------YEGFGQTELSTYLSSAPD 327
Cdd:COG1022 313 ARARLAGKSPSLLLRLKHAladklvfsklrEALGGRLrfavsggaalgpelarffralgipvLEGYGLTETSPVITVNRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 328 FPRKPGTVGRAQPGRCVAIlpedggdtslppGEAGMIAVhRSdPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGa 406
Cdd:COG1022 393 GDNRIGTVGPPLPGVEVKI------------AEDGEILV-RG-PNVMKGYYKNPEATAEAFDADgWLHTGDIGELDEDG- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 503186189 407 iaHL---GRASDLM-NAGGYRVSPVEVEAVLREHPLVAEAGVI 445
Cdd:COG1022 458 --FLritGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
47-510 |
6.75e-44 |
|
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: 160.20 E-value: 6.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDaaaIVL 126
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD---VKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 127 DDTlphgdfapglavvteaaliaaidsgpegafadtaaddpAFLIYTSGTTANPKGVLHAHRSVWgrrpmyrgWYGITAA 206
Cdd:cd05912 77 DDI--------------------------------------ATIMYTSGTTGKPKGVQQTFGNHW--------WSAIGSA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 DRLMHSGVINWTYAMG----TGLS---DPLANGATALLYtgER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQasGDRL 278
Cdd:cd05912 111 LNLGLTEDDNWLCALPlfhiSGLSilmRSVIYGMTVYLV--DKfDAEQVLHLINSGKVTIISVVPTMLQRLLEI--LGEG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 DLARLRHGLTAGDTLPDALEAEWSERtGTRLYEGFGQTELSTYLSSAP--DFPRKPGTVGRAQPGRCVAILPEDGgdtsl 356
Cdd:cd05912 187 YPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCSQIVTLSpeDALNKIGSAGKPLFPVELKIEDDGQ----- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 357 PPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREH 436
Cdd:cd05912 261 PPYEVGEILL--KGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSH 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 437 PLVAEAGVIDVPQPHGGTAITAFVVAREggaDLS-AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05912 339 PAIKEAGVVGIPDDKWGQVPVAFVVSER---PISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-512 |
9.90e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 166.67 E-value: 9.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNMAKHVLRAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFF 91
Cdd:PRK12316 2000 PRGPGVHQRIAEQAARAPEAIAVVF-------GDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALL 2071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 92 GAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV----LDDTLPHGDFAPGLAVVTEAALIAAIDSGPEgafADTAADDP 167
Cdd:PRK12316 2072 AVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLtqrhLLERLPLPAGVARLPLDRDAEWADYPDTAPA---VQLAGENL 2148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 168 AFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMgTGLSDPLANGATALLytgeRHPSIW 247
Cdd:PRK12316 2149 AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAH-EQWFHPLLNGARVLI----RDDELW 2223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 248 -PG----LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLArLRHGLTAGDTLPDALEAEWSERTGT-RLYEGFGQTE---L 318
Cdd:PRK12316 2224 dPEqlydEMERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPvYLFNGYGPTEavvT 2302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 319 STYLSSAPDFPRKPGTV--GRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG- 395
Cdd:PRK12316 2303 PLLWKCRPQDPCGAAYVpiGRALGNRRAYIL--DADLNLLAPGMAGELYL--GGEGLARGYLNRPGLTAERFVPDPFSAs 2378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 396 -------GDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVVAREGGAD 468
Cdd:PRK12316 2379 gerlyrtGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAED 2457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 503186189 469 LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKIP 512
Cdd:PRK12316 2458 LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP 2501
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
164-506 |
5.98e-43 |
|
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: 161.65 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAFLIYTSGTTANPKGVLHA-----------HRSVWGRRPMYRGWygiTAADrlmhsgvINWTyamgTGLS----DP 228
Cdd:TIGR02188 236 SEDPLFILYTSGSTGKPKGVLHTtggyllyaamtMKYVFDIKDGDIFW---CTAD-------VGWI----TGHSyivyGP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 LANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARLRHGLTAGDtlPDALEA-EWs 302
Cdd:TIGR02188 302 LANGATTVMFEGVptyPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEwvKKHDLSSLRLLGSVGE--PINPEAwMW- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 303 ertgtrLYEGFGQTE---LSTY---------LSSAPD-FPRKPGTVGRAQPGRCVAILPEDGgdTSLP-PGEAGMIAVHR 368
Cdd:TIGR02188 379 ------YYKVVGKERcpiVDTWwqtetggimITPLPGaTPTKPGSATLPFFGIEPAVVDEEG--NPVEgPGEGGYLVIKQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 369 SDPGLMLGYWQRPDEERE----MFRGEWFTgGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGV 444
Cdd:TIGR02188 451 PWPGMLRTIYGDHERFVDtyfsPFPGYYFT-GDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAV 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 445 IDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:TIGR02188 530 VGIPDDIKGQAIYAFVTLKDGyepDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
164-510 |
7.00e-43 |
|
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: 161.19 E-value: 7.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAFLIYTSGTTANPKGVLHA-----------HRSVWGRRPMYRGWygiTAADrlmhsgvINWTyamgTGLS----DP 228
Cdd:cd05966 230 SEDPLFILYTSGSTGKPKGVVHTtggyllyaattFKYVFDYHPDDIYW---CTAD-------IGWI----TGHSyivyGP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 LANGATALLYTGER---HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARLRHGLTAGDtlPDALEA-EWs 302
Cdd:cd05966 296 LANGATTVMFEGTPtypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEwvKKHDLSSLRVLGSVGE--PINPEAwMW- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 303 ertgtrLYEGFG-----------QTE----LSTYLSSApdFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVH 367
Cdd:cd05966 373 ------YYEVIGkercpivdtwwQTEtggiMITPLPGA--TPLKPGSATRPFFGIEPAILDEEGNE--VEGEVEGYLVIK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 368 RSDPGLMLGYWQrpDEEREM------FRGEWFTGgDlGCI-DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVA 440
Cdd:cd05966 443 RPWPGMARTIYG--DHERYEdtyfskFPGYYFTG-D-GARrDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVA 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 441 EAGVIDVPQPHGGTAITAFVVAREGGA---DLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05966 519 EAAVVGRPHDIKGEAIYAFVTLKDGEEpsdELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILR 591
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-510 |
6.24e-42 |
|
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: 153.20 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVW------GRRpmyrgwYGITAADR------LMH-SGVInwtyaMGTGLSdpLAN 231
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVnngyfiGER------LGLTEQDRlcipvpLFHcFGSV-----LGVLAC--LTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 232 GATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTG-TRLY 310
Cdd:cd05917 69 GATMVFPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTELS--TYLSSAPD-FPRKPGTVGRAQPGRCVAILPEDGGdTSLPPGEAGMIAVHRSdpGLMLGYWQRPDEEREM 387
Cdd:cd05917 149 IAYGMTETSpvSTQTRTDDsIEKRVNTVGRIMPHTEAKIVDPEGG-IVPPVGVPGELCIRGY--SVMKGYWNDPEKTAEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 388 FRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGG 466
Cdd:cd05917 226 IDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503186189 467 ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05917 306 ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
24-503 |
7.38e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 156.97 E-value: 7.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 24 AGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPA 103
Cdd:PRK07798 12 VADAVPDRVALV-------CGDRRLTYAELEERANRLAHYLIA-QGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 104 SPDLTARELGFLLDDSDAAAIVLDDT-----------LPH------------GDFAPGlAVVTEAALIAaidSGPEGAFA 160
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREfaprvaevlprLPKlrtlvvvedgsgNDLLPG-AVDYEDALAA---GSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 161 DTAADDpAFLIYTSGTTANPKGVLHAHRSVW----GRRPMYRGWY---------GITAADR--------LMHsGVINWTy 219
Cdd:PRK07798 160 ERSPDD-LYLLYTGGTTGMPKGVMWRQEDIFrvllGGRDFATGEPiedeeelakRAAAGPGmrrfpappLMH-GAGQWA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 220 AMGTglsdpLANGATALLYTGER-HP-SIWPgLIRAFDVTIFAGVPGLYHQIMRQA--SGDRLDLARLRHGLTAGDTLPD 295
Cdd:PRK07798 237 AFAA-----LFSGQTVVLLPDVRfDAdEVWR-TIEREKVNVITIVGDAMARPLLDAleARGPYDLSSLFAIASGGALFSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 296 ALEAEWSERTGTR-LYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPG--EAGMIAvhRSDPg 372
Cdd:PRK07798 311 SVKEALLELLPNVvLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNP--VEPGsgEIGWIA--RRGH- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 373 LMLGYWQRPDEEREMFR---GE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVP 448
Cdd:PRK07798 386 IPLGYYKDPEKTAETFPtidGVrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 449 QPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:PRK07798 466 DERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
76-506 |
3.99e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.27 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 76 VLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLphgDFAPGLA---VVTEAALIAAID 152
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEF---DAIVALEtpkIVIDAAAQADSR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 153 SGPEGAFADT-----AADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMhsgVINWTYAMGT---- 223
Cdd:PRK06145 132 RLAQGGLEIPpqaavAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLL---VVGPLYHVGAfdlp 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 224 GLSdPLANGATaLLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSE 303
Cdd:PRK06145 209 GIA-VLWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 304 R-TGTRLYEGFGQTEL---STYLSSAPDFpRKPGTVGRAQPGRCVAILPEDGGdtSLPPGEAGMIAVhrSDPGLMLGYWQ 379
Cdd:PRK06145 287 VfTRARYIDAYGLTETcsgDTLMEAGREI-EKIGSTGRALAHVEIRIADGAGR--WLPPNMKGEICM--RGPKVTKGYWK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 380 RPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAF 459
Cdd:PRK06145 362 DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 503186189 460 VVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK-LKR 506
Cdd:PRK06145 442 VVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKvLKR 489
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
46-515 |
4.43e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 155.42 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 LDD-------------------TLPHGD---FAPGLAV----------VTEAALIAAIDSGPEGAFA--------DTAAD 165
Cdd:PRK08751 129 VIDnfgttvqqviadtpvkqviTTGLGDmlgFPKAALVnfvvkyvkklVPEYRINGAIRFREALALGrkhsmptlQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVInwtyamgTGLsdPL-------ANGATALLY 238
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVI-------TAL--PLyhifaltANGLVFMKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 239 TGERH----PSIWPGLIR---AFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYE 311
Cdd:PRK08751 280 GGCNHlisnPRDMPGFVKelkKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 312 GFGQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRG 390
Cdd:PRK08751 360 AYGLTETSPAACINPlTLKEYNGSIGLPIPSTDACIKDDAG--TVLAIGEIGELCI--KGPQVMKGYWKRPEETAKVMDA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 E-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREggADL 469
Cdd:PRK08751 436 DgWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD--PAL 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 503186189 470 SAE-LAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKIPQPP 515
Cdd:PRK08751 514 TAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
163-510 |
6.66e-41 |
|
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: 155.55 E-value: 6.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 163 AADDPAFLIYTSGTTANPKGVL-----HAHRSVWGRRPMYrgwyGITAADRLMHSGVINWTYAMGTGLSDPLANGATALL 237
Cdd:cd05967 228 AATDPLYILYTSGTTGKPKGVVrdnggHAVALNWSMRNIY----GIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 238 YTGE--RHP--SIWPGLIRAFDVTIFAGVPGLYHQIMRQ----ASGDRLDLARLRHGLTAGDTLpDALEAEWSER-TGTR 308
Cdd:cd05967 304 YEGKpvGTPdpGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgKYIKKYDLSSLRTLFLAGERL-DPPTLEWAENtLGVP 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 309 LYEGFGQTELSTYLSSAP----DFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVHRS-DPGLMLGYWQrpDE 383
Cdd:cd05967 383 VIDHWWQTETGWPITANPvglePLPIKAGSPGKPVPGYQVQVLDEDG--EPVGPNELGNIVIKLPlPPGCLLTLWK--ND 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 384 ER------EMFRGEWFTGgDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAIT 457
Cdd:cd05967 459 ERfkklylSKFPGYYDTG-DAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPL 537
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 458 AFVVAREGG----ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05967 538 GLVVLKEGVkitaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
21-509 |
6.66e-41 |
|
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: 152.86 E-value: 6.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 21 VLRAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:cd12115 5 VEAQAARTPDAIALVC-------GDESLTYAELNRRANRLAARLRA-AGVGPESRVGVCLERTPDLVVALLAVLKAGAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVlddtlphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANP 180
Cdd:cd12115 77 VPLDPAYPPERLRFILEDAQARLVL------------------------------------TDPDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 181 KGVLHAHRSVWGRRpmyrGWYGIT-AADRLmhSGVINWTyAMGTGLS-----DPLANGATALLYTGERHPsiwPGLIRAF 254
Cdd:cd12115 121 KGVAIEHRNAAAFL----QWAAAAfSAEEL--AGVLAST-SICFDLSvfelfGPLATGGKVVLADNVLAL---PDLPAAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 255 DVTIFAGVPGLYHQIMRQasgDRLDlARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTELSTYLSSAPDFPRKPG 333
Cdd:cd12115 191 EVTLINTVPSAAAELLRH---DALP-ASVRVVNLAGEPLPRDLVQRLYARlQVERVVNLYGPSEDTTYSTVAPVPPGASG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 334 TV--GRAQPGRCVAILpeDGGDTSLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGEWFTG-------GDLGCIDED 404
Cdd:cd12115 267 EVsiGRPLANTQAYVL--DRALQPVPLGVPGELYIG--GAGVARGYLGRPGLTAERFLPDPFGPgarlyrtGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 405 GAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAY 484
Cdd:cd12115 343 GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAY 422
|
490 500
....*....|....*....|....*
gi 503186189 485 KRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd12115 423 MVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
17-506 |
6.82e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 154.93 E-value: 6.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 17 MAKHVLRAGAAAGDKTALVVIHdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNR-----TAYALAFF 91
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRH-----QALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCaewllTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 92 GAIaggLVPIpaSPDLTARELGFLLDDSDAAAIVLDDTLPHGDF-------APGLAVVTEAALI---------------- 148
Cdd:PRK12583 94 GAI---LVNI--NPAYRASELEYALGQSGVRWVICADAFKTSDYhamlqelLPGLAEGQPGALAcerlpelrgvvslapa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 149 --------AAIDSGPEGA-----FADTAA---DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHS 212
Cdd:PRK12583 169 pppgflawHELQARGETVsrealAERQASldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 213 gvINWTYAMGTGLSD--PLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAG 290
Cdd:PRK12583 249 --VPLYHCFGMVLANlgCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 291 DTLPDALEAE-WSERTGTRLYEGFGQTELS--TYLSSAPD-FPRKPGTVGRAQPGRCVAILPEDGGdtSLPPGEAGMIAV 366
Cdd:PRK12583 327 APCPIEVMRRvMDEMHMAEVQIAYGMTETSpvSLQTTAADdLERRVETVGRTQPHLEVKVVDPDGA--TVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 367 HRSDpgLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVI 445
Cdd:PRK12583 405 RGYS--VMKGYWNNPEATAESIDEDgWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503186189 446 DVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-512 |
1.32e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 153.32 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 52 ALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTLP 131
Cdd:PRK12406 16 ELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 132 HG---DFAPGLAVV---TEAALIAAIDSGPEGAFADTAADD------------------PAFLIYTSGTTANPKGVLHA- 186
Cdd:PRK12406 95 HGlasALPAGVTVLsvpTPPEIAAAYRISPALLTPPAGAIDwegwlaqqepydgppvpqPQSMIYTSGTTGHPKGVRRAa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 187 ----HRSVWGRrpMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLytGERHPSIWPGLIRAFDVTIFAGV 262
Cdd:PRK12406 175 ptpeQAAAAEQ--MRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQ--PRFDPEELLQLIERHRITHMHMV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 263 PGLYHQIMR--QASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTY-LSSAPDFPRKPGTVGRAQ 339
Cdd:PRK12406 251 PTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVtFATSEDALSHPGTVGKAA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 340 PGRCVAILPEDGgdTSLPPGEAGMIAVhRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNA 419
Cdd:PRK12406 331 PGAELRFVDEDG--RPLPQGEIGEIYS-RIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 420 GGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKT 499
Cdd:PRK12406 408 GGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPRE 487
|
490
....*....|...
gi 503186189 500 PNGKLKRSDLKIP 512
Cdd:PRK12406 488 DSGKIFKRRLRDP 500
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-509 |
5.41e-40 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 151.63 E-value: 5.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTalVVIHDPAGREAETwTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:cd12119 4 HAARLHGDRE--IVSRTHEGEVHRY-TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIVLDDTL--------------------PHGDFAPGLAVVTEAALIAAIDSG-PEGAFAD 161
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFlplleaiaprlptvehvvvmTDDAAMPEPAGVGVLAYEELLAAEsPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 162 TAADDPAFLIYTSGTTANPKGVLHAHRSVWgrrpmyrgwygitaadrlMHSGVINWTYAMGTGLSD------PL--ANG- 232
Cdd:cd12119 160 FDENTAAAICYTSGTTGNPKGVVYSHRSLV------------------LHAMAALLTDGLGLSESDvvlpvvPMfhVNAw 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 233 ---------ATALLYTGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWS 302
Cdd:cd12119 222 glpyaaamvGAKLVLPGPYlDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 303 ERtGTRLYEGFGQTELSTYLSSA--PDFPRKPG---------TVGRAQPGRCVAILPEDGGdtSLP--PGEAGMIAVhRS 369
Cdd:cd12119 302 ER-GVRVIHAWGMTETSPLGTVArpPSEHSNLSedeqlalraKQGRPVPGVELRIVDDDGR--ELPwdGKAVGELQV-RG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 370 dPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQ 449
Cdd:cd12119 378 -PWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPH 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 450 PHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd12119 457 PKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-513 |
1.21e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 154.34 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 45 AETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAI 124
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 125 V----LDDTLPhgdFAPGLAVVTEAALIAAIDSGPEGAFADTA-ADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRG 199
Cdd:PRK12316 613 LsqshLGRKLP---LAAGVQVLDLDRPAAWLEGYSEENPGTELnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQ 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 200 WYGITAADRLMHSGVINWTYAMgTGLSDPLANGATALLYTGERH--PSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDr 277
Cdd:PRK12316 690 AYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHrdPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA- 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 278 lDLARLRHGLTAGDTLP-DALEAEWSERTGTRLYEGFGQTELS---TYLSSAPDFPRKPgTVGRAQPGRCVAILpeDGGD 353
Cdd:PRK12316 768 -SCTSLRRIVCSGEALPaDAQEQVFAKLPQAGLYNLYGPTEAAidvTHWTCVEEGGDSV-PIGRPIANLACYIL--DANL 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 354 TSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF------RGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSP 426
Cdd:PRK12316 844 EPVPVGVLGELYL--AGRGLARGYHGRPGLTAERFvpspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 427 VEVEAVLREHPLVAEAGVIDVpqphGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK12316 922 GEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
....*..
gi 503186189 507 SDLKIPQ 513
Cdd:PRK12316 998 KALPAPE 1004
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-512 |
1.32e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 154.16 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIA-IGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TL------PHGDFApglAVVTEAALIAAIDSGPEgafADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYG 202
Cdd:PRK12467 3201 HLleqlpaPAGDTA---LTLDRLDLNGYSENNPS---TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE 3274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 203 ITAADRLMHSGVINWTYAMGTGLSdPLANGATALLYTGE-RHPSIWPGLIRAFDVTIFAGVPGLYHQIMrqASGDRLDLA 281
Cdd:PRK12467 3275 LDANDRVLLFMSFSFDGAQERFLW-TLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFA--EDAGGADCA 3351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 282 RLRHGLTAGDTLPDALEAEWSERTGTR-LYEGFGQTE-------LSTYLSSAPDFPRKPgtVGRAQPGRCVAILpeDGGD 353
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEavvtvtlWKCGGDAVCEAPYAP--IGRPVAGRSIYVL--DGQL 3427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 354 TSLPPGEAGmiAVHRSDPGLMLGYWQRPDEEREMFRGEWFTG--------GDLGCIDEDGAIAHLGRASDLMNAGGYRVS 425
Cdd:PRK12467 3428 NPVPVGVAG--ELYIGGVGLARGYHQRPSLTAERFVADPFSGsggrlyrtGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 426 PVEVEAVLREHPLVAEAGVIDVPQpHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLK 505
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDG-AGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
|
....*..
gi 503186189 506 RSDLKIP 512
Cdd:PRK12467 3585 RKALPDP 3591
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
6-509 |
2.23e-39 |
|
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: 149.40 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 6 YRGELPPRNLNMAKHVLRAGAAAGDKTALVvihDPAGReaetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTA 85
Cdd:cd05920 6 YRAAGYWQDEPLGDLLARSAARHPDRIAVV---DGDRR----LTYRELDRRADRLAAGLRG-LGIRPGDRVVVQLPNVAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 86 YALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDTlpHGDFAPGLAVVTEAALIAaidsgpegafadtaad 165
Cdd:cd05920 78 FVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDR--HAGFDHRALARELAESIP---------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWgrrpmyrgwYGITAADRLMHSGViNWTY------AMGTGLSDP-----LANGAT 234
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYA---------YNVRASAEVCGLDQ-DTVYlavlpaAHNFPLACPgvlgtLLAGGR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 235 ALLYTGERHPSIWPgLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFG 314
Cdd:cd05920 210 VVLAPDPSPDAAFP-LIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 315 QTE-LSTYlsSAPDFP--RKPGTVGR-AQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRG 390
Cdd:cd05920 289 MAEgLLNY--TRLDDPdeVIIHTQGRpMSPDDEIRVVDEEGNP--VPPGEEGELLTR--GPYTIRGYYRAPEHNARAFTP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 E-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADL 469
Cdd:cd05920 363 DgFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSA 442
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 503186189 470 SAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd05920 443 AQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
23-511 |
3.22e-39 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 149.90 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVvihDPAGreaETWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:PRK06087 31 QTARAMPDKIAVV---DNHG---ASYTYSALDHAASRLANWL-LAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIV----------------LDDTLPHGD-------FAPGLAVVTEAALIAaiDSGPEGAF 159
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFaptlfkqtrpvdlilpLQNQLPQLQqivgvdkLAPATSSLSLSQIIA--DYEPLTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 160 ADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYT 239
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 GERhPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALeAEWSERTGTRLYEGFGQTELS 319
Cdd:PRK06087 262 IFT-PDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV-ARECQQRGIKLLSVYGSTESS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 320 TYLSSAPDFP--RKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAvhRSDPGLMLGYWQRPDEEREMFRGE-WFTGG 396
Cdd:PRK06087 340 PHAVVNLDDPlsRFMHTDGYAAAGVEIKVVDEARKT--LPPGCEGEEA--SRGPNVFMGYLDEPELTARALDEEgWYYSG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 397 DLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAE--LA 474
Cdd:PRK06087 416 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEevVA 495
|
490 500 510
....*....|....*....|....*....|....*..
gi 503186189 475 ARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKI 511
Cdd:PRK06087 496 FFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
30-510 |
3.62e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 148.77 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVvihdpagREAETWTYRALESAALRVAFELRSNRSLAprTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:PRK07638 16 NKIAIK-------ENDRVLTYKDWFESVCKVANWLNEKESKN--KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLDDTLPHGDFAPGLAVV--------TEAALiaaidsgPEGAFADTAADDPAFLIYTSGTTANPK 181
Cdd:PRK07638 87 DELKERLAISNADMIVTERYKLNDLPDEEGRVIeidewkrmIEKYL-------PTYAPIENVQNAPFYMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 182 GVLHAHRSvwgrrpmyrgW----------YGITAADRLMhsgvinwtyAMGTGLSDPLANGATALLYTG-----ERH--P 244
Cdd:PRK07638 160 AFLRAQQS----------WlhsfdcnvhdFHMKREDSVL---------IAGTLVHSLFLYGAISTLYVGqtvhlMRKfiP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 245 SIWPGLIRAFDVTIFAGVPglyhqIMRQAsgdrldLARLRHGLTAGDTLPDA---LEAEWSERTGT-----RLYEGFGQT 316
Cdd:PRK07638 221 NQVLDKLETENISVMYTVP-----TMLES------LYKENRVIENKMKIISSgakWEAEAKEKIKNifpyaKLYEFYGAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 317 ELS--TYLSSApDFPRKPGTVGRaqPGRCVAILPEDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFT 394
Cdd:PRK07638 290 ELSfvTALVDE-ESERRPNSVGR--PFHNVQVRICNEAGEEVQKGEIGTVYV--KSPQFFMGYIIGGVLARELNADGWMT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 395 GGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVvarEGGADlSAELA 474
Cdd:PRK07638 365 VRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSAT-KQQLK 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 503186189 475 ARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07638 441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-514 |
3.23e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 150.31 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 7 RGELPPRNL--NMAKHVLRAGAAAG-DKTALVVihdpagrEAETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNR 83
Cdd:PRK12467 501 RWNAPATEYapDCVHQLIEAQARQHpERPALVF-------GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERS 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 84 TAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD-DTLPHGDFAPGLAVVTEAALiAAIDSGPEGAFADT 162
Cdd:PRK12467 573 IEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQsHLLAQLPVPAGLRSLCLDEP-ADLLCGYSGHNPEV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 163 A--ADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAmGTGLSDPLANGATALLYTG 240
Cdd:PRK12467 652 AldPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 ERH--PSIWPGLIRAFDVTIFAGVPGLYHQIMrQASGDRLDLaRLRHGLTAGDTLPDALEAEWSE-RTGTRLYEGFGQTE 317
Cdd:PRK12467 731 DCArdAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPR-PQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTE 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 318 ----LSTYLSSAPDFPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGmiAVHRSDPGLMLGYWQRPDEEREMF----- 388
Cdd:PRK12467 809 ttvgVSTYELSDEERDFGNVPIGQPLANLGLYIL--DHYLNPVPVGVVG--ELYIGGAGLARGYHRRPALTAERFvpdpf 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 389 ---RGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHgGTAITAFVVAREG 465
Cdd:PRK12467 885 gadGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAV 963
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 503186189 466 -----GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLkiPQP 514
Cdd:PRK12467 964 adgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL--PKP 1015
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
30-506 |
3.72e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 146.37 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpaGREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTA 109
Cdd:PRK13391 12 DKPAVIM-----ASTGEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLddTLPHGDFAPGLA-----VVTEAALIAAIDSGPEGAFADTAADDPAF----------LIYTS 174
Cdd:PRK13391 86 AEAAYIVDDSGARALIT--SAAKLDVARALLkqcpgVRHRLVLDGDGELEGFVGYAEAVAGLPATpiadeslgtdMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 175 GTTANPKGVLHAHRSVWGRRP-----MYRGWYGITAADR------LMHSGVINWTyamGTGLSDplanGATALLYtgER- 242
Cdd:PRK13391 164 GTTGRPKGIKRPLPEQPPDTPlpltaFLQRLWGFRSDMVylspapLYHSAPQRAV---MLVIRL----GGTVIVM--EHf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 243 HPSIWPGLIRAFDVTIFAGVPGLYHQIMR--QASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTE-LS 319
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 320 TYLSSAPDFPRKPGTVGRAQPGRcVAILPEDGGDtsLPPGEAGMIAVHRsdpGLMLGYWQRPDEEREMF--RGEWFTGGD 397
Cdd:PRK13391 315 FTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAE--LPPGEPGTIWFEG---GRPFEYLNDPAKTAEARhpDGTWSTVGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 398 LGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG---GADLSAELA 474
Cdd:PRK13391 389 IGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGvdpGPALAAELI 468
|
490 500 510
....*....|....*....|....*....|...
gi 503186189 475 ARAEASLAAYKRPRHYVFVERLPKTPNGKL-KR 506
Cdd:PRK13391 469 AFCRQRLSRQKCPRSIDFEDELPRLPTGKLyKR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-513 |
3.75e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.11 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 lddTLPHGDFAPGLAVVTEAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITA 205
Cdd:PRK12316 3160 ---SQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV 3236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADRLMHSGVINWTyAMGTGLSDPLANGATALLYTGERH--PSIWPGLIRAFDVTIFAGVPGLYHqiMRQASGDRLDLARL 283
Cdd:PRK12316 3237 GDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAGPEDWrdPALLVELINSEGVDVLHAYPSMLQ--AFLEEEDAHRCTSL 3313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTLPDALEAEWSerTGTRLYEGFGQTEL---STYLSSAPDFPRKPgTVGRAQPGRCVAILpeDGGDTSLPPGE 360
Cdd:PRK12316 3314 KRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEAtitVTHWQCVEEGKDAV-PIGRPIANRACYIL--DGSLEPVPVGA 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTGG-------DLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVL 433
Cdd:PRK12316 3389 LGELYL--GGEGLARGYHNRPGLTAERFVPDPFVPGerlyrtgDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 434 REHPLVAEAGVIDVpqphGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKIPQ 513
Cdd:PRK12316 3467 LEHPWVREAVVLAV----DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPD 3542
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
21-510 |
4.28e-38 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 146.44 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 21 VLRAGAAA-GDKTALVvihDPAGReaetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLV 99
Cdd:COG1021 30 LLRRRAERhPDRIAVV---DGERR----LSYAELDRRADRLAAGLLA-LGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 100 PIPASPDLTARELGFLLDDSDAAAIVLDDTLP---HGDFA-------PGLAVV-------TEAALIAAIDSGPEGAFADT 162
Cdd:COG1021 102 PVFALPAHRRAEISHFAEQSEAVAYIIPDRHRgfdYRALArelqaevPSLRHVlvvgdagEFTSLDALLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 163 AADDPAFLIYTSGTTANPKGVLHAHR----SVwgrRPMYRGWyGITAADRLMHSGVINWTYAMgtglSDPlanGATALLY 238
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDdylySV---RASAEIC-GLDADTVYLAALPAAHNFPL----SSP---GVLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 239 TGER---HPSIWPG----LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYE 311
Cdd:COG1021 251 AGGTvvlAPDPSPDtafpLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 312 GFGQTE-LSTYlsSAPDFPRKP--GTVGRAQ-PGRCVAILPEDGGDtsLPPGEAGMIAVhRSdPGLMLGYWQRPDEEREM 387
Cdd:COG1021 331 VFGMAEgLVNY--TRLDDPEEVilTTQGRPIsPDDEVRIVDEDGNP--VPPGEVGELLT-RG-PYTIRGYYRAPEHNARA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 388 FRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGG 466
Cdd:COG1021 405 FTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 503186189 467 ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:COG1021 485 LTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
26-507 |
6.60e-38 |
|
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: 146.23 E-value: 6.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 26 AAAGDKTALVVIHDPAGREaETWTYRALESAALRVAFELRsnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASP 105
Cdd:cd05931 4 AARPDRPAYTFLDDEGGRE-ETLTYAELDRRARAIAARLQ--AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 106 D---LTARELGFLLDDSDAAAI---------VLDDTLPHGDFAPGLAVVTEAALIAAIDSGPEgafADTAADDPAFLIYT 173
Cdd:cd05931 81 PtpgRHAERLAAILADAGPRVVlttaaalaaVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP---PSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 174 SGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRlmhsgVINW--TYA-MG--TGLSDPLANGATALLYTGE---RHPS 245
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV-----VVSWlpLYHdMGliGGLLTPLYSGGPSVLMSPAaflRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 246 IWPGLIRAFDVTIfAGVP----GLYHQIMRQASGDRLDLARLRHGLTAGDTL-PDALE--AEWSERTGTR---LYEGFGQ 315
Cdd:cd05931 233 RWLRLISRYRATI-SAAPnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVrPATLRrfAEAFAPFGFRpeaFRPSYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 316 TELSTYLSSAPDF---------------------PRKPGTV-----GRAQPGRCVAILPEDGGdTSLPPGEAGMIAVHrs 369
Cdd:cd05931 312 AEATLFVSGGPPGtgpvvlrvdrdalagravavaADDPAARelvscGRPLPDQEVRIVDPETG-RELPDGEVGEIWVR-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 370 DPGLMLGYWQRPDEEREMFR-------GEWFTGGDLGCIDeDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEA 442
Cdd:cd05931 389 GPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRP 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503186189 443 G---VIDVPQPHGGT-AITAFVVAREGGADLSAELAARAEASLAAYK-RPRHYVFVER--LPKTPNGKLKRS 507
Cdd:cd05931 468 GcvaAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIRAAVAREHGvAPADVVLVRPgsIPRTSSGKIQRR 539
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
6-510 |
8.97e-38 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 145.51 E-value: 8.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 6 YRGELP----PRNLNMAKHVLRAGAAAGDKTALvvIHDPAGReaeTWTYRALESAALRVAFELRSnrsLAPRT--RVLIR 79
Cdd:PLN02246 10 FRSKLPdiyiPNHLPLHDYCFERLSEFSDRPCL--IDGATGR---VYTYADVELLSRRVAAGLHK---LGIRQgdVVMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 80 LRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD----DTLPHGDFAPGLAVVTeaaliaaIDSGP 155
Cdd:PLN02246 82 LPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQscyvDKLKGLAEDDGVTVVT-------IDDPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 156 EGAF---------------ADTAADDPAFLIYTSGTTANPKGVLHAHRS--------VWGRRP-MYrgwygITAADRLM- 210
Cdd:PLN02246 155 EGCLhfseltqadenelpeVEISPDDVVALPYSSGTTGLPKGVMLTHKGlvtsvaqqVDGENPnLY-----FHSDDVILc 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 211 -----HsgvinwTYAMGTGLSDPLANGATALlytgerhpsIWP--------GLIRAFDVTIFAGVPGLYHQIMRQASGDR 277
Cdd:PLN02246 230 vlpmfH------IYSLNSVLLCGLRVGAAIL---------IMPkfeigallELIQRHKVTIAPFVPPIVLAIAKSPVVEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 278 LDLARLRHGLTA----GDTLPDALEAEWSertGTRLYEGFGQTELSTYLSSAPDFPRKPGTVgraQPGRC--------VA 345
Cdd:PLN02246 295 YDLSSIRMVLSGaaplGKELEDAFRAKLP---NAVLGQGYGMTEAGPVLAMCLAFAKEPFPV---KSGSCgtvvrnaeLK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 346 ILPEDGGDtSLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRV 424
Cdd:PLN02246 369 IVDPETGA-SLPRNQPGEICIR--GPQIMKGYLNDPEATANTIDKDgWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 425 SPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVaREGGADLSA-ELAARAEASLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV-RSNGSEITEdEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGK 524
|
....*..
gi 503186189 504 LKRSDLK 510
Cdd:PLN02246 525 ILRKDLR 531
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
46-509 |
1.11e-37 |
|
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: 143.55 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:cd17652 11 ETLTYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 lddtlphgdfapglavvteaaliaaidsgpegafadTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITA 205
Cdd:cd17652 90 ------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADRLMHSGVIN-----WTYAMGtglsdpLANGATALLYTGERhpsIWPG-----LIRAFDVTIFAGVPGLYhqimrqASG 275
Cdd:cd17652 134 GSRVLQFASPSfdasvWELLMA------LLAGATLVLAPAEE---LLPGepladLLREHRITHVTLPPAAL------AAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 276 DRLDLARLRHGLTAGDTLPDALEAEWSerTGTRLYEGFGQTELSTYLS-SAPDFPRKPGTVGRAQPGRCVAILpeDGGDT 354
Cdd:cd17652 199 PPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTVCATmAGPLPGGGVPPIGRPVPGTRVYVL--DARLR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 355 SLPPGEAGmiAVHRSDPGLMLGYWQRPDEEREMFRGEWFTG--------GDLGCIDEDGAIAHLGRASDLMNAGGYRVSP 426
Cdd:cd17652 275 PVPPGVPG--ELYIAGAGLARGYLNRPGLTAERFVADPFGApgsrmyrtGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 427 VEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
...
gi 503186189 507 SDL 509
Cdd:cd17652 433 RAL 435
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-510 |
1.12e-37 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 145.21 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 29 GDKTALVViHDPAGrEAETWTYRALESAALRVAfELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLT 108
Cdd:PRK08008 21 GHKTALIF-ESSGG-VVRRYSYLELNEEINRTA-NLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 109 ARELGFLLDDSDAAAIVL--------------DDTLPHGDFapgLAVVTEAALIAAIDSGPEGAFADT--------AADD 166
Cdd:PRK08008 98 REESAWILQNSQASLLVTsaqfypmyrqiqqeDATPLRHIC---LTRVALPADDGVSSFTQLKAQQPAtlcyapplSTDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 167 PAFLIYTSGTTANPKGVLHAHRSVwgrrpMYRGWYG-----ITAADRL---MHSGVINW--TYAMGTglsdpLANGATAL 236
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVVITHYNL-----RFAGYYSawqcaLRDDDVYltvMPAFHIDCqcTAAMAA-----FSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 237 L---YTGERhpsIWpGLIRAFDVTIFAGVPGLYHQIMRQ--ASGDRLDLAR-LRHGLTAGDTLPDALEaewsERTGTRLY 310
Cdd:PRK08008 245 LlekYSARA---FW-GQVCKYRATITECIPMMIRTLMVQppSANDRQHCLReVMFYLNLSDQEKDAFE----ERFGVRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTE-LSTYLSSAPDFPRKPGTVGRaqPGRC--VAILPEDGgdTSLPPGEAGMIAVhRSDPG--LMLGYWQRPDEER 385
Cdd:PRK08008 317 TSYGMTEtIVGIIGDRPGDKRRWPSIGR--PGFCyeAEIRDDHN--RPLPAGEIGEICI-KGVPGktIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 386 EMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVARE 464
Cdd:PRK08008 392 KVLEADgWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 503186189 465 gGADLS-AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK08008 472 -GETLSeEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
166-502 |
1.73e-37 |
|
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: 140.51 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVwgrrpMYRGW-----------YGITAADRLMHSGVINWTYAM----GTGLSDPLA 230
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQAL-----LAQALvlavlqaidegTVFLNSGPLFHIGTLMFTLATfhagGTNVFVRRV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 231 NGATALlytgerhpsiwpGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDAleAEWSERTGTRLY 310
Cdd:cd17636 76 DAEEVL------------ELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMA--TVDTSPWGRKPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 eGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRG 390
Cdd:cd17636 142 -GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGRE--VPDGEVGEIVAR--GPTVMAGYWNRPEVNARRTRG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLS 470
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
330 340 350
....*....|....*....|....*....|..
gi 503186189 471 AELAARAEASLAAYKRPRHYVFVERLPKTPNG 502
Cdd:cd17636 297 AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
32-506 |
3.29e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 144.05 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 32 TALVVIHDPAGR-EAETWTYRALESAALRVAFELRSnrsLAPRTR---VLIRLRNRTAYALAFFGAIAGGLVPIPASPDL 107
Cdd:PRK07867 12 LPLAEDDDRGLYfEDSFTSWREHIRGSAARAAALRA---RLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 108 TARELGFLLDDSDAAAIVLDDTLPH--GDFAPGLAVV-TEAALIAAIDSGPEGA---FADTAADDPAFLIYTSGTTANPK 181
Cdd:PRK07867 89 RGAALARDIAHADCQLVLTESAHAEllDGLDPGVRVInVDSPAWADELAAHRDAeppFRVADPDDLFMLIFTSGTSGDPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 182 GVLHAHRSVWGRRPMYRGWYGITAAD------RLMHSGvinwtyAMGTGLSDPLANGATALLytgERHPSIWPGL--IRA 253
Cdd:PRK07867 169 AVRCTHRKVASAGVMLAQRFGLGPDDvcyvsmPLFHSN------AVMAGWAVALAAGASIAL---RRKFSASGFLpdVRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 254 FDVTIF--AGVPGLYHQIMRQASGDRLDLARLRHGLTAGDtlPDAleAEWSERTGTRLYEGFGQTELSTYLSSAPDFPrk 331
Cdd:PRK07867 240 YGATYAnyVGKPLSYVLATPERPDDADNPLRIVYGNEGAP--GDI--ARFARRFGCVVVDGFGSTEGGVAITRTPDTP-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 332 PGTVGRAQPGrcVAILPEDGGdTSLPPGEAGMIAVHRSD-----------PGLMLGYWQRPDEEREMFRGEWFTGGDLGC 400
Cdd:PRK07867 314 PGALGPLPPG--VAIVDPDTG-TECPPAEDADGRLLNADeaigelvntagPGGFEGYYNDPEADAERMRGGVYWSGDLAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 401 IDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSAELAARAEAS 480
Cdd:PRK07867 391 RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAP-GAKFDPDAFAEFLAA 469
|
490 500 510
....*....|....*....|....*....|
gi 503186189 481 LAAY---KRPRHYVFVERLPKTPNGK-LKR 506
Cdd:PRK07867 470 QPDLgpkQWPSYVRVCAELPRTATFKvLKR 499
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
166-506 |
1.16e-36 |
|
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: 138.40 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGrrpMYRGW---YGITAADRLMhsgVIN---WTYAMGTGLSDPLANGAT----- 234
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR---AAAAWadcADLTEDDRYL---IINpffHTFGYKAGIVACLLTGATvvpva 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 235 -----ALLYTGERHpsiwpglirafDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDAL-EAEWSERTGTR 308
Cdd:cd17638 75 vfdvdAILEAIERE-----------RITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELvRRMRSELGFET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 309 LYEGFGQTELSTYLSSAP--DFPRKPGTVGRAQPGRCVAIlpedggdtslppGEAGMIAVHrsDPGLMLGYWQRPDEERE 386
Cdd:cd17638 144 VLTAYGLTEAGVATMCRPgdDAETVATTCGRACPGFEVRI------------ADDGEVLVR--GYNVMQGYLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 387 MFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG 465
Cdd:cd17638 210 AIDADgWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 503186189 466 GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd17638 290 VTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
44-509 |
1.60e-36 |
|
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: 140.38 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 44 EAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAA 123
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 124 IVLDdtlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGI 203
Cdd:cd17645 99 LLTN------------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTyAMGTGLSDPLANGATALLYTGERHPSIwPGLIRAFD---VTIFAGVPGLYHQIMRqasgdrLDL 280
Cdd:cd17645 143 TPADKSLVYASFSFD-ASAWEIFPHLTAGAALHVVPSERRLDL-DALNDYFNqegITISFLPTGAAEQFMQ------LDN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 281 ARLRHGLTAGDTLPDAleaewsERTGTRLYEGFGQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDggDTSLPPG 359
Cdd:cd17645 215 QSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTVVATSFEiDKPYANIPIGKPIDNTRVYILDEA--LQLQPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 360 EAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWF-TG------GDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAV 432
Cdd:cd17645 287 VAGELCI--AGEGLARGYLNRPELTAEKFIVHPFvPGermyrtGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPF 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 433 LREHPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSaELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd17645 365 LMNHPLIELAAVLAKEDADGRKYLVAYVTAPE-EIPHE-ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-514 |
2.05e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 144.92 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV--- 125
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIA-LGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLtqs 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 -LDDTLPHGDFAPGLAVVTEAALIAAI-DSGPEGAFADtaaDDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGI 203
Cdd:PRK12467 1680 hLQARLPLPDGLRSLVLDQEDDWLEGYsDSNPAVNLAP---QNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQL 1756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTYAMgTGLSDPLANGATALL--YTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLA 281
Cdd:PRK12467 1757 SAADVVLQFTSFAFDVSV-WELFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS 1835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 282 rLRHGLTAGDTLPDALEAEWSERTG-TRLYEGFGQTELS---TY--LSSAPDFPRKPGTVGRAQPGRCVAILpeDGGDTS 355
Cdd:PRK12467 1836 -LRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAvdvTHwtCRRKDLEGRDSVPIGQPIANLSTYIL--DASLNP 1912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 356 LPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF--------RGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPV 427
Cdd:PRK12467 1913 VPIGVAGELYL--GGVGLARGYLNRPALTAERFvadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 1990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 428 EVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVV--------AREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKT 499
Cdd:PRK12467 1991 EIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpglvdDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLT 2069
|
490
....*....|....*
gi 503186189 500 PNGKLKRSDLKIPQP 514
Cdd:PRK12467 2070 PNGKLDRKALPAPDA 2084
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
164-506 |
2.31e-36 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 142.59 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAFLIYTSGTTANPKGVLHA-----------HRSVWGRRP--MYR-----GWygITAadrlmHSGVinwTYAmgtgl 225
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLHTtggylvyaamtMKYVFDYKDgdVYWctadvGW--VTG-----HSYI---VYG----- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 226 sdPLANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARLRHGLTAGDtlPDALEA- 299
Cdd:PRK00174 309 --PLANGATTLMFEGVpnyPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpKKYDLSSLRLLGSVGE--PINPEAw 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 300 EWsertgtrLYEGFG-----------QTE----LSTYLSSApdFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMI 364
Cdd:PRK00174 385 EW-------YYKVVGgercpivdtwwQTEtggiMITPLPGA--TPLKPGSATRPLPGIQPAVVDEEG--NPLEGGEGGNL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 365 AVHRSDPGLMLGYWQrpDEER------EMFRGEWFTGgDlGCI-DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHP 437
Cdd:PRK00174 454 VIKDPWPGMMRTIYG--DHERfvktyfSTFKGMYFTG-D-GARrDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 529
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503186189 438 LVAEAGVIDVPQPHGGTAITAFVV---AREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK00174 530 KVAEAAVVGRPDDIKGQGIYAFVTlkgGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
30-514 |
2.43e-36 |
|
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: 140.93 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAI-AGG-LVPIpaSPDL 107
Cdd:cd17655 12 DHTAVVF-------EDQTLTYRELNERANQLARTLRE-KGVGPDTIVGIMAERSLEMIVGILGILkAGGaYLPI--DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 108 TARELGFLLDDSDAAAIvlddtLPHGDFAPGLAVVTEAALIA--AIDSGPEGAFA-DTAADDPAFLIYTSGTTANPKGVL 184
Cdd:cd17655 82 PEERIQYILEDSGADIL-----LTQSHLQPPIAFIGLIDLLDedTIYHEESENLEpVSKSDDLAYVIYTSGSTGKPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 185 HAHRSV-----WGRRPMYRGwygitAADRLMHSGVINWTyAMGTGLSDPLANGATALLYtgeRHPSIWPG-----LIRAF 254
Cdd:cd17655 157 IEHRGVvnlveWANKVIYQG-----EHLRVALFASISFD-ASVTEIFASLLSGNTLYIV---RKETVLDGqaltqYIRQN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 255 DVTIFAGVPGlyHQIMRQASGDRLDLaRLRHGLTAGDTLPDALEAEWSERTGT--RLYEGFGQTEL----STYLSSAPDF 328
Cdd:cd17655 228 RITIIDLTPA--HLKLLDAADDSEGL-SLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETtvdaSIYQYEPETD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 329 PRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF-------RGEWFTGGDLGCI 401
Cdd:cd17655 305 QQVSVPIGKPLGNTRIYIL--DQYGRPQPVGVAGELYI--GGEGVARGYLNRPELTAEKFvddpfvpGERMYRTGDLARW 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 402 DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREggaDL-SAELAARAEAS 480
Cdd:cd17655 381 LPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK---ELpVAQLREFLARE 457
|
490 500 510
....*....|....*....|....*....|....
gi 503186189 481 LAAYKRPRHYVFVERLPKTPNGKLKRSdlKIPQP 514
Cdd:cd17655 458 LPDYMIPSYFIKLDEIPLTPNGKVDRK--ALPEP 489
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
15-506 |
4.20e-36 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 141.86 E-value: 4.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 15 LNMAKHVLRAgAAAGDKTALVVIHDPAGREAETWTYRALESAALRVAFELRSNRsLAPRTRVLIRLRNRTAYALAFFGAI 94
Cdd:cd05968 60 MNIVEQLLDK-WLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALG-VGKGDRVGIYLPMIPEIVPAFLAVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 95 AGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD----------TLPHGDFAPGLAVVTEAALI---------------- 148
Cdd:cd05968 138 RIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevnLKEEADKACAQCPTVEKVVVvrhlgndftpakgrdl 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 149 --AAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRS--VWGRRPMYRGwYGITAADRLMHSGVINWTyaMGTG 224
Cdd:cd05968 218 syDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGfpLKAAQDMYFQ-FDLKPGDLLTWFTDLGWM--MGPW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 225 LS-DPLANGATALLYTG-ERHPS---IWPgLIRAFDVTIFAGVPGLYHQIM--RQASGDRLDLARLRhgLTAGDTLPDAL 297
Cdd:cd05968 295 LIfGGLILGATMVLYDGaPDHPKadrLWR-MVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLR--VLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 298 EAeWSERTGTRLYEGF------GQTELST-YLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDTslpPGEAGMIAVHRSD 370
Cdd:cd05968 372 EP-WNWLFETVGKGRNpiinysGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPA---RPEVGELVLLAPW 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 371 PGLMLGYWQrpDEER------EMFRGEWfTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGV 444
Cdd:cd05968 448 PGMTRGFWR--DEDRyletywSRFDNVW-VHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAA 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 445 IDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd05968 525 IGVPHPVKGEAIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-510 |
8.23e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 136.84 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVwgrrpMYRGWYG-----ITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYT 239
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNE-----VYNAWMLalnslFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 --GERHPS----IWpGLIRAFDVTIFAGVPGLYHQIMrQASGDRlDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGF 313
Cdd:cd05944 77 paGYRNPGlfdnFW-KLVERYRITSLSTVPTVYAALL-QVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTELSTYLS-SAPDFPRKPGTVGRAQPGRCVAILPEDG-GDTSLP--PGEAGMIAVhrSDPGLMLGYWQRPDEEREMFR 389
Cdd:cd05944 154 GLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGvGRLLRDcaPDEVGEICV--AGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 390 GEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADL 469
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 503186189 470 SAELAARAEASLAAYKR-PRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05944 312 EEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-510 |
8.45e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 139.76 E-value: 8.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 28 AGDKTALVVihdpaGREAETWTYRAL--ESAAL-RVAFElrsnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPAS 104
Cdd:PRK13390 10 APDRPAVIV-----AETGEQVSYRQLddDSAALaRVLYD----AGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 105 PDLTARELGFLLDDSDAAAIVLDDTLPhgdfapGLAVVTEAALIAAIDSGPE-GAFAD----TAADDP--------AFLI 171
Cdd:PRK13390 81 HHLTAPEADYIVGDSGARVLVASAALD------GLAAKVGADLPLRLSFGGEiDGFGSfeaaLAGAGPrlteqpcgAVML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 172 YTSGTTANPKGVLH--AHRSVwgRRP------MYRGWYGITAAD------RLMHSGVINW---TYAMGtglsdplanGAT 234
Cdd:PRK13390 155 YSSGTTGFPKGIQPdlPGRDV--DAPgdpivaIARAFYDISESDiyyssaPIYHAAPLRWcsmVHALG---------GTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 235 ALLYTGERHPSIwpGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEG 312
Cdd:PRK13390 224 VLAKRFDAQATL--GHVERYRITVTQMVPTMFVRLLKLDADvrTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 313 FGQTELS--TYLSSaPDFPRKPGTVGRAQPGRcVAILPEDGGDtsLPPGEAGMIAVHRSdpGLMLGYWQRPDEEREMFRG 390
Cdd:PRK13390 302 YSSTEAHgmTFIDS-PDWLAHPGSVGRSVLGD-LHICDDDGNE--LPAGRIGTVYFERD--RLPFRYLNDPEKTAAAQHP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 391 E---WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG-- 465
Cdd:PRK13390 376 AhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGir 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 503186189 466 -GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK13390 456 gSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
166-510 |
2.69e-34 |
|
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: 131.68 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR------LMHSG----VINWTYAMG-TGLSDPLANGAT 234
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSwllslpLYHVGglaiLVRSLLAGAeLVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 235 ALLYTGERHPSIWPG-LIRAFDvtifagvpglyhqimrqASGDRLDLARLRHGLTAGDTLPDALEAEWSERtGTRLYEGF 313
Cdd:cd17630 81 DLAPPGVTHVSLVPTqLQRLLD-----------------SGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTELST--YLSSAPDFPRkpGTVGRAQPGRCVAILpedggdtslppgEAGMIAVhrSDPGLMLGYWqRPDEEREMFRGE 391
Cdd:cd17630 143 GMTETASqvATKRPDGFGR--GGVGVLLPGRELRIV------------EDGEIWV--GGASLAMGYL-RGQLVPEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADlsA 471
Cdd:cd17630 206 WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--A 283
|
330 340 350
....*....|....*....|....*....|....*....
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
168-509 |
1.19e-33 |
|
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: 132.94 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 168 AFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTgLSDPLANGATALLYTGERHPSI- 246
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEE-IYVTLLSGATLVLRPEEMRSSLe 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 247 -WPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDL-ARLRHGLTAGDTLPDALEAEWSERTGT--RLYEGFGQTELST-- 320
Cdd:cd17644 188 dFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIaa 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 321 ---YLSSAPDFPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGMIavHRSDPGLMLGYWQRPDEEREMFRGEWFTG-- 395
Cdd:cd17644 268 tvcRLTQLTERNITSVPIGRPIANTQVYIL--DENLQPVPVGVPGEL--HIGGVGLARGYLNRPELTAEKFISHPFNSse 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 396 -------GDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGAD 468
Cdd:cd17644 344 serlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESP 423
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 503186189 469 LSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd17644 424 STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-503 |
1.40e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 133.78 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVVIHdpAGREaetWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNR-----TAYALAFFGAIagg 97
Cdd:PRK08315 24 RTAARYPDREALVYRD--QGLR---WTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNVpewvlTQFATAKIGAI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 98 LVPIpaSPDLTARELGFLLDDSDAAAIVLDDTLPHGDF-------APGLAVVTEAALIAA----------IDSGPEG--- 157
Cdd:PRK08315 95 LVTI--NPAYRLSELEYALNQSGCKALIAADGFKDSDYvamlyelAPELATCEPGQLQSArlpelrrvifLGDEKHPgml 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 158 AFADTAA-------------------DDPAFLIYTSGTTANPKGVLHAHRSV-----WGRRPMyrgwyGITAADR----- 208
Cdd:PRK08315 173 NFDELLAlgravddaelaarqatldpDDPINIQYTSGTTGFPKGATLTHRNIlnngyFIGEAM-----KLTEEDRlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 209 -LMHS-GVInwtyaMGTglsdpLA---NGATaLLYTGErhpsiwpglirAFD------------VTIFAGVPGLYHQIMR 271
Cdd:PRK08315 248 pLYHCfGMV-----LGN-----LAcvtHGAT-MVYPGE-----------GFDplatlaaveeerCTALYGVPTMFIAELD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 272 QASGDRLDLARLRHGLTAGDTLPdaleAEWSERTGTRLY--E---GFGQTE---LSTYLSSAPDFPRKPGTVGRAQPGRC 343
Cdd:PRK08315 306 HPDFARFDLSSLRTGIMAGSPCP----IEVMKRVIDKMHmsEvtiAYGMTEtspVSTQTRTDDPLEKRVTTVGRALPHLE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 344 VAILPEDGGDTsLPPGEAGMI-----AVhrsdpglMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLM 417
Cdd:PRK08315 382 VKIVDPETGET-VPRGEQGELctrgySV-------MKGYWNDPEKTAEAIDADgWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 418 NAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSAE-LAARAEASLAAYKRPRHYVFVERL 496
Cdd:PRK08315 454 IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP-GATLTEEdVRDFCRGKIAHYKIPRYIRFVDEF 532
|
....*..
gi 503186189 497 PKTPNGK 503
Cdd:PRK08315 533 PMTVTGK 539
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
49-509 |
1.69e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 129.12 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRsNRSLAPRTRVLIrLRNRTAYAL-AFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:cd17650 14 TYRELNERANQLARTLR-GLGVAPGSVVGV-CADRSLDAIvGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 dtlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRSVwgrRPMYRGWYGITAAD 207
Cdd:cd17650 92 ------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNV---AHAAHAWRREYELD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 208 RLMHSGVINWTYAMGTGLSD---PLANGATALLYTGER--HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLAR 282
Cdd:cd17650 133 SFPVRLLQMASFSFDVFAGDfarSLLNGGTLVICPDEVklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 283 LRHGLTAGDTLPDALEAEWSERTG--TRLYEGFGQTEL---STYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDTSLP 357
Cdd:cd17650 213 MRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEAtidSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 358 PGEAGMIAVhrSDPGLMLGYWQRPDEEREMFR-------GEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVE 430
Cdd:cd17650 293 VGVAGELYI--GGAGVARGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIE 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 431 AVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLsAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:cd17650 371 SQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA-TLNT-AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
6-510 |
3.74e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 129.71 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 6 YRGELP----PRNLNMAKHVLRAGAAAGDKTALVvihdpAGREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLR 81
Cdd:PLN02330 15 FRSRYPsvpvPDKLTLPDFVLQDAELYADKVAFV-----EAVTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 82 NRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDDT---------LP---HGDFAPGLAVVTEAALIA 149
Cdd:PLN02330 89 NVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTnygkvkglgLPvivLGEEKIEGAVNWKELLEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 150 AIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHR--------SVWGRRPMYRGwygitaadRLMHSGVINWTYAM 221
Cdd:PLN02330 169 ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRnlvanlcsSLFSVGPEMIG--------QVVTLGLIPFFHIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 222 G-TGLSDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARL--RHGLTAGDTL-PDAL 297
Cdd:PLN02330 241 GiTGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLaPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 298 EAEWSERTGTRLYEGFGQTELS--TYLSSAPDFPR---KPGTVGRAQPGRCVAILPEDGGdTSLPPGEAGMIAVhRSDpG 372
Cdd:PLN02330 321 TAFEAKFPGVQVQEAYGLTEHSciTLTHGDPEKGHgiaKKNSVGFILPNLEVKFIDPDTG-RSLPKNTPGELCV-RSQ-C 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 373 LMLGYWQRPDE-EREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPH 451
Cdd:PLN02330 398 VMQGYYNNKEEtDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 452 GGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PLN02330 478 AGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
166-506 |
6.66e-32 |
|
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: 124.83 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSdPLANGATALLYTGeRHPS 245
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRK-FNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 246 IWPGLIRAFDVTIFAGVPGLYHQIMRQasgDRLDLArLRHGLTAGDTLPDALEAEWSERT-GTRLYEGFGQTELSTYLSS 324
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALART---LEPESK-IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 325 APDFPRKPGTVGRAQPGRCVAILPEDGGdtslppgEAGMIAVhRSDPGLMlGYWqrpdEEREMFRGEWFTGGDLGCIDED 404
Cdd:cd17633 155 FNQESRPPNSVGRPFPNVEIEIRNADGG-------EIGKIFV-KSEMVFS-GYV----RGGFSNPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 405 GAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGtAITAFVVarEGGADLSAELAARAEASLAAY 484
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG-EIAVALY--SGDKLTYKQLKRFLKQKLSRY 298
|
330 340
....*....|....*....|..
gi 503186189 485 KRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd17633 299 EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
23-510 |
1.62e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 128.04 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTAlvVIHdpaGREAETW--TYRALEsaalRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:PLN02479 28 RAAVVHPTRKS--VVH---GSVRYTWaqTYQRCR----RLASAL-AKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVLDDTLPH--------------GDFAPGLAVVTE------AALIAAIDSGPEGAFA 160
Cdd:PLN02479 98 NCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTlaeealkilaekkkSSFKPPLLIVIGdptcdpKSLQYALGKGAIEYEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 161 DTAADDPAF-------------LIYTSGTTANPKGVLHAHRS----------VWGRR---------PMYR--GWygitaa 206
Cdd:PLN02479 178 FLETGDPEFawkppadewqsiaLGYTSGTTASPKGVVLHHRGaylmalsnalIWGMNegavylwtlPMFHcnGW------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 drlmhsgVINWTYAMGTGLSDPLANGATALLYTGerhpsiwpglIRAFDVTIFAGVPGLYHQIMRQASGDR-LDLARLRH 285
Cdd:PLN02479 252 -------CFTWTLAALCGTNICLRQVTAKAIYSA----------IANYGVTHFCAAPVVLNTIVNAPKSETiLPLPRVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 286 GLTAGDTLPDALEAEWSERtGTRLYEGFGQTEL---STYLSSAPDFPRKPGTVgRA-----QPGRCVAILPEDGGDT-SL 356
Cdd:PLN02479 315 VMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETygpSTVCAWKPEWDSLPPEE-QArlnarQGVRYIGLEGLDVVDTkTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 357 PPGEA-----GMIaVHRSDpGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEA 431
Cdd:PLN02479 393 KPVPAdgktmGEI-VMRGN-MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 432 VLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGG-----ADLSAELAARAEASLAAYKRPRHYVFvERLPKTPNGKLKR 506
Cdd:PLN02479 471 VVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVdksdeAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQK 549
|
....
gi 503186189 507 SDLK 510
Cdd:PLN02479 550 HVLR 553
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
13-512 |
1.79e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 127.57 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 13 RNLNMAKHVLRAGAAA--GDKTALVvihDPAGreaeTWTYRALESAALRVAFELRSNRSLAPRtRVLIRLRNRTAYALAF 90
Cdd:PRK13382 39 RREGMGPTSGFAIAAQrcPDRPGLI---DELG----TLTWRELDERSDALAAALQALPIGEPR-VVGIMCRNHRGFVEAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 91 FGA--IAGGLVPI------PASPDLTARE-LGFLLDDSDAAAIV---LDDTlPHG----DFAPGLAVVTEAALIAAidsg 154
Cdd:PRK13382 111 LAAnrIGADILLLntsfagPALAEVVTREgVDTVIYDEEFSATVdraLADC-PQAtrivAWTDEDHDLTVEVLIAA---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 155 PEGAFADTAADDPAFLIYTSGTTANPKGVLHAH-------RSVWGRRPMyRGWYGITAADRLMHSgvinWtyamgtGLSD 227
Cdd:PRK13382 186 HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGpggigtlKAILDRTPW-RAEEPTVIVAPMFHA----W------GFSQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 228 PLANGATALLYTGERH--PSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG--DRLDLARLRHGLTAGDTLPDALEAEWSE 303
Cdd:PRK13382 255 LVLAASLACTIVTRRRfdPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEvrNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 304 RTGTRLYEGFGQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVhRSDPgLMLGYWQRPD 382
Cdd:PRK13382 335 QFGDVIYNNYNATEAGMIATATPaDLRAAPDTAGRPAEGTEIRILDQDFRE--VPTGEVGTIFV-RNDT-QFDGYTSGST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 383 EEremFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVA 462
Cdd:PRK13382 411 KD---FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503186189 463 REGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLKIP 512
Cdd:PRK13382 488 KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
166-506 |
1.82e-31 |
|
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: 124.30 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVwgrrpmyrgwygITAADRLMhSGVINWTYAMGTGLSDPLANG------ATALLYT 239
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTF------------FAVPDILQ-KEGLNWVVGDVTYLPLPATHIgglwwiLTCLIHG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 GER--------HPSIWPgLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHgLTAGDTLP---DALEAEWSERTGTR 308
Cdd:cd17635 69 GLCvtggenttYKSLFK-ILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRL-IGYGGSRAiaaDVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 309 LYEGFGQTELSTYLSSAPDFpRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF 388
Cdd:cd17635 147 QVYGLSETGTALCLPTDDDS-IEINAVGRPYPGVDVYLAATDG--IAGPSASFGTIWI--KSPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 389 RGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVARE-GGA 467
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeLDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 503186189 468 DLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd17635 302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
49-510 |
1.96e-31 |
|
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: 125.88 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSNRsLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:cd17653 24 TYGELDAASNALANRLLQLG-VVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 tlphgdfapglavvteaaliaaidsgpegafadtAADDPAFLIYTSGTTANPKGVLHAHRSV-----WGRRPMYrgwygI 203
Cdd:cd17653 103 ----------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVlnyvsQPPARLD-----V 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTYAMGTGLSdPLANGATALLYTgerHPSIWPGLIRAfdVTIFAGVPGLYHQIMRQasgdrlDLARL 283
Cdd:cd17653 144 GPGSRVAQVLSIAFDACIGEIFS-TLCNGGTLVLAD---PSDPFAHVART--VDALMSTPSILSTLSPQ------DFPNL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTLPDALEAEWSErtGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGEAGM 363
Cdd:cd17653 212 KTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYIL--DADLQPVPEGVVGE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 364 IAVhrSDPGLMLGYWQRPDEEREMFR-GEWFTG------GDLGCIDEDGAIAHLGRASDLMNAGGYRVS-PVEVEAVLRE 435
Cdd:cd17653 288 ICI--SGVQVARGYLGNPALTASKFVpDPFWPGsrmyrtGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQS 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 436 HPLVAEAGVIdvpqPHGGTAItAFVVARegGADLSAeLAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd17653 366 QPEVTQAAAI----VVNGRLV-AFVTPE--TVDVDG-LRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
38-516 |
3.62e-31 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 128.62 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 38 HDPAGREAE-TWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLL 116
Cdd:PRK10252 473 DAPALADARyQFSYREMREQVVALANLLRE-RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 117 DDSDAAAIV----LDDTLPHGdfaPGLAVVTEAALIAAIDSGPEGAfadTAADDPAFLIYTSGTTANPKGVLHAHRSVWG 192
Cdd:PRK10252 552 EDARPSLLIttadQLPRFADV---PDLTSLCYNAPLAPQGAAPLQL---SQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 193 RRPMYRGWYGITAADRLMHS-----GVINWTYAMgtglsdPLANGATALLYTGERH--PSIWPGLIRAFDVTIFAGVPGL 265
Cdd:PRK10252 626 RLLWMQNHYPLTADDVVLQKtpcsfDVSVWEFFW------PFIAGAKLVMAEPEAHrdPLAMQQFFAEYGVTTTHFVPSM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 266 YHQIMRQASGDRLD--LARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTV-GRAQP-G 341
Cdd:PRK10252 700 LAAFVASLTPEGARqsCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVrGSSVPiG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 RCV---AILPEDGGDTSLPPGEAGmiavHRSDPGLML--GYWQRPDEEREMF------RGE-WFTGGDLGCIDEDGAIAH 409
Cdd:PRK10252 780 YPVwntGLRILDARMRPVPPGVAG----DLYLTGIQLaqGYLGRPDLTASRFiadpfaPGErMYRTGDVARWLDDGAVEY 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 410 LGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAG----VIDVPQPHGGTA--ITAFVVAREGGADLSAELAARAEASLAA 483
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRERLPP 935
|
490 500 510
....*....|....*....|....*....|...
gi 503186189 484 YKRPRHYVFVERLPKTPNGKLKRSDLkiPQPPL 516
Cdd:PRK10252 936 HMVPVVLLQLDQLPLSANGKLDRKAL--PLPEL 966
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
44-506 |
3.64e-31 |
|
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: 125.63 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 44 EAETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAA 123
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 124 IVLDDTlphgdfapglavvteaaliaaidsgpegafadtaaDDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGI 203
Cdd:cd05914 83 IFVSDE-----------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTgeRHPSIWPGLIRAFDVTIFAGVPGLYhQIMRQASGD---RLDL 280
Cdd:cd05914 128 GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD--KIPSAKIIALAFAQVTPTLGVPVPL-VIEKIFKMDiipKLTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 281 ARLRHGL-----------TAGDTLPDAL----------------EAEWSERT-GTRLYEGFGQTELSTYLSSAPDFPRKP 332
Cdd:cd05914 205 KKFKFKLakkinnrkirkLAFKKVHEAFggnikefviggakinpDVEEFLRTiGFPYTIGYGMTETAPIISYSPPNRIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 333 GTVGRAQPGRCVAILPEDggdtslPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLG 411
Cdd:cd05914 285 GSAGKVIDGVEVRIDSPD------PATGEGEIIVR--GPNVMKGYYKNPEATAEAFDKDgWFHTGDLGKIDAEGYLYIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 412 RASDLMNAG-GYRVSPVEVEAVLREHPLVAEAGVIdvpQPHGGTAITA-----FVVAREGGAD-----LSAELAARAEAS 480
Cdd:cd05914 357 RKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVV---VQEKKLVALAyidpdFLDVKALKQRniidaIKWEVRDKVNQK 433
|
490 500
....*....|....*....|....*..
gi 503186189 481 LAAYKRPRHYVFV-ERLPKTPNGKLKR 506
Cdd:cd05914 434 VPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
44-509 |
5.63e-31 |
|
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: 125.28 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 44 EAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAA 123
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLR-EKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 124 IVLDDTLPHGDFAPGLAVVTEAALIAAIDSgpEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGI 203
Cdd:cd17656 89 VLTQRHLKSKLSFNKSTILLEDPSISQEDT--SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTYAMGTGLSdPLANGATALLYTGE-------------RHPSIWPGLIRAFDVTIFAgvpgLYHQIM 270
Cdd:cd17656 167 NFSDKVLQFATCSFDVCYQEIFS-TLLSGGTLYIIREEtkrdveqlfdlvkRHNIEVVFLPVAFLKFIFS----EREFIN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 271 RQASGdrldlarLRHGLTAGDTLP-DALEAEWSERTGTRLYEGFGQTE---LSTY-LSSAPDFPRKPgTVGRaqPGRCVA 345
Cdd:cd17656 242 RFPTC-------VKHIITAGEQLViTNEFKEMLHEHNVHLHNHYGPSEthvVTTYtINPEAEIPELP-PIGK--PISNTW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 346 ILPEDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG-------GDLGCIDEDGAIAHLGRASDLMN 418
Cdd:cd17656 312 IYILDQEQQLQPQGIVGELYI--SGASVARGYLNRQELTAEKFFPDPFDPnermyrtGDLARYLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 419 AGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADlsAELAARAEASLAAYKRPRHYVFVERLPK 498
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPL 467
|
490
....*....|.
gi 503186189 499 TPNGKLKRSDL 509
Cdd:cd17656 468 TPNGKVDRKAL 478
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
51-510 |
6.07e-31 |
|
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: 125.18 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 51 RALESAALRVAFELRSNRSLAPRTRVLIRLRNrtaYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVL---- 126
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNAR---AAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSsrap 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 127 -----DDTLPHGDFAP-GLAVVTEAALIAAIDSGPEGAFADTAADD---PAFLIYTSGTTANPKGVLHAHRSVwgrrpmy 197
Cdd:cd05929 78 raeacAIIEIKAAALVcGLFTGGGALDGLEDYEAAEGGSPETPIEDeaaGWKMLYSGGTTGRPKGIKRGLPGG------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 198 rgwyGITAADRLMHSGVINWTYAMGTGLSDPLANGA------TALLYTG-----ER-HPSIWPGLIRAFDVTIFAGVPGL 265
Cdd:cd05929 151 ----PPDNDTLMAAALGFGPGADSVYLSPAPLYHAApfrwsmTALFMGGtlvlmEKfDPEEFLRLIERYRVTFAQFVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 266 YHQIMR--QASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTEL--STYLSSApDFPRKPGTVGRAQPG 341
Cdd:cd05929 227 FVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGqgLTIINGE-EWLTHPGSVGRAVLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 RcVAILPEDGGDtsLPPGEAGMIAVHRSDPGLmlgYWQRPD-EEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAG 420
Cdd:cd05929 306 K-VHILDEDGNE--VPPGEIGEVYFANGPGFE---YTNDPEkTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 421 GYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAfVVAREGGAD----LSAELAARAEASLAAYKRPRHYVFVERL 496
Cdd:cd05929 380 GVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA-VVQPAPGADagtaLAEELIAFLRDRLSRYKCPRSIEFVAEL 458
|
490
....*....|....
gi 503186189 497 PKTPNGKLKRSDLK 510
Cdd:cd05929 459 PRDDTGKLYRRLLR 472
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
166-510 |
7.73e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 126.29 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVW------------GRRPMYRgWygitaADRLMHSGviNWTYAMGTGlsdplANGA 233
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYlstlsaiigwemGTCPVYL-W-----TLPMFHCN--GWTFTWGTA-----ARGG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 234 TALLYTGERHPSIWPGlIRAFDVTIFAGVPGLYHQIMRqasGDRLDLARLR---HGLTAGDTLPDALEAEwSERTGTRLY 310
Cdd:PLN03102 254 TSVCMRHVTAPEIYKN-IEMHNVTHMCCVPTVFNILLK---GNSLDLSPRSgpvHVLTGGSPPPAALVKK-VQRLGFQVM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTELS------TYLSSAPDFPRKPGTVGRAQPGRCVAILPE-DGGDT----SLPPGEAGMIAVHRSDPGLMLGYWQ 379
Cdd:PLN03102 329 HAYGLTEATgpvlfcEWQDEWNRLPENQQMELKARQGVSILGLADvDVKNKetqeSVPRDGKTMGEIVIKGSSIMKGYLK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 380 RPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAF 459
Cdd:PLN03102 409 NPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAF 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503186189 460 VVAREG--GADLSAELAARAEASLAAYKR--------PRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PLN03102 489 VVLEKGetTKEDRVDKLVTRERDLIEYCRenlphfmcPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
24-510 |
1.99e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 124.65 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 24 AGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPA 103
Cdd:PRK07788 58 AARRAPDRAALI-------DERGTLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 104 SPDLTARELGFLLDDSDAAAIVLDD--------------------TLPHGDFAPGLAVVTEAALIAAIDSGPEGAFADTA 163
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDeftdllsalppdlgrlrawgGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 AddpaFLIYTSGTTANPKGVLHAH-------RSVWGRRPMYRGWYGITAADrLMHS-GVINWTYAMGTGLS-------DP 228
Cdd:PRK07788 210 G----IVILTSGTTGTPKGAPRPEpsplaplAGLLSRVPFRAGETTLLPAP-MFHAtGWAHLTLAMALGSTvvlrrrfDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 langATALlytgerhpsiwpGLIRAFDVTIFAGVPGLYHQIMR---QASGDRlDLARLRHGLTAGDtlpdALEAEWSERT 305
Cdd:PRK07788 285 ----EATL------------EDIAKHKATALVVVPVMLSRILDlgpEVLAKY-DTSSLKIIFVSGS----ALSPELATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 306 ----GTRLYEGFGQTELSTYLSSAP-DFPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHRSDPglMLGYWQR 380
Cdd:PRK07788 344 leafGPVLYNLYGSTEVAFATIATPeDLAEAPGTVGRPPKGVTVKILDENGNE--VPRGVVGRIFVGNGFP--FEGYTDG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 381 PDEEREmfrGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFV 460
Cdd:PRK07788 420 RDKQII---DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503186189 461 VAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07788 497 VKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
47-506 |
2.05e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 124.37 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRA-LESAALRVAFeLRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASP---------DLTARELGFLL 116
Cdd:PRK13388 26 TWTWREvLAEAAARAAA-LIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTtrrgaalaaDIRRADCQLLV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 117 DDSDAAAIVLDDTLPHGDFapgLAVVTEAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVL--HAHRSVWGRR 194
Cdd:PRK13388 105 TDAEHRPLLDGLDLPGVRV---LDVDTPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRcsHGRLAFAGRA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 195 PMYRgwYGITAAD------RLMHSGVI--NWTYAmgtglsdpLANGATALLyTGERHPSIWPGLIRAFDVTIFAGVPGLY 266
Cdd:PRK13388 182 LTER--FGLTRDDvcyvsmPLFHSNAVmaGWAPA--------VASGAAVAL-PAKFSASGFLDDVRRYGATYFNYVGKPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 267 HQIMrqASGDRLDLA--RLRHGLtaGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPrkPGTVGRAQPG--- 341
Cdd:PRK13388 251 AYIL--ATPERPDDAdnPLRVAF--GNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAPGvai 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 --------RCVAILPEDGgdTSLPPGEAGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRA 413
Cdd:PRK13388 325 ynpetlteCAVARFDAHG--ALLNADEAIGELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 414 SDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAA--RAEASLAAYKRPRHYV 491
Cdd:PRK13388 403 ADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVR 482
|
490
....*....|....*.
gi 503186189 492 FVERLPKTPNGK-LKR 506
Cdd:PRK13388 483 IAADLPSTATNKvLKR 498
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
49-445 |
2.97e-29 |
|
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: 120.16 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:cd17640 7 TYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRS-VWGRRPMYRG-------- 199
Cdd:cd17640 86 D----------------------------------SDDLATIIYTSGTTGNPKGVMLTHANlLHQIRSLSDIvppqpgdr 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 200 -------WYgitAADRLMHSGVINW----TYAMGTGLSDPLANGATALLYTGerhPSIWPGLIRAFDVTIFAGVPglyhq 268
Cdd:cd17640 132 flsilpiWH---SYERSAEYFIFACgcsqAYTSIRTLKDDLKRVKPHYIVSV---PRLWESLYSGIQKQVSKSSP----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 269 IMRQASGDRLDLARLRHGLTAGDTLPDALEaEWSERTGTRLYEGFGQTELSTYLSSapdfpRKP-----GTVGRAQPGRC 343
Cdd:cd17640 201 IKQFLFLFFLSGGIFKFGISGGGALPPHVD-TFFEAIGIEVLNGYGLTETSPVVSA-----RRLkcnvrGSVGRPLPGTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 344 VAILPEDGGdTSLPPGEAGmIAVHRSdPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASD-LMNAGG 421
Cdd:cd17640 275 IKIVDPEGN-VVLPPGEKG-IVWVRG-PQVMKGYYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDtIVLSNG 351
|
410 420
....*....|....*....|....
gi 503186189 422 YRVSPVEVEAVLREHPLVAEAGVI 445
Cdd:cd17640 352 ENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
26-506 |
7.08e-29 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 120.44 E-value: 7.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 26 AAAGDKTALVVIHDPAGREaETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRN--RTAYAL---AFFGAIA----G 96
Cdd:PRK10524 64 AKRPEQLALIAVSTETDEE-RTYTFRQLHDEVNRMAAMLRSL-GVQRGDRVLIYMPMiaEAAFAMlacARIGAIHsvvfG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 97 GLvpipASPDLTARelgflLDDSDAAAIV-----------------LDDTLPHGDFAP--------GLAvvtEAALIAA- 150
Cdd:PRK10524 142 GF----ASHSLAAR-----IDDAKPVLIVsadagsrggkvvpykplLDEAIALAQHKPrhvllvdrGLA---PMARVAGr 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 151 -IDSGPEGA-FADTA-------ADDPAFLIYTSGTTANPKGVlhaHRSVWG-----RRPMyRGWYGITAADRLMHSGVIN 216
Cdd:PRK10524 210 dVDYATLRAqHLGARvpvewleSNEPSYILYTSGTTGKPKGV---QRDTGGyavalATSM-DTIFGGKAGETFFCASDIG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 217 WTYAMGTGLSDPLANGATALLYTGERH---PSIWPGLIRAFDVTIFAGVPGLYHQIMRQ--ASGDRLDLARLRHGLTAGD 291
Cdd:PRK10524 286 WVVGHSYIVYAPLLAGMATIMYEGLPTrpdAGIWWRIVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 292 TLpDALEAEW-SERTGTRLYEGFGQTELS-TYLSSAP---DFPRKPGTVGRAQPGRCVAILPEDGGdTSLPPGEAGMIAV 366
Cdd:PRK10524 366 PL-DEPTASWiSEALGVPVIDNYWQTETGwPILAIARgveDRPTRLGSPGVPMYGYNVKLLNEVTG-EPCGPNEKGVLVI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 367 HRS-DPGLMLGYWQrpDEER------EMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLV 439
Cdd:PRK10524 444 EGPlPPGCMQTVWG--DDDRfvktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAV 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 440 AEAGVIDVPQPHGGTAITAFVVAREGG--------ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK10524 522 AEVAVVGVKDALKGQVAVAFVVPKDSDsladrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
47-506 |
1.26e-28 |
|
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: 118.41 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 47 TWTYRALESAALRVAFELRSnRSLAPRTRVLIRL-RNRTAYAlAFFGAI-AGG-LVPI-PASPdlTAReLGFLLDDSDAA 122
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFeKSKWAVV-AMLAVLkAGGaFVPLdPSHP--LQR-LQEILQDTGAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 123 AIVLDDtlphgdfapglavvteaaliaaidsgpegafadtaADDPAFLIYTSGTTANPKGVLHAHRSV------WGRRpm 196
Cdd:cd05918 99 VVLTSS-----------------------------------PSDAAYVIFTSGSTGKPKGVVIEHRALstsalaHGRA-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 197 yrgwYGITAADRLMHSGvinwTYAMGTGLSD---PLANGATALLYT-GERHPSIwPGLIRAFDVTIFAGVPGLYHQImrq 272
Cdd:cd05918 142 ----LGLTSESRVLQFA----SYTFDVSILEiftTLAAGGCLCIPSeEDRLNDL-AGFINRLRVTWAFLTPSVARLL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 273 asgDRLDLARLRHGLTAGDTLPDALEAEWSERtgTRLYEGFGQTELSTY-LSSAPDFPRKPGTVGRAQPGRCVAILPEDg 351
Cdd:cd05918 210 ---DPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECTIAaTVSPVVPSTDPRNIGRPLGATCWVVDPDN- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 352 GDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF---------RGEWFTG-----GDLGCIDEDGAIAHLGRASDLM 417
Cdd:cd05918 284 HDRLVPIGAVGELLI--EGPILARGYLNDPEKTAAAFiedpawlkqEGSGRGRrlyrtGDLVRYNPDGSLEYVGRKDTQV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 418 NAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTA---ITAFVVARE------GGADLSAELAARAEASLA------ 482
Cdd:cd05918 362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVLDGsssgsgDGDSLFLEPSDEFRALVAelrskl 441
|
490 500
....*....|....*....|....*....
gi 503186189 483 -----AYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:cd05918 442 rqrlpSYMVPSVFLPLSHLPLTASGKIDR 470
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
165-510 |
1.27e-28 |
|
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: 119.17 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRG-WYGITAADRLMHSGVINWTYAMG--TGLSDPLANGATALLYTGE 241
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAILTVIPFHHGFGmfTTLGYLICGFRVVLMYKFE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 242 RhpSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTR-LYEGFGQTELST 320
Cdd:cd17642 264 E--ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTS 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 321 YLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDTsLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE-WFTGGDLG 399
Cdd:cd17642 342 AILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKT-LGPNERGELCV--KGPMIMKGYVNNPEATKALIDKDgWLHSGDIA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 400 CIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEA 479
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVAS 498
|
330 340 350
....*....|....*....|....*....|..
gi 503186189 480 SLAAYKRPRHYV-FVERLPKTPNGKLKRSDLK 510
Cdd:cd17642 499 QVSTAKRLRGGVkFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
50-509 |
4.11e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 50 YRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD-- 127
Cdd:PRK05857 44 YRELVAEVGGLAADLRA-QSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVApg 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 -----DTLPHGDFAPGLAVVTEAALIAAIDSGPEGAFA----DTAADDPAFLIYTSGTTANPKGVLHAHRSVWGrrpmyr 198
Cdd:PRK05857 123 skmasSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLagnaDQGSEDPLAMIFTSGTTGEPKAVLLANRTFFA------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 199 gwygitAADRLMHSGvINW-TYAMGTGLSDPLAngAT---------------ALLYTGERHPSIWPGLIRAFDVTIFAGV 262
Cdd:PRK05857 197 ------VPDILQKEG-LNWvTWVVGETTYSPLP--AThigglwwiltclmhgGLCVTGGENTTSLLEILTTNAVATTCLV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 263 PGLYHQIMRQASGDRLDLARLRHgLTAGDTLPDALEAEWSERTGTRLYEGFGQTELS-TYLSSAPDFPR----KPGTVGR 337
Cdd:PRK05857 268 PTLLSKLVSELKSANATVPSLRL-VGYGGSRAIAADVRFIEATGVRTAQVYGLSETGcTALCLPTDDGSivkiEAGAVGR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 338 AQPGRCVAILPEDGGDTSLPPG--EAGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASD 415
Cdd:PRK05857 347 PYPGVDVYLAATDGIGPTAPGAgpSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 416 LMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAR-----EGGADLSAELAARAEASLAAYKRPRHY 490
Cdd:PRK05857 427 MIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASaeldeSAARALKHTIAARFRRESEPMARPSTI 506
|
490
....*....|....*....
gi 503186189 491 VFVERLPKTPNGKLKRSDL 509
Cdd:PRK05857 507 VIVTDIPRTQSGKVMRASL 525
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-513 |
1.03e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.35 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTALVvihdpagREAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP 102
Cdd:PRK05691 1139 EQARQTPERIALV-------WDGGSLDYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 103 ASPDLTARELGFLLDDSDAAAIV----LDDTLPHgdfAPGLAVVTEAALiaAIDSGPEGAFA-DTAADDPAFLIYTSGTT 177
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLtqshLLERLPQ---AEGVSAIALDSL--HLDSWPSQAPGlHLHGDNLAYVIYTSGST 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 178 ANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSdPLANGATALLYT-GE-RHPSIWPGLIRAFD 255
Cdd:PRK05691 1286 GQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFW-PLITGCRLVLAGpGEhRDPQRIAELVQQYG 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 256 VTIFAGVPGLYHQIMRQAsgDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTE----LSTYLSSAPDFPR 330
Cdd:PRK05691 1365 VTTLHFVPPLLQLFIDEP--LAAACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTEtainVTHWQCQAEDGER 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 331 KPgtVGRAQPGRCVAILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF-------RGE-WFTGGDLGCID 402
Cdd:PRK05691 1443 SP--IGRPLGNVLCRVL--DAELNLLPPGVAGELCI--GGAGLARGYLGRPALTAERFvpdplgeDGArLYRTGDRARWN 1516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 403 EDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIdVPQPHGGTAITAFVVAREGGADLSAELAARAEASLA 482
Cdd:PRK05691 1517 ADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELP 1595
|
490 500 510
....*....|....*....|....*....|.
gi 503186189 483 AYKRPRHYVFVERLPKTPNGKLKRSDLKIPQ 513
Cdd:PRK05691 1596 EYMVPAQLIRLDQMPLGPSGKLDRRALPEPV 1626
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
23-506 |
2.81e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 115.43 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 23 RAGAAAGDKTAlvVIHDPAGRE-AETWTY-RALESAALRvafelrsnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP 100
Cdd:PRK08162 26 RAAEVYPDRPA--VIHGDRRRTwAETYARcRRLASALAR--------RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 101 IPASPDLTARELGFLLDDSDAAAIVLDDtlphgDFAPglaVVTEAAL------IAAID----SGPEGAFADT-------A 163
Cdd:PRK08162 96 NTLNTRLDAASIAFMLRHGEAKVLIVDT-----EFAE---VAREALAllpgpkPLVIDvddpEYPGGRFIGAldyeaflA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAF-------------LIYTSGTTANPKGVLHAHRsvwgrrpmyrGWY-----GITAADRLMHSgVINWTYAM--GT 223
Cdd:PRK08162 168 SGDPDFawtlpadewdaiaLNYTSGTTGNPKGVVYHHR----------GAYlnalsNILAWGMPKHP-VYLWTLPMfhCN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 224 GLSDP---LANGATALLYTGERHPSIWpGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDA-LEA 299
Cdd:PRK08162 237 GWCFPwtvAARAGTNVCLRKVDPKLIF-DLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAvIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 300 ewSERTGTRLYEGFGQTElsTYlssapdfprKPGTVGRAQPGrcVAILPED----------------GGDTSLPPgeAGM 363
Cdd:PRK08162 316 --MEEIGFDLTHVYGLTE--TY---------GPATVCAWQPE--WDALPLDeraqlkarqgvryplqEGVTVLDP--DTM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 364 IAVHRSDPGL----------MLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVL 433
Cdd:PRK08162 379 QPVPADGETIgeimfrgnivMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 434 REHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVErLPKTPNGKLKR 506
Cdd:PRK08162 459 YRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQK 530
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-503 |
4.98e-27 |
|
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: 112.09 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDpAFLIYTSGTTANPKGVLHAHRSVW----GRRPMYRGWYG----------------ITAADRLMH-SGVINWTYAMG 222
Cdd:cd05924 3 ADD-LYILYTGGTTGMPKGVMWRQEDIFrmlmGGADFGTGEFTpsedahkaaaaaagtvMFPAPPLMHgTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 223 TG----LSDPLANgATALLYTGERHpsiwpgliRAFDVTIfagVPGLYHQIMRQA--SGDRLDLARLR----HGLTAGDT 292
Cdd:cd05924 82 GGqtvvLPDDRFD-PEEVWRTIEKH--------KVTSMTI---VGDAMARPLIDAlrDAGPYDLSSLFaissGGALLSPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 293 LPDALEAEWSERTgtrLYEGFGQTELSTYLSSAPDfPRKPGTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHRSdpG 372
Cdd:cd05924 150 VKQGLLELVPNIT---LVDAFGSSETGFTGSGHSA-GSGPETGPFTRANPDTVVLDDDGRV--VPPGSGGVGWIARR--G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 373 LM-LGYWQRPDEEREMFR---GE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDV 447
Cdd:cd05924 222 HIpLGYYGDEAKTAETFPevdGVrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGR 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 503186189 448 PQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:cd05924 302 PDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
42-468 |
1.30e-26 |
|
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: 112.95 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 42 GREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDA 121
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 122 AAIV---LDDtlpHGDFAPGLAVVTEAALIAAIDSG--------------PEGAFADTAADDPAFLIYTSGTTANPKGVL 184
Cdd:cd05932 80 KALFvgkLDD---WKAMAPGVPEGLISISLPPPSAAncqyqwddliaqhpPLEERPTRFPEQLATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 185 HAHRS-VWGRRPMYRGwYGITAADRLMhsgvinwTYAmgtglsdPLAngatallYTGER----HPSIWPGLIRAF----- 254
Cdd:cd05932 157 LTFGSfAWAAQAGIEH-IGTEENDRML-------SYL-------PLA-------HVTERvfveGGSLYGGVLVAFaesld 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 255 ----DV-----TIFAGVP--------GLYHQIMRQ-------------------ASGDRLDLARLRHGLTAgdTLPDALe 298
Cdd:cd05932 215 tfveDVqrarpTLFFSVPrlwtkfqqGVQDKIPQQklnlllkipvvnslvkrkvLKGLGLDQCRLAGCGSA--PVPPAL- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 299 AEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAIlpedggdtslppGEAGMIAVhRSdPGLMLGYW 378
Cdd:cd05932 292 LEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI------------SEDGEILV-RS-PALMMGYY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 379 QRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLM-NAGGYRVSPVEVEAVLREHPLVAEAGVI--DVPQPHGGT 454
Cdd:cd05932 358 KDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIgsGLPAPLALV 437
|
490
....*....|....
gi 503186189 455 AITAFVVAREGGAD 468
Cdd:cd05932 438 VLSEEARLRADAFA 451
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-506 |
1.99e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 112.67 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 24 AGAAAGDKTALVVIHDpagREAETwtYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPA 103
Cdd:PRK05852 25 AATRLPEAPALVVTAD---RIAIS--YRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 104 SPDLTARELGFLLDDSDAAAIVLDDTLPHgDFAPGLAVVTEAALIAAIDSGPEGA-----FADTAA------------DD 166
Cdd:PRK05852 99 DPALPIAEQRVRSQAAGARVVLIDADGPH-DRAEPTTRWWPLTVNVGGDSGPSGGtlsvhLDAATEptpatstpeglrPD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 167 PAFLIYTSGTTANPKGVlhahrsVWGRRPMYRGWYGITAADRL--MHSGVINWTYAMGTGLS----DPLANGATALLYTG 240
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMV------PWTHANIASSVRAIITGYRLspRDATVAVMPLYHGHGLIaallATLASGGAVLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 ERHP--SIWPGlIRAFDVTIFAGVPGLyHQIMRQASgDRLDLARLRHGLTAGDTLPDALEAEWSE----RTGTRLYEGFG 314
Cdd:PRK05852 252 GRFSahTFWDD-IKAVGATWYTAVPTI-HQILLERA-ATEPSGRKPAALRFIRSCSAPLTAETAQalqtEFAAPVVCAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 315 QTELSTYLSSA-------PDFPR-KPGTVGRAQPGRcVAILPEDGGdtSLPPGEAGMIAVHrsDPGLMLGYWQRPDEERE 386
Cdd:PRK05852 329 MTEATHQVTTTqiegigqTENPVvSTGLVGRSTGAQ-IRIVGSDGL--PLPAGAVGEVWLR--GTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 387 MFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGG 466
Cdd:PRK05852 404 NFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 503186189 467 ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK05852 484 PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-510 |
1.06e-25 |
|
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: 109.75 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:cd05940 2 EALTYAELDAMANRYARWLKS-LGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 LDdtlphgdfapglavvteaaliaaidsgpegafadtaaddPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITA 205
Cdd:cd05940 81 VD---------------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADR------LMHS-GVInwtyamgTGLSDPLANGATALLYTGERHPSIWPGlIRAFDVTIFAGVPGLYHQIMRQAsgdRL 278
Cdd:cd05940 122 SDVlytclpLYHStALI-------VGWSACLASGATLVIRKKFSASNFWDD-IRKYQATIFQYIGELCRYLLNQP---PK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 DLARlRHGLTA--GDTL-PDALEaEWSERTGT-RLYEGFGQTELStylSSAPDFPRKPGTVGRAQP-GRCVA-------- 345
Cdd:cd05940 191 PTER-KHKVRMifGNGLrPDIWE-EFKERFGVpRIAEFYAATEGN---SGFINFFGKPGAIGRNPSlLRKVAplalvkyd 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 346 ------ILPEDGGDTSLPPGEAGMIAVHRSDPGLMLGYWQRPDEE----REMFR-GE-WFTGGDLGCIDEDGAIAHLGRA 413
Cdd:cd05940 266 lesgepIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAATEkkilRDVFKkGDaWFNTGDLMRLDGEGFWYFVDRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 414 SDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQP-HGGTA-ITAFVVAREGGADLSAeLAARAEASLAAYKRPRHYV 491
Cdd:cd05940 346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAgMAAIVLQPNEEFDLSA-LAAHLEKNLPGYARPLFLR 424
|
490
....*....|....*....
gi 503186189 492 FVERLPKTPNGKLKRSDLK 510
Cdd:cd05940 425 LQPEMEITGTFKQQKVDLR 443
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
49-509 |
1.09e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 110.47 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:PRK13383 62 SYRELQRATESLARRL-TRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TLPHGDFAPGLAV-VTEAALIAAIDSGPEGAFADTAAddpaFLIYTSGTTANPKGVlhahrsvwGRRPMYRG----WYGI 203
Cdd:PRK13383 141 EFAERIAGADDAVaVIDPATAGAEESGGRPAVAAPGR----IVLLTSGTTGKPKGV--------PRAPQLRSavgvWVTI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 204 TAADRLMHSGVINWTYAMGTGLSD-----PLANGATALLYtgeRHPSIWPGLIRA--FDVTIFAGVPGLYHQIMRQASGD 276
Cdd:PRK13383 209 LDRTRLRTGSRISVAMPMFHGLGLgmlmlTIALGGTVLTH---RHFDAEAALAQAslHRADAFTAVPVVLARILELPPRV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 277 RL--DLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELST-YLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgd 353
Cdd:PRK13383 286 RArnPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRNN-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 354 TSLPPGEAGMIAVHrsdpGLMLGYWQRPDEEREMFRGEWFTgGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVL 433
Cdd:PRK13383 364 RPVGPRVTGRIFVG----GELAGTRYTDGGGKAVVDGMTST-GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENAL 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503186189 434 REHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:PRK13383 439 AAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
49-510 |
1.11e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 110.60 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:PRK06164 37 SRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TLPHGDFAPGLAVVTEAAL-----IAAIDSGPEG-------------AFADTAA-----------DDPAFLIYTSGTTAN 179
Cdd:PRK06164 116 GFKGIDFAAILAAVPPDALpplraIAVVDDAADAtpapapgarvqlfALPDPAPpaaageraadpDAGALLFTTSGTTSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 180 PKGVLHAHRSVWGRRPMYRGWYGITAADRLM----HSGVINWTYAMGTglsdpLANGATALL---YTGERHPSiwpgLIR 252
Cdd:PRK06164 196 PKLVLHRQATLLRHARAIARAYGYDPGAVLLaalpFCGVFGFSTLLGA-----LAGGAPLVCepvFDAARTAR----ALR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 253 AFDVTIFAGVPGLYHQIMRQAsGDRLDLARLRHgLTAGDTLPDALE-AEWSERTGTRLYEGFGQTELSTYLS----SAPD 327
Cdd:PRK06164 267 RHRVTHTFGNDEMLRRILDTA-GERADFPSARL-FGFASFAPALGElAALARARGVPLTGLYGSSEVQALVAlqpaTDPV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 328 FPRKPGTVGRAQPGRCVAIL-PEDGGdtSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDG 405
Cdd:PRK06164 345 SVRIEGGGRPASPEARVRARdPQDGA--LLPDGESGEIEI--RAPSLMRGYLDNPDATARALTDDgYFRTGDLGYTRGDG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 406 AIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVpQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYK 485
Cdd:PRK06164 421 QFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFK 499
|
490 500
....*....|....*....|....*...
gi 503186189 486 RPRHYVFVERLPKTPNG---KLKRSDLK 510
Cdd:PRK06164 500 VPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
12-510 |
1.99e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 109.68 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNmakHVLRAGAAAGDKTALVVIHDpAGREaETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFF 91
Cdd:cd05906 9 PRTLL---ELLLRAAERGPTKGITYIDA-DGSE-EFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIPAFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 92 GAIAGGLVPIPASP----DLTARELGFL------LDDsdaaAIVLDDTLPHGDFAP-----GLAVVTEAALIAAIDSGPE 156
Cdd:cd05906 83 ACVLAGFVPAPLTVpptyDEPNARLRKLrhiwqlLGS----PVVLTDAELVAEFAGletlsGLPGIRVLSIEELLDTAAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 157 GAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRrpmYRG---WYGITAADRLM------HSGVINWTYAMGTGLSD 227
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR---SAGkiqHNGLTPQDVFLnwvpldHVGGLVELHLRAVYLGC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 228 PLANGATALLYtgeRHPSIWPGLIRAFDVTI-FAgvPGLYHQIMRQA----SGDRLDLARLRHGLTAGDtlpdALEAEWS 302
Cdd:cd05906 236 QQVHVPTEEIL---ADPLRWLDLIDRYRVTItWA--PNFAFALLNDLleeiEDGTWDLSSLRYLVNAGE----AVVAKTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 303 ERTgTRLYE-----------GFGQTELS---TYLSSAPDFPRKPGT----VGRAQPGRCVAILPEDGGdtSLPPGEAGMI 364
Cdd:cd05906 307 RRL-LRLLEpyglppdairpAFGMTETCsgvIYSRSFPTYDHSQALefvsLGRPIPGVSMRIVDDEGQ--LLPEGEVGRL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 365 AVHrsDPGLMLGYWQRPDEEREMFR-GEWFTGGDLGCIDeDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLV---- 439
Cdd:cd05906 384 QVR--GPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsf 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 440 -AEAGVIDVPQPHGGTAITaFVVAREGGADLSAELAARAEASLAAYKRPRHYVF-VER--LPKTPNGKLKRSDLK 510
Cdd:cd05906 461 tAAFAVRDPGAETEELAIF-FVPEYDLQDALSETLRAIRSVVSREVGVSPAYLIpLPKeeIPKTSLGKIQRSKLK 534
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-516 |
2.95e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.64 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRE-RGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL 2290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 LD----DTLphGDFAPGLA---VVTEAALIAAIDSGPEGAFadTAADDPAFLIYTSGTTANPKGVLHAH-------RSVW 191
Cdd:PRK05691 2291 SDralfEAL--GELPAGVArwcLEDDAAALAAYSDAPLPFL--SLPQHQAYLIYTSGSTGKPKGVVVSHgeiamhcQAVI 2366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 192 GRrpmyrgwYGITAADRLMHSGVINWTyAMGTGLSDPLANGATALLytgeRHPSIWP-----GLIRAFDVTIFAGVPGlY 266
Cdd:PRK05691 2367 ER-------FGMRADDCELHFYSINFD-AASERLLVPLLCGARVVL----RAQGQWGaeeicQLIREQQVSILGFTPS-Y 2433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 267 HQIMRQASGDRLDLARLRHGLTAGDTL-PDALEAEWSERTGTRLYEGFGQTE--LSTYLSSAPD-FPRKPGTV--GRAQP 340
Cdd:PRK05691 2434 GSQLAQWLAGQGEQLPVRMCITGGEALtGEHLQRIRQAFAPQLFFNAYGPTEtvVMPLACLAPEqLEEGAASVpiGRVVG 2513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 341 GRCVAILPEDGGdtSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF--------RGEWFTGGDLGCIDEDGAIAHLGR 412
Cdd:PRK05691 2514 ARVAYILDADLA--LVPQGATGELYV--GGAGLAQGYHDRPGLTAERFvadpfaadGGRLYRTGDLVRLRADGLVEYVGR 2589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 413 ASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPhGGTAITAFVVAREGGAD------LSAELAARAEASLAAYKR 486
Cdd:PRK05691 2590 IDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLVSAVAGQDdeaqaaLREALKAHLKQQLPDYMV 2668
|
490 500 510
....*....|....*....|....*....|
gi 503186189 487 PRHYVFVERLPKTPNGKLKRSDLKIPQPPL 516
Cdd:PRK05691 2669 PAHLILLDSLPLTANGKLDRRALPAPDPEL 2698
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
46-460 |
3.60e-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: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 ------LDDTLPHGDFAPGL-----------------------AVVTEAALIAAIDSGP-EGAFADTAADDPAFLIYTSG 175
Cdd:cd17641 89 aedeeqVDKLLEIADRIPSVryviycdprgmrkyddprlisfeDVVALGRALDRRDPGLyEREVAAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 176 TTANPKGVLHAHRSVWGR-------RPMYRG----------WYG---ITAADRLMHSGVINWTYAMGTGLSDPLANGATA 235
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHcaaylaaDPLGPGdeyvsvlplpWIGeqmYSVGQALVCGFIVNFPEEPETMMEDLREIGPTF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 236 LLYTgerhPSIWPGL-----IRAFDVT--------------------IFAGVP---------GLYHQIMRQASGDRLDLA 281
Cdd:cd17641 249 VLLP----PRVWEGIaadvrARMMDATpfkrfmfelgmklglraldrGKRGRPvslwlrlasWLADALLFRPLRDRLGFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 282 RLRHGLTAGDTL-PDALEaeWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAIlpedggdtslppGE 360
Cdd:cd17641 325 RLRSAATGGAALgPDTFR--FFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI------------DE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGMIAVHrsDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMN-AGGYRVSPVEVEAVLREHPL 438
Cdd:cd17641 391 VGEILVR--SPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPY 468
|
490 500
....*....|....*....|..
gi 503186189 439 VAEAGVIDvpqpHGGTAITAFV 460
Cdd:cd17641 469 IAEAVVLG----AGRPYLTAFI 486
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
159-510 |
1.31e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 159 FADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLM------HSGVINWTYAMgtglsdPLANG 232
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILsslpffHSFGLTVTLWL------PLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 233 ATALLytgerHPSIWPG-----LIRAFDVTIFAGVP---GLYhqiMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSER 304
Cdd:PRK08633 850 IKVVY-----HPDPTDAlgiakLVAKHRATILLGTPtflRLY---LRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 305 TGTRLYEGFGQTELSTYLS-SAPDFPR---------KPGTVGRAQPGRCVAIL-PEDGgdTSLPPGEAGMIAVhrSDPGL 373
Cdd:PRK08633 922 FGIRILEGYGATETSPVASvNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVdPETF--EELPPGEDGLILI--GGPQV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 374 MLGYWQRPDEE----REMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHpLVAEAGVI---D 446
Cdd:PRK08633 998 MKGYLGDPEKTaeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKA-LGGEEVVFavtA 1076
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503186189 447 VPQPHGGTAITafVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLkrsDLK 510
Cdd:PRK08633 1077 VPDEKKGEKLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKL---DLK 1135
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
164-510 |
4.06e-24 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 106.14 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAFLIYTSGTTANPKGVLHAhrsvwgrrpmyRGWYGITAADRLMHS-----GVINWTYA---MGTGLS----DPLAN 231
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVLHT-----------TGGYMVYTATTFKYAfdykpTDVYWCTAdcgWITGHSyvtyGPMLN 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 232 GATALLYTGE-RHPSiwPG----LIRAFDVTIFAGVPGLYHQIMRqaSGDRLDLARLRHGL------------------- 287
Cdd:PLN02654 343 GATVLVFEGApNYPD--SGrcwdIVDKYKVTIFYTAPTLVRSLMR--DGDEYVTRHSRKSLrvlgsvgepinpsawrwff 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 288 -TAGDTLPDALEAEWSERTGtrlyeGFgqteLSTYLSSApdFPRKPGTVGRAQPGRCVAILPEDGGDTSlppGE-AGMIA 365
Cdd:PLN02654 419 nVVGDSRCPISDTWWQTETG-----GF----MITPLPGA--WPQKPGSATFPFFGVQPVIVDEKGKEIE---GEcSGYLC 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 366 VHRSDPGLMLGYWQrpDEER------EMFRGEWFTGGdlGCI-DEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPL 438
Cdd:PLN02654 485 VKKSWPGAFRTLYG--DHERyettyfKPFAGYYFSGD--GCSrDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503186189 439 VAEAGVIDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEGvpySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
48-510 |
8.22e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 101.71 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 48 WTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAA-LGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 DTlphgdFAP-------------GLAVVTEAALIAAiDSGPEGAFAD--TAADD----PAF-------LIYTSGTTANPK 181
Cdd:PRK07008 119 LT-----FLPlvdalapqcpnvkGWVAMTDAAHLPA-GSTPLLCYETlvGAQDGdydwPRFdenqassLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 182 GVLHAHRSVwgrrpMYRGW-------YGITAADRLMHSGVINWTYAMGTGLSDPLaNGATALLytgerhpsiwPG----- 249
Cdd:PRK07008 193 GALYSHRST-----VLHAYgaalpdaMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVL----------PGpdldg 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 250 -----LIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELS----- 319
Cdd:PRK07008 257 kslyeLIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgtl 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 320 -----TYLSSAPDFPRKPGT-VGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHRSDPGLMLGYWQRpdEEREMFRGeWF 393
Cdd:PRK07008 337 cklkwKHSQLPLDEQRKLLEkQGRVIYGVDMKIVGDDGRE--LPWDGKAFGDLQVRGPWVIDRYFRG--DASPLVDG-WF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 394 TGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHgGTAITAFVVAREGGADLS-AE 472
Cdd:PRK07008 412 PTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPK-WDERPLLVVVKRPGAEVTrEE 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 503186189 473 LAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07008 491 LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
49-430 |
1.00e-22 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 102.10 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRsnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGlvPIPASPDLTARELGfLLDDSDAAAIVLDD 128
Cdd:PRK08043 233 SYRKLLKKTLFVGRILE--KYSVEGERIGLMLPNATISAAVIFGASLRR--RIPAMMNYTAGVKG-LTSAITAAEIKTIF 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 T----LPHGDFAPGLAVVTEA-----------------ALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAH 187
Cdd:PRK08043 308 TsrqfLDKGKLWHLPEQLTQVrwvyledlkddvttadkLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSH 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 188 RSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIWPGLIRAFDVTIFAGVPGLYH 267
Cdd:PRK08043 388 KSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLG 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 268 QIMRQAsgDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAIL 347
Cdd:PRK08043 468 NYARFA--NPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 348 P----EDGGDTSLppgeagmiavhrSDPGLMLGYW--QRP---------DEEREMFRGeWFTGGDLGCIDEDGAIAHLGR 412
Cdd:PRK08043 546 SvpgiEQGGRLQL------------KGPNIMNGYLrvEKPgvlevptaeNARGEMERG-WYDTGDIVRFDEQGFVQIQGR 612
|
410
....*....|....*...
gi 503186189 413 ASDLMNAGGYRVSPVEVE 430
Cdd:PRK08043 613 AKRFAKIAGEMVSLEMVE 630
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
11-510 |
4.33e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 99.95 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 11 PPRNLNMAKHVLRAGAAAGDKTALVVihdpagrEAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNR-----TA 85
Cdd:PRK08279 33 PDSKRSLGDVFEEAAARHPDRPALLF-------EDQSISYAELNARANRYAHWAAA-RGVGKGDVVALLMENRpeylaAW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 86 YALAFFGAIAGGLvpipaSPDLTARELGFLLDDSDAAAIVLDDTL--------PHGDFAPGLAVVTEA---------ALI 148
Cdd:PRK08279 105 LGLAKLGAVVALL-----NTQQRGAVLAHSLNLVDAKHLIVGEELveafeearADLARPPRLWVAGGDtlddpegyeDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 149 AAIDSGPEGAFADTA---ADDPAFLIYTSGTTANPKGVLHAHRsvwgRRPMYRGWYG----ITAADRLM------HS--G 213
Cdd:PRK08279 180 AAAAGAPTTNPASRSgvtAKDTAFYIYTSGTTGLPKAAVMSHM----RWLKAMGGFGgllrLTPDDVLYcclplyHNtgG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 214 VINWTYAmgtglsdpLANGATALLytgERHPS---IWPGlIRAFDVTIFAGVPGLYHQIMRQ--ASGDRldlarlRHGLT 288
Cdd:PRK08279 256 TVAWSSV--------LAAGATLAL---RRKFSasrFWDD-VRRYRATAFQYIGELCRYLLNQppKPTDR------DHRLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 289 --AGDTL-PDALEaEWSERTGT-RLYEGFGQTELSTYLSsapDFPRKPGTVGR-----AQPGRCVAILPEDGGdtslpP- 358
Cdd:PRK08279 318 lmIGNGLrPDIWD-EFQQRFGIpRILEFYAASEGNVGFI---NVFNFDGTVGRvplwlAHPYAIVKYDVDTGE-----Pv 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 359 -GEAG-MIAVHRSDPGLML----------GYWQRPDEEREMFRG------EWFTGGDLGCIDEDGAIAHLGRASDLMNAG 420
Cdd:PRK08279 389 rDADGrCIKVKPGEVGLLIgritdrgpfdGYTDPEASEKKILRDvfkkgdAWFNTGDLMRDDGFGHAQFVDRLGDTFRWK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 421 GYRVSPVEVEAVLREHPLVAEAGVIDVPQP-HGGTAITAFVVAREGGA-DLsAELAARAEASLAAYKRPrhyVFV---ER 495
Cdd:PRK08279 469 GENVATTEVENALSGFPGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEfDL-AALAAHLYERLPAYAVP---LFVrlvPE 544
|
570
....*....|....*
gi 503186189 496 LPKTPNGKLKRSDLK 510
Cdd:PRK08279 545 LETTGTFKYRKVDLR 559
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
15-503 |
4.57e-22 |
|
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: 99.65 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 15 LNMAKHVLRAGAAAGdktALVVIHDPAGREAETwTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAI 94
Cdd:cd05943 70 LNYAENLLRHADADD---PAAIYAAEDGERTEV-TWAELRRRVARLAAALRAL-GVKPGDRVAGYLPNIPEAVVAMLATA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 95 AGGLVPIPASPDLTAR---------ELGFLLDD------------------------SDAAAIVLDDTLPHG--DFAPGL 139
Cdd:cd05943 145 SIGAIWSSCSPDFGVPgvldrfgqiEPKVLFAVdaytyngkrhdvrekvaelvkglpSLLAVVVVPYTVAAGqpDLSKIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 140 AVVTEAALIAAIDSGPEGaFADTAADDPAFLIYTSGTTANPKGVLHAHRSV-----------WGRRPmyrgwygitaADR 208
Cdd:cd05943 225 KALTLEDFLATGAAGELE-FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTllqhlkehilhCDLRP----------GDR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 209 LMHSGVINWTyaMGTGLSDPLANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGVPGLYHQIMR--QASGDRLDLARL 283
Cdd:cd05943 294 LFYYTTCGWM--MWNWLVSGLAVGATIVLYDGSpfyPDTNALWDLADEEGITVFGTSAKYLDALEKagLKPAETHDLSSL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 284 RHGLTAGDTL-PDALEAEWSERTGTRLYEGF-GQTEL-STYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDTslpPGE 360
Cdd:cd05943 372 RTILSTGSPLkPESFDYVYDHIKPDVLLASIsGGTDIiSCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPV---WGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGMIAVHRSDPGLMLGYWQRPDEER------EMFRGEWfTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLR 434
Cdd:cd05943 449 KGELVCTKPFPSMPVGFWNDPDGSRyraayfAKYPGVW-AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVE 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503186189 435 EHPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSAELAARAEASLAAYKRPRH----YVFVERLPKTPNGK 503
Cdd:cd05943 528 KIPEVEDSLVVGQEWKDGDERVILFVKLRE-GVELDDELRKRIRSTIRSALSPRHvpakIIAVPDIPRTLSGK 599
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
49-504 |
6.20e-22 |
|
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: 98.24 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:cd17648 14 TYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TlphgdfapglavvteaaliaaidsgpegafadtaadDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADR 208
Cdd:cd17648 94 T------------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 209 LMHSGVINWTYAMGT-GLSDPLANGATALLYTGE--RHPSIWPGLIRAFDVTIFAGVPGLYHQImrqasgdrlDLARLRH 285
Cdd:cd17648 138 EAVLFFSNYVFDFFVeQMTLALLNGQKLVVPPDEmrFDPDRFYAYINREKVTYLSGTPSVLQQY---------DLARLPH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 286 ---GLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTY--LSSAPDFPRKPGTVGRAQPGRCVAILpeDGGDTSLPPGE 360
Cdd:cd17648 209 lkrVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTnhKRFFPGDQRFDKSLGRPVRNTKCYVL--NDAMKRVPVGA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 361 AGmiAVHRSDPGLMLGYWQRPDEEREMF------------RGEW---FTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVS 425
Cdd:cd17648 287 VG--ELYLGGDGVARGYLNRPELTAERFlpnpfqteqeraRGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 426 PVEVEAVLREHPLVAEAGVI-----DVPQPHGGTAITAFVVAREGGADlSAELAARAEASLAAYKRPRHYVFVERLPKTP 500
Cdd:cd17648 365 PGEVEAALASYPGVRECAVVakedaSQAQSRIQKYLVGYYLPEPGHVP-ESDLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
|
....
gi 503186189 501 NGKL 504
Cdd:cd17648 444 NGKL 447
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
27-510 |
7.13e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 98.91 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 27 AAGDKTALVVIHdpagreaETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPD 106
Cdd:PRK10946 35 AASDAIAVICGE-------RQFSYRELNQASDNLACSLRR-QGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 107 LTARELGFLLDDSDAAAIVLDdtLPHGDFA------------PGLAVV------TEAALIAAIDSGPEGAFAD-TAADDP 167
Cdd:PRK10946 107 HQRSELNAYASQIEPALLIAD--RQHALFSdddflntlvaehSSLRVVlllnddGEHSLDDAINHPAEDFTATpSPADEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 168 AFLIYTSGTTANPKGVLHAH--------RSV--WGRRPMYRGWYGITAADRLMHS--GVINWTYAMGTGL--SDPLANGA 233
Cdd:PRK10946 185 AFFQLSGGSTGTPKLIPRTHndyyysvrRSVeiCGFTPQTRYLCALPAAHNYPMSspGALGVFLAGGTVVlaPDPSATLC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 234 TALLytgERHpsiwpglirafDVTIFAGVP---GLYHQIMrQASGDRLDLARLRHGLTAGDTLPDALEAEWSERTGTRLY 310
Cdd:PRK10946 265 FPLI---EKH-----------QVNVTALVPpavSLWLQAI-AEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 EGFGQTE-LSTYLSSAPDFPRKPGTVGRA-QPGRCVAILPEDGGDtsLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMF 388
Cdd:PRK10946 330 QVFGMAEgLVNYTRLDDSDERIFTTQGRPmSPDDEVWVADADGNP--LPQGEVGRLMTR--GPYTFRGYYKSPQHNASAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 389 RGEWF-TGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVARE--- 464
Cdd:PRK10946 406 DANGFyCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEplk 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 465 -----------GGADlsaelaaraeaslaaYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK10946 486 avqlrrflreqGIAE---------------FKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
344-510 |
1.70e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 96.99 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 344 VAILPED---GGDTS---LP-------PGEAGMIAVHrsDPGLMLGYWQRPDEEREMFrgewfTGGDLGCIDEDGAIAHL 410
Cdd:PRK07445 271 ATLKPDDflaGNNSSgqvLPhaqitipANQTGNITIQ--AQSLALGYYPQILDSQGIF-----ETDDLGYLDAQGYLHIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 411 GRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSaELAARAEASLAAYKRPRHY 490
Cdd:PRK07445 344 GRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE-ELKTAIKDQLSPFKQPKHW 422
|
170 180
....*....|....*....|
gi 503186189 491 VFVERLPKTPNGKLKRSDLK 510
Cdd:PRK07445 423 IPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
49-510 |
6.34e-21 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.97 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRSNrSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLDD 128
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 129 TlphgdFAPGLA-------------VVTEAALI--------AAIDSGPEGAFADTAADD-----PAFLIYTSGTTANPKG 182
Cdd:PRK06018 120 T-----FVPILEkiadklpsveryvVLTDAAHMpqttlknaVAYEEWIAEADGDFAWKTfdentAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 183 VLHAHRS--VWGRRPMYRGWYGITAADRLM------HS---GVINWTYAMGTGLSDPLANGATALLYTgerhpsiwpgLI 251
Cdd:PRK06018 195 VLYSHRSnvLHALMANNGDALGTSAADTMLpvvplfHAnswGIAFSAPSMGTKLVMPGAKLDGASVYE----------LL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 252 RAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSErTGTRLYEGFGQTELS---TYLSSAPDF 328
Cdd:PRK06018 265 DTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMSplgTLAALKPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 329 PRKPG--------TVGRAQPGRCVAILPEDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQrpdEEREMFRGE-WFTGGDLG 399
Cdd:PRK06018 344 SKLPGdarldvlqKQGYPPFGVEMKITDDAGKELPWDGKTFGRLKV--RGPAVAAAYYR---VDGEILDDDgFFDTGDVA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 400 CIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEA 479
Cdd:PRK06018 419 TIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDG 498
|
490 500 510
....*....|....*....|....*....|.
gi 503186189 480 SLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK06018 499 KIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
428-503 |
1.91e-20 |
|
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: 85.29 E-value: 1.91e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503186189 428 EVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
163-510 |
2.89e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.10 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 163 AADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVInwtYAMGtGLSDPLAN---GATALLYT 239
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPL---CHIG-GLSSALAMlmvGACHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 gERHPSIWPGLIRAFDVTIFAGVPGLYHQIMR--QASGDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQT 316
Cdd:PLN02860 246 -KFDAKAALQAIKQHNVTSMITVPAMMADLISltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 317 E---------------------LSTYLSSAPD-FPRKPGT-VGRAQPGRCVAIlpedGGDTSLPPGEagmiaVHRSDPGL 373
Cdd:PLN02860 325 EacssltfmtlhdptlespkqtLQTVNQTKSSsVHQPQGVcVGKPAPHVELKI----GLDESSRVGR-----ILTRGPHV 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 374 MLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHG 452
Cdd:PLN02860 396 MLGYWGQNSETASVLSNDgWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRL 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503186189 453 GTAITAFVVAREG-------------GADLSAELAAR--AEASLAAYKRPRHYVFVER-LPKTPNGKLKRSDLK 510
Cdd:PLN02860 476 TEMVVACVRLRDGwiwsdnekenakkNLTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
165-510 |
6.01e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.98 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMY----RGWYGITAADRLmHSGVINWTYAMGtglsdpLANGATALLYTG 240
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNV-YLAALPMFHIYG------LSLFVVGLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 ER-------HPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASG------DRLDLARLRHGLTAGDTLPDALEAewseRTGT 307
Cdd:PLN02574 271 STivvmrrfDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGvcgevlKSLKQVSCGAAPLSGKFIQDFVQT----LPHV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 308 RLYEGFGQTElSTYLSSA---PDFPRKPGTVGRAQPGRCVAILPEDGGdTSLPPGEAGMIAVHrsDPGLMLGYWQRPD-E 383
Cdd:PLN02574 347 DFIQGYGMTE-STAVGTRgfnTEKLSKYSSVGLLAPNMQAKVVDWSTG-CLLPPGNCGELWIQ--GPGVMKGYLNNPKaT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 384 EREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAR 463
Cdd:PLN02574 423 QSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRR 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 503186189 464 EGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PLN02574 503 QGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
75-450 |
1.06e-19 |
|
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: 91.75 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 75 RVLIRLRNRTAYALAFFGAIAG--GLVPIPASPDLTAreLGFLLDDSDAAAIVLDdtlphgdfaPGLAVVTEAALIaaID 152
Cdd:cd05910 6 RELDERSDRIAQGLTAYGIRRGmrAVLMVPPGPDFFA--LTFALFKAGAVPVLID---------PGMGRKNLKQCL--QE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 153 SGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLS------ 226
Cdd:cd05910 73 AEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTsvipdm 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 227 DPLANGATallytgerHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEWSE--R 304
Cdd:cd05910 153 DPTRPARA--------DPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKmlS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 305 TGTRLYEGFGQTE-----------LSTYLSSAPDfpRKPGT-VGRAQPGRCVAILPED-------GGDTSLPPGEAGMIA 365
Cdd:cd05910 225 DEAEILTPYGATEalpvssigsreLLATTTAATS--GGAGTcVGRPIPGVRVRIIEIDdepiaewDDTLELPRGEIGEIT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 366 VhrSDPGLMLGYWQRP--------DEEREMFrgeWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHP 437
Cdd:cd05910 303 V--TGPTVTPTYVNRPvatalakiDDNSEGF---WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHP 377
|
410
....*....|...
gi 503186189 438 LVAEAGVIDVPQP 450
Cdd:cd05910 378 GVRRSALVGVGKP 390
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
162-510 |
2.23e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 90.10 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 162 TAADDPAFLIYTSGTTANPKGVlhahrsvwgrrpmYRGWYGItaaDRLMHSGV----------------INWTYAMGTGL 225
Cdd:PRK08308 98 YLAEEPSLLQYSSGTTGEPKLI-------------RRSWTEI---DREIEAYNealnceqdetpivacpVTHSYGLICGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 226 SDPLANGATALLYTgERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRldlaRLRHGLTAGDTLPDALEAEWSERT 305
Cdd:PRK08308 162 LAALTRGSKPVIIT-NKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 306 gTRLYEGFGQTElstylssapdfprkpgtvgraqpGRCVAILP--EDGGDTSLPPGEAGMIAvhRSDPGlmlgywqRPDE 383
Cdd:PRK08308 237 -TYMMQQYGCSE-----------------------AGCVSICPdmKSHLDLGNPLPHVSVSA--GSDEN-------APEE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 384 -EREMFRGEWFTGgDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVA 462
Cdd:PRK08308 284 iVVKMGDKEIFTK-DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 503186189 463 REGGAdlSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:PRK08308 363 HEEID--PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
35-431 |
2.96e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.57 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 35 VVIHDPAGreaETWTYRALESAALRVAFELRsnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVP----IPASPD---- 106
Cdd:PRK06814 649 LAVEDPVN---GPLTYRKLLTGAFVLGRKLK--KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPaminFSAGIAnils 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 107 ----------LTAR------ELGFLLD--DSDAAAIVLDDtlphgdFAPGLAVVTE-AALIAAidSGPEGAFADTAADDP 167
Cdd:PRK06814 724 ackaaqvktvLTSRafiekaRLGPLIEalEFGIRIIYLED------VRAQIGLADKiKGLLAG--RFPLVYFCNRDPDDP 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 168 AFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIW 247
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRII 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 248 PGLIRAFDVTIFAGVPGLYHQIMRQASGdrLDLARLRHGLTAGDTLPDALEAEWSERTGTRLYEGFGQTELSTYLSSAPD 327
Cdd:PRK06814 876 PELIYDTNATILFGTDTFLNGYARYAHP--YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTP 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 328 FPRKPGTVGRAQPGRCVAILPEDGGDtslppgEAGMIAVhrSDPGLMLGYWqRPDEER--EMFRGEWFTGGDLGCIDEDG 405
Cdd:PRK06814 954 MHNKAGTVGRLLPGIEYRLEPVPGID------EGGRLFV--RGPNVMLGYL-RAENPGvlEPPADGWYDTGDIVTIDEEG 1024
|
410 420
....*....|....*....|....*.
gi 503186189 406 AIAHLGRASDLMNAGGYRVSPVEVEA 431
Cdd:PRK06814 1025 FITIKGRAKRFAKIAGEMISLAAVEE 1050
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
11-472 |
1.42e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.80 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 11 PPRNLNMAKHVLRAGAAAGDKTALVVihdPAGREA------ETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRT 84
Cdd:PRK09274 2 MASMANIARHLPRAAQERPDQLAVAV---PGGRGAdgklayDELSFAELDARSDAIAHGLN-AAGIGRGMRAVLMVTPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 85 A-YALAF--FGAiagGLVPIPASPDLTARELGFLLDDSDAA-------AIVLDDTLPHGdFAPGLAVVT-------EAAL 147
Cdd:PRK09274 78 EfFALTFalFKA---GAVPVLVDPGMGIKNLKQCLAEAQPDafigipkAHLARRLFGWG-KPSVRRLVTvggrllwGGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 148 IAAIDSGPEGA---FADTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHsgvinwtyamgT- 223
Cdd:PRK09274 154 LATLLRDGAAApfpMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP-----------Tf 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 224 ---GLSDPLANGATALLYTGERHP------SIWPGlIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLP 294
Cdd:PRK09274 223 plfALFGPALGMTSVIPDMDPTRPatvdpaKLFAA-IERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 295 DALEAEWSE--RTGTRLYEGFGQTE---LSTYLSSAPDFPRKPGT-------VGRAQPGRCVAI-------LPEDGGDTS 355
Cdd:PRK09274 302 IAVIERFRAmlPPDAEILTPYGATEalpISSIESREILFATRAATdngagicVGRPVDGVEVRIiaisdapIPEWDDALR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 356 LPPGEAGMIAVhrSDPGLMLGYWQRPDEERE--MFRGE---WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVE 430
Cdd:PRK09274 382 LATGEIGEIVV--AGPMVTRSYYNRPEATRLakIPDGQgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCE 459
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 503186189 431 AVLREHPLVAEAGVIDVPQPhgGTAITAFVVAREGGADLSAE 472
Cdd:PRK09274 460 RIFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSKS 499
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
132-472 |
5.71e-18 |
|
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: 86.50 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 132 HGDFAPGLAVVT------EAALIAAID-SGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHRSvwgrrpMYRGWYGIT 204
Cdd:cd17639 48 LGCWSQNIPIVTvyatlgEDALIHSLNeTECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGN------LVAGIAGLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 205 AadrlmhsGVINWTYAMGTGLSD-PLAN-------------GAT-------ALLYTGERHPSiwpGLIRAFDVTIFAGVP 263
Cdd:cd17639 122 D-------RVPELLGPDDRYLAYlPLAHifelaaenvclyrGGTigygsprTLTDKSKRGCK---GDLTEFKPTLMVGVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 264 GLYHQImRQASGDRLD-----------------LARLRHGLTAGdtlpdaleaEWSER--------TGTRLY-------- 310
Cdd:cd17639 192 AIWDTI-RKGVLAKLNpmgglkrtlfwtayqskLKALKEGPGTP---------LLDELvfkkvraaLGGRLRymlsggap 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 311 -----------------EGFGQTELS--TYLSSAPDFprKPGTVGraQPGRCVAIL----PEDGGDTSLPP--GEagmIA 365
Cdd:cd17639 262 lsadtqeflnivlcpviQGYGLTETCagGTVQDPGDL--ETGRVG--PPLPCCEIKlvdwEEGGYSTDKPPprGE---IL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 366 VhrSDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLM-NAGGYRVSPVEVEAVLREHPLVAEAG 443
Cdd:cd17639 335 I--RGPNVFKGYYKNPEKTKEAFDGDgWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNIC 412
|
410 420
....*....|....*....|....*....
gi 503186189 444 VIDVPQPhggTAITAFVVAREGGADLSAE 472
Cdd:cd17639 413 VYADPDK---SYPVAIVVPNEKHLTKLAE 438
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
166-510 |
1.30e-17 |
|
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: 85.56 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 166 DPAFLIYTSGTTANPKGVLHAHRSVWGRR---------------------PMYR--GWYGItaadrlmhsgvinWTY-AM 221
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVLHSlaaslvdgtalsekdvvlpvvPMFHvnAWCLP-------------YAAtLV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 222 GtglsdplanGATALLYTGERHPSIWPGLIRaFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALeAEW 301
Cdd:cd05915 221 G---------AKQVLPGPRLDPASLVELFDG-EGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSL-IAR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 302 SERTGTRLYEGFGQTE---LSTYLSSAPDF---PRKPGTVGRAQPG-----RCVAILpeDGGDTSLPPGEAGMIAVHRSD 370
Cdd:cd05915 290 FERMGVEVRQGYGLTEtspVVVQNFVKSHLeslSEEEKLTLKAKTGlpiplVRLRVA--DEEGRPVPKDGKALGEVQLKG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 371 PGLMLGYWQ-RPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQ 449
Cdd:cd05915 368 PWITGGYYGnEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPH 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503186189 450 PHGGTAITAFVVAREGGADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05915 448 PKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
9-507 |
2.82e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.61 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 9 ELPprnLNMAKHVLRAGAAAGDKTALVVIHDpAGREAETWTYRALESAALRVAFELRSNRSLAPRTRVLirLRNRTAYAL 88
Cdd:PRK05691 6 ELP---LTLVQALQRRAAQTPDRLALRFLAD-DPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLL--FPSGPDYVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 89 AFFGAIAGGLVPIPASPDLTAR--------------ELGFLLDDSDAAAIVLDDTLPHGDFAPG-LAVVTEAALIAAIDS 153
Cdd:PRK05691 80 AFFGCLYAGVIAVPAYPPESARrhhqerllsiiadaEPRLLLTVADLRDSLLQMEELAAANAPElLCVDTLDPALAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 154 GPegafaDTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADrlmHSGVINWT---YAMGT--GLSDP 228
Cdd:PRK05691 160 EP-----ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP---DDVIVSWLplyHDMGLigGLLQP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 LANGATALL----YTGERhPSIWPGLIRAFDVTIFAGVPGLY---HQIMRQASGDRLDLARLRHGLTAGDTL-PDALEAe 300
Cdd:PRK05691 232 IFSGVPCVLmspaYFLER-PLRWLEAISEYGGTISGGPDFAYrlcSERVSESALERLDLSRWRVAYSGSEPIrQDSLER- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 301 WSER------TGTRLYEGFGQTELSTYLS-------------SAPDFPR---KPGT------VGRAQPGRCVAILPEDGG 352
Cdd:PRK05691 310 FAEKfaacgfDPDSFFASYGLAEATLFVSggrrgqgipalelDAEALARnraEPGTgsvlmsCGRSQPGHAVLIVDPQSL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 353 DTsLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMF---RGE-WFTGGDLGCIdEDGAIAHLGRASDLMNAGGYRVSPVE 428
Cdd:PRK05691 390 EV-LGDNRVGEIWA--SGPSIAHGYWRNPEASAKTFvehDGRtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 429 VEAVLREHPLVAEAGvidvpqphggtAITAFVVAREG--GADLSAELAAR---AEASLAAYKRPRHYV---FVE------ 494
Cdd:PRK05691 466 IEKTVEREVEVVRKG-----------RVAAFAVNHQGeeGIGIAAEISRSvqkILPPQALIKSIRQAVaeaCQEapsvvl 534
|
570
....*....|....*...
gi 503186189 495 -----RLPKTPNGKLKRS 507
Cdd:PRK05691 535 llnpgALPKTSSGKLQRS 552
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
12-510 |
1.26e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.91 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNMAKhVLRAGAAAGDKTALVVIHdpaGREAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFF 91
Cdd:PRK05620 7 DVPLSLTR-ILEYGSTVHGDTTVTTWG---GAEQEQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 92 GAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD--------DTLPHGDFAPGLAVVTEAALIAAIDSGPEG------ 157
Cdd:PRK05620 83 AVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADprlaeqlgEILKECPCVRAVVFIGPSDADSAAAHMPEGikvysy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 158 -AFADTAA----------DDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGW--YGITAADRLM------HsgVINWT 218
Cdd:PRK05620 163 eALLDGRStvydwpeldeTTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLccvpiyH--VLSWG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 219 YAMGTGLSdplangATALLYTGER-HPSIWPGLIRAFDVTIFAGVPGLYHQIM---RQASGDRLDLARLRHGltaGDTLP 294
Cdd:PRK05620 241 VPLAAFMS------GTPLVFPGPDlSAPTLAKIIATAMPRVAHGVPTLWIQLMvhyLKNPPERMSLQEIYVG---GSAVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 295 DALEAEWSERTGTRLYEGFGQTELSTYLSSApdfpRKPGTVG-------RAQPGRCVAILP----EDGGDTSLPPGEAGM 363
Cdd:PRK05620 312 PILIKAWEERYGVDVVHVWGMTETSPVGTVA----RPPSGVSgearwayRVSQGRFPASLEyrivNDGQVMESTDRNEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 364 IAVHrsDPGLMLGYWQRPDEER----EMFRGE-------------WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSP 426
Cdd:PRK05620 388 IQVR--GNWVTASYYHSPTEEGggaaSTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 427 VEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREG---GADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGK 503
Cdd:PRK05620 466 AQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGK 545
|
....*..
gi 503186189 504 LKRSDLK 510
Cdd:PRK05620 546 FDKKDLR 552
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
37-507 |
8.40e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 80.05 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 37 IHDPAGREAETWTYRALESAALRVAFELrSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIP-------ASPDLTA 109
Cdd:PRK09192 39 FYDRRGQLEEALPYQTLRARAEAGARRL-LALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlplpmgfGGRESYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 110 RELGFLLDDSDAAAIVLDDTLphGDFA-------PGLAVVTEAALIAAidSGPEGAFADTAADDPAFLIYTSGTTANPKG 182
Cdd:PRK09192 118 AQLRGMLASAQPAAIITPDEL--LPWVneathgnPLLHVLSHAWFKAL--PEADVALPRPTPDDIAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 183 VLHAHRSVWGR-RPMYRGWYGITAADRlmhsgVINWT---YAMG-TG-LSDPLANGATA-LLYTGE--RHPSIWPGLIRA 253
Cdd:PRK09192 194 VIITHRALMANlRAISHDGLKVRPGDR-----CVSWLpfyHDMGlVGfLLTPVATQLSVdYLPTRDfaRRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 254 FDVTIFAGVPGLYHQIMRQASG---DRLDLARLRHGLTAGDTL-PDALEAeWSERTGTRlyeGF---------GQTELST 320
Cdd:PRK09192 269 NRGTISYSPPFGYELCARRVNSkdlAELDLSCWRVAGIGADMIrPDVLHQ-FAEAFAPA---GFddkafmpsyGLAEATL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 321 YLSSAP----------------------DFPRKPGTV------GRAQPGRCVAILPEDGgdTSLPPGEAGMIAVhrSDPG 372
Cdd:PRK09192 345 AVSFSPlgsgivveevdrdrleyqgkavAPGAETRRVrtfvncGKALPGHEIEIRNEAG--MPLPERVVGHICV--RGPS 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 373 LMLGYWQRPDEEREMFRGEWFTGGDLGCIdEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLV--AEAGVIDVPQp 450
Cdd:PRK09192 421 LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQ- 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503186189 451 HGGTAITAFVVAREGGADLSAELaaraEASLAAYKRPRHYVFV-------ERLPKTPNGKLKRS 507
Cdd:PRK09192 499 ENGEKIVLLVQCRISDEERRGQL----IHALAALVRSEFGVEAavelvppHSLPRTSSGKLSRA 558
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
43-465 |
1.52e-15 |
|
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: 79.26 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 43 REAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAA 122
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 123 AIV--------LDDTLP-------------HGDFAPGLAVVTEAALIAAIDSGPEGAFADTAADDPAFLIYTSGTTANPK 181
Cdd:cd05938 81 VLVvapelqeaVEEVLPalradgvsvwylsHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 182 GVLHAHRSVWGRRPMYRgWYGITAADR------LMHSGvinwtyAMGTGLSDPLANGATALLYTGERHPSIWPGlIRAFD 255
Cdd:cd05938 161 AARISHLRVLQCSGFLS-LCGVTADDViyitlpLYHSS------GFLLGIGGCIELGATCVLKPKFSASQFWDD-CRKHN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 256 VTIFagvpgLY-HQIMR------QASGDRLDLARLrhglTAGDTL-PDALEaEWSERTG-TRLYEGFGQTELSTylsSAP 326
Cdd:cd05938 233 VTVI-----QYiGELLRylcnqpQSPNDRDHKVRL----AIGNGLrADVWR-EFLRRFGpIRIREFYGSTEGNI---GFF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 327 DFPRKPGTVGRA--------------------QP-----GRCVAIlpedggdtslPPGEAGMIA--VHRSDPglMLGYwq 379
Cdd:cd05938 300 NYTGKIGAVGRVsylykllfpfelikfdvekeEPvrdaqGFCIPV----------AKGEPGLLVakITQQSP--FLGY-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 380 RPDEE-------REMFR-GE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQP 450
Cdd:cd05938 366 AGDKEqtekkllRDVFKkGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVP 445
|
490
....*....|....*.
gi 503186189 451 -HGGTAITAFVVAREG 465
Cdd:cd05938 446 gHEGRIGMAAVKLKPG 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-509 |
2.40e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.44 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNrtayaLAFFGAIAG----GLVPIPASPDLTARELGFLLDDSD- 120
Cdd:PRK05691 3744 QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERG-----LDLLGMIVGsfkaGAGYLPLDPGLPAQRLQRIIELSRt 3818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 121 ----------AAAIVLDDTLPhGDFAPGLAVVTEAALIAAIDSGPeGAFadTAADDPAFLIYTSGTTANPKGVLHAHRSV 190
Cdd:PRK05691 3819 pvlvcsaacrEQARALLDELG-CANRPRLLVWEEVQAGEVASHNP-GIY--SGPDNLAYVIYTSGSTGLPKGVMVEQRGM 3894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 191 WGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALL-YTGERHPSIWPGLIRAFDVTIFAGVPGLyhqI 269
Cdd:PRK05691 3895 LNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVpNAIAHDPQGLLAHVQAQGITVLESVPSL---I 3971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 270 MRQASGDRLDLARLRHGLTAGDTLPDALEAEWSER-TGTRLYEGFGQTELSTYLSSAP-DFPRKPGT---VGRAQPGRCV 344
Cdd:PRK05691 3972 QGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRL 4051
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 345 AILpeDGGDTSLPPGEAGMIAVhrSDPGLMLGYWQRPDEEREMFRGEWFTG--------GDLGCIDEDGAIAHLGRASDL 416
Cdd:PRK05691 4052 YLL--DEALELVPLGAVGELCV--AGTGVGRGYVGDPLRTALAFVPHPFGApgerlyrtGDLARRRSDGVLEYVGRIDHQ 4127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 417 MNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHgGTAITAFVVAREGGADLSA---ELAARAEASLAAYKRPRHYVFV 493
Cdd:PRK05691 4128 VKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYLVPHQTVLAQGAlleRIKQRLRAELPDYMVPLHWLWL 4206
|
490
....*....|....*.
gi 503186189 494 ERLPKTPNGKLKRSDL 509
Cdd:PRK05691 4207 DRLPLNANGKLDRKAL 4222
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
120-507 |
2.93e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 78.50 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 120 DAAAIVLDDtlPHGDFAP-----GLAVVTEAALIAAIDSGPEgafaDTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRR 194
Cdd:PRK07768 108 GAKAVVVGE--PFLAAAPvleekGIRVLTVADLLAADPIDPV----ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 195 pmyrgwYGITAADRL--MHSGVINW---TYAMGT--GLSDPLANGATALLYTGE---RHPSIWPGLIRAFDVTIFAGvPG 264
Cdd:PRK07768 182 ------EAMFVAAEFdvETDVMVSWlplFHDMGMvgFLTVPMYFGAELVKVTPMdflRDPLLWAELISKYRGTMTAA-PN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 265 LYHQIM-----RQASGDRLDLARLRHGLTAGDTL-PDALE--AEWSERTGTR---LYEGFGQTElSTYLSSAPDFPRK-- 331
Cdd:PRK07768 255 FAYALLarrlrRQAKPGAFDLSSLRFALNGAEPIdPADVEdlLDAGARFGLRpeaILPAYGMAE-ATLAVSFSPCGAGlv 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 332 ----------------PGTVGRAQ---------PGRCVAILPEDGgdTSLPPGEAGMIAVhRSDPgLMLGYWQRPDEERE 386
Cdd:PRK07768 334 vdevdadllaalrravPATKGNTRrlatlgpplPGLEVRVVDEDG--QVLPPRGVGVIEL-RGES-VTPGYLTMDGFIPA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 387 MFRGEWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGG 466
Cdd:PRK07768 410 QDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNA 489
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 503186189 467 ADLSAELAARAEASLAAYK-----RPRHYVFVE--RLPKTPNGKLKRS 507
Cdd:PRK07768 490 FEDPAEVRRIRHQVAHEVVaevgvRPRNVVVLGpgSIPKTPSGKLRRA 537
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
15-504 |
1.06e-14 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 76.76 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 15 LNMAKHVLRAgaAAGDKTALVVIHDpaGREAETWTYRALESAALRVAFELRSNrSLAPRTRVLIRLRNrTAYALAFFGAI 94
Cdd:PRK03584 86 LNYAENLLRH--RRDDRPAIIFRGE--DGPRRELSWAELRRQVAALAAALRAL-GVGPGDRVAAYLPN-IPETVVAMLAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 95 AG-GLVPIPASPDLTAR-------------------------------ELGFLLD--DSDAAAIVLDDTLPHGDFAPGLA 140
Cdd:PRK03584 160 ASlGAIWSSCSPDFGVQgvldrfgqiepkvliavdgyryggkafdrraKVAELRAalPSLEHVVVVPYLGPAAAAAALPG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 141 VVTEAALIAAIdSGPEGAFADTAADDPAFLIYTSGTTANPKGVLHAHrsvwgrrpmyrgwyG---------------ITA 205
Cdd:PRK03584 240 ALLWEDFLAPA-EAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH--------------GgillehlkelglhcdLGP 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADRLMH---SGVINWTYAMGTglsdpLANGATALLYTGerHPSiWPGLIRAFD------VTIFAGVPGlYHQIMRQAS-- 274
Cdd:PRK03584 305 GDRFFWyttCGWMMWNWLVSG-----LLVGATLVLYDG--SPF-YPDPNVLWDlaaeegVTVFGTSAK-YLDACEKAGlv 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 275 -GDRLDLARLRHGLTAGDTLPDalEA-EWsertgtrLYEGFGQTELSTYLSSAPDF--------PRKPGTVGRAQpGRC- 343
Cdd:PRK03584 376 pGETHDLSALRTIGSTGSPLPP--EGfDW-------VYEHVKADVWLASISGGTDIcscfvggnPLLPVYRGEIQ-CRGl 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 344 ---VAILPEDGgdTSLPpGEAGMIAVHRSDPGLMLGYWQRPDEER------EMFRGEWfTGGDLGCIDEDGAIAHLGRAS 414
Cdd:PRK03584 446 gmaVEAWDEDG--RPVV-GEVGELVCTKPFPSMPLGFWNDPDGSRyrdayfDTFPGVW-RHGDWIEITEHGGVVIYGRSD 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 415 DLMNAGG--------YRVspveVEAVlrehPLVAEAGVIDVPQPHGGTAITAFVVAREgGADLSAELAARAEASLAAYKR 486
Cdd:PRK03584 522 ATLNRGGvrigtaeiYRQ----VEAL----PEVLDSLVIGQEWPDGDVRMPLFVVLAE-GVTLDDALRARIRTTIRTNLS 592
|
570 580
....*....|....*....|..
gi 503186189 487 PRHY----VFVERLPKTPNGKL 504
Cdd:PRK03584 593 PRHVpdkiIAVPDIPRTLSGKK 614
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
30-435 |
1.44e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 76.13 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 30 DKTALVVI---HDPAGReAETWTYRALESAALRVAFELRSNRSlaPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPD 106
Cdd:PRK05850 16 DDAAFTFIdyeQDPAGV-AETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 107 LTA---RELGFLLDDSDAAAI-----VLDDTLPHGDFAPGLAvvteAALIAAID-----SGPEGAFADTAADDPAFLIYT 173
Cdd:PRK05850 93 QGGahdERVSAVLRDTSPSVVlttsaVVDDVTEYVAPQPGQS----APPVIEVDlldldSPRGSDARPRDLPSTAYLQYT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 174 SGTTANPKGVLHAHRSVWGR-RPMYRGWYGITAADRLMHSGVINWT---YAMG--TGLSDPLANGATALLYTGE---RHP 244
Cdd:PRK05850 169 SGSTRTPAGVMVSHRNVIANfEQLMSDYFGDTGGVPPPDTTVVSWLpfyHDMGlvLGVCAPILGGCPAVLTSPVaflQRP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 245 SIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDR---LDLARLRHGLTAGDTLPDALEAEWSERTG------TRLYEGFGQ 315
Cdd:PRK05850 249 ARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDmagLDLGGVLGIISGSERVHPATLKRFADRFApfnlreTAIRPSYGL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 316 TELSTYLSSAPdfPRKPGTVGRAQP-----GRcvAILPEDGGDTSL----------------------PPGEAGMIAVHR 368
Cdd:PRK05850 329 AEATVYVATRE--PGQPPESVRFDYeklsaGH--AKRCETGGGTPLvsygsprsptvrivdpdtciecPAGTVGEIWVHG 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 369 SDpgLMLGYWQRPDEEREMF------------RGEWFTGGDLGCIDeDGAIAHLGRASDLMNAGGYRVSPVEVEAVLRE 435
Cdd:PRK05850 405 DN--VAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQE 480
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-440 |
2.06e-14 |
|
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: 75.71 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRS-NRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVLD 127
Cdd:cd05927 7 SYKEVAERADNIGSALRSlGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 dtlphgdfaPGLAVVTeaaLIAAIDSGPEGAFADT--AADDPAFLIYTSGTTANPKGVLHAHRSVWGrrpmyrgwyGITA 205
Cdd:cd05927 87 ---------AGVKVYS---LEEFEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVS---------NVAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 206 ADRLMHSgvinwTYAMGTGLSD----PLA-----NGATALLYTGERhPSIWPGLIRAF--DV-----TIFAGVPGL---- 265
Cdd:cd05927 146 VFKILEI-----LNKINPTDVYisylPLAhiferVVEALFLYHGAK-IGFYSGDIRLLldDIkalkpTVFPGVPRVlnri 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 266 YHQIMRQASGD------------RLDLARLRHGLTAGDTLPDAL-------------------EAEWSERT--------G 306
Cdd:cd05927 220 YDKIFNKVQAKgplkrklfnfalNYKLAELRSGVVRASPFWDKLvfnkikqalggnvrlmltgSAPLSPEVleflrvalG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 307 TRLYEGFGQTElstylSSAPDFPRKP-----GTVGraQPGRCVAI----LPEDGGDTSLPPGEaGMIAVhRSdPGLMLGY 377
Cdd:cd05927 300 CPVLEGYGQTE-----CTAGATLTLPgdtsvGHVG--GPLPCAEVklvdVPEMNYDAKDPNPR-GEVCI-RG-PNVFSGY 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503186189 378 WQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDL--MNAGGYrVSPVEVEAVLREHPLVA 440
Cdd:cd05927 370 YKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIfkLSQGEY-VAPEKIENIYARSPFVA 434
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
43-510 |
4.00e-14 |
|
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: 74.39 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 43 REAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAA 122
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 123 AIVLDDtlphgdfapglavvteaaliaaidsgpegafadtaaDDPAFLIYTSGTTANPKGVLHAHRSVW----------- 191
Cdd:cd05937 81 FVIVDP------------------------------------DDPAILIYTSGTTGLPKAAAISWRRTLvtsnllshdln 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 192 ---GRR-----PMYRGWYGITAADRLMHSG---VINWTYAMGTGLSDPLANGATALLYTGErhpsiwpgLIRafdvTIFA 260
Cdd:cd05937 125 lknGDRtytcmPLYHGTAAFLGACNCLMSGgtlALSRKFSASQFWKDVRDSGATIIQYVGE--------LCR----YLLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 261 GVPGLYHQI--MRQASGDrldlarlrhGLTagdtlPDALEAeWSERTGT-RLYEGFGQTE--LSTYLSSAPDFprKPGTV 335
Cdd:cd05937 193 TPPSPYDRDhkVRVAWGN---------GLR-----PDIWER-FRERFNVpEIGEFYAATEgvFALTNHNVGDF--GAGAI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 336 GRAQPGR---------CVAILPED---------GGDTSLPPGEAG-MIAVHRSDP-GLMLGYWQRPDEE-----REMFR- 389
Cdd:cd05937 256 GHHGLIRrwkfenqvvLVKMDPETddpirdpktGFCVRAPVGEPGeMLGRVPFKNrEAFQGYLHNEDATesklvRDVFRk 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 390 GE-WFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQP-HGGTAITAFVVAREGGA 467
Cdd:cd05937 336 GDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSA 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 503186189 468 DLS----AELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDLK 510
Cdd:cd05937 416 VPTeftkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
167-507 |
4.29e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 74.78 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 167 PAFLIYTSGTTANPKGVLHAHRSvwGRRPMYRGWYGITAAD---RLMHSGVINWTYAMGtGLSDPLANGATALLYTG--- 240
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDiptVVFSHSSIGWVSFHG-FLYGSLSLGNTFVMFEGgii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 -ERHPS--IWpGLIRAFDVTIFAGVPG-LYHQIMRQASGDRL----DLARLRHGLTAGDTLPDALEAEWSERTGTRLYEG 312
Cdd:PTZ00237 333 kNKHIEddLW-NTIEKHKVTHTLTLPKtIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 313 FGQTELS-TYLSSApDFPRKP-GTVGRAQPGRCVAILPEDGGDtsLPPGEAGMIAVHRS-DPGLMLGYWQRPDEEREMFR 389
Cdd:PTZ00237 412 YGQTEIGiTYLYCY-GHINIPyNATGVPSIFIKPSILSEDGKE--LNVNEIGEVAFKLPmPPSFATTFYKNDEKFKQLFS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 390 G--EWFTGGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGA 467
Cdd:PTZ00237 489 KfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS 568
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 503186189 468 -------DLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRS 507
Cdd:PTZ00237 569 nqsidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
164-453 |
1.17e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 73.31 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 164 ADDPAFLIYTSGTTANPKGVLHAHRSVWgrRPMYRGWygitAADRLMHSGVINWTYAMG-----TGLSDPLANGATALLY 238
Cdd:PLN03051 118 VESVTNILFSSGTTGEPKAIPWTHLSPL--RCASDGW----AHMDIQPGDVVCWPTNLGwmmgpWLLYSAFLNGATLALY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 239 TGERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGD--RLDLARLRHGLTAGDTlPDALEAEW--SERTGTR-LYEGF 313
Cdd:PLN03051 192 GGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFAmeGLDWSKLRVFASTGEA-SAVDDVLWlsSVRGYYKpVIEYC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTEL-STYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGGDTSLPPGEAGMIAVHRsdpgLMLGYWQR---PDEEREMFR 389
Cdd:PLN03051 271 GGTELaSGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVGEVALAP----PMLGASDRllnADHDKVYYK 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503186189 390 GEWFTG---------GDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVE-AVLREHPLVAEAGVIDVPQPHGG 453
Cdd:PLN03051 347 GMPMYGskgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVAPPDGG 420
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
161-436 |
1.88e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 72.54 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 161 DTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMHSGVINWTYAMGTGLSDPLANGATALLYTG 240
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 ERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPDALEAEwSERT--GTRLYEGFGQTEL 318
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQE-ALKTfpHIQLRQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 319 STYLS-SAPDFPRKPGTVGRAQPGRCVAILPEDGgDTSLPPGEAGMIAVHRSDpgLMLGYWQRpDEEREMFR--GE-WFT 394
Cdd:PRK06334 338 SPVITiNTVNSPKHESCVGMPIRGMDVLIVSEET-KVPVSSGETGLVLTRGTS--LFSGYLGE-DFGQGFVElgGEtWYV 413
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503186189 395 GGDLGCIDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREH 436
Cdd:PRK06334 414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
392-509 |
3.14e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.84 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 392 WFTGGDLGCIDeDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLSA 471
Cdd:PRK07824 235 WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE 313
|
90 100 110
....*....|....*....|....*....|....*...
gi 503186189 472 ELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKRSDL 509
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
76-448 |
4.60e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 71.06 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 76 VLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIVlddTLPHGDFAPGLAVVTEAALIAAIDsgp 155
Cdd:PRK09029 56 VALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFAL---VLEGENTFSALTSLHLQLVEGAHA--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 156 egafADTAADDPAFLIYTSGTTANPKGVLHAHR----SVwgrrpmyRG---WYGITAADR------LMH-SGV-INWTYa 220
Cdd:PRK09029 130 ----VAWQPQRLATMTLTSGSTGLPKAAVHTAQahlaSA-------EGvlsLMPFTAQDSwllslpLFHvSGQgIVWRW- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 221 mgtglsdpLANGATalLYTGERHPsiwpgLIRAFDVTIFAG-VPGlyhQIMRQASGDRLDLArLRHGLTAGDTLPDALeA 299
Cdd:PRK09029 198 --------LYAGAT--LVVRDKQP-----LEQALAGCTHASlVPT---QLWRLLDNRSEPLS-LKAVLLGGAAIPVEL-T 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 300 EWSERTGTRLYEGFGQTEL-STYLSSAPDfpRKPGtVGRAQPGRCVAIlpedggdtslppgEAGMIAVhRSDpGLMLGYW 378
Cdd:PRK09029 258 EQAEQQGIRCWCGYGLTEMaSTVCAKRAD--GLAG-VGSPLPGREVKL-------------VDGEIWL-RGA-SLALGYW 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503186189 379 Q----RP--DEEremfrGeWFTGGDLGCIDeDGAIAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVP 448
Cdd:PRK09029 320 RqgqlVPlvNDE-----G-WFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
89-506 |
3.53e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.38 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 89 AFFGAI-AG-GLVPIPASpdlTARE-LGFLLDDSDAAAIVLDDTLPHGDfaPGLAVVTEAALIAAIDSGPEGAFAD-TAA 164
Cdd:PRK04813 68 TFLGAVkAGhAYIPVDVS---SPAErIEMIIEVAKPSLIIATEELPLEI--LGIPVITLDELKDIFATGNPYDFDHaVKG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVlhahrsvwgrrpmyrgwyGITAADRLMHSGVINWTYAMGTG---LSDP------------- 228
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGV------------------QISHDNLVSFTNWMLEDFALPEGpqfLNQApysfdlsvmdlyp 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 229 -LANGAT------------ALLYTgerhpsiwpgLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDTLPD 295
Cdd:PRK04813 205 tLASGGTlvalpkdmtanfKQLFE----------TLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPH 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 296 ALEAEWSER-TGTRLYEGFGQTELSTYLSSAP-------DFPRKPgtVGRAQPGRCVAILPEDGgdTSLPPGEAGMIAVh 367
Cdd:PRK04813 275 KTAKKLLERfPSATIYNTYGPTEATVAVTSIEitdemldQYKRLP--IGYAKPDSPLLIIDEEG--TKLPDGEQGEIVI- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 368 rSDPGLMLGYWQRPDEEREMF---RGEW-FTGGDLGCIDeDGAIAHLGRAsDL---MNagGYRVSPVEVEAVLREHPLVA 440
Cdd:PRK04813 350 -SGPSVSKGYLNNPEKTAEAFftfDGQPaYHTGDAGYLE-DGLLFYQGRI-DFqikLN--GYRIELEEIEQNLRQSSYVE 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 441 EAGVIDVPQPHGGTAITAFVVAREGG----ADLSAELAARAEASLAAYKRPRHYVFVERLPKTPNGKLKR 506
Cdd:PRK04813 425 SAVVVPYNKDHKVQYLIAYVVPKEEDfereFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
41-393 |
8.26e-11 |
|
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: 64.38 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 41 AGREAETWTYRALESAALRVAFELRSnRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASP-------DLTarELG 113
Cdd:cd05921 19 GNGGWRRVTYAEALRQVRAIAQGLLD-LGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslmsqDLA--KLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 114 FLLDDSDAAAIVLDDTLPHGD-----FAPGLAVVTEAALIAAIDS--------GPEG-----AFADTAADDPAFLIYTSG 175
Cdd:cd05921 96 HLFELLKPGLVFAQDAAPFARalaaiFPLGTPLVVSRNAVAGRGAisfaelaaTPPTaavdaAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 176 TTANPKGVLHAHRSVWGRRPMYRGWYGITAADRLMhsgVINW-----TYAMGTGLSDPLANGATalLYTGERHPSiwPGL 250
Cdd:cd05921 176 STGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPV---LVDWlpwnhTFGGNHNFNLVLYNGGT--LYIDDGKPM--PGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 251 I-------RAFDVTIFAGVPGLYHQIMRQASGD----RLDLARLRHGLTAGDTLP----DALEAEWSERTGTR--LYEGF 313
Cdd:cd05921 249 FeetlrnlREISPTVYFNVPAGWEMLVAALEKDealrRRFFKRLKLMFYAGAGLSqdvwDRLQALAVATVGERipMMAGL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 314 GQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEDggdtslppgeaGMIAVHRSDPGLMLGYWQRPDEEREMFRGEWF 393
Cdd:cd05921 329 GATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-----------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF 397
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
9-469 |
1.08e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 63.99 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 9 ELPPrNLNMAKHVLRAGAAAGDKTA---LVVIHDPAGREAE-TWTyralesaALRV---AFELRSNRSLAPRTRVLIRLR 81
Cdd:PRK12476 29 ALPP-GTTLISLIERNIANVGDTVAyryLDHSHSAAGCAVElTWT-------QLGVrlrAVGARLQQVAGPGDRVAILAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 82 NRTAYALAFFGAIAGGLVPIPA-SPDLT--ARELGFLLDDSDAAaIVLDDTL---PHGDFAPGLAVVTEAALIAaIDSGP 155
Cdd:PRK12476 101 QGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPT-VVLTTTAaaeAVEGFLRNLPRLRRPRVIA-IDAIP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 156 EGAFADTAA-----DDPAFLIYTSGTTANPKGVLHAHRSVWGRrpMYRGWYGITAADRLMHSgvINWT---YAMGtgLS- 226
Cdd:PRK12476 179 DSAGESFVPveldtDDVSHLQYTSGSTRPPVGVEITHRAVGTN--LVQMILSIDLLDRNTHG--VSWLplyHDMG--LSm 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 227 ---DPLANGATALLYTGE--RHPSIWpglIRAF-----DVTIFAGVPGLYHQIMRQ----ASGDRLDLAR--LRHG---- 286
Cdd:PRK12476 253 igfPAVYGGHSTLMSPTAfvRRPQRW---IKALsegsrTGRVVTAAPNFAYEWAAQrglpAEGDDIDLSNvvLIIGsepv 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 287 -LTAGDTLPDALEAEWSERTGTRlyEGFGQTELSTYLSS-APD-------FPRKPGTVGRA-----------------QP 340
Cdd:PRK12476 330 sIDAVTTFNKAFAPYGLPRTAFK--PSYGIAEATLFVATiAPDaepsvvyLDREQLGAGRAvrvaadapnavahvscgQV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 341 GRCV-AILPEDGGDTSLPPGEAGMIAVHRSDPGLmlGYWQRPDEEREMFR-------------------GEWFTGGDLGc 400
Cdd:PRK12476 408 ARSQwAVIVDPDTGAELPDGEVGEIWLHGDNIGR--GYWGRPEETERTFGaklqsrlaegshadgaaddGTWLRTGDLG- 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503186189 401 IDEDGAIAHLGRASDLMNAGGYRVSPVEVEAVlrehplVAEAGvidvPQPHGGTaITAFVVAREGGADL 469
Cdd:PRK12476 485 VYLDGELYITGRIADLIVIDGRNHYPQDIEAT------VAEAS----PMVRRGY-VTAFTVPAEDNERL 542
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-467 |
1.96e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.46 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSvwgrrpMYRGWYGItaADRL----------------------MHSGVINWTYAMG 222
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGS------LTAGILAL--EDRLndligppeedetycsylplahiMEFGVTNIFLARG 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 223 T--------GLSDPLANGATALLytgERHPSIWPGLIRAFDvTIFAGV------PG-LYHQIMRQASGDRL--------- 278
Cdd:PTZ00216 336 AligfgsprTLTDTFARPHGDLT---EFRPVFLIGVPRIFD-TIKKAVeaklppVGsLKRRVFDHAYQSRLralkegkdt 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 --------DLAR------LRHGLTAGDTLPDALEaEWSERTGTRLYEGFGQTElsTYLSSAPDFP--RKPGTVGRAQPGR 342
Cdd:PTZ00216 412 pywnekvfSAPRavlggrVRAMLSGGGPLSAATQ-EFVNVVFGMVIQGWGLTE--TVCCGGIQRTgdLEPNAVGQLLKGV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 343 CVAILPEDG---GDTSLPPGEagmiaVHRSDPGLMLGYWQRPDEEREMF-RGEWFTGGDLGCIDEDGAIAHLGRASDLM- 417
Cdd:PTZ00216 489 EMKLLDTEEykhTDTPEPRGE-----ILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAk 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 503186189 418 NAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHgGTAITAFVVAREGGA 467
Cdd:PTZ00216 564 NCLGEYIALEALEALYGQNELVVPNGVCVLVHPA-RSYICALVLTDEAKA 612
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-510 |
7.57e-09 |
|
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: 57.82 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 46 ETWTYRALESAALRVAfELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLLDDSDAAAIV 125
Cdd:cd05939 2 RHWTFRELNEYSNKVA-NFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 126 LDdtlphgdfapglavvTEAALIAAIDSGPEGAfADTAADDPAFLIYTSGTTANPKGVLHAH-RSVWGRRPMYRGwYGIT 204
Cdd:cd05939 81 FN---------------LLDPLLTQSSTEPPSQ-DDVNFRDKLFYIYTSGTTGLPKAAVIVHsRYYRIAAGAYYA-FGMR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 205 AADRLMHSGVINWTYAMGTGLSDPLANGATALLYTGERHPSIWPGLIRaFDVTIFAGVPGLYHQIMRQASGDRLDLARLR 284
Cdd:cd05939 144 PEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVK-YNCTIVQYIGEICRYLLAQPPSEEEQKHNVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 285 hgLTAGDTLPDALEAEWSERTG-TRLYEGFGQTELStylSSAPDFPRKPGTVG---------------RAQPGRCVAILP 348
Cdd:cd05939 223 --LAVGNGLRPQIWEQFVRRFGiPQIGEFYGATEGN---SSLVNIDNHVGACGfnsrilpsvypirliKVDEDTGELIRD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 349 EDGGDTSLPPGEAGMIA--VHRSDPGL-MLGYWQRPDEEREMFRG------EWFTGGDLGCIDEDGAIAHLGRASDLMNA 419
Cdd:cd05939 298 SDGLCIPCQPGEPGLLVgkIIQNDPLRrFDGYVNEGATNKKIARDvfkkgdSAFLSGDVLVMDELGYLYFKDRTGDTFRW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 420 GGYRVSPVEVEAVLreHPLV--AEAGVIDVPQPHG-GTAITAFVVAREGGADLsAELAARAEASLAAYKRPRHYVFVERL 496
Cdd:cd05939 378 KGENVSTTEVEGIL--SNVLglEDVVVYGVEVPGVeGRAGMAAIVDPERKVDL-DRFSAVLAKSLPPYARPQFIRLLPEV 454
|
490
....*....|....
gi 503186189 497 PKTPNGKLKRSDLK 510
Cdd:cd05939 455 DKTGTFKLQKTDLQ 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
9-393 |
2.71e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.59 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 9 ELPPRNLnmaKHVLRAGAAAGDKTALVVIHDPAGREAETWTYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYAL 88
Cdd:PRK12582 45 GPYPRSI---PHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALL-DLGLDPGRPVMILSGNSIEHAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 89 AFFGAIAGGLVPIPASPDLTARELGFL----LDDSDAAAIVLDDTLPHgdFAPGLAVVTEAAL-IAAIDSGPEG----AF 159
Cdd:PRK12582 121 MTLAAMQAGVPAAPVSPAYSLMSHDHAklkhLFDLVKPRVVFAQSGAP--FARALAALDLLDVtVVHVTGPGEGiasiAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 160 ADTAADDP----------------AFLIYTSGTTANPKGVLHAHRSVWGRRPMYRgwyGITAADR-LMHSGVINW----- 217
Cdd:PRK12582 199 ADLAATPPtaavaaaiaaitpdtvAKYLFTSGSTGMPKAVINTQRMMCANIAMQE---QLRPREPdPPPPVSLDWmpwnh 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 218 TYAMGTGLSDPLANGATalLYTGERHPSiwPGLI-------RAFDVTIFAGVPGLYHQIMRQASGD----RLDLARLRHG 286
Cdd:PRK12582 276 TMGGNANFNGLLWGGGT--LYIDDGKPL--PGMFeetirnlREISPTVYGNVPAGYAMLAEAMEKDdalrRSFFKNLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 287 LTAGDTLPDAL----EAEWSERTGTR--LYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPGRCVAILPEdgGDTslppge 360
Cdd:PRK12582 352 AYGGATLSDDLyermQALAVRTTGHRipFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV--GDK------ 423
|
410 420 430
....*....|....*....|....*....|...
gi 503186189 361 agmIAVHRSDPGLMLGYWQRPDEEREMFRGEWF 393
Cdd:PRK12582 424 ---YEVRVKGPNVTPGYHKDPELTAAAFDEEGF 453
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
170-511 |
3.07e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 56.24 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 170 LIYTSGTTANPKGVLHAHRSvwgrrPMYrgwygiTAADRLMHSGV---------INWTYAMG-TGLSDPLANGATALLYT 239
Cdd:PLN03052 361 ILFSSGTTGEPKAIPWTQLT-----PLR------AAADAWAHLDIrkgdivcwpTNLGWMMGpWLVYASLLNGATLALYN 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 240 GERHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRLDLARLRHGLTAGDT--LPDALeaeW-SERTGTR-LYEGFGQ 315
Cdd:PLN03052 430 GSPLGRGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEAssVDDYL---WlMSRAGYKpIIEYCGG 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 316 TEL-STYLSSAPDFPRKPGTVGRAQPGRCVAILPEDGgdTSLPPGEAGM--IAVHrsdPgLMLGYWQR---PDEEREMFR 389
Cdd:PLN03052 507 TELgGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSG--NPYPDDAPCTgeLALF---P-LMFGASSTllnADHYKVYFK 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 390 G-EWFTGGDL---GCIDEDGA----IAHlGRASDLMNAGGYRVSPVEVEAVL-REHPLVAEAGVIDVPQPHGGTA--ITA 458
Cdd:PLN03052 581 GmPVFNGKILrrhGDIFERTSggyyRAH-GRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEqlVIA 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 503186189 459 FVVAREGGADLSAELAARAEASLAAYK-----RPRHYVFVERLPKTPNGKLKRSDLKI 511
Cdd:PLN03052 660 AVLKDPPGSNPDLNELKKIFNSAIQKKlnplfKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
49-509 |
3.09e-08 |
|
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: 55.96 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 49 TYRALESAALRVAFELRsNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDltarelgfllDDSDAAAIVLD- 127
Cdd:cd05908 17 SYRHLREEALGYLGALQ-ELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIG----------SNEEHKLKLNKv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 128 -DTLPHgdfaPGLaVVTEAALiaaidsgpegafaDTAADDPAFLIYTSGTTANPKGVLHAHRSVWGRRPMYRGWYGITAA 206
Cdd:cd05908 86 wNTLKN----PYL-ITEEEVL-------------CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 207 DRLMhsGVINWTYAMGTG---LSDPLANGATALLYTGE--RHPSIWPGLIRAFDVTIFAGVPGLYHQIMRQASGDRL--- 278
Cdd:cd05908 148 DRIL--SWMPLTHDMGLIafhLAPLIAGMNQYLMPTRLfiRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAndw 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 279 DLARLRHGLTAGDTLPDALEAEWSERTG------TRLYEGFGQTELSTYLSSAP-DFPRKPGTVGR--AQPG-------- 341
Cdd:cd05908 226 DLSSIRMILNGAEPIDYELCHEFLDHMSkyglkrNAILPVYGLAEASVGASLPKaQSPFKTITLGRrhVTHGepepevdk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 ---RCVAILPE------------DGGDTSLPPGEAGMIAVHRSDpgLMLGYWQRPDEEREMFRGE-WFTGGDLGCIdEDG 405
Cdd:cd05908 306 kdsECLTFVEVgkpidetdiricDEDNKILPDGYIGHIQIRGKN--VTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 406 AIAHLGRASDLMNAGGYRVSPVEVEAVLRE-HPL----VAEAGVIDvpQPHGGTAITAFVVAREGGADLSAELAARAEAS 480
Cdd:cd05908 383 RLVITGREKDIIFVNGQNVYPHDIERIAEElEGVelgrVVACGVNN--SNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL 460
|
490 500 510
....*....|....*....|....*....|
gi 503186189 481 LAAYKRPRHYVF-VERLPKTPNGKLKRSDL 509
Cdd:cd05908 461 NKRGGWQINEVLpIRRIPKTTSGKVKRYEL 490
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
12-190 |
3.55e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.89 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 12 PRNLNMAKHVLRAGAAAGDKTALVVIHDPAGREAE----TWtyrALESAALRvAFELRSNRSLAPRTRVLIRLRNRTAYA 87
Cdd:PRK07769 18 PPNTNLVRHVERWAKVRGDKLAYRFLDFSTERDGVardlTW---SQFGARNR-AVGARLQQVTKPGDRVAILAPQNLDYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 88 LAFFGAIAGG--LVPI--PASPDLTAReLGFLLDDSDAAAIVLDDTLPHG--DFAPGLAVvTEAALIAAIDSGPEGAFA- 160
Cdd:PRK07769 94 IAFFGALYAGriAVPLfdPAEPGHVGR-LHAVLDDCTPSAILTTTDSAEGvrKFFRARPA-KERPRVIAVDAVPDEVGAt 171
|
170 180 190
....*....|....*....|....*....|....
gi 503186189 161 ----DTAADDPAFLIYTSGTTANPKGVLHAHRSV 190
Cdd:PRK07769 172 wvppEANEDTIAYLQYTSGSTRIPAGVQITHLNL 205
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-444 |
9.20e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 54.72 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 104 SPDLTARELGFLLDDSDAAAIVL----DDTLPHGDFAPGLAVVTEAALIAAIDSGPEgAFADTAADDPAFLIYTSGTTAN 179
Cdd:PLN02736 157 VPQTLNTLLSCLSEIPSVRLIVVvggaDEPLPSLPSGTGVEIVTYSKLLAQGRSSPQ-PFRPPKPEDVATICYTSGTTGT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 180 PKGVLHAHR----SVWGrrpmyrgwygiTAADRLMHSGVINWTYAmgtglsdPLAN-------------GATALLYTGER 242
Cdd:PLN02736 236 PKGVVLTHGnliaNVAG-----------SSLSTKFYPSDVHISYL-------PLAHiyervnqivmlhyGVAVGFYQGDN 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 243 HpsiwpGL---IRAFDVTIFAGVPGLYHQIMR------QASG----------------------------DRLDL----- 280
Cdd:PLN02736 298 L-----KLmddLAALRPTIFCSVPRLYNRIYDgitnavKESGglkerlfnaaynakkqalengknpspmwDRLVFnkika 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 281 ---ARLRHGLTAGDTL-PDALEAewsERT--GTRLYEGFGQTELSTYLSSAPDFPRKPGTVGRAQPgrCVAI----LPED 350
Cdd:PLN02736 373 klgGRVRFMSSGASPLsPDVMEF---LRIcfGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNP--ACEVklvdVPEM 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 351 GGDTSLPPGEAGMIAVHrsDPGLMLGYWQRPDEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLMN-AGGYRVSPVE 428
Cdd:PLN02736 448 NYTSEDQPYPRGEICVR--GPIIFKGYYKDEVQTREVIDEDgWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEK 525
|
410
....*....|....*.
gi 503186189 429 VEAVLREHPLVAEAGV 444
Cdd:PLN02736 526 IENVYAKCKFVAQCFV 541
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
39-116 |
1.70e-07 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 53.89 E-value: 1.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503186189 39 DPAGREAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAYALAFFGAIAGGLVPIPASPDLTARELGFLL 116
Cdd:cd05905 6 DSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL 83
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
327-510 |
1.87e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.62 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 327 DFPRKPGTVGRAQPGRCVAILPEDGgDTSLPPGEAGMIAVHRSdpGLMLGYWQRPDEERemfrGEWFTGGDLGCIdEDGA 406
Cdd:PRK05851 339 SGARRHAVLGNPIPGMEVRISPGDG-AAGVAGREIGEIEIRGA--SMMSGYLGQAPIDP----DDWFPTGDLGYL-VDGG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 407 IAHLGRASDLMNAGGYRVSPVEVEAVLREHPLVAEAGVIDVPQPHGGTAITAFVVAREGGADLS---AELAARAEASLAA 483
Cdd:PRK05851 411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAgarSEVVQRVASECGV 490
|
170 180
....*....|....*....|....*....
gi 503186189 484 YkrPRHYVFVE--RLPKTPNGKLKRSDLK 510
Cdd:PRK05851 491 V--PSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
165-462 |
5.79e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.15 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 165 DDPAFLIYTSGTTANPKGVLHAHRSVWGrrpmyrgwyGITAADRLMH--SGVINWTYAMGTGLsdPLANGATALL--YTG 240
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIA---------EVLSTDHLLKvtDRVATEEDSYFSYL--PLAHVYDQVIetYCI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 241 ERHPSI--WPGLIR-------AFDVTIFAGVPGLYHQI-----MRQASG------------------------------- 275
Cdd:PLN02861 289 SKGASIgfWQGDIRylmedvqALKPTIFCGVPRVYDRIytgimQKISSGgmlrkklfdfaynyklgnlrkglkqeeaspr 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 276 -DRLDLARLRHGL--------TAGDTLPDALEAEWSERTGTRLYEGFGQTEL--STYLSSAPDFPRKpGTVGRAQP---G 341
Cdd:PLN02861 369 lDRLVFDKIKEGLggrvrlllSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScgGCFTSIANVFSMV-GTVGVPMTtieA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 342 RCVAIlPEDGGD--TSLPPGEagmIAVHRSDpgLMLGYWQRPDEEREMFRGEWFTGGDLGCIDEDGAIAHLGRASDL--M 417
Cdd:PLN02861 448 RLESV-PEMGYDalSDVPRGE---ICLRGNT--LFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIfkL 521
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 503186189 418 NAGGYrVSPVEVEAVLREHPLVAEAGVIdvpqphgGTAITAFVVA 462
Cdd:PLN02861 522 SQGEY-VAVENLENTYSRCPLIASIWVY-------GNSFESFLVA 558
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
308-445 |
9.56e-07 |
|
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: 51.59 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 308 RLYEGFGQTElstylSSAPDFPRKPG-----TVGRAQPG-RCVAILPEDGGDtslppGEAGMIAVHrsdpgLMLGYWQRP 381
Cdd:cd05933 346 PIMELYGMSE-----TSGPHTISNPQayrllSCGKALPGcKTKIHNPDADGI-----GEICFWGRH-----VFMGYLNME 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 382 DEEREMFRGE-WFTGGDLGCIDEDGAIAHLGRASDLM-NAGGYRVSPVEVE-AVLREHPLVAEAGVI 445
Cdd:cd05933 411 DKTEEAIDEDgWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENVPPVPIEdAVKKELPIISNAMLI 477
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
44-235 |
3.87e-05 |
|
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: 46.29 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 44 EAETWTYRALESAALRVAFELRSNRSLAPRTRVLIRLRNRTAY-----ALAFFGAIAgglVPIPAS-------------- 104
Cdd:cd17632 64 RFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYatvdlALTRLGAVS---VPLQAGasaaqlapilaete 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503186189 105 PDLTARELGFLLDDSDAAA-------IVLDDTLPHGD------------FAPGLAVVTEAALIAAIDSG---PEGAFADT 162
Cdd:cd17632 141 PRLLAVSAEHLDLAVEAVLeggtpprLVVFDHRPEVDahraalesarerLAAVGIPVTTLTLIAVRGRDlppAPLFRPEP 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503186189 163 AADDPAFLIYTSGTTANPKGVLHAHRSVwgrRPMYRgWYGITAADRLMHSGVINW---TYAMGTG-LSDPLANGATA 235
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLV---ATFWL-KVSSIQDIRPPASITLNFmpmSHIAGRIsLYGTLARGGTA 293
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
136-188 |
1.11e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 41.79 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503186189 136 APGLAVVTEAALIAAIDSGP-EGAFADTAADDPAFLIYTSGTTANPKGVLHAHR 188
Cdd:PRK08180 179 VPGRAATPFAALLATPPTAAvDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHR 232
|
|
| |
