|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
95-630 |
0e+00 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 650.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 95 AIRSDQKSYNLVQLIASALDVYNILRNKnmtqngstgssvkgingTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVP 174
Cdd:cd05941 4 AIVDDGDSITYADLVARAARLANRLLAL-----------------GKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 175 LALSYPEAELLHVMNDSDISLILstkehqdimenistkcsahcsllpsvtsipvnidcqepsstevtssissliaeidss 254
Cdd:cd05941 67 LNPSYPLAELEYVITDSEPSLVL--------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 255 keirgdDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP 334
Cdd:cd05941 90 ------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 335 KFSVRGIWQRwresypnngsKNDEAITVFTGVPTMYTRLLQGYDGMDPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWE 414
Cdd:cd05941 164 KFDPKEVAIS----------RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 415 EVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTS--EVGELCIRSPSLFKEYWRKPEVTA 492
Cdd:cd05941 234 AITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPrgEVGEIQVRGPSVFKEYWNKPEATK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPK 572
Cdd:cd05941 314 EEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLR 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002235085 573 EDskkraeldsKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:cd05941 394 AG---------AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
145-634 |
1.04e-142 |
|
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: 422.30 E-value: 1.04e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsahcsllpsvt 224
Cdd:COG0318 49 GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-------------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeirgddpALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:COG0318 103 --------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLQgydgmDPEQ 384
Cdd:COG0318 145 LVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIER----------ERVTVLFGVPTMLARLLR-----HPEF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSA--SSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE-FVMALSNPL-HGARKEGTVGKPLPCVEAKIIM 460
Cdd:COG0318 210 ARYdlSS-----LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVTVNPEdPGERRPGSVGRPLPGVEVRIVD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 461 EDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIE 539
Cdd:COG0318 285 EDGRELpPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRK-KDMIISGGENVYPAEVE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 540 SVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNA 619
Cdd:COG0318 363 EVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA----------ELDAEELRAFLRERLARYKVPRRVEFVDELPRTA 432
|
490
....*....|....*
gi 1002235085 620 MGKVNKKELKKLLGA 634
Cdd:COG0318 433 SGKIDRRALRERYAA 447
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
139-629 |
7.49e-121 |
|
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: 366.89 E-value: 7.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENistkcsahcs 218
Cdd:cd05936 43 NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLAA---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 llpsvtsipvnidcQEPSSTEVtssissliaeidsskEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQIlSEAW-- 296
Cdd:cd05936 113 --------------GAPLGERV---------------ALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWle 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 297 -GYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLQ 375
Cdd:cd05936 163 dLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRK----------HRVTIFPGVPTMYIALLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 376 gydgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF--VMALsNPLHGARKEGTVGKPLPC 453
Cdd:cd05936 233 --------APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspVVAV-NPLDGPRKPGSIGIPLPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYK 532
Cdd:cd05936 304 TEVKIVDDDGEELPPgEVGELWVRGPQVMKGYWNRPEETAEAFVDG-WLRTGDIGYMDEDGYFFIVDRKK-DMIIVGGFN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 533 LSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLW 612
Cdd:cd05936 382 VYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS----------LTEEEIIAFCREQLAGYKVPRQVEFR 451
|
490
....*....|....*..
gi 1002235085 613 DSLPRNAMGKVNKKELK 629
Cdd:cd05936 452 DELPKSAVGKILRRELR 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
145-629 |
1.46e-112 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 346.86 E-value: 1.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAhcsllPSVT 224
Cdd:PRK07514 53 GDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGA-----PHVE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNidcQEPSSTEVTSSISSLIAEIDSSkeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:PRK07514 128 TLDAD---GTGSLLEAAAAAPDDFETVPRG----ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWRESypnngskndeaiTVFTGVPTMYTRLLQGyDGMDPEq 384
Cdd:PRK07514 201 IHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRA------------TVMMGVPTFYTRLLQE-PRLTRE- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 qsassfAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKII-MEDG 463
Cdd:PRK07514 267 ------AAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTdPETG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 464 AE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVL 542
Cdd:PRK07514 341 AElPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 543 LQHEIVLECAVLGLPDEAYGEIICAIIVPkedsKKRAELDskPALTLEALtswsKDKLAPYKIPTRLYLWDSLPRNAMGK 622
Cdd:PRK07514 420 DELPGVVESAVIGVPHPDFGEGVTAVVVP----KPGAALD--EAAILAAL----KGRLARFKQPKRVFFVDELPRNTMGK 489
|
....*..
gi 1002235085 623 VNKKELK 629
Cdd:PRK07514 490 VQKNLLR 496
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
261-623 |
2.32e-110 |
|
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: 335.02 E-value: 2.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFnALFAPLYSGSVVEFMPKFSVRG 340
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRWREsypnngskndEAITVFTGVPTMYTRLLQgYDGMDPEQQSAssfaakqLRLMMCGSSALPSPLMKRWEEVTGHR 420
Cdd:cd04433 80 ALELIER----------EKVTILLGVPTLLARLLK-APESAGYDLSS-------LRALVSGGAPLPPELLERFEEAPGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 421 LLERYGMTE--FVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFID 497
Cdd:cd04433 142 LVNGYGLTEtgGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELpPGEIGELVVRGPSVMKGYWNNPEATAAVDED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 498 gGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKk 577
Cdd:cd04433 222 -GWYRTGDLGRLDEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD- 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002235085 578 raeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 623
Cdd:cd04433 299 ---------LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
143-629 |
8.33e-110 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 338.50 E-value: 8.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 143 LGGA-RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKehqdimenistkcSAHCSLLP 221
Cdd:PRK07787 42 VAGArRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPA-------------PDDPAGLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 222 SVtsiPVnidcqepsstEVTSSISSLIAEIDSskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE 301
Cdd:PRK07787 109 HV---PV----------RLHARSWHRYPEPDP------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 302 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVrgiwQRWRESYPNNGskndeaiTVFTGVPTMYTRLLQgydgmD 381
Cdd:PRK07787 170 DVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTP----EAYAQALSEGG-------TLYFGVPTVWSRIAA-----D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 382 PEQQSASSFAakqlRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIME 461
Cdd:PRK07787 234 PEAARALRGA----RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 462 DGAETTSE---VGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKVGGYKLSALEI 538
Cdd:PRK07787 310 DGGPVPHDgetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 539 ESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpalTLEALTSWSKDKLAPYKIPTRLYLWDSLPRN 618
Cdd:PRK07787 390 ETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV------------AADELIDFVAQQLSVHKRPREVRFVDALPRN 457
|
490
....*....|.
gi 1002235085 619 AMGKVNKKELK 629
Cdd:PRK07787 458 AMGKVLKKQLL 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
141-629 |
6.88e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 327.53 E-value: 6.88e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENIStkcsahcSLL 220
Cdd:PRK06187 52 GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIL-------PQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIPVNIDCQEPSSTEVTSSISSLIAEIDSS---KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWG 297
Cdd:PRK06187 125 PTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTfdfPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 298 YRSEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLQgy 377
Cdd:PRK06187 205 LSRDDVYLVIVPMFHVHAW-GLPYLALMAGAKQVIPRRFDPENLLDLIET----------ERVTFFFAVPTIWQMLLK-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 378 dGMDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE----FVMALSNP--LHGARKEGTVGKPL 451
Cdd:PRK06187 272 -APRAYFVDFSS-----LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtspvVSVLPPEDqlPGQWTKRRSAGRPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 452 PCVEAKIIMEDGAE---TTSEVGELCIRSPSLFKEYWRKPEVTAEsFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV 528
Cdd:PRK06187 346 PGVEARIVDDDGDElppDGGEVGEIIVRGPWLMQGYWNRPEATAE-TIDGGWLHTGDVGYIDEDGYLYITDRIK-DVIIS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTR 608
Cdd:PRK06187 424 GGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGAT----------LDAKELRAFLRGRLAKFKLPKR 493
|
490 500
....*....|....*....|.
gi 1002235085 609 LYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK06187 494 IAFVDELPRTSVGKILKRVLR 514
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
145-529 |
3.77e-98 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 306.55 E-value: 3.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILsTKEHQDIMENISTKcsahcSLLPSVT 224
Cdd:pfam00501 46 GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEAL-----GKLEVVK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQV----QILSEAWGYRS 300
Cdd:pfam00501 120 LVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWRESypnngskNDEAITVFTGVPTMYTRLLQGydgM 380
Cdd:pfam00501 200 DDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDPAALLELI-------ERYKVTVLYGVPTLLNMLLEA---G 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE---FVMALSNPLHGARKEGTVGKPLPCVEAK 457
Cdd:pfam00501 270 APKRALLSS-----LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEttgVVTTPLPLDEDLRSLGSVGRPLPGTEVK 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 458 IIMEDGAET--TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVG 529
Cdd:pfam00501 345 IVDDETGEPvpPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKK-DQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
145-625 |
7.55e-98 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 306.46 E-value: 7.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILstkehqdimenistkcsahcsllpsvt 224
Cdd:cd17631 45 GDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd17631 98 -----------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLQgydgmdpeQ 384
Cdd:cd17631 143 LVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIER----------HRVTSFFLVPTMIQALLQ--------H 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSASSFAAKQLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEFVMALS--NPLHGARKEGTVGKPLPCVEAKIIMED 462
Cdd:cd17631 205 PRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 463 GAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESV 541
Cdd:cd17631 284 GREVpPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKK-DMIISGGENVYPAEVEDV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 542 LLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMG 621
Cdd:cd17631 362 LYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE----------LDEDELIAHCRERLARYKIPKSVEFVDALPRNATG 431
|
....
gi 1002235085 622 KVNK 625
Cdd:cd17631 432 KILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
145-630 |
2.90e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 304.90 E-value: 2.90e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKcsahcslLPSVT 224
Cdd:PRK07656 55 GDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTR-------LPALE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSSISSLIAEIDSSK---EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE 301
Cdd:PRK07656 128 HVVICETEEDDPHTEKMKTFTDFLAAGDPAErapEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 302 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLQGYDGmd 381
Cdd:PRK07656 208 DRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIET----------ERITVLPGPPTMYNSLLQHPDR-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 382 peqqsaSSFAAKQLRLMMCGSSALPSPLMKRWEEVTG-HRLLERYGMTEFV-MALSNPLHGARKE--GTVGKPLPCVEAK 457
Cdd:PRK07656 276 ------SAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLDDDRKTvaGTIGTAIAGVENK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 IIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESfIDG-GFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSA 535
Cdd:PRK07656 350 IVNELGEEVpVGEVGELLVRGPNVMKGYYDDPEATAAA-IDAdGWLHTGDLGRLDEEGYLYIVDRKK-DMFIVGGFNVYP 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 536 LEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldsKPALTLEALTSWSKDKLAPYKIPTRLYLWDSL 615
Cdd:PRK07656 428 AEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP----------GAELTEEELIAYCREHLAKYKVPRSIEFLDEL 497
|
490
....*....|....*
gi 1002235085 616 PRNAMGKVNKKELKK 630
Cdd:PRK07656 498 PKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-630 |
2.24e-95 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 301.92 E-value: 2.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 130 TGSSVKGINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdimENI 209
Cdd:cd05926 24 VDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKG-----ELG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 210 STKCSAHCSLLPSVTS-IPVNIDCQEPSSTEVTSSISSLiAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQ 288
Cdd:cd05926 99 PASRAASKLGLAILELaLDVGVLIRAPSAESLSNLLADK-KNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAAS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 289 VQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWResypnngsknDEAITVFTGVPT 368
Cdd:cd05926 178 ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVR----------DYNATWYTAVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 369 MYTRLLQGYDGmDPEQQSASsfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV--MAlSNPL-HGARKEG 445
Cdd:cd05926 248 IHQILLNRPEP-NPESPPPK------LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPLpPGPRKPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 446 TVGKPLPcVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaD 524
Cdd:cd05926 320 SVGKPVG-VEVRILDEDGEILPPgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIK-E 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 525 IMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldsKPALTLEALTSWSKDKLAPYK 604
Cdd:cd05926 398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE----------GASVTEEELRAFCRKHLAAFK 467
|
490 500
....*....|....*....|....*.
gi 1002235085 605 IPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:cd05926 468 VPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
145-632 |
3.30e-90 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 290.47 E-value: 3.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTK--CSAHCSLLPS 222
Cdd:COG0365 64 GDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKekVDEALEELPS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 223 VTSIPVNIDCQEPSSTEVTSSISSLIAEIDSS---KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAW-GY 298
Cdd:COG0365 144 LEHVIVVGRTGADVPMEGDLDWDELLAAASAEfepEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLhCLP-LHHVHGLFNALFAPLYSGSVVeFM----PKFSVRGIWqrWR--EsypnngsknDEAITVFTGVPTMYt 371
Cdd:COG0365 224 KPGDVFW-CTAdIGWATGHSYIVYGPLLNGATV-VLyegrPDFPDPGRL--WEliE---------KYGVTVFFTAPTAI- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 372 RLLQGYDGMDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHG-ARKEGTVGKP 450
Cdd:COG0365 290 RALMKAGDEPLKKYDLSS-----LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGlPVKPGSMGKP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 451 LPCVEAKIIMEDGAE-TTSEVGELCIRS--PSLFKEYWRKPEVTAESFID--GGFFKTGDTVTVDDEGYFIILGRTNaDI 525
Cdd:COG0365 365 VPGYDVAVVDEDGNPvPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGrfPGWYRTGDGARRDEDGYFWILGRSD-DV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 MKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKI 605
Cdd:COG0365 444 INVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDEL-------AKELQAHVREELGPYAY 516
|
490 500
....*....|....*....|....*..
gi 1002235085 606 PTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:COG0365 517 PREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
141-624 |
4.80e-83 |
|
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: 269.47 E-value: 4.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimenistKCSAHCSLL 220
Cdd:cd05911 31 GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLE-------KVKEAAKEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSI---PVNIDCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWG 297
Cdd:cd05911 104 GPKDKIivlDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 298 --YRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVR---GIWQRWResypnngskndeaITVFTGVPTMYTR 372
Cdd:cd05911 184 gnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVI-IMPKFDSElflDLIEKYK-------------ITFLYLVPPIAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 373 LLQgydgmDPE--QQSASSfaakqLRLMMCGSSalpsPLMKRWEE-----VTGHRLLERYGMTEFVMALSNPLHGARKEG 445
Cdd:cd05911 250 LAK-----SPLldKYDLSS-----LRVILSGGA----PLSKELQEllakrFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 446 TVGKPLPCVEAKIIMEDGAETTS--EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNa 523
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGpnEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 524 DIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPY 603
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK----------LTEKEVKDYVAKKVASY 464
|
490 500
....*....|....*....|....*
gi 1002235085 604 KiptRL----YLWDSLPRNAMGKVN 624
Cdd:cd05911 465 K---QLrggvVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-629 |
2.03e-80 |
|
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: 260.30 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsahcsllpsvt 224
Cdd:cd05934 28 GDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeirgdDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd05934 82 ------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWRESypnnGSkndeaiTVFTGVPTMYTRLLQGYDGMDPeq 384
Cdd:cd05934 126 LTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRY----GA------TVTNYLGAMLSYLLAQPPSPDD-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 qsassfAAKQLRLmmCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGA 464
Cdd:cd05934 194 ------RAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 465 ET-TSEVGELCIRS---PSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIES 540
Cdd:cd05934 266 ELpAGEPGELVIRGlrgWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRK-KDMIRRRGENISSAEVER 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 541 VLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAM 620
Cdd:cd05934 344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET----------LDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPT 413
|
....*....
gi 1002235085 621 GKVNKKELK 629
Cdd:cd05934 414 EKVAKAQLR 422
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
136-628 |
1.25e-78 |
|
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: 256.25 E-value: 1.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDImenistkcsa 215
Cdd:cd05935 17 FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSELDDL---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 216 hcsllpsvtsipvnidcqepsstevtssissliaeidsskeirgddpALILYTSGTTGKPKGVVHTHKGIVSQVQILSEA 295
Cdd:cd05935 87 -----------------------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 296 WGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMpkfsvrGIWQrwRESYPNNGSKNdeAITVFTGVPTMYTRLLQ 375
Cdd:cd05935 120 TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM------ARWD--RETALELIEKY--KVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 376 gydgmDPEQQsASSFAAkqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfVMALS--NPlHGARKEGTVGKPLPC 453
Cdd:cd05935 190 -----TPEFK-TRDLSS--LKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE-TMSQThtNP-PLRPKLQCLGIP*FG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKII-MEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFI-DGG--FFKTGDTVTVDDEGYFIILGRTNaDIMKV 528
Cdd:cd05935 260 VDARVIdIETGRElPPNEVGEIVVRGPQIFKGYWNRPEETEESFIeIKGrrFFRTGDLGYMDEEGYFFFVDRVK-RMINV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAeldskpalTLEALTSWSKDKLAPYKIPTR 608
Cdd:cd05935 339 SGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKV--------TEEDIIEWAREQMAAYKYPRE 410
|
490 500
....*....|....*....|
gi 1002235085 609 LYLWDSLPRNAMGKVNKKEL 628
Cdd:cd05935 411 VEFVDELPRSASGKILWRLL 430
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
251-632 |
1.26e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 257.62 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 251 IDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVqILSEAW--GYRSEDQ-FLHCLPLHHVHGL-FNALFAPLYS 326
Cdd:PRK05605 210 DVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWvpGLGDGPErVLAALPMFHAYGLtLCLTLAVSIG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 327 GSVVeFMPKFSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLQGydgmdpeqqsassfAAKQ------LRLMMC 400
Cdd:PRK05605 289 GELV-LLPAPDIDLILDAMKKHPP----------TWLPGVPPLYEKIAEA--------------AEERgvdlsgVRNAFS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 401 GSSALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKEGTVGKPLPCVEAKII-MEDGAETTS--EVGELCIR 476
Cdd:PRK05605 344 GAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVdPEDPDETMPdgEEGELLVR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 477 SPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTNADIMkVGGYKLSALEIESVLLQHEIVLECAVLGL 556
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELII-TGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002235085 557 PDEAYGEIICAIIVPKEDskkrAELDSkpaltlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PRK05605 502 PREDGSEEVVAAVVLEPG----AALDP------EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREEL 567
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
145-628 |
7.37e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 246.80 E-value: 7.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAHCSL----- 219
Cdd:PRK08314 61 GDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIvaqys 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 --LPSVTSIPV------NIDCQEPSSTEVTSSISSLIAEID-SSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVq 290
Cdd:PRK08314 141 dyLPAEPEIAVpawlraEPPLQALAPGGVVAWKEALAAGLApPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 291 ILSEAW-GYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPkfsvrgiwqRW-RESYPNNGSKNdeAITVFTGVPT 368
Cdd:PRK08314 220 VGSVLWsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---------RWdREAAARLIERY--RVTHWTNIPT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 369 MYTRLLqgydgMDP--EQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfVMA--LSNPLHGARKE 444
Cdd:PRK08314 289 MVVDFL-----ASPglAERDLSS-----LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAqtHSNPPDRPKLQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 gTVGKPLPCVEAKII-MEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFI--DGG-FFKTGDTVTVDDEGYFIILG 519
Cdd:PRK08314 358 -CLGIPTFGVDARVIdPETLEELpPGEVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGKrFFRTGDLGRMDEEGYFFITD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 520 RTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAeldskpalTLEALTSWSKDK 599
Cdd:PRK08314 437 RLKRMI-NASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKT--------TEEEIIAWAREH 507
|
490 500
....*....|....*....|....*....
gi 1002235085 600 LAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK08314 508 MAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
87-629 |
9.04e-74 |
|
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: 245.74 E-value: 9.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 87 GSTQGVHAAIRSDQKSYNLVQLIASALDVYNILRnknmtqngstgssvkginGTGFLGGARIGIVAKPSPEFVAGIFGTW 166
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALR------------------ALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 167 LSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKcsahcsllpSVTSIPVNIDCQEPSSTEVTSSISS 246
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTK---------SEHTLVVLIVSGGAGPEAGALLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 247 LIAEIDSSKE---IRGDDPALILYTSGTTGKPKGVVHTHKGIvsqvQILSEAW-----GYRSEDQFLHCLPLHHVHGLFN 318
Cdd:cd05959 147 LVAAEAEQLKpaaTHADDPAFWLYSSGSTGRPKGVVHLHADI----YWTAELYarnvlGIREDDVCFSAAKLFFAYGLGN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 319 ALFAPLYSGSVVEFMPKF-SVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLQgydgmDPEQQSASsfaakQLRL 397
Cdd:cd05959 223 SLTFPLSVGATTVLMPERpTPAAVFKRIRRYRP----------TVFFGVPTLYAAMLA-----APNLPSRD-----LSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 398 MMCGSS--ALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNpLHGARKEGTVGKPLPCVEAKIIMEDGAETTS-EVGEL 473
Cdd:cd05959 283 RLCVSAgeALPAEVGERWKARFGLDILDGIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELRDEDGGDVADgEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 474 CIRSPSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAV 553
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002235085 554 LGLPDEAYGEIICAIIVPKEDSKKRAELDskpaltlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05959 440 VGVEDEDGLTKPKAFVVLRPGYEDSEALE-------EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
157-630 |
3.35e-73 |
|
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: 241.90 E-value: 3.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 157 EFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKE-----HQDImenistkcsahcsllpsvtsipvnid 231
Cdd:cd05903 38 EFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERfrqfdPAAM-------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 232 cqepsstevtssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLH 311
Cdd:cd05903 92 ---------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 312 HVHGLFNALFAPLYSGSVVEFMpkfsvrgiwQRWResyPNNG--SKNDEAITVFTGVPTMYTRLLQGYDGMDPeqqsass 389
Cdd:cd05903 145 HQTGFVYGFTLPLLLGAPVVLQ---------DIWD---PDKAlaLMREHGVTFMMGATPFLTDLLNAVEEAGE------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 390 fAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHG--ARKEGTVGKPLPCVEAKIIMEDGAE-T 466
Cdd:cd05903 206 -PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVDDTGATlA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 467 TSEVGELCIRSPSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHE 546
Cdd:cd05903 285 PGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGR-SKDIIIRGGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 547 IVLECAVLGLPDEAYGEIICAIIVPKedskkraeldSKPALTLEALTSW-SKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 625
Cdd:cd05903 363 GVIEAAVVALPDERLGERACAVVVTK----------SGALLTFDELVAYlDRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
....*
gi 1002235085 626 KELKK 630
Cdd:cd05903 433 FRLRE 437
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
145-632 |
1.29e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 242.07 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAhcsllpsvt 224
Cdd:PRK06839 53 GERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYV--------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcQEPSSteVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:PRK06839 124 --------QRVIS--ITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNALFAPLYSGSVV----EFMPKFSVRGIwqrwresypnngskNDEAITVFTGVPTMYTRLLQGYDGM 380
Cdd:PRK06839 194 IVLLPLFHIGGIGLFAFPTLFAGGVIivprKFEPTKALSMI--------------EKHKVTVVMGVPTIHQALINCSKFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSassfaakqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTE-----FVMALSNplhGARKEGTVGKPLPCVE 455
Cdd:PRK06839 260 TTNLQS--------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsptvFMLSEED---ARRKVGSIGKPVLFCD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 AKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESfIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKvGGYKLS 534
Cdd:PRK06839 328 YELIDENKNKVeVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 535 ALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKedskkraeldSKPALTLEALTSWSKDKLAPYKIPTRLYLWDS 614
Cdd:PRK06839 406 PLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKK----------SSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKE 475
|
490
....*....|....*...
gi 1002235085 615 LPRNAMGKVNKKELKKLL 632
Cdd:PRK06839 476 LPKNATGKIQKAQLVNQL 493
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
145-628 |
6.49e-72 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 238.58 E-value: 6.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcsahcsllpsvt 224
Cdd:cd05930 37 GDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTD------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd05930 92 ----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNaLFAPLYSGSVVEFMPKFSVRGIWQRWRESypnngskNDEAITVFTGVPTMYTRLLQgydgmDPEQ 384
Cdd:cd05930 138 LQFTSFSFDVSVWE-IFGALLAGATLVVLPEEVRKDPEALADLL-------AEEGITVLHLTPSLLRLLLQ-----ELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSASSfaakqLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEF-VMALSNPLHGARKEG---TVGKPLPCVEAKII 459
Cdd:cd05930 205 AALPS-----LRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 460 MEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFF------KTGDTVTVDDEGYFIILGRTnADIMKVGGYK 532
Cdd:cd05930 280 DENLRPvPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRI-DDQVKIRGYR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 533 LSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkraeldskPALTLEALTSWSKDKLAPYKIPTRLYLW 612
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG----------GELDEEELRAHLAERLPDYMVPSAFVVL 428
|
490
....*....|....*.
gi 1002235085 613 DSLPRNAMGKVNKKEL 628
Cdd:cd05930 429 DALPLTPNGKVDRKAL 444
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
136-630 |
1.64e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 237.52 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSA 215
Cdd:PRK08316 52 ALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 216 HCSLLPSVTSipvnidcQEPSSTEVTSSISSLIAEIDS--SKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS 293
Cdd:PRK08316 132 DTLILSLVLG-------GREAPGGWLDFADWAEAGSVAepDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRL 373
Cdd:PRK08316 205 VAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEA----------ERITSFFAPPTVWISL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LQGYDgmdpeqqsassFAAKQLR-LMMC--GSSALPSPLMKRWEE-VTGHRLLERYGMTEfvMAlsnPLHG-------AR 442
Cdd:PRK08316 275 LRHPD-----------FDTRDLSsLRKGyyGASIMPVEVLKELRErLPGLRFYNCYGQTE--IA---PLATvlgpeehLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 KEGTVGKPLPCVEAKIIMEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRT 521
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDvAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRK 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 522 NaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLA 601
Cdd:PRK08316 418 K-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA----------TVTEDELIAHCRARLA 486
|
490 500
....*....|....*....|....*....
gi 1002235085 602 PYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
139-630 |
3.95e-70 |
|
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: 233.38 E-value: 3.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdimenistkcsahcs 218
Cdd:cd05972 19 KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 llpsvtsipvnidcqepsstevtssissliaeidsskeirgdDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGY 298
Cdd:cd05972 82 ------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLHCLPLHHVHGLFNALFAPLYSGS--VVEFMPKFSVRgIWQRWRESYPnngskndeaITVFTGVPTMYTRLLQg 376
Cdd:cd05972 120 RPDDIHWNIADPGWAKGAWSSFFGPWLLGAtvFVYEGPRFDAE-RILELLERYG---------VTSFCGPPTAYRMLIK- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 377 ydgmdpeqQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEA 456
Cdd:cd05972 189 --------QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEDGAETT-SEVGELCIR--SPSLFKEYWRKPEVTAESFIdGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKL 533
Cdd:cd05972 261 AIIDDDGRELPpGEEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRDEDGYFWFVGR-ADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 534 SALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKIPTRLYLWD 613
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEEL-------AEELQGHVKKVLAPYKYPREIEFVE 411
|
490
....*....|....*..
gi 1002235085 614 SLPRNAMGKVNKKELKK 630
Cdd:cd05972 412 ELPKTISGKIRRVELRD 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
140-630 |
1.09e-69 |
|
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: 231.85 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 140 TGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLilstkehqdimenistkcsahcsl 219
Cdd:cd05912 21 LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 lpsvtsipvnidcqepsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYR 299
Cdd:cd05912 77 ----------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 300 SEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGIWQrwresypnngSKNDEAITVFTGVPTMYTRLLQGYDG 379
Cdd:cd05912 117 EDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLH----------LINSGKVTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 380 MDPEQqsassfaakqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEF---VMALsNPLHGARKEGTVGKPLPCVEA 456
Cdd:cd05912 186 GYPNN----------LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETcsqIVTL-SPEDALNKIGSAGKPLFPVEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEDGAEttSEVGELCIRSPSLFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSAL 536
Cdd:cd05912 254 KIEDDGQPP--YEVGEILLKGPNVTKGYLNRPDATEESFENG-WFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 537 EIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLP 616
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP------------ISEEELIAYCSEKLAKYKVPKKIYFVDELP 397
|
490
....*....|....
gi 1002235085 617 RNAMGKVNKKELKK 630
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
139-632 |
3.93e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 234.94 E-value: 3.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCS---- 214
Cdd:PRK06178 77 QRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSlrhv 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 215 AHCSL---LPSVTSIPVNIDCQEPSsTEVTSSISSLIAEIDSSKEIRG-----DDPALILYTSGTTGKPKGVVHTHKGIV 286
Cdd:PRK06178 157 IVTSLadvLPAEPTLPLPDSLRAPR-LAAAGAIDLLPALRACTAPVPLpppalDALAALNYTGGTTGMPKGCEHTQRDMV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 287 SQVQILSEAWGYRSEDQ-FLHCLPLHHVHGLFNALFAPLYSGSVVEFMpkfsvrgiwQRWresypnngskndEAITVFTG 365
Cdd:PRK06178 236 YTAAAAYAVAVVGGEDSvFLSFLPEFWIAGENFGLLFPLFSGATLVLL---------ARW------------DAVAFMAA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 366 VPTmY--TRLLQGYDGMDP--EQQSASSFAAKQLRLMMCGS--SALPSPLMKRWEEVTGHRLLE-RYGMTE------FVM 432
Cdd:PRK06178 295 VER-YrvTRTVMLVDNAVElmDHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEaAWGMTEthtcdtFTA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 433 ALSNPLHGARKEGT-VGKPLPCVEAKIIMEDGAETT--SEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTV 509
Cdd:PRK06178 374 GFQDDDFDLLSQPVfVGLPVPGTEFKICDFETGELLplGAEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 510 DDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTL 589
Cdd:PRK06178 453 DEQGFLHYLGR-RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA----------DLTA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1002235085 590 EALTSWSKDKLAPYKIPTrLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PRK06178 522 AALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALA 563
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
145-592 |
9.82e-69 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 234.61 E-value: 9.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDIS-LILSTKEHQDimenistKCSAHCSLLPSV 223
Cdd:COG1022 65 GDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKvLFVEDQEQLD-------KLLEVRDELPSL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 224 TSIpVNIDCQEPSSTEVTSSISSLIA---------EIDSSK-EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS 293
Cdd:COG1022 138 RHI-VVLDPRGLRDDPRLLSLDELLAlgrevadpaELEARRaAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMPkfSVRGIWQRWRESYPnngskndeaiTVFTGVP----TM 369
Cdd:COG1022 217 ERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAE--SPDTLAEDLREVKP----------TFMLAVPrvweKV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 370 YTRLLQGYDGMDPEQQSASSFAAK----------------------------------------QLRLMMCGSSALPSPL 409
Cdd:COG1022 284 YAGIQAKAEEAGGLKRKLFRWALAvgrryararlagkspslllrlkhaladklvfsklrealggRLRFAVSGGAALGPEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 410 MkRWEEVTGHRLLERYGMTE-FVMALSNPLhGARKEGTVGKPLPCVEAKIimedgaettSEVGELCIRSPSLFKEYWRKP 488
Cdd:COG1022 364 A-RFFRALGIPVLEGYGLTEtSPVITVNRP-GDNRIGTVGPPLPGVEVKI---------AEDGEILVRGPNVMKGYYKNP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 489 EVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV-GGYKLSALEIESVLLQHEIVLECAVLGlPDEAYgeiICA 567
Cdd:COG1022 433 EATAEAFDADGWLHTGDIGELDEDGFLRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG-DGRPF---LAA 507
|
490 500
....*....|....*....|....*.
gi 1002235085 568 IIVPKEDS-KKRAELDSKPALTLEAL 592
Cdd:COG1022 508 LIVPDFEAlGEWAEENGLPYTSYAEL 533
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
145-553 |
4.81e-65 |
|
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: 219.44 E-value: 4.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcSAHCSLLPSVT 224
Cdd:TIGR01733 25 GDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD--------------SALASRLAGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSsissliAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:TIGR01733 91 LPVILLDPLELAALDDAP------APPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFnALFAPLYSGSVVEFMPKFSVR---GIWQRWRESYPnngskndeaITVFTGVPTMYTRLLQgydgmd 381
Cdd:TIGR01733 165 LQFASLSFDASVE-EIFGALLAGATLVVPPEDEERddaALLAALIAEHP---------VTVLNLTPSLLALLAA------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 382 peqqsASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTE---FVMALSNPLHGARKEGTV--GKPLPCVE 455
Cdd:TIGR01733 229 -----ALPPALASLRLVILGGEALTPALVDRWRARGPGaRLINLYGPTEttvWSTATLVDPDDAPRESPVpiGRPLANTR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 AKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF--------FKTGDTVTVDDEGYFIILGRTNADIm 526
Cdd:TIGR01733 304 LYVLDDDLRPVpVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLGRIDDQV- 382
|
410 420
....*....|....*....|....*..
gi 1002235085 527 KVGGYKLSALEIESVLLQHEIVLECAV 553
Cdd:TIGR01733 383 KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
145-632 |
1.59e-64 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 220.22 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimeNISTKCSAHCSLLPSVT 224
Cdd:PRK03640 52 GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEA---KLIPGISVKFAELMNGP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVnidcqepsstevtssisSLIAEIDSskeirgDDPALILYTSGTTGKPKGVVHTHK----GIVSQVQILseawGYRS 300
Cdd:PRK03640 129 KEEA-----------------EIQEEFDL------DEVATIMYTSGTTGKPKGVIQTYGnhwwSAVGSALNL----GLTE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGIwqrwresypnNGSKNDEAITVFTGVPTMYTRLLQGYdgm 380
Cdd:PRK03640 182 DDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKI----------NKLLQTGGVTIISVVSTMLQRLLERL--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 dPEQQSASSFaakqlRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEF---VMALSnPLHGARKEGTVGKPLPCVEAK 457
Cdd:PRK03640 248 -GEGTYPSSF-----RCMLLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETasqIVTLS-PEDALTKLGSAGKPLFPCELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 IIMEDGAETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALE 537
Cdd:PRK03640 320 IEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-WFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 538 IESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPR 617
Cdd:PRK03640 398 IEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE------------VTEEELRHFCEEKLAKYKVPKRFYFVEELPR 465
|
490
....*....|....*
gi 1002235085 618 NAMGKVNKKELKKLL 632
Cdd:PRK03640 466 NASGKLLRHELKQLV 480
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
141-629 |
2.32e-64 |
|
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: 218.53 E-value: 2.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENistkcsahcsll 220
Cdd:cd05969 21 GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYERTDP------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 psvtsipvnidcqepsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRS 300
Cdd:cd05969 89 ---------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNALFAPLYSG-SVVEFMPKFSVRgiwqRWresYpnnGSKNDEAITVFTGVPTMYtRLLQGYDg 379
Cdd:cd05969 130 DDIYWCTADPGWVTGTVYGIWAPWLNGvTNVVYEGRFDAE----SW---Y---GIIERVKVTVWYTAPTAI-RMLMKEG- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 380 mdpeQQSASSFAAKQLRLMMCGSSALpSPLMKRW-EEVTGHRLLERYGMTEF-VMALSNPLHGARKEGTVGKPLPCVEAK 457
Cdd:cd05969 198 ----DELARKYDLSSLRFIHSVGEPL-NPEAIRWgMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 IIMEDGAET-TSEVGELCIRS--PSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLS 534
Cdd:cd05969 273 VVDENGNELpPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRAD-DIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 535 ALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELDskpaltlEALTSWSKDKLAPYKIPTRLYLWDS 614
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELK-------EEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*
gi 1002235085 615 LPRNAMGKVNKKELK 629
Cdd:cd05969 424 LPKTRSGKIMRRVLK 438
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-629 |
7.22e-64 |
|
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: 214.45 E-value: 7.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM-PKFSV 338
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 339 RGIWQrwresypnngSKNDEAITVFTGVPTMYTRLLqgydgmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTG 418
Cdd:cd05917 82 LAVLE----------AIEKEKCTALHGVPTMFIAEL--------EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 419 HR-LLERYGMTEF--VMALSNPLHGA-RKEGTVGKPLPCVEAKIIMEDGAET--TSEVGELCIRSPSLFKEYWRKPEVTA 492
Cdd:cd05917 144 MKdVTIAYGMTETspVSTQTRTDDSIeKRVNTVGRIMPHTEAKIVDPEGGIVppVGVPGELCIRGYSVMKGYWNDPEKTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESfIDG-GFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVP 571
Cdd:cd05917 224 EA-IDGdGWLHTGDLAVMDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002235085 572 KEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05917 302 KEGAE----------LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
139-634 |
9.91e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 219.65 E-value: 9.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFlgGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehQDIMENISTKCSAHCS 218
Cdd:PRK07786 63 GVGF--GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT----EAALAPVATAVRDIVP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 LLPSVTSIPvnidcqePSSTEVTSSISSLIAEIDSSK---EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEA 295
Cdd:PRK07786 137 LLSTVVVAG-------GSSDDSVLGYEDLLAEAGPAHapvDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 296 WGYRSEDQFLHC-LPLHHVHGLFNALFAPLYSGSVV-----EFMPKfSVRGIWQRwresypnngskndEAITVFTGVPTM 369
Cdd:PRK07786 210 NGADINSDVGFVgVPLFHIAGIGSMLPGLLLGAPTViyplgAFDPG-QLLDVLEA-------------EKVTGIFLVPAQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 370 YTRLL--QGYDGMDpeqqsassfaakqLRLMMCGSSALPSP--LMKRWEEV-TGHRLLERYGMTEF--VMALSNPLHGAR 442
Cdd:PRK07786 276 WQAVCaeQQARPRD-------------LALRVLSWGAAPASdtLLRQMAATfPEAQILAAFGQTEMspVTCMLLGEDAIR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 KEGTVGKPLPCVEAKII---MEDGAetTSEVGELCIRSPSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILG 519
Cdd:PRK07786 343 KLGSVGKVIPTVAARVVdenMNDVP--VGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 520 RTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpALTLEALTSWSKDK 599
Cdd:PRK07786 420 RKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDA---------ALTLEDLAEFLTDR 489
|
490 500 510
....*....|....*....|....*....|....*
gi 1002235085 600 LAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
257-629 |
1.93e-63 |
|
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: 216.17 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 257 IRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS-EAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK 335
Cdd:cd05919 88 TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMArEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 336 F-SVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLqgyDGMDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWE 414
Cdd:cd05919 168 WpTAERVLATLARFRP----------TVLYGVPTFYANLL---DSCAGSPDALRS-----LRLCVSAGEALPRGLGERWM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 415 EVTGHRLLERYGMTE-FVMALSNPLhGARKEGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTA 492
Cdd:cd05919 230 EHFGGPILDGIGATEvGHIFLSNRP-GAWRLGSTGRPVPGYEIRLVDEEGHTIPPgEEGDLLVRGPSAAVGYWNNPEKSR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESFiDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPK 572
Cdd:cd05919 309 ATF-NGGWYRTGDKFCRDADGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLK 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 573 EdskkraELDSKPALtLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05919 387 S------PAAPQESL-ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
145-629 |
2.37e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 218.32 E-value: 2.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLalsYPEAEL---LHVMNDSDIS-LILSTKEHQDIMENISTKCSAhcslL 220
Cdd:PRK06188 62 GDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLGSLddhAYVLEDAGIStLIVDPAPFVERALALLARVPS----L 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIpvnidcqepSSTEVTSSISSLIAEIDSSKEIRGD---DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWG 297
Cdd:PRK06188 135 KHVLTL---------GPVPDGVDLLAAAAKFGPAPLVAAAlppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 298 YRSEDQFLHCLPLHHVHGlfnALFAP-LYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLqg 376
Cdd:PRK06188 206 WPADPRFLMCTPLSHAGG---AFFLPtLLRGGTVIVLAKFDPAEVLRAIEE----------QRITATFLVPTMIYALL-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 377 yDGMDPEQQSASSfaakqLRLMMCGSSAL-PSPL---MKRWeevtGHRLLERYGMTEFVMALS------NPLHGARKEGT 446
Cdd:PRK06188 271 -DHPDLRTRDLSS-----LETVYYGASPMsPVRLaeaIERF----GPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 447 VGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRTNaDI 525
Cdd:PRK06188 341 CGRPTPGLRVALLDEDGREVaQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKK-DM 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 MKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAeldskpaltlEALTSWSKDKLAPYKI 605
Cdd:PRK06188 419 IVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA----------AELQAHVKERKGSVHA 488
|
490 500
....*....|....*....|....
gi 1002235085 606 PTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK06188 489 PKQVDFVDSLPLTALGKPDKKALR 512
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
141-630 |
3.01e-63 |
|
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: 217.88 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKcsahcslL 220
Cdd:cd12119 46 GVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPR-------L 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIPVNIDCQEPSSTEVTSSIS--SLIAEIDSS---KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQ--VQILS 293
Cdd:cd12119 119 PTVEHVVVMTDDAAMPEPAGVGVLAyeELLAAESPEydwPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHamAALLT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGlFNALFAPLYSGS--V---VEFMPKFSVRgIWQRwresypnngskndEAITVFTGVPT 368
Cdd:cd12119 199 DGLGLSESDVVLPVVPMFHVNA-WGLPYAAAMVGAklVlpgPYLDPASLAE-LIER-------------EGVTFAAGVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 369 MYTRLLQGYDGMDPEQQSassfaakqLRLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEF----VMALSNPLHGARKE 444
Cdd:cd12119 264 VWQGLLDHLEANGRDLSS--------LRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETsplgTVARPPSEHSNLSE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 G-------TVGKPLPCVEAKIIMEDGAE---TTSEVGELCIRSPSLFKEYWRKPEvTAESFIDGGFFKTGDTVTVDDEGY 514
Cdd:cd12119 335 DeqlalraKQGRPVPGVELRIVDDDGRElpwDGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 515 FIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTS 594
Cdd:cd12119 414 LTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT----------VTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....*.
gi 1002235085 595 WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
135-631 |
7.37e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 217.72 E-value: 7.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 135 KGINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLIL------STKEH---QDI 205
Cdd:PRK12583 60 RGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIcadafkTSDYHamlQEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 206 MENI-STKCSA-HCSLLPSVTSIpVNIDCQEPSSTEVTSSISSL--------IAEIDSSkeIRGDDPALILYTSGTTGKP 275
Cdd:PRK12583 140 LPGLaEGQPGAlACERLPELRGV-VSLAPAPPPGFLAWHELQARgetvsreaLAERQAS--LDRDDPINIQYTSGTTGFP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 276 KGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV-----EFMPKFSVRGIwqrwresyp 350
Cdd:PRK12583 217 KGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLvypneAFDPLATLQAV--------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 351 nngskNDEAITVFTGVPTMYTRLLqgydgmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTE 429
Cdd:PRK12583 288 -----EEERCTALYGVPTMFIAEL--------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 430 -----FVMALSNPLHgaRKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKT 503
Cdd:PRK12583 355 tspvsLQTTAADDLE--RRVETVGRTQPHLEVKVVDPDGATVpRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 504 GDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedskkraeLDS 583
Cdd:PRK12583 433 GDLATMDEQGYVRIVGRSK-DMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVR----------LHP 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1002235085 584 KPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK12583 502 GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
252-631 |
9.53e-63 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 219.06 E-value: 9.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 252 DSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVE 331
Cdd:PRK07529 205 FSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 332 FMPKFSVRG------IW---QRWResypnngskndeaITVFTGVPTMYTRLLQgydgMDPEQQSASSfaakqLRLMMCGS 402
Cdd:PRK07529 285 LATPQGYRGpgvianFWkivERYR-------------INFLSGVPTVYAALLQ----VPVDGHDISS-----LRYALCGA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALPSPLMKRWEEVTGHRLLERYGMTEFVMALS-NPLHGARKEGTVGKPLPCVEAKIIMEDGAET------TSEVGELCI 475
Cdd:PRK07529 343 APLPVEVFRRFEAATGVRIVEGYGLTEATCVSSvNPPDGERRIGSVGLRLPYQRVRVVILDDAGRylrdcaVDEVGVLCI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 476 RSPSLFKEYWRkPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKvGGYKLSALEIESVLLQHEIVLECAVLG 555
Cdd:PRK07529 423 AGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEALLRHPAVALAAAVG 500
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 556 LPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLA-PYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK07529 501 RPDAHAGELPVAYVQLKPGA----------SATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
127-628 |
1.62e-62 |
|
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: 215.56 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 127 NGSTGSSV-------------KGINGTGFLGGARIGIVAKPSPEFVAGIFG-TWLsGGVAVPLALSYPEAELLHVMNDSD 192
Cdd:cd05904 26 DAATGRALtyaelerrvrrlaAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAvLSL-GAVVTTANPLSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 193 ISLILSTkehqdimenistkcsahCSLLPSVTSIPVNIDCQEpSSTEVTSSISSLIAEIDSSK----EIRGDDPALILYT 268
Cdd:cd05904 105 AKLAFTT-----------------AELAEKLASLALPVVLLD-SAEFDSLSFSDLLFEADEAEppvvVIKQDDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 269 SGTTGKPKGVVHTHKGIVSQVQIL--SEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG---IWQ 343
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEEllaAIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 344 RWResypnngskndeaITVFTGVPTMYTRLLQgydgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGH-RLL 422
Cdd:cd05904 247 RYK-------------VTHLPVVPPIVLALVK--------SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNvDLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 423 ERYGMTE---FVMALSNPLHGARKEGTVGKPLPCVEAKII-MEDG-AETTSEVGELCIRSPSLFKEYWRKPEVTAESFID 497
Cdd:cd05904 306 QGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVdPETGeSLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 498 GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKk 577
Cdd:cd05904 386 EGWLHTGDLCYIDEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSS- 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1002235085 578 raeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd05904 464 ---------LTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
137-628 |
3.62e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 216.05 E-value: 3.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 137 INGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLIL--------------STKEH 202
Cdd:PRK06710 66 LQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsATKIE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 203 QDIMENISTKCSAHCSLL-PSVTSIPVNIdCQEPSSTEVTSSISSLIAEIDSSKEIRGD---DPALILYTSGTTGKPKGV 278
Cdd:PRK06710 146 HVIVTRIADFLPFPKNLLyPFVQKKQSNL-VVKVSESETIHLWNSVEKEVNTGVEVPCDpenDLALLQYTGGTTGFPKGV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 279 VHTHKGIVSQVqILSEAWGY---RSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngsk 355
Cdd:PRK06710 225 MLTHKNLVSNT-LMGVQWLYnckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKK-------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 356 ndEAITVFTGVPTMYTRLLQgydgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV-MAL 434
Cdd:PRK06710 296 --HKVTLFPGAPTIYIALLN--------SPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTH 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 435 SNPLHGARKEGTVGKPLPCVEAKIIMEDGAET--TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDE 512
Cdd:PRK06710 366 SNFLWEKRVPGSIGVPWPDTEAMIMSLETGEAlpPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDG-WLHTGDVGYMDED 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 513 GYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEAL 592
Cdd:PRK06710 445 GFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTE----------CSEEEL 513
|
490 500 510
....*....|....*....|....*....|....*.
gi 1002235085 593 TSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK06710 514 NQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-630 |
4.24e-61 |
|
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: 211.95 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSA 215
Cdd:TIGR03098 41 GLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 216 HCSLLPSVTSIPVNIDCQEPSSTevtsSISSLIAEIDSSKEIRG--DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS 293
Cdd:TIGR03098 121 LRTLIIVGDPAHASEGHPGEEPA----SWPKLLALGDADPPHPVidSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV--EF-MPKFSVRGIWQrwresypnngskndEAITVFTGVPTMY 370
Cdd:TIGR03098 197 TYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVlhDYlLPRDVLKALEK--------------HGITGLAAVPPLW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 371 TRLLQgydgMD-PEQqsassfAAKQLRLMMCGSSALPSPLMKRWEE-VTGHRLLERYGMTE-FVMALSNPLHGARKEGTV 447
Cdd:TIGR03098 263 AQLAQ----LDwPES------AAPSLRYLTNSGGAMPRATLSRLRSfLPNARLFLMYGLTEaFRSTYLPPEEVDRRPDSI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 448 GKPLPCVEAKIIMEDGAETT-SEVGELCIRSPSLFKEYWRKPEVTAESF-----------IDGGFFKTGDTVTVDDEGYF 515
Cdd:TIGR03098 333 GKAIPNAEVLVLREDGSECApGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpgelhLPELAVWSGDTVRRDEEGFL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 516 IILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkrAELDskpaltLEALTSW 595
Cdd:TIGR03098 413 YFVGRRDEMI-KTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGG----EELD------RAALLAE 481
|
490 500 510
....*....|....*....|....*....|....*
gi 1002235085 596 SKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:TIGR03098 482 CRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
260-629 |
5.78e-61 |
|
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: 209.64 E-value: 5.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVS-----QVQILseawGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP 334
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLAsadryAVNVL----RLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 335 kfsvrgiwqrwrESYPNN--GSKNDEAITVFTGVPTMYTRLLQGYDGMDPEQQSassfaakqLRLMMCGSSALPSPLMKR 412
Cdd:cd05958 173 ------------EATPDLllSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSS--------LRKCVSAGEALPAALHRA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 413 WEEVTGHRLLERYGMTE-FVMALSNPLHGARKeGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLfkeYWRKPEV 490
Cdd:cd05958 233 WKEATGIPIIDGIGSTEmFHIFISARPGDARP-GATGKPVPGYEAKVVDDEGNPVPDgTIGRLAVRGPTG---CRYLADK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 491 TAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIV 570
Cdd:cd05958 309 RQRTYVQGGWNITGDTYSRDPDGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002235085 571 PkedskkRAELDSKPALtLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05958 388 L------RPGVIPGPVL-ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
147-630 |
7.05e-61 |
|
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: 211.24 E-value: 7.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKcsahcslLPSVTSI 226
Cdd:TIGR02262 57 RVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGK-------SPHLEHR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PVNIDCQEPsstevTSSISSLIA---EIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHkgivSQVQILSEAW-----GY 298
Cdd:TIGR02262 130 VVVGRPEAG-----EVQLAELLAtesEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTH----SNPYWTAELYarntlGI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP-KFSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLQgy 377
Cdd:TIGR02262 201 REDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGeRPTPDAVFDRLRRHQP----------TIFYGVPTLYAAMLA-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 378 dgmDPEQQSassfaAKQLRLMMCGSS--ALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNpLHGARKEGTVGKPLPCV 454
Cdd:TIGR02262 269 ---DPNLPS-----EDQVRLRLCTSAgeALPAEVGQRWQARFGVDIVDGIGSTEMLhIFLSN-LPGDVRYGTSGKPVPGY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 EAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIdGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKL 533
Cdd:TIGR02262 340 RLRLVGDGGQDVADgEPGELLISGPSSATMYWNNRAKSRDTFQ-GEWTRSGDKYVRNDDGSYTYAGRTD-DMLKVSGIYV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 534 SALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWD 613
Cdd:TIGR02262 418 SPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQT----------ALETELKEHVKDRLAPYKYPRWIVFVD 487
|
490
....*....|....*..
gi 1002235085 614 SLPRNAMGKVNKKELKK 630
Cdd:TIGR02262 488 DLPKTATGKIQRFKLRE 504
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
169-630 |
4.30e-60 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 209.99 E-value: 4.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 169 GGVAVPLALSYPEAELLHVMNDSD-ISLILSTKEHQDIMENISTKCSAHcslLPSVTSIpVNIDCQEPSSTEVTssISSL 247
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQaKMFFAPTLFKQTRPVDLILPLQNQ---LPQLQQI-VGVDKLAPATSSLS--LSQI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 248 IAE---IDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAP- 323
Cdd:PRK06087 172 IADyepLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPf 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 324 LYSGSVV---EFMPKFSVRGIwqrwresypnngskNDEAITVFTGVpTMYTrllqgYDGMDPEQQSASSFAAkqLRLMMC 400
Cdd:PRK06087 252 LIGARSVlldIFTPDACLALL--------------EQQRCTCMLGA-TPFI-----YDLLNLLEKQPADLSA--LRFFLC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 401 GSSALPSPLMKRWEEvTGHRLLERYGMTE----FVMALSNPLhgARKEGTVGKPLPCVEAKIIMEDGAETT-SEVGELCI 475
Cdd:PRK06087 310 GGTTIPKKVARECQQ-RGIKLLSVYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVVDEARKTLPpGCEGEEAS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 476 RSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLG 555
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVA 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002235085 556 LPDEAYGEIICAIIVPKEDSKkraeldskpALTLEALTSW-SKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK06087 466 MPDERLGERSCAYVVLKAPHH---------SLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
135-609 |
6.17e-60 |
|
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: 207.06 E-value: 6.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 135 KGINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILstkehqdimenistkcs 214
Cdd:cd05907 20 KGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 215 ahcsllpsvtsipvnidCQEPsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSE 294
Cdd:cd05907 83 -----------------VEDP------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 295 AWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPkfSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLL 374
Cdd:cd05907 122 RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRP----------TVFLAVPRVWEKVY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 375 QGYDGMD-PEQQSASSFAAK--QLRLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEF--VMALSNPlhGARKEGTVGK 449
Cdd:cd05907 190 AAIKVKAvPGLKRKLFDLAVggRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETsaVVTLNPP--GDNRIGTVGK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 450 PLPCVEAKIimedgaettSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV- 528
Cdd:cd05907 267 PLPGVEVRI---------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK-DLIITs 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGlPDEAYgeiICAIIVPKEdskkraeldskpaltlEALTSWSKDKLAPYKIPTR 608
Cdd:cd05907 337 GGKNISPEPIENALKASPLISQAVVIG-DGRPF---LVALIVPDP----------------EALEAWAEEHGIAYTDVAE 396
|
.
gi 1002235085 609 L 609
Cdd:cd05907 397 L 397
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-631 |
1.26e-57 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 198.09 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 259 GDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSV 338
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 339 RG------IW---QRWResypnngskndeaITVFTGVPTMYTRLLQGYDGMDpeqqsASSfaakqLRLMMCGSSALPSPL 409
Cdd:cd05944 81 RNpglfdnFWklvERYR-------------ITSLSTVPTVYAALLQVPVNAD-----ISS-----LRFAMSGAAPLPVEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 410 MKRWEEVTGHRLLERYGMTEFVMALS-NPLHGARKEGTVGKPLPCVEAKIIMEDGAETT------SEVGELCIRSPSLFK 482
Cdd:cd05944 138 RARFEDATGLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLlrdcapDEVGEICVAGPGVFG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 483 EYWRKpEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:cd05944 218 GYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAK-DLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 563 EIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPY-KIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:cd05944 296 ELPVAYVQLKPGAV----------VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
155-629 |
9.67e-57 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 200.29 E-value: 9.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 155 SPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAhcsllpSVTSIPVnIDCQE 234
Cdd:PRK08008 72 CPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAT------PLRHICL-TRVAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 235 PSSTEVtSSISSLIA----EIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIvsQVQILSEAW--GYRSEDQFLHCL 308
Cdd:PRK08008 145 PADDGV-SSFTQLKAqqpaTLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWqcALRDDDVYLTVM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 309 PLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWResypnngsknDEAITVFTGVPTMY-TRLLQgyDGMDPEQQSA 387
Cdd:PRK08008 222 PAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVC----------KYRATITECIPMMIrTLMVQ--PPSANDRQHC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 388 ssfaakqLRLMMcgsSALP-SPLMKR-WEEVTGHRLLERYGMTE-FVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGA 464
Cdd:PRK08008 290 -------LREVM---FYLNlSDQEKDaFEERFGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 465 E-TTSEVGELCIRS---PSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIES 540
Cdd:PRK08008 360 PlPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELEN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 541 VLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAM 620
Cdd:PRK08008 439 IIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET----------LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCS 508
|
....*....
gi 1002235085 621 GKVNKKELK 629
Cdd:PRK08008 509 GKIIKKNLK 517
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
127-634 |
1.03e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 199.26 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 127 NGSTGSSVKGINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILstkeHQDIM 206
Cdd:PRK09088 29 DALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL----GDDAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 207 EnistkcSAHCSLLpSVTSIPVNIDCQEPSSTEvtssissliaeidsskEIRGDDPALILYTSGTTGKPKGVVHTHKGIV 286
Cdd:PRK09088 105 A------AGRTDVE-DLAAFIASADALEPADTP----------------SIPPERVSLILFTSGTSGQPKGVMLSERNLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 287 SQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFsvrgiwqrwrESYPNNGSKNDEA--ITVFT 364
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF----------EPKRTLGRLGDPAlgITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 365 GVPTMyTRLLQGYDGMDPEqqsassfAAKQLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEFVMALSNPLHGAR-- 442
Cdd:PRK09088 232 CVPQM-AQAFRAQPGFDAA-------ALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDVir 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 -KEGTVGKPLPCVEAKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGR 520
Cdd:PRK09088 303 aKAGAAGIPTPTVQTRVVDDQGNDCPAGVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 521 tNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKL 600
Cdd:PRK09088 383 -KKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA----------PLDLERIRSHLSTRL 451
|
490 500 510
....*....|....*....|....*....|....
gi 1002235085 601 APYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK09088 452 AKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
138-629 |
1.17e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 201.15 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 138 NGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAV---PLalsYPEAELLHVMNDSDIS--LILSTKEHQ--------D 204
Cdd:PRK05677 68 QHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPL---YTAREMEHQFNDSGAKalVCLANMAHLaekvlpktG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 205 IMENISTKCSahcSLLPSVTSIPVNIDCQE----------PSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGK 274
Cdd:PRK05677 145 VKHVIVTEVA---DMLPPLKRLLINAVVKHvkkmvpayhlPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 275 PKGVVHTHKGIVS---QVQILSEAWGYRSEDQFLHCLPLHHVHGL-FNALFAPLYSGSVVEF-----MPKFsVRGIwQRW 345
Cdd:PRK05677 222 AKGAMLTHRNLVAnmlQCRALMGSNLNEGCEILIAPLPLYHIYAFtFHCMAMMLIGNHNILIsnprdLPAM-VKEL-GKW 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 346 ResypnngskndeaITVFTGVPTMYTRLLQGydgmdpEQQSASSFAAkqLRLMMCGSSALPSPLMKRWEEVTGHRLLERY 425
Cdd:PRK05677 300 K-------------FSGFVGLNTLFVALCNN------EAFRKLDFSA--LKLTLSGGMALQLATAERWKEVTGCAICEGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 426 GMTEFV-MALSNPLHGARKeGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKT 503
Cdd:PRK05677 359 GMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPLgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 504 GDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKedskkraeldS 583
Cdd:PRK05677 438 GDIALIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVK----------P 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1002235085 584 KPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK05677 507 GETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
136-633 |
2.11e-56 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 199.73 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMN--DSDISLILSTKEHQdimenistkc 213
Cdd:PRK05852 59 QLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQaaGARVVLIDADGPHD---------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 214 sahcSLLPSVTSIPVNI-----DCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQ 288
Cdd:PRK05852 129 ----RAEPTTRWWPLTVnvggdSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 289 VQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMP---KFSVRGIWQRWResypnngsknDEAITVFTG 365
Cdd:PRK05852 205 VRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPargRFSAHTFWDDIK----------AVGATWYTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 366 VPTMYTRLLQGYDgmdpEQQSASSFAAkqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKE 444
Cdd:PRK05852 274 VPTIHQILLERAA----TEPSGRKPAA--LRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThQVTTTQIEGIGQT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 -------GTVGKPlPCVEAKIIMEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFI 516
Cdd:PRK05852 348 enpvvstGLVGRS-TGAQIRIVGSDGLPlPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 517 ILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWS 596
Cdd:PRK05852 426 IRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA----------PPTAEELVQFC 494
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002235085 597 KDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLG 633
Cdd:PRK05852 495 RERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFG 531
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
261-632 |
6.16e-56 |
|
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: 192.55 E-value: 6.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFnALFAPLYSGSVvefmpkFSVRG 340
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAE------LVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRWRESYPNNGskndeaITVFTGVPTMYTRLLQgyDGMDPEqqsassfAAKQLRLMMCGSSALPSPLMKRWEEvTGHR 420
Cdd:cd17630 74 RNQALAEDLAPPG------VTHVSLVPTQLQRLLD--SGQGPA-------ALKSLRAVLLGGAPIPPELLERAAD-RGIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 421 LLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIimedgaettSEVGELCIRSPSLFKEYWRKPEVtaESFIDGGF 500
Cdd:cd17630 138 LYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRI---------VEDGEIWVGGASLAMGYLRGQLV--PEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 501 FKTGDTVTVDDEGYFIILGRtnADIMKV-GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedskkra 579
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGR--ADNMIIsGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--------- 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 580 eldSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:cd17630 276 ---GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
260-629 |
2.11e-54 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 194.66 E-value: 2.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQ----------FLHCLPLHHVHGLFNALFAPLYSGS- 328
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGqplmkegqevMIAPLPLYHIYAFTANCMCMMVSGNh 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 -VVEFMPKfSVRGI---WQRWResypnngskndeaITVFTGVPTMYTRLlqgydgMDPEQQSASSFAAkqLRLMMCGSSA 404
Cdd:PRK12492 287 nVLITNPR-DIPGFikeLGKWR-------------FSALLGLNTLFVAL------MDHPGFKDLDFSA--LKLTNSGGTA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 405 LPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETT-SEVGELCIRSPSLFK 482
Cdd:PRK12492 345 LVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPlGERGELCIKGPQVMK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 483 EYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:PRK12492 425 GYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSG 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 563 EIICAIIVPKEdskkraeldskPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK12492 504 EAVKLFVVARD-----------PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
155-634 |
6.38e-54 |
|
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: 192.67 E-value: 6.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 155 SPEFVAGIFGTWLSGgvAVP-LAL-SYPEAELLHVMNDSDISLILSTKEH-----QDIMENISTKCsahcsllPSVTSIP 227
Cdd:COG1021 85 VAEFVIVFFALFRAG--AIPvFALpAHRRAEISHFAEQSEAVAYIIPDRHrgfdyRALARELQAEV-------PSLRHVL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VNIDCQEpsstevTSSISSLIAEIDSSKEIR--GDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFL 305
Cdd:COG1021 156 VVGDAGE------FTSLDALLAAPADLSEPRpdPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 306 HCLPLHHvhglfNA------LFAPLYSGSVVEFMPKFSvrgiwqrwresyPnngsknDEA--------ITVFTGVPTMYT 371
Cdd:COG1021 230 AALPAAH-----NFplsspgVLGVLYAGGTVVLAPDPS------------P------DTAfpliererVTVTALVPPLAL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 372 RLLQgydgmDPEQQSA--SSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfvmALSN------PLHgaRK 443
Cdd:COG1021 287 LWLD-----AAERSRYdlSS-----LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GLVNytrlddPEE--VI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 444 EGTVGKPL-PCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRT 521
Cdd:COG1021 352 LTTQGRPIsPDDEVRIVDEDGNPVPPgEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 522 NaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldskPALTLEALTSWSKDK-L 600
Cdd:COG1021 432 K-DQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRG-----------EPLTLAELRRFLRERgL 499
|
490 500 510
....*....|....*....|....*....|....
gi 1002235085 601 APYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:COG1021 500 AAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
145-631 |
9.79e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 190.02 E-value: 9.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQD-----IMENISTKCSA---- 215
Cdd:PRK08315 68 GDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDsdyvaMLYELAPELATcepg 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 216 --HCSLLPSVTSIpVNIDCQEPSSTEVTSSISSLIAEIDS------SKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVS 287
Cdd:PRK08315 148 qlQSARLPELRRV-IFLGDEKHPGMLNFDELLALGRAVDDaelaarQATLDPDDPINIQYTSGTTGFPKGATLTHRNILN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 288 QVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGS-----VVEFMPKFSVRGIwqrwresypnngskNDEAITV 362
Cdd:PRK08315 227 NGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAtmvypGEGFDPLATLAAV--------------EEERCTA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 363 FTGVPTMYTRLLQgydgmDPEqqsASSFAAKQLRL-MMCGSSAlPSPLMKR------WEEVTghrllERYGMTE-----F 430
Cdd:PRK08315 293 LYGVPTMFIAELD-----HPD---FARFDLSSLRTgIMAGSPC-PIEVMKRvidkmhMSEVT-----IAYGMTEtspvsT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 431 VMALSNPLHgaRKEGTVGKPLPCVEAKIIMEDGAET--TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVT 508
Cdd:PRK08315 359 QTRTDDPLE--KRVTTVGRALPHLEVKIVDPETGETvpRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAV 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 509 VDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALT 588
Cdd:PRK08315 437 MDEEGYVNIVGR-IKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA----------TLT 505
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1002235085 589 LEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK08315 506 EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-629 |
1.19e-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: 187.65 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGG----VAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMEnistkcsah 216
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 217 csllpsvtsiPVNIDCQEPSSTEVTSSISSLIAEIDSsKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAW 296
Cdd:cd05922 85 ----------DALPASPDPGTVLDADGIRAARASAPA-HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 297 GYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKfsvRGIWQRWRESypnngskndeAITVFTGVPTMYTRL 373
Cdd:cd05922 154 GITADDRALTVLPLSYDYGLSVLNTHLLRGATLVltnDGVLD---DAFWEDLREH----------GATGLAGVPSTYAML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LQGydGMDPEqqsassfAAKQLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEF--VMALSNPLHGARKEGTVGKP 450
Cdd:cd05922 221 TRL--GFDPA-------KLPSLRYLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 451 LPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVG 529
Cdd:cd05922 292 IPGGEFEILDDDGTPTpPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGR-RDRMIKLF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 530 GYKLSALEIESVLLQHEIVLECAVLGLPDEAyGEIICAIIVpkedskkraeldSKPALTLEALTSWSKDKLAPYKIPTRL 609
Cdd:cd05922 371 GNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVT------------APDKIDPKDVLRSLAERLPPYKVPATV 437
|
490 500
....*....|....*....|
gi 1002235085 610 YLWDSLPRNAMGKVNKKELK 629
Cdd:cd05922 438 RVVDELPLTASGKVDYAALR 457
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
144-631 |
1.33e-52 |
|
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: 188.31 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 144 GGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQ-------------------- 203
Cdd:cd05909 30 EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIeklklhhlfdveydarivyl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 204 -DIMENIST--KCSA--HCSLLPSVTSIPVNIDCQEPsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGV 278
Cdd:cd05909 110 eDLRAKISKadKCKAflAGKFPPKWLLRIFGVAPVQP------------------------DDPAVILFTSGSEGLPKGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 279 VHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKfsvrgiwqrwresyPNNGSKNDE 358
Cdd:cd05909 166 VLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPN--------------PLDYKKIPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 359 AI-----TVFTGVPTmytrLLQGYdgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF--V 431
Cdd:cd05909 232 LIydkkaTILLGTPT----FLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 432 MALSNPlHGARKEGTVGKPLPCVEAKIIMEDGAETTS--EVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTV 509
Cdd:cd05909 302 ISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPigEGGLLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 510 DDEGYFIILGRTNAdIMKVGGYKLSALEIESVLLQH-EIVLECAVLGLPDEAYGEIICAIIVPKEDSkkRAELDskpalt 588
Cdd:cd05909 380 DGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTD--PSSLN------ 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1002235085 589 lEALTSWSKDKLApykIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:cd05909 451 -DILKNAGISNLA---KPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
256-629 |
1.58e-52 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 189.49 E-value: 1.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 256 EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVqiLSEAWGY-----RSEDQFLHCLPLHHVHGL-FNAL-FAPLYSGS 328
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHIFALtVNCLlFIELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 VVEFMPkfsvRGIWQRWRE--SYPnngskndeaITVFTGVPTMYTRLLQGydgmdpEQQSASSFAAkqLRLMMCGSSALP 406
Cdd:PRK08974 280 LLITNP----RDIPGFVKElkKYP---------FTAITGVNTLFNALLNN------EEFQELDFSS--LKLSVGGGMAVQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 407 SPLMKRWEEVTGHRLLERYGMTE---FVMAlsNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFK 482
Cdd:PRK08974 339 QAVAERWVKLTGQYLLEGYGLTEcspLVSV--NPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPgEPGELWVKGPQVML 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 483 EYWRKPEVTAEsFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:PRK08974 417 GYWQRPEATDE-VIKDGWLATGDIAVMDEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSG 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 563 EIICAIIVPKEDSkkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK08974 495 EAVKIFVVKKDPS-----------LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-625 |
1.97e-52 |
|
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: 183.47 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG 340
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRwresypnngsKNDEAITVFTGVPTMYTRLLqgydgmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKRW-EEVTGH 419
Cdd:cd17638 81 ILEA----------IERERITVLPGPPTLFQSLL--------DHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 RLLERYGMTEFVMA-LSNPLHGARK-EGTVGKPLPCVEAKIimedgaettSEVGELCIRSPSLFKEYWRKPEVTAESFID 497
Cdd:cd17638 143 TVLTAYGLTEAGVAtMCRPGDDAETvATTCGRACPGFEVRI---------ADDGEVLVRGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 498 GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkk 577
Cdd:cd17638 214 DGWLHTGDVGELDERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV-- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1002235085 578 raeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 625
Cdd:cd17638 291 --------TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
155-630 |
3.80e-52 |
|
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: 185.80 E-value: 3.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 155 SPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimenistkcsahcsllpsvtsipvnidcqe 234
Cdd:cd05973 35 TPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAANRH------------------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 235 psstevtssissliaEIDSskeirgdDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVH 314
Cdd:cd05973 85 ---------------KLDS-------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 315 GLFNALFAPLYSGSVVEFMP-KFSVRGIWQRWRESypnngskndeAITVFTGVPTMYTRLLQGydgmdpeqqSASSFAAK 393
Cdd:cd05973 143 GLYYAITGPLALGHPTILLEgGFSVESTWRVIERL----------GVTNLAGSPTAYRLLMAA---------GAEVPARP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 394 QLRLMMCGSSALP-SPLMKRWEEVT-GHRLLERYGMTEFVMALSNPLHGAR--KEGTVGKPLPCVEAKIIMEDGAETT-S 468
Cdd:cd05973 204 KGRLRRVSSAGEPlTPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGpG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 469 EVGELCI---RSPSL-FKEYWRKPEVTaesfIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQ 544
Cdd:cd05973 284 EPGRLAIdiaNSPLMwFRGYQLPDTPA----IDGGYYLTGDTVEFDPDGSFSFIGRAD-DVITMSGYRIGPFDVESALIE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 545 HEIVLECAVLGLPDEAYGEIICAIIVpkedskKRAELDSKPALTlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 624
Cdd:cd05973 359 HPAVAEAAVIGVPDPERTEVVKAFVV------LRGGHEGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQ 431
|
....*.
gi 1002235085 625 KKELKK 630
Cdd:cd05973 432 RFLLRR 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
256-629 |
1.11e-51 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 187.39 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 256 EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSeAW----GYRSEDQ--FLHCLPLHHVHGLF-NALFAPLYSG- 327
Cdd:PRK08751 204 QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAH-QWlagtGKLEEGCevVITALPLYHIFALTaNGLVFMKIGGc 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 328 ----SVVEFMPKFsVRGIwQRWResypnngskndeaITVFTGVPTMYTRLLQ--GYDGMDpeqqsassFAAkqLRLMMCG 401
Cdd:PRK08751 283 nhliSNPRDMPGF-VKEL-KKTR-------------FTAFTGVNTLFNGLLNtpGFDQID--------FSS--LKMTLGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 402 SSALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKEGTVGKPLPCVEAKIIMEDG-AETTSEVGELCIRSPS 479
Cdd:PRK08751 338 GMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGtVLAIGEIGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 480 LFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDE 559
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 560 AYGEIICAIIVPKEdskkraeldskPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK08751 497 KSGEIVKVVIVKKD-----------PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
260-634 |
1.81e-51 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 186.41 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSG-SVVefmpkfsV 338
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGaTAV-------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 339 RGIWQRWRESypnnGSKNDEAITvFTGVPTMYTrllqgYDGMDPEQQSASSFAakQLRLMMCGSSALPSPLMKRWEEVTG 418
Cdd:PRK13295 270 QDIWDPARAA----ELIRTEGVT-FTMASTPFL-----TDLTRAVKESGRPVS--SLRTFLCAGAPIPGALVERARAALG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 419 HRLLERYGMTE----FVMALSNPLHgaRKEGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAE 493
Cdd:PRK13295 338 AKIVSAWGMTEngavTLTKLDDPDE--RASTTDGCPLPGVEVRVVDADGAPLPAgQIGRLQVRGCSNFGGYLKRPQLNGT 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 494 SFidGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKE 573
Cdd:PRK13295 416 DA--DGWFDTGDLARIDADGYIRISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRP 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 574 DSkkraeldskpALTLEALTSWSKD-KLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK13295 493 GQ----------SLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
261-625 |
2.97e-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: 180.16 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLfNALFAPLYSG--SVVefMPKFSv 338
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGgaNVV--MEKFD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 339 rgiwqrwresyPNNGSK--NDEAITVFTGVPTMYTRLLqgydgmdpEQQSASSFAAKQLRLMmcgsSALPSP-LMKRWEE 415
Cdd:cd17637 77 -----------PAEALEliEEEKVTLMGSFPPILSNLL--------DAAEKSGVDLSSLRHV----LGLDAPeTIQRFEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 416 VTGHRLLERYGMTEFVMALSnpLHGAR-KEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAE 493
Cdd:cd17637 134 TTGATFWSLYGQTETSGLVT--LSPYReRPGSAGRPGPLVRVRIVDDNDRPVpAGETGEIVVRGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 494 SFiDGGFFKTGDTVTVDDEGYFIILGRTNA-DIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPK 572
Cdd:cd17637 212 TF-RNGWHHTGDLGRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 573 EDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 625
Cdd:cd17637 291 PGA----------TLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
148-628 |
2.97e-51 |
|
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: 184.45 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILsTKEHQDIMENISTKCsahcsllpsvtsip 227
Cdd:cd17655 50 VGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL-TQSHLQPPIAFIGLI-------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VNIDCQEPSSTEVTSsissliAEIDSskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAwGYRSE-DQFLH 306
Cdd:cd17655 115 DLLDEDTIYHEESEN------LEPVS----KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV-IYQGEhLRVAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 307 CLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGIwQRWRESYpnngskNDEAITVFTGVPTmytrLLQGYDGMDp 382
Cdd:cd17655 184 FASIS-----FDAsvteIFASLLSGNTLYIVRKETVLDG-QALTQYI------RQNRITIIDLTPA----HLKLLDAAD- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 383 eqqsasSFAAKQLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTE-FVMALSNPLHGARKEGT---VGKPLPCVEA 456
Cdd:cd17655 247 ------DSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTEtTVDASIYQYEPETDQQVsvpIGKPLGNTRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEDG-AETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNADImKVG 529
Cdd:cd17655 321 YILDQYGrPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQV-KIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 530 GYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkraeldskpaLTLEALTSWSKDKLAPYKIPTRL 609
Cdd:cd17655 400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE------------LPVAQLREFLARELPDYMIPSYF 467
|
490
....*....|....*....
gi 1002235085 610 YLWDSLPRNAMGKVNKKEL 628
Cdd:cd17655 468 IKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
256-629 |
3.33e-51 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 185.99 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 256 EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVqILSEAW------GYRSEDQ--FLHCLPLHHVHGL-FNALFApLYS 326
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANV-LQMEAWlqpafeKKPRPDQlnFVCALPLYHIFALtVCGLLG-MRT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 327 GSVVEFMPkfSVRGIWQRWRE--SYPnngskndeaITVFTGVPTMYTRLLQ--GYDGMDpeqqsassfaAKQLRLMMCGS 402
Cdd:PRK07059 278 GGRNILIP--NPRDIPGFIKElkKYQ---------VHIFPAVNTLYNALLNnpDFDKLD----------FSKLIVANGGG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSL 480
Cdd:PRK07059 337 MAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLpLGEPGEICIRGPQV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 481 FKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEA 560
Cdd:PRK07059 417 MAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002235085 561 YGEIICAIIVPKEdskkraeldskPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK07059 496 SGEAVKLFVVKKD-----------PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
137-628 |
3.56e-51 |
|
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: 183.22 E-value: 3.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 137 INGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcsah 216
Cdd:cd05945 33 LASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAD----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 217 csllpsvtsipvnidcqepsstevtssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAW 296
Cdd:cd05945 96 ------------------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 297 GYRSEDQFLHCLPLH---HVHGLFNALFaplySGSVVEFMPKfSVRGIWQRWRESYPNNGskndeaITVFTGVPTMYTRL 373
Cdd:cd05945 134 PLGPGDVFLNQAPFSfdlSVMDLYPALA----SGATLVPVPR-DATADPKQLFRFLAEHG------ITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LqgydgMDPEQQSASSfaaKQLRLMM-CGSsALPSPLMKRWEEVT-GHRLLERYGMTEFVMALS------NPLHGArKEG 445
Cdd:cd05945 203 L-----LSPTFTPESL---PSLRHFLfCGE-VLPHKTARALQQRFpDARIYNTYGPTEATVAVTyievtpEVLDGY-DRL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 446 TVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESF--IDG-GFFKTGDTVTVDDEGYFIILGRT 521
Cdd:cd05945 273 PIGYAKPGAKLVILDEDGRPVPPgEKGELVISGPSVSKGYLNNPEKTAAAFfpDEGqRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 522 NADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldSKPALTLEALTSWSKDKLA 601
Cdd:cd05945 353 DFQV-KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP---------GAEAGLTKAIKAELAERLP 422
|
490 500
....*....|....*....|....*..
gi 1002235085 602 PYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd05945 423 PYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
145-629 |
6.91e-51 |
|
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: 190.45 E-value: 6.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimenistkcsahcsLLPSVT 224
Cdd:COG1020 526 GDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAA--------------RLPELG 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSSISsliaeidsskEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:COG1020 592 VPVLALDALALAAEPATNPPV----------PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGI--WQRWREsypnngsknDEAITVFTGVPTMYTRLLQGyd 378
Cdd:COG1020 662 LQFASLS-----FDAsvweIFGALLSGATLVLAPPEARRDPaaLAELLA---------RHRVTVLNLTPSLLRALLDA-- 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmDPEQQSassfaakQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEF-VMALSNPLHGARKEG---TVGKPLPC 453
Cdd:COG1020 726 --APEALP-------SLRLVLVGGEALPPELVRRWRARLPGaRLVNLYGPTETtVDSTYYEVTPPDADGgsvPIGRPIAN 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKIIME------DGAettseVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGR 520
Cdd:COG1020 797 TRVYVLDAhlqpvpVGV-----PGELYIGGAGLARGYLNRPELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGR 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 521 tNADIMKVGGYK--LSalEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPkedskkRAELDSKPALTLEALtswsKD 598
Cdd:COG1020 872 -ADDQVKIRGFRieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP------EAGAAAAAALLRLAL----AL 938
|
490 500 510
....*....|....*....|....*....|.
gi 1002235085 599 KLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:COG1020 939 LLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
145-630 |
1.12e-50 |
|
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: 183.82 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKC-SAHCSLLPSv 223
Cdd:cd05928 67 GDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECpSLKTKLLVS- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 224 tsipvnidcqePSSTEVTSSISSLIAEIDSSK---EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAW-GYR 299
Cdd:cd05928 146 -----------EKSRDGWLNFKELLNEASTEHhcvETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 300 SEDQFLHCLPLHHVHGLFNALFAPLYSGSVV--EFMPKFSVRGIWQRWrESYPnngskndeaITVFTGVPTMYTRLLQgy 377
Cdd:cd05928 215 ASDIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHHLPRFDPLVILKTL-SSYP---------ITTFCGAPTVYRMLVQ-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 378 dgmdpeqQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAK 457
Cdd:cd05928 283 -------QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 IIMEDGAETTS-EVGELCIR-SP----SLFKEYWRKPEVTAESfIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGY 531
Cdd:cd05928 356 IIDDNGNVLPPgTEGDIGIRvKPirpfGLFSGYVDNPEKTAAT-IRGDFYLTGDRGIMDEDGYFWFMGRAD-DVINSSGY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 532 KLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAeldsKPALTLEaLTSWSKDKLAPYKIPTRLYL 611
Cdd:cd05928 434 RIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHD----PEQLTKE-LQQHVKSVTAPYKYPRKVEF 508
|
490
....*....|....*....
gi 1002235085 612 WDSLPRNAMGKVNKKELKK 630
Cdd:cd05928 509 VQELPKTVTGKIQRNELRD 527
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
260-630 |
2.28e-50 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 183.85 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALfAPLYSGSVVEFMPKFSVR 339
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 GIWQRWResypnngsknDEAITVFTGVPTMYTRLLQgydgmdPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEV-TG 418
Cdd:PLN02860 251 AALQAIK----------QHNVTSMITVPAMMADLIS------LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 419 HRLLERYGMTE------FvMALSNP-----------------LHGARKEGT-VGKPLPCVEAKIIMEDgaetTSEVGELC 474
Cdd:PLN02860 315 AKLFSAYGMTEacssltF-MTLHDPtlespkqtlqtvnqtksSSVHQPQGVcVGKPAPHVELKIGLDE----SSRVGRIL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 475 IRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVL 554
Cdd:PLN02860 390 TRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRI-KTGGENVYPEEVEAVLSQHPGVASVVVV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 555 GLPDEAYGEIICAIIVPKED---SKKRAELDSKP-ALTLEALTSW-SKDKLAPYKIPTRLYLW-DSLPRNAMGKVNKKEL 628
Cdd:PLN02860 469 GVPDSRLTEMVVACVRLRDGwiwSDNEKENAKKNlTLSSETLRHHcREKNLSRFKIPKLFVQWrKPFPLTTTGKIRRDEV 548
|
..
gi 1002235085 629 KK 630
Cdd:PLN02860 549 RR 550
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
141-629 |
2.56e-50 |
|
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: 181.03 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcsahcsll 220
Cdd:cd17649 33 GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTH--------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 psvtsipvnidcqepsstevtssissliaeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRS 300
Cdd:cd17649 92 -------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLhHVHGLFNALFAPLYSGSVVEFMPKfsvrgiwQRWRESYPNNGSKNDEAITVfTGVPTMYTRLLQgyDGM 380
Cdd:cd17649 135 GDRELQFASF-NFDGAHEQLLPPLICGACVVLRPD-------ELWASADELAEMVRELGVTV-LDLPPAYLQQLA--EEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSassfAAKQLRLMMCGSSALPSPLMKRWeEVTGHRLLERYGMTEFVMA--LSNPLHGARKEGT---VGKPLPCVE 455
Cdd:cd17649 204 DRTGDG----RPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVTplVWKCEAGAARAGAsmpIGRPLGGRS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 AKIIMEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFF-------KTGDTVTVDDEGYFIILGRTNADImK 527
Cdd:cd17649 279 AYILDADLNPvPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGapgsrlyRTGDLARWRDDGVIEYLGRVDHQV-K 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 528 VGGYKLSALEIESVLLQHEIVLECAVLGLPDeAYGEIICAIIVPKEDSKKraeldskpALTLEALTSWSKDKLAPYKIPT 607
Cdd:cd17649 358 IRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQLVAYVVLRAAAAQ--------PELRAQLRTALRASLPDYMVPA 428
|
490 500
....*....|....*....|..
gi 1002235085 608 RLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd17649 429 HLVFLARLPLTPNGKLDRKALP 450
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
261-628 |
2.65e-50 |
|
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: 181.76 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHH-----VHGLFNALFAplySGSVVeFMPK 335
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplaCPGVLGTLLA---GGRVV-LAPD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 336 FS---VRGIWQRwresypnngskndEAITVFTGVPTMYTRLLQGYDGMDPEQQSassfaakqLRLMMCGSSALPSPLMKR 412
Cdd:cd05920 216 PSpdaAFPLIER-------------EGVTVTALVPALVSLWLDAAASRRADLSS--------LRLLQVGGARLSPALARR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 413 WEEVTGHRLLERYGMTEFVM---ALSNPlhGARKEGTVGKPL-PCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRK 487
Cdd:cd05920 275 VPPVLGCTLQQVFGMAEGLLnytRLDDP--DEVIIHTQGRPMsPDDEIRVVDEEGNPVPPgEEGELLTRGPYTIRGYYRA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 488 PEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICA 567
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 568 IIVPKEdskkraeldskPALTLEALTSWSKDK-LAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd05920 432 FVVLRD-----------PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
145-629 |
4.64e-49 |
|
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: 179.61 E-value: 4.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhQDIMENIStkcsahcSLLPSVT 224
Cdd:cd05970 72 GDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE-DNIPEEIE-------KAAPECP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPssteVTSSISSLIAEIDSSKEI----------RGDDPALILYTSGTTGKPKGVVHTHKGIVSQVqILSE 294
Cdd:cd05970 144 SKPKLVWVGDP----VPEGWIDFRKLIKNASPDferptansypCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHI-VTAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 295 AWGYRSEDQflhclpLHHV---HGLFNALFAPLY----SGSVVeF---MPKFSVRGIWQRWresypnngSKNDeaITVFT 364
Cdd:cd05970 219 YWQNVREGG------LHLTvadTGWGKAVWGKIYgqwiAGAAV-FvydYDKFDPKALLEKL--------SKYG--VTTFC 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 365 GVPTMYTRLLQgydgmdpeqQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKE 444
Cdd:cd05970 282 APPTIYRFLIR---------EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 GTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPS-----LFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIIL 518
Cdd:cd05970 353 GSMGKPAPGYEIDLIDREGRSCeAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDG-YYHTGDAAWMDEDGYLWFV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 519 GRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELDSKpaltleaLTSWSKD 598
Cdd:cd05970 432 GRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKE-------LQDHVKK 503
|
490 500 510
....*....|....*....|....*....|.
gi 1002235085 599 KLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05970 504 VTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
145-628 |
5.02e-49 |
|
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: 178.16 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKehqdimenistkcsahcSLLPSVT 224
Cdd:cd12117 47 GDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDR-----------------SLAGRAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSSISSLIAeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVqiLSEAWG-YRSEDQ 303
Cdd:cd12117 110 GLEVAVVIDEALDAGPAGNPAVPVS---------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV--KNTNYVtLGPDDR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 304 FLHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGIwQRWRESYPNNGskndeaITVF---TGVPTMYTRLlqg 376
Cdd:cd12117 179 VLQTSPLA-----FDAstfeIWGALLNGARLVLAPKGTLLDP-DALGALIAEEG------VTVLwltAALFNQLADE--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 377 ydgmDPEqqsasSFAakQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTE---FVMALSNPlHGARKEGTV--GKP 450
Cdd:cd12117 244 ----DPE-----CFA--GLRELLTGGEVVSPPHVRRVLAACPGlRLVNGYGPTEnttFTTSHVVT-ELDEVAGSIpiGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 451 LPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNa 523
Cdd:cd12117 312 IANTRVYVLDEDGRPVpPGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRID- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 524 DIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldskpALTLEALTSWSKDKLAPY 603
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG------------ALDAAELRAFLRERLPAY 458
|
490 500
....*....|....*....|....*
gi 1002235085 604 KIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd12117 459 MVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
258-628 |
6.98e-49 |
|
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: 178.09 E-value: 6.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 258 RGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYR--SEDQFLHCLPLHHVHGLFNALFAPLYSGS----VVE 331
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGtyvvVEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 332 FMPKFSVRGIWQrwresypnngskndEAITVFTGVPTMYTRLLqgydgmdpeqqSASSFAA---KQLRLMMCGSSALPSP 408
Cdd:cd05923 228 FDPADALKLIEQ--------------ERVTSLFATPTHLDALA-----------AAAEFAGlklSSLRHVTFAGATMPDA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 LMKRWEEVTGHRLLERYGMTEFVMALSNPlhgARKEGTVGKPLPCVEAKII----MEDGAETTSEVGELCIR--SPSLFK 482
Cdd:cd05923 283 VLERVNQHLPGEKVNIYGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVriggSPDEALANGEEGELIVAaaADAAFT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 483 EYWRKPEVTAESFIDGGFFkTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:cd05923 360 GYLNQPEATAKKLQDGWYR-TGDVGYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWG 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002235085 563 EIICAIIVPKEDSKKRAELDSKpaltleALTSwskdKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd05923 438 QSVTACVVPREGTLSADELDQF------CRAS----ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
141-629 |
7.70e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 178.16 E-value: 7.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIG---IVA---KPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDImenistkcs 214
Cdd:PRK06145 42 GMLHARGIGqgdVVAllmKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAI--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 215 ahcsllPSVTSIPVNIDCQEPSSTEVTSSISSLIAEIDSSKEirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSE 294
Cdd:PRK06145 113 ------VALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAP---TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 295 AWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQrwresypnngSKNDEAITVFTGVPTMYTRLL 374
Cdd:PRK06145 184 ALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA----------AIERHRLTCAWMAPVMLSRVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 375 QGydgmdPEQQSassFAAKQLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEFVMAlsNPLHGARKE----GTVGK 449
Cdd:PRK06145 254 TV-----PDRDR---FDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCSG--DTLMEAGREiekiGSTGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 450 PLPCVEAKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFIdGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV 528
Cdd:PRK06145 324 ALAHVEIRIADGAGRWLPPNMkGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKK-DMIIS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedskkraeLDSKPALTLEALTSWSKDKLAPYKIPTR 608
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV----------LNPGATLTLEALDRHCRQRLASFKVPRQ 471
|
490 500
....*....|....*....|.
gi 1002235085 609 LYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK06145 472 LKVRDELPRNPSGKVLKRVLR 492
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
145-629 |
1.93e-48 |
|
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: 175.31 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPL-ALSYPEAeLLHVMNDSDISLILStkehqdimenistkcsahcsllpsv 223
Cdd:cd05971 31 GDRVGVFLSQGPECAIAHIAILRSGAIAVPLfALFGPEA-LEYRLSNSGASALVT------------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 224 tsipvnidcqepsstevtssissliaeiDSSkeirgDDPALILYTSGTTGKPKGVVHTHK---GIVSQVQILSEAWGyRS 300
Cdd:cd05971 85 ----------------------------DGS-----DDPALIIYTSGTTGPPKGALHAHRvllGHLPGVQFPFNLFP-RD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNALFAPLYSG-SVVEF-MPKFSVRGIWQ---RWResypnngskndeAITVFtgVPTMYTRLLQ 375
Cdd:cd05971 131 GDLYWTPADWAWIGGLLDVLLPSLYFGvPVLAHrMTKFDPKAALDlmsRYG------------VTTAF--LPPTALKMMR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 376 gydgmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGARKEGTVGKPLPCV 454
Cdd:cd05971 197 -------QQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNcSALFPIKPGSMGKPIPGH 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 EAKIIMEDGAETT-SEVGELCIRSPS--LFKEYWRKPEVTAESFIdGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGY 531
Cdd:cd05971 270 RVAIVDDNGTPLPpGEVGEIAVELPDpvAFLGYWNNPSATEKKMA-GDWLLTGDLGRKDSDGYFWYVGRDD-DVITSSGY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 532 KLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELDskpaltlEALTSWSKDKLAPYKIPTRLYL 611
Cdd:cd05971 348 RIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA-------REIQELVKTRLAAHEYPREIEF 420
|
490
....*....|....*...
gi 1002235085 612 WDSLPRNAMGKVNKKELK 629
Cdd:cd05971 421 VNELPRTATGKIRRRELR 438
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
145-632 |
5.34e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 176.39 E-value: 5.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkeHQDIMENISTkCSAHCSLLPSVT 224
Cdd:PRK07470 57 GDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC---HADFPEHAAA-VRAASPDLTHVV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIpvnidcqepSSTEVTSSISSLIAEIDSSK----EIRGDDPALILYTSGTTGKPKGVVHTHK--GIVSQVQILSEAWGY 298
Cdd:PRK07470 133 AI---------GGARAGLDYEALVARHLGARvanaAVDHDDPCWFFFTSGTTGRPKAAVLTHGqmAFVITNHLADLMPGT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLHCLPLHH---VHGLFNALFAplySGSVVEFMPKFSVRGIWQ---RWRESypnngskndeaiTVFTgVPTMYTR 372
Cdd:PRK07470 204 TEQDASLVVAPLSHgagIHQLCQVARG---AATVLLPSERFDPAEVWAlveRHRVT------------NLFT-VPTILKM 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 373 LLqgydgmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF---VMALSNPLHGAR-----KE 444
Cdd:PRK07470 268 LV--------EHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVtgnITVLPPALHDAEdgpdaRI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 GTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIILGRTnA 523
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGRELpPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-WFRTGDLGHLDARGFLYITGRA-S 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 524 DIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPY 603
Cdd:PRK07470 418 DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA----------PVDEAELLAWLDGKVARY 487
|
490 500
....*....|....*....|....*....
gi 1002235085 604 KIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PRK07470 488 KLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
145-629 |
1.51e-47 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 175.33 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFG-TWLsGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMEnistkcsahcSLLPSV 223
Cdd:PRK06155 71 GDRVALMCGNRIEFLDVFLGcAWL-GAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALE----------AADPGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 224 TSIPVNIDCQEPSSTEV-----TSSISSLIAEIDSSkEIRGDDPALILYTSGTTGKPKGVVHTHK-----GIVSqvqilS 293
Cdd:PRK06155 140 LPLPAVWLLDAPASVSVpagwsTAPLPPLDAPAPAA-AVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwGRNS-----A 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGIWQRWRESypnngskndeAITVFTGVPTMYTRL 373
Cdd:PRK06155 214 EDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSASGFWPAVRRH----------GATVTYLLGAMVSIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LQgydgmDPEQQSASsfaAKQLRLMMCGssALPSPLMKRWEEVTGHRLLERYGMTE--FVMALSnplHGARKEGTVGKPL 451
Cdd:PRK06155 283 LS-----QPARESDR---AHRVRVALGP--GVPAALHAAFRERFGVDLLDGYGSTEtnFVIAVT---HGSQRPGSMGRLA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 452 PCVEAKIIMEDGAETTS-EVGELCIRS--PSLFKE-YWRKPEVTAESFIDGgFFKTGDTVTVDDEGYFIILGRTNaDIMK 527
Cdd:PRK06155 350 PGFEARVVDEHDQELPDgEPGELLLRAdePFAFATgYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIK-DAIR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 528 VGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPT 607
Cdd:PRK06155 428 RRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGT----------ALEPVALVRHCEPRLAYFAVPR 497
|
490 500
....*....|....*....|..
gi 1002235085 608 RLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK06155 498 YVEFVAALPKTENGKVQKFVLR 519
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
145-628 |
1.55e-47 |
|
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: 173.63 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehQDIMENISTKCSAHCSLLPSVT 224
Cdd:cd12116 37 GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD---DALPDRLPAGLPVLLLALAAAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPvnidcqEPSSTEVTssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd12116 114 AAP------AAPRTPVS-----------------PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCL-PLHHVHGLfnALFAPLYSGSVVEFMPKFSVRGiwqrwresypnnGSK-----NDEAITVFTGVPTMYTRLLqgyd 378
Cdd:cd12116 171 LAVTtYAFDISLL--ELLLPLLAGARVVIAPRETQRD------------PEAlarliEAHSITVMQATPATWRMLL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmDPEQQSASSFAAkqlrlmMCGSSALPSPLMKRWEEVTGhRLLERYGMTE-FVMALSNPLHGARKEGTVGKPLPCVEAK 457
Cdd:cd12116 233 --DAGWQGRAGLTA------LCGGEALPPDLAARLLSRVG-SLWNLYGPTEtTIWSTAARVTAAAGPIPIGRPLANTQVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 IIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTNADImKVG 529
Cdd:cd12116 304 VLDAALRPVpPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQV-KIR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 530 GYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIIcAIIVPKEDskkraeldskPALTLEALTSWSKDKLAPYKIPTRL 609
Cdd:cd12116 383 GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG----------AAPDAAALRAHLRATLPAYMVPSAF 451
|
490
....*....|....*....
gi 1002235085 610 YLWDSLPRNAMGKVNKKEL 628
Cdd:cd12116 452 VRLDALPLTANGKLDRKAL 470
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
140-550 |
5.46e-47 |
|
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: 172.24 E-value: 5.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 140 TGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdimenistkcsahcsl 219
Cdd:cd05914 27 NGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE------------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 lpsvtsipvnidcqepsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYR 299
Cdd:cd05914 89 ----------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 300 SEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIwqrwresypnnGSKNDEAITVFTGVPTMY-------TR 372
Cdd:cd05914 129 KGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-----------IALAFAQVTPTLGVPVPLviekifkMD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 373 LLQGYDG--------MDPEQQSASSFAAKQL--------RLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEFVMALSN 436
Cdd:cd05914 198 IIPKLTLkkfkfklaKKINNRKIRKLAFKKVheafggniKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 437 PLHGARKEGTVGKPLPCVEAKIIMEDGAETTsevGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFI 516
Cdd:cd05914 277 SPPNRIRLGSAGKVIDGVEVRIDSPDPATGE---GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLY 353
|
410 420 430
....*....|....*....|....*....|....
gi 1002235085 517 ILGRTNADIMKVGGYKLSALEIESVLLQHEIVLE 550
Cdd:cd05914 354 IRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLE 387
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
145-628 |
1.67e-45 |
|
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: 167.48 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsahcsllpsvt 224
Cdd:cd17643 37 GDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT-------------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd17643 91 ---------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHClplHH------VHGLFNALfapLYSGSVVefMPKFSVRgiwqRWRESYPNngSKNDEAITVFTGVPTMYTRLLQGYD 378
Cdd:cd17643 138 TLF---HSyafdfsVWEIWGAL---LHGGRLV--VVPYEVA----RSPEDFAR--LLRDEGVTVLNQTPSAFYQLVEAAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 GMDPEQQSassfaakqLRLMMCGSSALPSPLMKRWEEVTGH---RLLERYGMTE---FVM--ALSNPLHGARKEGTVGKP 450
Cdd:cd17643 204 RDGRDPLA--------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITEttvHVTfrPLDAADLPAAAASPIGRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 451 LPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTN 522
Cdd:cd17643 276 LPGLRVYVLDADGRPVpPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 523 ADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAP 602
Cdd:cd17643 356 EQV-KIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGA----------AADIAELRALLKELLPD 424
|
490 500
....*....|....*....|....*.
gi 1002235085 603 YKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17643 425 YMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
261-623 |
3.06e-45 |
|
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: 163.35 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMPKFSVRG 340
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWqRWRESYpnngskndeAITVFTGVPTMYTRLLQGYDgmdPEQQSASSFaakqlrlmmCGSSALPSPLMKRWEEVTGH- 419
Cdd:cd17633 80 WI-RKINQY---------NATVIYLVPTMLQALARTLE---PESKIKSIF---------SSGQKLFESTKKKLKNIFPKa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 RLLERYGMTE--FVMALSNplHGARKEGTVGKPLPCVEAKIIMEDGaettSEVGELCIRSPSLFKEYWRKPEVTAesfid 497
Cdd:cd17633 138 NLIEFYGTSElsFITYNFN--QESRPPNSVGRPFPNVEIEIRNADG----GEIGKIFVKSEMVFSGYVRGGFSNP----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 498 GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskk 577
Cdd:cd17633 207 DGWMSVGDIGYVDEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK---- 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002235085 578 raeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 623
Cdd:cd17633 282 ---------LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
138-634 |
6.33e-45 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 168.48 E-value: 6.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 138 NGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHqdiMENIStkcsahc 217
Cdd:PLN02574 85 HVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPEN---VEKLS------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 218 SLLPSVTSIPVNIDCQEPSSTEVT-SSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS--E 294
Cdd:PLN02574 155 PLGVPVIGVPENYDFDSKRIEFPKfYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 295 AWGYR---SEDQFLHCLPLHHVHGLfnALFAP--LYSGSVVEFMPKFS----VRGIwQRWResypnngskndeaITVFTG 365
Cdd:PLN02574 235 ASQYEypgSDNVYLAALPMFHIYGL--SLFVVglLSLGSTIVVMRRFDasdmVKVI-DRFK-------------VTHFPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 366 VPTMYTRLLQGYDGMdpeqqSASSFaaKQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEFVMALSNPLHGA--R 442
Cdd:PLN02574 299 VPPILMALTKKAKGV-----CGEVL--KSLKQVSCGAAPLSGKFIQDFVQTLPHvDFIQGYGMTESTAVGTRGFNTEklS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 KEGTVGKPLPCVEAKII-MEDGA-ETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGR 520
Cdd:PLN02574 372 KYSSVGLLAPNMQAKVVdWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 521 TNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKL 600
Cdd:PLN02574 452 LK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS----------TLSQEAVINYVAKQV 520
|
490 500 510
....*....|....*....|....*....|....
gi 1002235085 601 APYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
141-629 |
1.35e-44 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 167.38 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdIMENISTKcsahcsLL 220
Cdd:PRK04319 94 GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA---LLERKPAD------DL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIPVnIDcQEPSSTEVTSSISSLIAEIDSSKEIRG---DDPALILYTSGTTGKPKGVVHTHKGIVSQVQilSEAWG 297
Cdd:PRK04319 165 PSLKHVLL-VG-EDVEEGPGTLDFNALMEQASDEFDIEWtdrEDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ--TGKYV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 298 yrsedqflhcLPLHH------------VHGLFNALFAPLYSG--SVV---EFMPkfsvrgiwQRWresYpnnGSKNDEAI 360
Cdd:PRK04319 241 ----------LDLHEddvywctadpgwVTGTSYGIFAPWLNGatNVIdggRFSP--------ERW---Y---RILEDYKV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 361 TVFTGVPTMYTRLLQGydGMDPeqqsASSFAAKQLRLMMCGSSALpSPLMKRW-EEVTGHRLLERYGMTEF--VMaLSNP 437
Cdd:PRK04319 297 TVWYTAPTAIRMLMGA--GDDL----VKKYDLSSLRHILSVGEPL-NPEVVRWgMKVFGLPIHDNWWMTETggIM-IANY 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 438 LHGARKEGTVGKPLPCVEAKIIMEDGAETT-SEVGELCIRS--PSLFKEYWRKPEVTAESFIdGGFFKTGDTVTVDDEGY 514
Cdd:PRK04319 369 PAMDIKPGSMGKPLPGIEAAIVDDQGNELPpNRMGNLAIKKgwPSMMRGIWNNPEKYESYFA-GDWYVSGDSAYMDEDGY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 515 FIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTS 594
Cdd:PRK04319 448 FWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEEL-------KEEIRG 519
|
490 500 510
....*....|....*....|....*....|....*
gi 1002235085 595 WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK04319 520 FVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
77-632 |
3.33e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 164.95 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 77 MEVVQEVLKHGSTQGVHAAIRSDQKS------YNLVQLIASALdvynilrnknmtqnGSTGSSVKgingtgflggaRIGI 150
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVltykdwFESVCKVANWL--------------NEKESKNK-----------TIAI 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 151 VAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHqdiMENIStkcsahcsllpsvtsipvNI 230
Cdd:PRK07638 56 LLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYK---LNDLP------------------DE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 231 DCQEPSSTEVTSSISSLIAEIdSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPL 310
Cdd:PRK07638 115 EGRVIEIDEWKRMIEKYLPTY-APIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 311 HHVHGLFNALFApLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLqgydgmdpeqqSASSF 390
Cdd:PRK07638 194 VHSLFLYGAIST-LYVGQTVHLMRKFIPNQVLDKLET----------ENISVMYTVPTMLESLY-----------KENRV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 391 AAKQLRLMMCGSSaLPSPLMKRWEEVTGH-RLLERYGMTE--FVMALSnPLHGARKEGTVGKPLPCVEAKIIMEDGAET- 466
Cdd:PRK07638 252 IENKMKIISSGAK-WEAEAKEKIKNIFPYaKLYEFYGASElsFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVq 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 467 TSEVGELCIRSPSLFKEYwRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMkVGGYKLSALEIESVLLQHE 546
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMIL-FGGINIFPEEIESVLHEHP 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 547 IVLECAVLGLPDEAYGEIICAIIVPKEDSKKraeldskpaltleaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKK 626
Cdd:PRK07638 408 AVDEIVVIGVPDSYWGEKPVAIIKGSATKQQ--------------LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
....*.
gi 1002235085 627 ELKKLL 632
Cdd:PRK07638 474 EAKSWI 479
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-559 |
3.74e-44 |
|
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: 165.87 E-value: 3.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLAL--SYPEAE-LLHVMNDSDISLILSTKEHQDimenistkcsahcsllp 221
Cdd:cd05931 48 GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptPGRHAErLAAILADAGPRVVLTTAAALA----------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 222 SVTSIPVNIDCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE 301
Cdd:cd05931 111 AVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 302 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFS-VR--GIWQRWRESYPNngskndeaitVFTGVPTMytrllqGYD 378
Cdd:cd05931 191 DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAfLRrpLRWLRLISRYRA----------TISAAPNF------AYD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 ----GMDPEQQSA---SSfaakqLRLMMCGSSALPSPLMKRWEE------------------------VTGHRLLERYGM 427
Cdd:cd05931 255 lcvrRVRDEDLEGldlSS-----WRVALNGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfVSGGPPGTGPVV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 428 TEF-VMALSNPLHGARKEGT-------VGKPLPCVEAKIIMEDGAETTS--EVGELCIRSPSLFKEYWRKPEVTAESFI- 496
Cdd:cd05931 330 LRVdRDALAGRAVAVAADDPaarelvsCGRPLPDQEVRIVDPETGRELPdgEVGEIWVRGPSVASGYWGRPEATAETFGa 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002235085 497 -----DGGFFKTGDTVTVDDeGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIVLE---CAVLGLPDE 559
Cdd:cd05931 410 laatdEGGWLRTGDLGFLHD-GELYITGRL-KDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDD 478
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
260-630 |
1.08e-43 |
|
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: 163.24 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVsqVQILSEA--WGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFS 337
Cdd:cd12118 133 WDPIALNYTSGTTGRPKGVVYHHRGAY--LNALANIleWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNV-CLRKVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 338 VRGIWQRWREsypnngskndEAITVFTGVPTMYTRLLqgyDGMDPEQQSASsfaaKQLRlMMCGSSALPSPLMKRWEEVt 417
Cdd:cd12118 210 AKAIYDLIEK----------HKVTHFCGAPTVLNMLA---NAPPSDARPLP----HRVH-VMTAGAPPPAAVLAKMEEL- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 418 GHRLLERYGMTEFV--------MALSNPLHG---ARKEGTVGKPLPCVEA-----KIIMEDGAETTSEVGELCIRSPSLF 481
Cdd:cd12118 271 GFDVTHVYGLTETYgpatvcawKPEWDELPTeerARLKARQGVRYVGLEEvdvldPETMKPVPRDGKTIGEIVFRGNIVM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 482 KEYWRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAY 561
Cdd:cd12118 351 KGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKW 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002235085 562 GEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPtRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:cd12118 429 GEVPCAFVELKEGAK----------VTEEEIIAFCREHLAGFMVP-KTVVFGELPKTSTGKIQKFVLRD 486
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
261-625 |
1.23e-43 |
|
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: 159.73 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQIL-SEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 339
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 GIWQRWresypnngSKNDEAITVFtgVPTMYTRLLQGYDGMDPEqqsassfaAKQLRLMMCGSSaLPSPLMKRWEEVTGH 419
Cdd:cd17635 82 SLFKIL--------TTNAVTTTCL--VPTLLSKLVSELKSANAT--------VPSLRLIGYGGS-RAIAADVRFIEATGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 -RLLERYGMTEFVMALSNPLHGARKE-GTVGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFI 496
Cdd:cd17635 143 tNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSaSFGTIWIKSPANMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 497 DGgFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedsk 576
Cdd:cd17635 223 DG-WVNTGDLGERREDGFLFITGRS-SESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV------ 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1002235085 577 kRAELDSKPALTLEALTswSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 625
Cdd:cd17635 295 -ASAELDENAIRALKHT--IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
145-594 |
1.62e-43 |
|
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: 163.41 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLalsYPEAellhvmNDSDISLILstkEHQDIMENISTKCSAHCSLLPSVT 224
Cdd:cd05932 31 GSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTL------NPDTIRYVL---EHSESKALFVGKLDDWKAMAPGVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTSSISSLIAEIDSSKE--IRGDDP-ALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE 301
Cdd:cd05932 99 EGLISISLPPPSAANCQYQWDDLIAQHPPLEErpTRFPEQlATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEEN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 302 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPkfSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLQG-YDGM 380
Cdd:cd05932 179 DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDVQRARP----------TLFFSVPRLWTKFQQGvQDKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQ----------------QSASSFAAKQLRLMMCGSSALPSPLMKrWEEVTGHRLLERYGMTE--FVMALSNPlhGAR 442
Cdd:cd05932 247 PQQKlnlllkipvvnslvkrKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTEnfAYSHLNYP--GRD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 KEGTVGKPLPCVEAKIimedgaettSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTN 522
Cdd:cd05932 324 KIGTVGNAGPGVEVRI---------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 523 aDIMKVGGYKLSA-LEIESVLLQHEIVLECAVLG--LPDEAYGEIICAIIVPKEDSKKRAELDSKPALTLEALTS 594
Cdd:cd05932 395 -DIFKTSKGKYVApAPIENKLAEHDRVEMVCVIGsgLPAPLALVVLSEEARLRADAFARAELEASLRAHLARVNS 468
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
147-628 |
8.01e-43 |
|
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: 160.90 E-value: 8.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimenistkcsaHCSLLPSVTSI 226
Cdd:cd17646 50 RVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLAA-----------RLPAGGDVALL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PVNIDCQEPSStevtssissliaeiDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLH 306
Cdd:cd17646 119 GDEALAAPPAT--------------PPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 307 CLPLHhvhglF----NALFAPLYSGSVVEFM-------PKFSVRGIwqrwresypnngskNDEAITVFTGVPTMYTRLLQ 375
Cdd:cd17646 185 KTPLS-----FdvsvWELFWPLVAGARLVVArpgghrdPAYLAALI--------------REHGVTTCHFVPSMLRVFLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 376 gydgmDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGARKEGTV--GKPLP 452
Cdd:cd17646 246 -----EPAAGSCAS-----LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 453 CVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNaDI 525
Cdd:cd17646 316 NTRLYVLDDALRPVpVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSD-DQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 MKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskPALTLEALTSWSKDKLAPYKI 605
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA---------AGPDTAALRAHLAERLPEYMV 465
|
490 500
....*....|....*....|...
gi 1002235085 606 PTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-631 |
9.57e-43 |
|
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: 161.54 E-value: 9.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKcsahcslLPSVTSI 226
Cdd:cd17642 71 RIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKK-------LKIIKTI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PV---NIDCQEPSSTE--VTSSISSLIAEIDSSKEI--RGDDPALILYTSGTTGKPKGVVHTHKGIVSQV---------- 289
Cdd:cd17642 144 IIldsKEDYKGYQCLYtfITQNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFshardpifgn 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 290 QILSEAwgyrsedQFLHCLPLHHVHGLFNALfAPLYSGSVVEFMPKFSVRGIWQrwresypnngSKNDEAITVFTGVPTM 369
Cdd:cd17642 224 QIIPDT-------AILTVIPFHHGFGMFTTL-GYLICGFRVVLMYKFEEELFLR----------SLQDYKVQSALLVPTL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 370 Y-----TRLLQGYDgmdpeqqsassfaAKQLRLMMCGSSalpsPLMKRWEEVTGHR-----LLERYGMTEFVMALSNPLH 439
Cdd:cd17642 286 FaffakSTLVDKYD-------------LSNLHEIASGGA----PLSKEVGEAVAKRfklpgIRQGYGLTETTSAILITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 440 GARKEGTVGKPLPCVEAKIIMEDGAET--TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFII 517
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDLDTGKTlgPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 518 LGRTNAdIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedskkraeLDSKPALTLEALTSWSK 597
Cdd:cd17642 429 VDRLKS-LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV----------LEAGKTMTEKEVMDYVA 497
|
490 500 510
....*....|....*....|....*....|....*...
gi 1002235085 598 DKLAPYKiptRL----YLWDSLPRNAMGKVNKKELKKL 631
Cdd:cd17642 498 SQVSTAK---RLrggvKFVDEVPKGLTGKIDRRKIREI 532
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
260-573 |
1.85e-42 |
|
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: 160.46 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVS----QVQILSEAWGyrSEDQFLHCLPLHHV-----------HG--------- 315
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVPELLG--PDDRYLAYLPLAHIfelaaenvclyRGgtigygspr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 316 -LFNALFAPLYsGSVVEFMPKF--SVRGIWQRWRESY-----PNNGSKNdeaiTVFTGVptMYTRLLQGYDGMDPEQQSA 387
Cdd:cd17639 166 tLTDKSKRGCK-GDLTEFKPTLmvGVPAIWDTIRKGVlaklnPMGGLKR----TLFWTA--YQSKLKALKEGPGTPLLDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 388 SSFAA------KQLRLMMCGSSALpSPLMKRWEEVTGHRLLERYGMTEFV--MALSNPlhGARKEGTVGKPLPCVEAKI- 458
Cdd:cd17639 239 LVFKKvraalgGRLRYMLSGGAPL-SADTQEFLNIVLCPVIQGYGLTETCagGTVQDP--GDLETGRVGPPLPCCEIKLv 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 459 -IMEDGAETTSEV--GELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV--GGYkl 533
Cdd:cd17639 316 dWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKK-DLVKLqnGEY-- 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002235085 534 SALE-IESVLLQHEIVLECAVLGLPDEAYgeiICAIIVPKE 573
Cdd:cd17639 393 IALEkLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNE 430
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
256-629 |
1.92e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 160.07 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 256 EIRGDDpalILYTSGTTGKPKGVVH--THKGI---VSQVQILSEAWGYRSEDQ-FLHCLPLHHVhglfnalfAPL-YSGS 328
Cdd:PRK08276 139 ETAGAD---MLYSSGTTGRPKGIKRplPGLDPdeaPGMMLALLGFGMYGGPDSvYLSPAPLYHT--------APLrFGMS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 V------VEFMPKFS----VRGIwQRWResypnngskndeaITVFTGVPTMYTRLL-------QGYDgmdpeqqsASSfa 391
Cdd:PRK08276 208 AlalggtVVVMEKFDaeeaLALI-ERYR-------------VTHSQLVPTMFVRMLklpeevrARYD--------VSS-- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 392 akqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVM-ALSNPLHGARKEGTVGKPLPCvEAKIIMEDGAE-TTSE 469
Cdd:PRK08276 264 ---LRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGvTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNElPPGE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 470 VGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVL 549
Cdd:PRK08276 340 IGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENLLVTHPKVA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 550 ECAVLGLPDEAYGEIICAIIVPKEDSkkraelDSKPALTLEaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK08276 419 DVAVFGVPDEEMGERVKAVVQPADGA------DAGDALAAE-LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
141-628 |
4.39e-42 |
|
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: 159.05 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMEnistkcsahcsll 220
Cdd:cd17651 41 GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELA------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 psVTSIPVNIDCQEPSSTEVTSSissLIAEIDsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRS 300
Cdd:cd17651 108 --VELVAVTLLDQPGAAAGADAE---PDPALD------ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHhvhglFNA----LFAPLYSGSVVEFMP---KFSVRGIWQRWREsypnngskndEAIT-VFtgVPTMYTR 372
Cdd:cd17651 177 GARTLQFAGLG-----FDVsvqeIFSTLCAGATLVLPPeevRTDPPALAAWLDE----------QRISrVF--LPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 373 LLQgydgmdpEQQSASSFAAKQLRLMMCGSSALP-SPLMKRW-EEVTGHRLLERYGMTE--FVMALSNPLHGARKEGT-- 446
Cdd:cd17651 240 ALA-------EHGRPLGVRLAALRYLLTGGEQLVlTEDLREFcAGLPGLRLHNHYGPTEthVVTALSLPGDPAAWPAPpp 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 447 VGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILG 519
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVpPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 520 RtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDK 599
Cdd:cd17651 393 R-ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAP----------VDAAELRAALATH 461
|
490 500
....*....|....*....|....*....
gi 1002235085 600 LAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
158-629 |
9.27e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 158.32 E-value: 9.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 158 FVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkeHQDIMENISTKCSAHCSLLpSVTSIP-----VNIDC 232
Cdd:PRK12406 49 FFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---HADLLHGLASALPAGVTVL-SVPTPPeiaaaYRISP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 233 QEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVH---THKGIVSQVQILSEAWGYRSEDQFLHCLP 309
Cdd:PRK12406 125 ALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 310 LHH----VHGLFNALFaplysGSVVEFMPKF---SVRGIWQRWResypnngskndeaITVFTGVPTMYTRLLQgydgmDP 382
Cdd:PRK12406 205 LYHsapnAYGLRAGRL-----GGVLVLQPRFdpeELLQLIERHR-------------ITHMHMVPTMFIRLLK-----LP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 383 EQQSASsFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGARKEGTVGKPLPCVEAKIIME 461
Cdd:PRK12406 262 EEVRAK-YDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESgAVTFATSEDALSHPGTVGKAAPGAELRFVDE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 462 DGAET-TSEVGELCIRSP--SLFKeYWRKPEVTAEsfID-GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALE 537
Cdd:PRK12406 341 DGRPLpQGEIGEIYSRIAgnPDFT-YHNKPEKRAE--IDrGGFITSGDVGYLDADGYLFLCDRKR-DMVISGGVNIYPAE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 538 IESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkrAELDskpaltLEALTSWSKDKLAPYKIPTRLYLWDSLPR 617
Cdd:PRK12406 417 IEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG----ATLD------EADIRAQLKARLAGYKVPKHIEIMAELPR 486
|
490
....*....|..
gi 1002235085 618 NAMGKVNKKELK 629
Cdd:PRK12406 487 EDSGKIFKRRLR 498
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
261-631 |
1.26e-41 |
|
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: 159.65 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSE-AWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSG--SVV-EFMPKF 336
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGatTVMfEGTPTY 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 SVRGIW----QRWResypnngskndeaITVFTGVPTMyTRLLQGYDGMDPEQQSASSfaakqLRLMmcGSSALP-SPLMK 411
Cdd:cd05966 312 PDPGRYwdivEKHK-------------VTIFYTAPTA-IRALMKFGDEWVKKHDLSS-----LRVL--GSVGEPiNPEAW 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 412 RW-EEVTGHR---LLERYGMTEFVMALSNPLHGAR--KEGTVGKPLPCVEAKIIMEDGAETTSEV-GELCIRS--PSLFK 482
Cdd:cd05966 371 MWyYEVIGKErcpIVDTWWQTETGGIMITPLPGATplKPGSATRPFFGIEPAILDEEGNEVEGEVeGYLVIKRpwPGMAR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 483 EYWRKPEvtaeSFIDG------GFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGL 556
Cdd:cd05966 451 TIYGDHE----RYEDTyfskfpGYYFTGDGARRDEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGR 525
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 557 PDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:cd05966 526 PHDIKGEAIYAFVTLKDGEEPSDEL-------RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
136-631 |
1.36e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 158.55 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGtwlSGGVAVPLAL---SYPEAELLHVMNDSDISLILSTKEHQDIMENISTK 212
Cdd:PRK07788 90 GLLALGVRAGDGVAVLARNHRGFVLALYA---AGKVGARIILlntGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 213 csahcslLPSVTSIPVNIDCQEPSSTEVtSSISSLIAEIDSSKEIRGDDPA-LILYTSGTTGKPKGVVHTH-KGIVSQVQ 290
Cdd:PRK07788 167 -------LGRLRAWGGNPDDDEPSGSTD-ETLDDLIAGSSTAPLPKPPKPGgIVILTSGTTGTPKGAPRPEpSPLAPLAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 291 ILSEAwGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKFSVRGIwQRWResypnngskndeaITVFTGVP 367
Cdd:PRK07788 239 LLSRV-PFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVlrrRFDPEATLEDI-AKHK-------------ATALVVVP 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 368 TMYTRLLqgydgmDPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGARKEGT 446
Cdd:PRK07788 304 VMLSRIL------DLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVaFATIATPEDLAEAPGT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 447 VGKPLPCVEAKIIMEDGAE-TTSEVGELCIRSPSLFKEYW--RKPEvtaesfIDGGFFKTGDTVTVDDEGYFIILGRtnA 523
Cdd:PRK07788 378 VGRPPKGVTVKILDENGNEvPRGVVGRIFVGNGFPFEGYTdgRDKQ------IIDGLLSSGDVGYFDEDGLLFVDGR--D 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 524 DIMKV-GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAP 602
Cdd:PRK07788 450 DDMIVsGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGA----------ALDEDAIKDYVRDNLAR 519
|
490 500
....*....|....*....|....*....
gi 1002235085 603 YKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK07788 520 YKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
264-629 |
1.59e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 155.30 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 264 LILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKFSVRG 340
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVtrrRFDPEATLDL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IwQRWRESypnngskndeAITVftgVPTMYTRLlqgydgMDPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHR 420
Cdd:PRK13382 280 I-DRHRAT----------GLAV---VPVMFDRI------MDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 421 LLERYGMTEFVM-ALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYwrkPEVTAESFIDG 498
Cdd:PRK13382 340 IYNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRILDQDFREVpTGEVGTIFVRNDTQFDGY---TSGSTKDFHDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 499 gFFKTGDTVTVDDEGYFIILGRTnaDIMKV-GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkk 577
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRD--DEMIVsGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA-- 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 578 raeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK13382 492 --------SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
139-630 |
1.88e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 159.56 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMEnistkcsahcs 218
Cdd:PRK12467 556 AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLP----------- 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 LLPSVTSIPVNIDCQEPSSTevtssissliAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGY 298
Cdd:PRK12467 625 VPAGLRSLCLDEPADLLCGY----------SGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLHCLPLhHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWRESypnngskNDEAITVFTGVPTMYTRLLQgyd 378
Cdd:PRK12467 695 AADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDCARDAEAFAALM-------ADQGVTVLKIVPSHLQALLQ--- 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVT-GHRLLERYGMTE-FVMALSNPLHG-ARKEGTV--GKPLPC 453
Cdd:PRK12467 764 --ASRVALPRP-----QRALVCGGEALQVDLLARVRALGpGARLINHYGPTEtTVGVSTYELSDeERDFGNVpiGQPLAN 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFI------DGG-FFKTGDTVTVDDEGYFIILGRTNaDI 525
Cdd:PRK12467 837 LGLYILDHYLNPVPVGVvGELYIGGAGLARGYHRRPALTAERFVpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMD-HQ 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 MKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAyGEIICAIIVPKEDSKkraelDSKPALTLEALTSWSKDKLAPYKI 605
Cdd:PRK12467 916 VKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAVAD-----GAEHQATRDELKAQLRQVLPDYMV 989
|
490 500
....*....|....*....|....*
gi 1002235085 606 PTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK12467 990 PAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
136-634 |
5.66e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 153.98 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGV---AVPLalsYPEAELLHVMNDSDISLILSTKEHQDIMENIstk 212
Cdd:PLN02246 66 GLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttANPF---YTPAEIAKQAKASGAKLIITQSCYVDKLKGL--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 213 csAHCSLLPSVTsipvnIDcqepSSTEVTSSISSLIAEIDSS---KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQV 289
Cdd:PLN02246 140 --AEDDGVTVVT-----ID----DPPEGCLHFSELTQADENElpeVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 290 --QILSEA--WGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKF---SVRGIWQRWResypnngskndeaITV 362
Cdd:PLN02246 209 aqQVDGENpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFeigALLELIQRHK-------------VTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 363 FTGVPTMYTRL-----LQGYDgmdpeqqsASSfaakqLRLMMCGSSalpsPLMKRWEEVTGHR-----LLERYGMTEFVM 432
Cdd:PLN02246 276 APFVPPIVLAIakspvVEKYD--------LSS-----IRMVLSGAA----PLGKELEDAFRAKlpnavLGQGYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 433 ALSNPLHGArKEGTVGKPLPC------VEAKIIMEDGAETTS--EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTG 504
Cdd:PLN02246 339 VLAMCLAFA-KEPFPVKSGSCgtvvrnAELKIVDPETGASLPrnQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 505 DTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldsk 584
Cdd:PLN02246 418 DIGYIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSE-------- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1002235085 585 paLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PLN02246 489 --ITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
260-631 |
1.22e-39 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 156.24 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSG-SVVEFMPKFSV 338
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGiKVVYHPDPTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 339 RGIWQRWREsypnNGSkndeaiTVFTGVPT---MYTRLLQgydgMDPEQqsassFAAkqLRLMMCGSSALPSPLMKRWEE 415
Cdd:PRK08633 862 LGIAKLVAK----HRA------TILLGTPTflrLYLRNKK----LHPLM-----FAS--LRLVVAGAEKLKPEVADAFEE 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 416 VTGHRLLERYGMTEF--VMALSNP--------LHGARKEGTVGKPLPCVEAKIIMEDGAET--TSEVGELCIRSPSLFKE 483
Cdd:PRK08633 921 KFGIRILEGYGATETspVASVNLPdvlaadfkRQTGSKEGSVGMPLPGVAVRIVDPETFEElpPGEDGLILIGGPQVMKG 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 484 YWRKPEVTAESF--IDG-GFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQ--HEIVLECAVLGLPD 558
Cdd:PRK08633 1001 YLGDPEKTAEVIkdIDGiGWYVTGDKGHLDEDGFLTITDRY-SRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPD 1079
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 559 EAYGEIICAIIVPKEDSKkrAELdskpaltLEALTswsKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK08633 1080 EKKGEKLVVLHTCGAEDV--EEL-------KRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
145-610 |
5.39e-39 |
|
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: 149.82 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLIlstkehqdIMENistkcsahcsllpsvt 224
Cdd:cd17640 30 GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL--------VVEN---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd17640 86 ---------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHV------HGLFNALFAPLYSgsvvefmpkfSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRLLQGYD 378
Cdd:cd17640 133 LSILPIWHSyersaeYFIFACGCSQAYT----------SIRTLKDDLKRVKP----------HYIVSVPRLWESLYSGIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmdpEQQSASSFAAKQL----------RLMMCGSSALPsPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVG 448
Cdd:cd17640 193 ----KQVSKSSPIKQFLflfflsggifKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 449 KPLPCVEAKIIMEDGAE--TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIM 526
Cdd:cd17640 268 RPLPGTEIKIVDPEGNVvlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 527 KVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGeiicAIIVPKEDSKKRAELDSKPALtLEALTSWSKDklapyKIP 606
Cdd:cd17640 348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVPNFEELEKWAKESGVKL-ANDRSQLLAS-----KKV 417
|
....
gi 1002235085 607 TRLY 610
Cdd:cd17640 418 LKLY 421
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
145-628 |
7.74e-39 |
|
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: 149.34 E-value: 7.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkCSAHCSLLPSVt 224
Cdd:cd12114 37 GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT--------------DGPDAQLDVAV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sIPVNIDCQEPSSTEvtssissliaEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd12114 102 -FDVLILDLDALAAP----------APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHH---VHGLFNALFAplySGSVVefMPKFSVRGIWQRWRESYPNNGskndeaITVFTGVPTMYTRLLQGYDGMD 381
Cdd:cd12114 171 LALSSLSFdlsVYDIFGALSA---GATLV--LPDEARRRDPAHWAELIERHG------VTLWNSVPALLEMLLDVLEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 382 PEQQSassfaakqLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEfVMALSN-----PLHGARKEGTVGKPLPCVE 455
Cdd:cd12114 240 ALLPS--------LRLVLLSGDWIPLDLPARLRALAPDaRLISLGGATE-ASIWSIyhpidEVPPDWRSIPYGRPLANQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 AKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFID----GGFFKTGDTVTVDDEGYFIILGRTNADImKVGG 530
Cdd:cd12114 311 YRVLDPRGRDCPDWVpGELWIGGRGVALGYLGDPELTAARFVThpdgERLYRTGDLGRYRPDGTLEFLGRRDGQV-KVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 531 YKLSALEIESVLLQHEIVLECAVLGLpDEAYGEIICAIIVPKEDSkkraeldskPALTLEALTSWSKDKLAPYKIPTRLY 610
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDG---------TPIAPDALRAFLAQTLPAYMIPSRVI 459
|
490
....*....|....*...
gi 1002235085 611 LWDSLPRNAMGKVNKKEL 628
Cdd:cd12114 460 ALEALPLTANGKVDRAAL 477
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
136-629 |
3.83e-38 |
|
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: 149.56 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILST-----KEHQDIMENIS 210
Cdd:cd05968 107 GLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrRGREVNLKEEA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 211 TKCSAHCsllPSVTSIPV-----NIDCQEP----SSTEVTSSISSLIAEIDSskeirgDDPALILYTSGTTGKPKGVVHT 281
Cdd:cd05968 187 DKACAQC---PTVEKVVVvrhlgNDFTPAKgrdlSYDEEKETAGDGAERTES------EDPLMIIYTSGTTGKPKGTVHV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 282 HKGI-VSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFnALFAPLYSGSVV---EFMPKFSVRGiwQRWRESypnngskND 357
Cdd:cd05968 258 HAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMvlyDGAPDHPKAD--RLWRMV-------ED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 358 EAITVFTGVPTMyTRLLQGYdGMDPEQQSASSfaakQLRLM-MCGSSALPSPLMKRWEEVTGHRL--LERYGMTEFVMA- 433
Cdd:cd05968 328 HEITHLGLSPTL-IRALKPR-GDAPVNAHDLS----SLRVLgSTGEPWNPEPWNWLFETVGKGRNpiINYSGGTEISGGi 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 434 LSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTSEVGELCIRSP--SLFKEYWRKPEVTAESFID--GGFFKTGDTVTV 509
Cdd:cd05968 402 LGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPwpGMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 510 DDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELDskpaltl 589
Cdd:cd05968 482 DEEGYFYILGRSD-DTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALA------- 553
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1002235085 590 EALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05968 554 EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
261-631 |
4.43e-38 |
|
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: 149.71 E-value: 4.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEA-WGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGS---VVEFMPKF 336
Cdd:TIGR02188 238 DPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYvFDIKDGDIFWCTADVGWITGHSYIVYGPLANGAttvMFEGVPTY 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 SVRGIWQRWRESYpnngskndeAITVFTGVPTMyTRLLQGYDGMDPEQQSASSfaakqLRLMmcGSSALP-SPLMKRW-- 413
Cdd:TIGR02188 318 PDPGRFWEIIEKH---------KVTIFYTAPTA-IRALMRLGDEWVKKHDLSS-----LRLL--GSVGEPiNPEAWMWyy 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 414 EEVTGHR--LLERYGMTEFVMALSNPLHGA--RKEGTVGKPLPCVEAKIIMEDGAETTSEV--GELCIRS--PSLFKEYW 485
Cdd:TIGR02188 381 KVVGKERcpIVDTWWQTETGGIMITPLPGAtpTKPGSATLPFFGIEPAVVDEEGNPVEGPGegGYLVIKQpwPGMLRTIY 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 486 RKPevtaESFIDG------GFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDE 559
Cdd:TIGR02188 461 GDH----ERFVDTyfspfpGYYFTGDGARRDKDGYIWITGRVD-DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDD 535
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 560 AYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:TIGR02188 536 IKGQAIYAFVTLKDGYEPDDEL-------RKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKI 600
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
253-629 |
8.72e-38 |
|
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: 146.37 E-value: 8.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 253 SSKEIRGDDpalILYTSGTTGKPKGVVHTHKGIVSQVQILSEA---WGYRSEDQFLHCLPLHHVHGL---FNALFAplys 326
Cdd:cd05929 121 IEDEAAGWK---MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgFGPGADSVYLSPAPLYHAAPFrwsMTALFM---- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 327 GSVVEFMPKFSVRGIW---QRWResypnngskndeaITVFTGVPTMYTRLLQGYDgmdpEQQSASSFAAkqLRLMMCGSS 403
Cdd:cd05929 194 GGTLVLMEKFDPEEFLrliERYR-------------VTFAQFVPTMFVRLLKLPE----AVRNAYDLSS--LKRVIHAAA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 404 ALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGARKEGTVGKPLPCvEAKIIMEDGAET-TSEVGELCIRSPSLF 481
Cdd:cd05929 255 PCPPWVKEQWIDWGGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVpPGEIGEVYFANGPGF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 482 kEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAY 561
Cdd:cd05929 334 -EYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002235085 562 GEIICAIIVPKEDSkkraelDSKPALTlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:cd05929 412 GQRVHAVVQPAPGA------DAGTALA-EELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
145-628 |
1.22e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.88 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDimenistkcsahcsLLPSVT 224
Cdd:PRK12316 561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGR--------------KLPLAA 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVnIDCQEPSSTEVTSSISSLIAEIDsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:PRK12316 627 GVQV-LDLDRPAAWLEGYSEENPGTELN------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTV 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGIWQRWresypnnGSKNDEAITVFTGVPTMYTRLLQgydgm 380
Cdd:PRK12316 700 LQKTPFS-----FDVsvweFFWPLMSGARLVVAAPGDHRDPAKLV-------ELINREGVDTLHFVPSMLQAFLQ----- 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSASSfaakqLRLMMCGSSALPSPLM-----KRWEEvtghRLLERYGMTEFVMALSNplHGARKEG----TVGKPL 451
Cdd:PRK12316 763 DEDVASCTS-----LRRIVCSGEALPADAQeqvfaKLPQA----GLYNLYGPTEAAIDVTH--WTCVEEGgdsvPIGRPI 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 452 PCVEAKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNaD 524
Cdd:PRK12316 832 ANLACYILDANLEPVPVGVlGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEYAGRID-H 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 525 IMKVGGYKLSALEIESVLLQHEIVLECAVLGLPdeayGEIICAIIVPkedskkraelDSKPALTLEALTSWSKDKLAPYK 604
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL----------ESEGGDWREALKAHLAASLPEYM 976
|
490 500
....*....|....*....|....
gi 1002235085 605 IPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK12316 977 VPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
261-634 |
2.50e-37 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 144.75 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILY-TSGTTGKPKGVVHTHKGIVSQVQILSEawgYRSEDQfLHC---LPLHHVHGLFNALFAPLYSGSVVefmpkf 336
Cdd:PRK07445 120 ETGWIMIpTGGSSGQIRFAIHTWETLTASVQGFQR---YFQLQQ-VNSfcvLPLYHVSGLMQFMRSFLTGGKLV------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 svrgIWqRWR--ESYPNNGSKNDEAitVFTGVPTMYTRLLQGYdgmdpeQQSASSFAAkqlrLMMCGSSALPSPLmkrwE 414
Cdd:PRK07445 190 ----IL-PYKrlKSGQELPPNPSDF--FLSLVPTQLQRLLQLR------PQWLAQFRT----ILLGGAPAWPSLL----E 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 415 EVTGH--RLLERYGMTE---FVMALSnP---LHGARkegTVGKPLPcvEAKIIMEDGAettseVGELCIRSPSLFKEYWr 486
Cdd:PRK07445 249 QARQLqlRLAPTYGMTEtasQIATLK-PddfLAGNN---SSGQVLP--HAQITIPANQ-----TGNITIQAQSLALGYY- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 487 kPEVTAESfidgGFFKTGDTVTVDDEGYFIILGRTNADIMKvGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIIC 566
Cdd:PRK07445 317 -PQILDSQ----GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVT 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002235085 567 AIIVPKedskkraeldsKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK07445 391 AIYVPK-----------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
205-630 |
1.00e-36 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 144.51 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 205 IMENISTKcsahcslLPSVTSIPVNIDCQEPSSTEVTSSIS--SLIAEIDSS---KEIRGDDPALILYTSGTTGKPKGVV 279
Cdd:PRK06018 124 ILEKIADK-------LPSVERYVVLTDAAHMPQTTLKNAVAyeEWIAEADGDfawKTFDENTAAGMCYTSGTTGDPKGVL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 280 HTHKGIVSQVQILS--EAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVefMPkfsvrgiwqrwresypnnGSKND 357
Cdd:PRK06018 197 YSHRSNVLHALMANngDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLV--MP------------------GAKLD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 358 ----------EAITVFTGVPTMYTRLLQgydgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVtGHRLLERYGM 427
Cdd:PRK06018 257 gasvyelldtEKVTFTAGVPTVWLMLLQ--------YMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 428 TEF-----VMALSNPLHGARKEG------TVGKPLPCVEAKIIMEDGAETTSE---VGELCIRSPSLFKEYWRkpeVTAE 493
Cdd:PRK06018 328 TEMsplgtLAALKPPFSKLPGDArldvlqKQGYPPFGVEMKITDDAGKELPWDgktFGRLKVRGPAVAAAYYR---VDGE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 494 SFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKE 573
Cdd:PRK06018 405 ILDDDGFFDTGDVATIDAYGYMRITDRSK-DVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP 483
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 574 DSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK06018 484 GE----------TATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
148-628 |
2.36e-36 |
|
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: 142.23 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcSAHCSLLPSVTSIP 227
Cdd:cd17656 41 VAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT---------------QRHLKSKLSFNKST 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VNIDcqEPSSTEVTSSissliaEIDSSKEirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSED---QF 304
Cdd:cd17656 106 ILLE--DPSISQEDTS------NIDYINN--SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDkvlQF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHClplhHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRwresypNNGSKNDEAITVFtgVPTMYTRLLQGydgmdpEQ 384
Cdd:cd17656 176 ATC----SFDVCYQEIFSTLLSGGTLYIIREETKRDVEQL------FDLVKRHNIEVVF--LPVAFLKFIFS------ER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE---FVMALSNPLHGARKEGTVGKPLPCVEAKIIME 461
Cdd:cd17656 238 EFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSEthvVTTYTINPEAEIPELPPIGKPISNTWIYILDQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 462 DGA-ETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLS 534
Cdd:cd17656 318 EQQlQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRAD-HQVKIRGYRIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 535 ALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDS 614
Cdd:cd17656 397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ------------ELNISQLREYLAKQLPEYMIPSFFVPLDQ 464
|
490
....*....|....
gi 1002235085 615 LPRNAMGKVNKKEL 628
Cdd:cd17656 465 LPLTPNGKVDRKAL 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
148-628 |
5.11e-36 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 141.03 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdimenistkcsahcsllpsvtsip 227
Cdd:cd17644 53 VGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPE-------------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 vNIdcqepsstevtssissliaeidsskeirgddpALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHC 307
Cdd:cd17644 107 -NL--------------------------------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 308 LPLHhvhglFNA----LFAPLYSGSVVEFMPK---FSVRGIWQRWREsypnngskndEAITVFTgVPTMYTRLLQGyDGM 380
Cdd:cd17644 154 ASIA-----FDVaaeeIYVTLLSGATLVLRPEemrSSLEDFVQYIQQ----------WQLTVLS-LPPAYWHLLVL-ELL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTEFVMA-----LSNPLHGARKEGTVGKPLPC 453
Cdd:cd17644 217 LSTIDLPSS-----LRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIAN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFIDGGF--------FKTGDTVTVDDEGYFIILGRTNAD 524
Cdd:cd17644 292 TQVYILDENLQPVPVGVpGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 525 ImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKedskkraeldSKPALTLEALTSWSKDKLAPYK 604
Cdd:cd17644 372 V-KIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPH----------YEESPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....
gi 1002235085 605 IPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
141-628 |
8.55e-36 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 140.15 E-value: 8.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcsahcsll 220
Cdd:cd12115 45 GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD--------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 psvtsipvnidcqepsstevtssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRS 300
Cdd:cd12115 104 --------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNaLFAPLYSGSVVefmpkFSVRGIWQrwresYPNNGSKNDeaITVFTGVPTMYTRLLQgydgM 380
Cdd:cd12115 146 LAGVLASTSICFDLSVFE-LFGPLATGGKV-----VLADNVLA-----LPDLPAAAE--VTLINTVPSAAAELLR----H 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEQQSassfaakqLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTE---FVMALSNPLhGARKEGTVGKPLPCVEA 456
Cdd:cd12115 209 DALPAS--------VRVVNLAGEPLPRDLVQRlYARLQVERVVNLYGPSEdttYSTVAPVPP-GASGEVSIGRPLANTQA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNaDIMKVG 529
Cdd:cd12115 280 YVLDRALQPVPLgVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRAD-NQVKVR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 530 GYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRL 609
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGA----------AGLVEDLRRHLGTRLPAYMVPSRF 428
|
490
....*....|....*....
gi 1002235085 610 YLWDSLPRNAMGKVNKKEL 628
Cdd:cd12115 429 VRLDALPLTPNGKIDRSAL 447
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
141-632 |
1.21e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 141.84 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCsahcsll 220
Cdd:PRK05620 60 GITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKEC------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSI----PVNID---CQEPSSTEVTSsissLIAEIDSSK------EIRGDDPALILYTSGTTGKPKGVVHTHKGIVS 287
Cdd:PRK05620 133 PCVRAVvfigPSDADsaaAHMPEGIKVYS----YEALLDGRStvydwpELDETTAAAICYSTGTTGAPKGVVYSHRSLYL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 288 QVQIL--SEAWGYRSEDQFLHCLPLHHVHGlFNALFAPLYSGSVVEFM-PKFSVRGIWQRWRESYPNngskndeaitVFT 364
Cdd:PRK05620 209 QSLSLrtTDSLAVTHGESFLCCVPIYHVLS-WGVPLAAFMSGTPLVFPgPDLSAPTLAKIIATAMPR----------VAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 365 GVPTMYTRLLQGYDGMDPEQQSassfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF--VMALSNPLHGAR 442
Cdd:PRK05620 278 GVPTLWIQLMVHYLKNPPERMS--------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETspVGTVARPPSGVS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 KEG------TVGKPLPCVEAKIImEDG---AETTSEVGELCIRSPSLFKEYWRKP----------------EVTAESFID 497
Cdd:PRK05620 350 GEArwayrvSQGRFPASLEYRIV-NDGqvmESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 498 GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKK 577
Cdd:PRK05620 429 DGWLRTGDVGSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEP 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 578 RAEldskpalTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PRK05620 508 TRE-------TAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
260-578 |
1.29e-35 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 141.20 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQV----QILSEAWGYRSEDQFLHCLPLHHVHGLFNALFApLYSGSVVefmpk 335
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKI----- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 336 fsvrGIWQRwresyPNNGSKNDEAI---TVFTGVPTMYTRLlqgYDG-MDPEQQS------------------------- 386
Cdd:cd05927 188 ----GFYSG-----DIRLLLDDIKAlkpTVFPGVPRVLNRI---YDKiFNKVQAKgplkrklfnfalnyklaelrsgvvr 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 387 ASSFAAK------------QLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCV 454
Cdd:cd05927 256 ASPFWDKlvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 EAKII----MEDGAETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKV-- 528
Cdd:cd05927 336 EVKLVdvpeMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKK-NIFKLsq 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYkLSALEIESVLLQHEIVLECAVLGLPDEAYgeiICAIIVPKEDSKKR 578
Cdd:cd05927 415 GEY-VAPEKIENIYARSPFVAQIFVYGDSLKSF---LVAIVVPDPDVLKE 460
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
145-628 |
1.67e-35 |
|
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: 138.92 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcsahcsllpsvt 224
Cdd:cd17652 37 ERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd17652 92 ----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKfsvrgiwQRWRESYPNNGSKNDEAITVFTGVPTMYtrllqgyDGM 380
Cdd:cd17652 138 LQFASPS-----FDAsvweLLMALLAGATLVLAPA-------EELLPGEPLADLLREHRITHVTLPPAAL-------AAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 381 DPEqqsassfAAKQLRLMMCGSSALPSPLMKRWeeVTGHRLLERYGMTEF-VMALSNPLHGARKEGTVGKPLPCVEAKIi 459
Cdd:cd17652 199 PPD-------DLPDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTETtVCATMAGPLPGGGVPPIGRPVPGTRVYV- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 460 MEDGAETT--SEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTNaDIMKVGG 530
Cdd:cd17652 269 LDARLRPVppGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRAD-DQVKIRG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 531 YKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPkedskkraelDSKPALTLEALTSWSKDKLAPYKIPTRLY 610
Cdd:cd17652 348 FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVP----------APGAAPTAAELRAHLAERLPGYMVPAAFV 417
|
490
....*....|....*...
gi 1002235085 611 LWDSLPRNAMGKVNKKEL 628
Cdd:cd17652 418 VLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
145-630 |
3.50e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 143.17 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkeHQDIMENIstkcsahcsLLP-SV 223
Cdd:PRK12316 2053 EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT---QRHLLERL---------PLPaGV 2120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 224 TSIPVNIDCQEPSStevtssissliAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQ 303
Cdd:PRK12316 2121 ARLPLDRDAEWADY-----------PDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADC 2189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 304 FLHCLPLHhVHGLFNALFAPLYSGSVVEFMPKfsvrGIW---QRWRESYpnngsknDEAITVFTGVPTMYTRLLQ--GYD 378
Cdd:PRK12316 2190 ELQFMSFS-FDGAHEQWFHPLLNGARVLIRDD----ELWdpeQLYDEME-------RHGVTILDFPPVYLQQLAEhaERD 2257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 GMDPeqqsassfaakQLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMALSnpLHGARKEGTVGKPLPCVEAK 457
Cdd:PRK12316 2258 GRPP-----------AVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPL--LWKCRPQDPCGAAYVPIGRA 2324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 458 I------IMEDGAE--TTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTN 522
Cdd:PRK12316 2325 LgnrrayILDADLNllAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRID 2404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 523 ADImKVGGYKLSALEIESVLLQHEIVLECAVLGLpDEAYGEIICAIIVPkedskkraelDSKPALTLEALTSWSKDKLAP 602
Cdd:PRK12316 2405 HQV-KIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVP----------DDAAEDLLAELRAWLAARLPA 2472
|
490 500
....*....|....*....|....*...
gi 1002235085 603 YKIPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
147-631 |
1.21e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.63 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsaHCSLLPSVtSI 226
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT-----------------QSHLLQRL-PI 4664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PVNIDCQEPSSTEVTSSISsliaEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLH 306
Cdd:PRK12316 4665 PDGLASLALDRDEDWEGFP----AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQ 4740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 307 CLPLhHVHGLFNALFAPLYSGSVVEFMPKfsvrGIW---QRWRESYpnngsknDEAITVFTGVPTMYTRLLQGydgmDPE 383
Cdd:PRK12316 4741 FMSF-SFDGSHEGLYHPLINGASVVIRDD----SLWdpeRLYAEIH-------EHRVTVLVFPPVYLQQLAEH----AER 4804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 384 QQSASSfaakqLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMalsNPLHGARKEGT--------VGKPLPCV 454
Cdd:PRK12316 4805 DGEPPS-----LRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTV---TVLLWKARDGDacgaaympIGTPLGNR 4876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 EAKIImeDGA---ETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTNAD 524
Cdd:PRK12316 4877 SGYVL--DGQlnpLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQ 4954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 525 ImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDeAYGEIICAIIVPkeDSKKRAELDSKPALTLEALTSWSKDKLAPYK 604
Cdd:PRK12316 4955 V-KIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVP--QDPALADADEAQAELRDELKAALRERLPEYM 5030
|
490 500
....*....|....*....|....*..
gi 1002235085 605 IPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK12316 5031 VPAHLVFLARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
93-628 |
4.12e-34 |
|
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: 134.99 E-value: 4.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 93 HAAIRSDQKSYNLVQLIASALDVYNILRNKNMTQNgstgssvkgingtgflggARIGIVAKPSPEFVAGIFGTWLSGGVA 172
Cdd:cd17645 14 HVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPD------------------DQVGIMLDKSLDMIAAILGVLKAGGAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 173 VPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsahcsllpsvtsipvnidcqepsstevtssissliaeid 252
Cdd:cd17645 76 VPIDPDYPGERIAYMLADSSAKILLT------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 253 sskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQflhclPLHHVHGLFNA----LFAPLYSGS 328
Cdd:cd17645 102 -----NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK-----SLVYASFSFDAsaweIFPHLTAGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 VVEFMP---KFSVRGIwqrwresypnNGSKNDEAITVfTGVPTmytrllqgydgmdpeqQSASSFAA---KQLRLMMCGS 402
Cdd:cd17645 172 ALHVVPserRLDLDAL----------NDYFNQEGITI-SFLPT----------------GAAEQFMQldnQSLRVLLTGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALpsplmKRWEEvTGHRLLERYGMTE-FVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGA-ETTSEVGELCIRSPSL 480
Cdd:cd17645 225 DKL-----KKIER-KGYKLVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQlQPIGVAGELCIAGEGL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 481 FKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVL 554
Cdd:cd17645 299 ARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQV-KIRGYRIEPGEIEPFLMNHPLIELAAVL 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 555 GLPDEAYGEIICAIIVPKEDskkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17645 378 AKEDADGRKYLVAYVTAPEE------------IPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
258-631 |
5.09e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 134.62 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 258 RGDDPALILYTSGTTGKPKGVVHTHKGIvsQVQILSEAW--GYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM-- 333
Cdd:cd05974 83 HADDPMLLYFTSGTTSKPKLVEHTHRSY--PVGHLSTMYwiGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFny 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 PKFSVRGIWQRWRESypnngskndeAITVFTGVPTMYTRLLQgydgmdpeqQSASSFAAKqLRLMMCGSSALPSPLMKRW 413
Cdd:cd05974 161 ARFDAKRVLAALVRY----------GVTTLCAPPTVWRMLIQ---------QDLASFDVK-LREVVGAGEPLNPEVIEQV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 414 EEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTSevGELCI-----RSPSLFKEYWRKP 488
Cdd:cd05974 221 RRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE--GEVALdlgdtRPVGLMKGYAGDP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 489 EVTAESfIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAygeiicAI 568
Cdd:cd05974 299 DKTAHA-MRGGYYRTGDIAMRDEDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPV------RL 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 569 IVPKEDSKKRAELDSKPALTLEaLTSWSKDKLAPYKIPTRLYLWDsLPRNAMGKVNKKELKKL 631
Cdd:cd05974 371 SVPKAFIVLRAGYEPSPETALE-IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRR 431
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
261-624 |
5.51e-34 |
|
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: 132.43 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVRG 340
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNV-FVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRwresypnngSKNDEAITVFTGVPTMyTRLLQGYDGMDPEQQSASSFAAKQLRLMMcgSSALPSPLMKRweevtghr 420
Cdd:cd17636 80 VLEL---------IEAERCTHAFLLPPTI-DQIVELNADGLYDLSSLRSSPAAPEWNDM--ATVDTSPWGRK-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 421 lLERYGMTEfVMALSNPLH-GARKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFIDG 498
Cdd:cd17636 140 -PGGYGQTE-VMGLATFAAlGGGAIGGAGRPSPLVQVRILDEDGREVpDGEVGEIVARGPTVMAGYWNRPEVNARRTRGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 499 GFfKTGDtvtvddegyfiiLGRTNAD-----------IMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICA 567
Cdd:cd17636 218 WH-HTND------------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKA 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 568 IIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 624
Cdd:cd17636 285 IVVLKPGA----------SVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
146-631 |
7.06e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.14 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 146 ARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTkehqdimenistkcSAHCSLLPSVTS 225
Cdd:PRK12467 1625 VLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ--------------SHLQARLPLPDG 1690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 226 IPVNIDCQEPSSTEvTSSISSLIAEIDsskeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFL 305
Cdd:PRK12467 1691 LRSLVLDQEDDWLE-GYSDSNPAVNLA------PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL 1763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 306 HCLPLHhvhglFN----ALFAPLYSGSVVEFMPKfsvrGIWQRWRESYpnnGSKNDEAITVFTGVPTMYTRLLQgydgMD 381
Cdd:PRK12467 1764 QFTSFA-----FDvsvwELFWPLINGARLVIAPP----GAHRDPEQLI---QLIERQQVTTLHFVPSMLQQLLQ----MD 1827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 382 PEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHR-LLERYGMTEFVMALSN-PLHGARKEGT----VGKPLPCVE 455
Cdd:PRK12467 1828 EQVEHPLS-----LRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDVTHwTCRRKDLEGRdsvpIGQPIANLS 1902
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 AKIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFI-------DGGFFKTGDTVTVDDEGYFIILGRTNADImK 527
Cdd:PRK12467 1903 TYILDASLNPVPIGVaGELYLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQV-K 1981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 528 VGGYKLSALEIESVLLQHEIVLECAVLGLpDEAYGEIICAIIVPKEDSKkrAELDSKPALTLEALTSWSKDKLAPYKIPT 607
Cdd:PRK12467 1982 IRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGL--VDDDEAQVALRAILKNHLKASLPEYMVPA 2058
|
490 500
....*....|....*....|....
gi 1002235085 608 RLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK12467 2059 HLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
257-631 |
1.31e-33 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 136.29 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 257 IRGDDPALILYTSGTTGKPKGVVHTHKG-IVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSG--SVV-EF 332
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGatTVLyEG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 333 MPkfsVR----GIWQRWRESYPNNGskndeaitVFTgVPTMYTRLLQgydgMDPEQQSASSFAAKQLRLMMCGSSALPSP 408
Cdd:cd05967 307 KP---VGtpdpGAFWRVIEKYQVNA--------LFT-APTAIRAIRK----EDPDGKYIKKYDLSSLRTLFLAGERLDPP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 LMKRWEEVTGHRLLERYGMTEFVMALSNPLHG----ARKEGTVGKPLPCVEAKIIMEDGAET-TSEVGELCIR---SPSL 480
Cdd:cd05967 371 TLEWAENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVLDEDGEPVgPNELGNIVIKlplPPGC 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 481 FKEYWRKPEVTAESFI--DGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPD 558
Cdd:cd05967 451 LLTLWKNDERFKKLYLskFPGYYDTGDAGYKDEDGYLFIMGRTD-DVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 559 EAYGEIICAIIVPKEDSKKRAEldskpalTLE-ALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:cd05967 530 ELKGQVPLGLVVLKEGVKITAE-------ELEkELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
267-632 |
2.49e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 134.45 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 267 YTSGTTGKPKGVVHTHKGIV--SQVQILSEAWGYRSEDQFLHCLPLHHVH--GLFNAlfAPLYSGSVVEFMPKFSVRGIW 342
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNawGLPYS--APLTGAKLVLPGPDLDGKSLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 343 QRWREsypnngskndEAITVFTGVPTMYTRLLQgydGMDPEQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLL 422
Cdd:PRK07008 261 ELIEA----------ERVTFSAGVPTVWLGLLN---HMREAGLRFST-----LRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 423 ERYGMTEFvmalsNPL---------HGARKEGTV-------GKPLPCVEAKIIMEDGAETTSE---VGELCIRSPSLFKE 483
Cdd:PRK07008 323 HAWGMTEM-----SPLgtlcklkwkHSQLPLDEQrkllekqGRVIYGVDMKIVGDDGRELPWDgkaFGDLQVRGPWVIDR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 484 YWRKpevtAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGE 563
Cdd:PRK07008 398 YFRG----DASPLVDGWFPTGDVATIDADGFMQITDRSK-DVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002235085 564 IICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PRK07008 473 RPLLVVVKRPGAE----------VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
147-628 |
5.59e-33 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.45 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsaHCSLLPSVTSI 226
Cdd:PRK05691 2240 RVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLS-----------------DRALFEALGEL 2302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PVNID--CQEPSSTEVTSSISSLIAEIDSSkeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:PRK05691 2303 PAGVArwCLEDDAAALAAYSDAPLPFLSLP-----QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCE 2377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHhvhglFNA----LFAPLYSGS--VVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTRLlqgyd 378
Cdd:PRK05691 2378 LHFYSIN-----FDAaserLLVPLLCGArvVLRAQGQWGAEEICQLIRE----------QQVSILGFTPSYGSQL----- 2437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmdpEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLL-ERYGMTE-FVMALSNPLHGARKEGTVGKPLPCV-- 454
Cdd:PRK05691 2438 ----AQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTEtVVMPLACLAPEQLEEGAASVPIGRVvg 2513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 --EAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAESFI------DGG-FFKTGDTVTVDDEGYFIILGRTNAD 524
Cdd:PRK05691 2514 arVAYILDADLALVpQGATGELYVGGAGLAQGYHDRPGLTAERFVadpfaaDGGrLYRTGDLVRLRADGLVEYVGRIDHQ 2593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 525 ImKVGGYKLSALEIESVLLQHEIVLECAVLGLpDEAYGEIICAIIVpkedSKKRAELDSKPALTLEALTSWSKDKLAPYK 604
Cdd:PRK05691 2594 V-KIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV----SAVAGQDDEAQAALREALKAHLKQQLPDYM 2667
|
490 500
....*....|....*....|....
gi 1002235085 605 IPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK05691 2668 VPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
258-631 |
6.91e-33 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 135.48 E-value: 6.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 258 RGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK-F 336
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSpL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 SVRGIwqrwresyPnngskndEAI-----TVFTGVPTmytrLLQGYdgmdpeQQSASSFAAKQLRLMMCGSSALPSPLMK 411
Cdd:PRK06814 871 HYRII--------P-------ELIydtnaTILFGTDT----FLNGY------ARYAHPYDFRSLRYVFAGAEKVKEETRQ 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 412 RWEEVTGHRLLERYGMTEF--VMALSNPLHGarKEGTVGKPLPCVEAKIimeDGAETTSEVGELCIRSPSLFKEYWR--K 487
Cdd:PRK06814 926 TWMEKFGIRILEGYGVTETapVIALNTPMHN--KAGTVGRLLPGIEYRL---EPVPGIDEGGRLFVRGPNVMLGYLRaeN 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 488 PEVTAESfiDGGFFKTGDTVTVDDEGYFIILGRTNAdIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEiicA 567
Cdd:PRK06814 1001 PGVLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKR-FAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE---R 1074
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 568 IIVpkedskkraeLDSKPALTLEALTSWSKDKLAP-YKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK06814 1075 IIL----------LTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
148-630 |
8.26e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.86 E-value: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILsTKEHQDimenistkcsahcslLPSVTSip 227
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL-SQSHLR---------------LPLAQG-- 3171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VNIDCQEPSSTEVtssissliAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHC 307
Cdd:PRK12316 3172 VQVLDLDRGDENY--------AEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF 3243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 308 LPLhHVHGLFNALFAPLYSGSVVefmpkfsVRGIWQRWRESYPNNGSKNDEAITVFTGVPTMYTRLLQgydgmDPEQQSA 387
Cdd:PRK12316 3244 TTF-SFDVFVEELFWPLMSGARV-------VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE-----EEDAHRC 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 388 SSfaakqLRLMMCGSSALPSPLMKRWeeVTGHRLLERYGMTEFVMALSNPLHGARKEGT--VGKPLPCVEAKIImeDGAE 465
Cdd:PRK12316 3311 TS-----LKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYIL--DGSL 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 466 TTSEVG---ELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNADImKVGGYKLSAL 536
Cdd:PRK12316 3382 EPVPVGalgELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQV-KIRGFRIELG 3460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 537 EIESVLLQHEIVLECAVLGLPdeayGEIICAIIVPKedskkraelDSKPALTlEALTSWSKDKLAPYKIPTRLYLWDSLP 616
Cdd:PRK12316 3461 EIEARLLEHPWVREAVVLAVD----GRQLVAYVVPE---------DEAGDLR-EALKAHLKASLPEYMVPAHLLFLERMP 3526
|
490
....*....|....
gi 1002235085 617 RNAMGKVNKKELKK 630
Cdd:PRK12316 3527 LTPNGKLDRKALPR 3540
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
148-630 |
8.48e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 132.88 E-value: 8.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMEnistkcsahcSLLPSVTSIP 227
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLD----------GLDPGVRVIN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VnidcqepSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHC 307
Cdd:PRK07867 127 V-------DSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 308 LPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIW---QRWRESYPNngskndeaitvFTGVPTMYtrLLQgydgmDPEQ 384
Cdd:PRK07867 200 MPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLpdvRRYGATYAN-----------YVGKPLSY--VLA-----TPER 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSAssfAAKQLRLMMcGSSALPSPLmKRWEEVTGHRLLERYGMTEFVMALsnplhgARKEGT----VGKPLPCVE----- 455
Cdd:PRK07867 262 PDD---ADNPLRIVY-GNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAI------TRTPDTppgaLGPLPPGVAivdpd 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 ------AKIIMEDGAETTSE-VGELC-IRSPSLFKEYWRKPEVTAESfIDGGFFKTGDTVTVDDEGYFIILGRTnADIMK 527
Cdd:PRK07867 331 tgtecpPAEDADGRLLNADEaIGELVnTAGPGGFEGYYNDPEADAER-MRGGVYWSGDLAYRDADGYAYFAGRL-GDWMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 528 VGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkrAELDskPALTLEALTswSKDKLAPYKIPT 607
Cdd:PRK07867 409 VDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG----AKFD--PDAFAEFLA--AQPDLGPKQWPS 480
|
490 500
....*....|....*....|...
gi 1002235085 608 RLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PRK07867 481 YVRVCAELPRTATFKVLKRQLSA 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
141-623 |
9.62e-33 |
|
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: 133.47 E-value: 9.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAHCSLL 220
Cdd:cd17634 105 GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIP---------VNIDCQEPSSTEVTSSISSLIAEIDSSKeIRGDDPALILYTSGTTGKPKGVVHTHKG-IVSQVQ 290
Cdd:cd17634 185 PNVTSVEhvivlkrtgSDIDWQEGRDLWWRDLIAKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAAT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 291 ILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKFSVRG-IWQrwresypnngSKNDEAITVFTGV 366
Cdd:cd17634 264 TMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTllyEGVPNWPTPArMWQ----------VVDKHGVNILYTA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 367 PTMyTRLLQGYDGMDPEQQSASSfaakqLR-LMMCGSSALPSPLMKRWEEVTGHR--LLERYGMTEFVMALSNPLHGAR- 442
Cdd:cd17634 334 PTA-IRALMAAGDDAIEGTDRSS-----LRiLGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIe 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 -KEGTVGKPLPCVEAKIIMEDG-AETTSEVGELCIRS--PSLFKEYWRKPEVTAESFID--GGFFKTGDTVTVDDEGYFI 516
Cdd:cd17634 408 lKAGSATRPVFGVQPAVVDNEGhPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYW 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 517 ILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVpkedskKRAELDSKPALTLEaLTSWS 596
Cdd:cd17634 488 ITGRSD-DVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV------LNHGVEPSPELYAE-LRNWV 559
|
490 500
....*....|....*....|....*..
gi 1002235085 597 KDKLAPYKIPTRLYLWDSLPRNAMGKV 623
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
267-630 |
1.51e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 132.38 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 267 YTSGTTGKPKGVVHTHKG--IVSQVQILseAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVRGIWQR 344
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNV-CLRKVDPKLIFDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 345 WREsypnngskndEAITVFTGVPTMYTRLLQGydgmdPEQQSASsfAAKQLRLMMCGSsALPSPLMKRWEEVtGHRLLER 424
Cdd:PRK08162 266 IRE----------HGVTHYCGAPIVLSALINA-----PAEWRAG--IDHPVHAMVAGA-APPAAVIAKMEEI-GFDLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 425 YGMTEF-----VMALSN-----PLHG-ARKEGTVGKPLPCVEAKIIMEdgAETTSEV-------GELCIRSPSLFKEYWR 486
Cdd:PRK08162 327 YGLTETygpatVCAWQPewdalPLDErAQLKARQGVRYPLQEGVTVLD--PDTMQPVpadgetiGEIMFRGNIVMKGYLK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 487 KPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIIC 566
Cdd:PRK08162 405 NPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSK-DIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPC 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 567 AIIvpkedskkraELDSKPALTLEALTSWSKDKLAPYKIPTRLYLwDSLPRNAMGKVNKKELKK 630
Cdd:PRK08162 483 AFV----------ELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
157-630 |
1.72e-32 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 132.02 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 157 EFVAGIFGTWLSGGVAVPL--ALSYPEAE-----LLHVMNDSDISLILSTKEHQDIMENISTkcsahcsllpsvtsipvn 229
Cdd:cd05906 76 DFIPAFWACVLAGFVPAPLtvPPTYDEPNarlrkLRHIWQLLGSPVVLTDAELVAEFAGLET------------------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 230 iDCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLP 309
Cdd:cd05906 138 -LSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 310 LHHVHGLFNALFAPLYSGS---------VVEFMPKFsVRGIwQRWRESY---PNngskndeaitvFtgvptMYTRLLQgy 377
Cdd:cd05906 217 LDHVGGLVELHLRAVYLGCqqvhvpteeILADPLRW-LDLI-DRYRVTItwaPN-----------F-----AFALLND-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 378 dgmDPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEevtghRLLERY-----------GMTE------FVMALSNPLHG 440
Cdd:cd05906 277 ---LLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLL-----RLLEPYglppdairpafGMTEtcsgviYSRSFPTYDHS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 441 ARKEGT-VGKPLPCVEAKIIMEDG-AETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDeGYFIIL 518
Cdd:cd05906 349 QALEFVsLGRPIPGVSMRIVDDEGqLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTIT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 519 GRTnADIMKVGGYKLSALEIESVLLQHEIVLE---CAVLGLPDEAYGEIICAIIVPkedskkRAELDSKPALTLEALTSW 595
Cdd:cd05906 428 GRT-KDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVP------EYDLQDALSETLRAIRSV 500
|
490 500 510
....*....|....*....|....*....|....*...
gi 1002235085 596 SKDK--LAP-YKIPTRLylwDSLPRNAMGKVNKKELKK 630
Cdd:cd05906 501 VSREvgVSPaYLIPLPK---EEIPKTSLGKIQRSKLKA 535
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
182-629 |
1.74e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 131.74 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 182 AELLHVMNDSDISLILSTKEHQDImenistkCSAHCSLLPSVT-SIPVNIDCQEPSSTEVTSSISSLIAE-IDSskEIRG 259
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDV-------ARALLKQCPGVRhRLVLDGDGELEGFVGYAEAVAGLPATpIAD--ESLG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDpalILYTSGTTGKPKGVVH--THKGIVSQVQI---LSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---E 331
Cdd:PRK13391 157 TD---MLYSSGTTGRPKGIKRplPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIvmeH 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 332 FMPKFSVRGIwQRWResypnngskndeaITVFTGVPTMYTRLLQGydgmdPEQQSaSSFAAKQLRLMMcgSSALPSPL-- 409
Cdd:PRK13391 234 FDAEQYLALI-EEYG-------------VTHTQLVPTMFSRMLKL-----PEEVR-DKYDLSSLEVAI--HAAAPCPPqv 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 410 ---MKRWeevTGHRLLERYGMTE--FVMALSNPLHGARKeGTVGKPLpCVEAKIIMEDGAET-TSEVGELCIRSPSLFkE 483
Cdd:PRK13391 292 keqMIDW---WGPIIHEYYAATEglGFTACDSEEWLAHP-GTVGRAM-FGDLHILDDDGAELpPGEPGTIWFEGGRPF-E 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 484 YWRKPEVTAES-FIDGGFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:PRK13391 366 YLNDPAKTAEArHPDGTWSTVGDIGYVDEDGYLYLTDRA-AFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 563 EIICAIIVPKEDSkkraelDSKPALTLEaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK13391 445 EEVKAVVQPVDGV------DPGPALAAE-LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
148-628 |
2.17e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 131.69 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENIStkcsahcslLPSVTSIP 227
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLD---------LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 VNidcqEPSSTEVTSSISSLIAEidssKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHC 307
Cdd:PRK13388 126 VD----TPAYAELVAAAGALTPH----REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 308 LPLHHVHGLFnALFAP-LYSGSVVEFMPKFSVRGIW---QRWRESYPNngskndeaitvFTGVPTMYtrLLQGydgmdPE 383
Cdd:PRK13388 198 MPLFHSNAVM-AGWAPaVASGAAVALPAKFSASGFLddvRRYGATYFN-----------YVGKPLAY--ILAT-----PE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 384 QQSAssfAAKQLRLMMcGSSALPSPlMKRWEEVTGHRLLERYGMTEF-VMALSNPlhgARKEGTVGKPLPCVE------- 455
Cdd:PRK13388 259 RPDD---ADNPLRVAF-GNEASPRD-IAEFSRRFGCQVEDGYGSSEGaVIVVREP---GTPPGSIGRGAPGVAiynpetl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 456 ----AKIIMEDGAETTSE--VGELCIRS-PSLFKEYWRKPEVTAESfIDGGFFKTGDTVTVDDEGYFIILGRTnADIMKV 528
Cdd:PRK13388 331 tecaVARFDAHGALLNADeaIGELVNTAgAGFFEGYYNNPEATAER-MRHGMYWSGDLAYRDADGWIYFAGRT-ADWMRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSW--SKDKLAPYKIP 606
Cdd:PRK13388 409 DGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAT----------FDPDAFAAFlaAQPDLGTKAWP 478
|
490 500
....*....|....*....|..
gi 1002235085 607 TRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK13388 479 RYVRIAADLPSTATNKVLKREL 500
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
145-574 |
2.42e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 132.79 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLIL----STKEHQDIMENISTKcsaHCSLL 220
Cdd:PTZ00216 146 GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVcngkNVPNLLRLMKSGGMP---NTTII 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 pSVTSIPVNID---CQEPSSTEV----TSSISSLIAEIDSSKeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQV---- 289
Cdd:PTZ00216 223 -YLDSLPASVDtegCRLVAWTDVvakgHSAGSHHPLNIPENN----DDLALIMYTSGTTGDPKGVMHTHGSLTAGIlale 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 290 QILSEAWGYRSEDQ-FLHCLPLHHV--HGLFNALFA-------------------PlySGSVVEFMPKFSVrGIwQRWRE 347
Cdd:PTZ00216 298 DRLNDLIGPPEEDEtYCSYLPLAHImeFGVTNIFLArgaligfgsprtltdtfarP--HGDLTEFRPVFLI-GV-PRIFD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 348 SYpnngSKNDEAI---------TVFTgvpTMY-TRLLQGYDGMDPEQQSASSFAA------KQLRLMMCGSSALpSPLMK 411
Cdd:PTZ00216 374 TI----KKAVEAKlppvgslkrRVFD---HAYqSRLRALKEGKDTPYWNEKVFSApravlgGRVRAMLSGGGPL-SAATQ 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 412 RWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTSEV---GELCIRSPSLFKEYWRKP 488
Cdd:PTZ00216 446 EFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHTDTPeprGEILLRGPFLFKGYYKQE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 489 EVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKVGGYKLsALE-IESVLLQHEIVLE---CaVLGLPDEAYgei 564
Cdd:PTZ00216 526 ELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYI-ALEaLEALYGQNELVVPngvC-VLVHPARSY--- 600
|
490
....*....|
gi 1002235085 565 ICAIIVPKED 574
Cdd:PTZ00216 601 ICALVLTDEA 610
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
255-633 |
4.13e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 130.87 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 255 KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQvqILSEAWGYRSE--DQF--LHCLPLHHVHGLFNALFAPLYSGSVV 330
Cdd:PLN02330 179 EEILQTDLCALPFSSGTTGISKGVMLTHRNLVAN--LCSSLFSVGPEmiGQVvtLGLIPFFHIYGITGICCATLRNKGKV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 331 EFMPKFSVRGIWqrwresypnNGSKNDEaITVFTGVPTMYTRLLQgydgmDP--EQQSASSFaakQLRLMMCGSSALPSP 408
Cdd:PLN02330 257 VVMSRFELRTFL---------NALITQE-VSFAPIVPPIILNLVK-----NPivEEFDLSKL---KLQAIMTAAAPLAPE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 LMKRWE-EVTGHRLLERYGMTE---FVMALSNPL--HGARKEGTVGKPLPCVEAKIIMEDGAETTSE--VGELCIRSPSL 480
Cdd:PLN02330 319 LLTAFEaKFPGVQVQEAYGLTEhscITLTHGDPEkgHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKntPGELCVRSQCV 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 481 FKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEA 560
Cdd:PLN02330 399 MQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 561 YGEIICAIIVPKEDSKKRAeldskpaltlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLG 633
Cdd:PLN02330 478 AGEIPAACVVINPKAKESE----------EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKML 540
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
260-520 |
1.24e-31 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 130.99 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQV-QILSEAwGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK-FS 337
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVeQIKTIA-DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 338 VRGIWQRwreSYpnngsknDEAITVFTGVPTM---YTRLLQGYDgmdpeqqsassFAakQLRLMMCGSSALPSPLMKRWE 414
Cdd:PRK08043 444 YRIVPEL---VY-------DRNCTVLFGTSTFlgnYARFANPYD-----------FA--RLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 415 EVTGHRLLERYGMTEF--VMALSNPLhgARKEGTVGKPLPCVEAKIIMEDGAEttsEVGELCIRSPSLFKEYWR--KPEV 490
Cdd:PRK08043 501 DKFGLRILEGYGVTECapVVSINVPM--AAKPGTVGRILPGMDARLLSVPGIE---QGGRLQLKGPNIMNGYLRveKPGV 575
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002235085 491 -------TAESFIDGGFFKTGDTVTVDDEGYFIILGR 520
Cdd:PRK08043 576 levptaeNARGEMERGWYDTGDIVRFDEQGFVQIQGR 612
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
257-629 |
3.62e-31 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 129.38 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 257 IRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQIL-SEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGS--VVEFM 333
Cdd:PRK06060 142 MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGsaVINSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 P--KFSVRGIWQRWRESypnngskndeaitVFTGVPTMYTRLLQGYdgmdpeqqSASSFaaKQLRLMMCGSSALPSPLMK 411
Cdd:PRK06060 222 PvtPEAAAILSARFGPS-------------VLYGVPNFFARVIDSC--------SPDSF--RSLRCVVSAGEALELGLAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 412 RWEEVTGH-RLLERYGMTE----FVmalSNPLHGARKeGTVGKPLPCVEAKIIMEDGAETTSEV-GELCIRSPSLFKEYW 485
Cdd:PRK06060 279 RLMEFFGGiPILDGIGSTEvgqtFV---SNRVDEWRL-GTLGRVLPPYEIRVVAPDGTTAGPGVeGDLWVRGPAIAKGYW 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 486 RKPEVTAEsfiDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEII 565
Cdd:PRK06060 355 NRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRAD-DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTL 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 566 CAIIVPKEDskkrAELDSKpalTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK06060 431 QAFLVATSG----ATIDGS---VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
148-631 |
6.84e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.90 E-value: 6.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkeHQDIMENistkcsahcslLPSVTSIp 227
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT---QAHLLEQ-----------LPAPAGD- 3212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 228 vnidcqepssTEVTSSISSLIAEIDSSKEIR--GDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFL 305
Cdd:PRK12467 3213 ----------TALTLDRLDLNGYSENNPSTRvmGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVL 3282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 306 hclplhhvhglfnaLFAPL-YSGSVVEFMP------KFSVRGiwQRWRESYPNNGSKNDEAITVFTGVPTMYTRLLQGYD 378
Cdd:PRK12467 3283 --------------LFMSFsFDGAQERFLWtlicggCLVVRD--NDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG 3346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 GMDpeqqsassfaAKQLRLMMCGSSALPSPLMKRWEEVTGHR-LLERYGMTEfvmALSNPLH-----GARKEGT---VGK 449
Cdd:PRK12467 3347 GAD----------CASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTE---AVVTVTLwkcggDAVCEAPyapIGR 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 450 PLPCVEAKIImeDGAETTSEVG---ELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILG 519
Cdd:PRK12467 3414 PVAGRSIYVL--DGQLNPVPVGvagELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLG 3491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 520 RTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGLpDEAYGEIICAIIVPkedskkraelDSKPALTLEALTSWSKDK 599
Cdd:PRK12467 3492 RIDHQV-KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP----------ADPQGDWRETLRDHLAAS 3559
|
490 500 510
....*....|....*....|....*....|..
gi 1002235085 600 LAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PRK12467 3560 LPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
270-634 |
9.67e-31 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 126.64 E-value: 9.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 270 GTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVH-----GLFNALFAplySGSVV-----EFMPKFSvr 339
Cdd:PRK10946 192 GSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYpmsspGALGVFLA---GGTVVlapdpSATLCFP-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 gIWQRWResypnngskndeaITVFTGVPTMYTRLLQGYDGMDPEQQSASsfaakqLRLMMCGSSALPSPLMKRWEEVTGH 419
Cdd:PRK10946 267 -LIEKHQ-------------VNVTALVPPAVSLWLQAIAEGGSRAQLAS------LKLLQVGGARLSETLARRIPAELGC 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 RLLERYGMTEFVM---ALSNPlhGARKEGTVGKPL-PCVEAKIIMEDGAET-TSEVGELCIRSPSLFKEYWRKPEVTAES 494
Cdd:PRK10946 327 QLQQVFGMAEGLVnytRLDDS--DERIFTTQGRPMsPDDEVWVADADGNPLpQGEVGRLMTRGPYTFRGYYKSPQHNASA 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 495 FIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKvGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKED 574
Cdd:PRK10946 405 FDANGFYCSGDLVSIDPDGYITVVGREKDQINR-GGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002235085 575 SKkraeldskpALtleALTSWSKDK-LAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK10946 484 LK---------AV---QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
260-634 |
1.12e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 123.62 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGyrSEDQFLHCLPLHHVHGLfNALFAPLYSGS---VVEFMPKF 336
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGL-QVLVRSVIAGSepvELDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 SVrgiwqrwrESYPNngskndeAITVFTGvPTMYTRL--LQGYDGMDpeqQSASSFAAKQLRLMMCGSSALPSPLMKRWE 414
Cdd:PRK07824 112 DP--------TALPR-------AVAELGG-GRRYTSLvpMQLAKALD---DPAATAALAELDAVLVGGGPAPAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 415 EVtGHRLLERYGMTEfvmalsnplhgaRKEGTV--GKPLPCVEAKIimedgaettsEVGELCIRSPSLFKEYwRKPeVTA 492
Cdd:PRK07824 173 AA-GINVVRTYGMSE------------TSGGCVydGVPLDGVRVRV----------EDGRIALGGPTLAKGY-RNP-VDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESFIDGGFFKTGDTVTVDDeGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPk 572
Cdd:PRK07824 228 DPFAEPGWFRTDDLGALDD-GVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG- 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 573 edskkraelDSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLGA 634
Cdd:PRK07824 305 ---------DGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
155-634 |
2.47e-30 |
|
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: 124.58 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 155 SPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILstkehqdimenistkcsahcsllpsvtsipvnidcqe 234
Cdd:cd05918 59 SKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVL------------------------------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 235 psstevTSSIssliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHclplhhvh 314
Cdd:cd05918 102 ------TSSP---------------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 315 glFNA---------LFAPLYSGSVVeFMPKfsvrgiwqrwRESYPNN--GSKNDEAITVFTGVPTMyTRLLqgydgmDPE 383
Cdd:cd05918 153 --FASytfdvsileIFTTLAAGGCL-CIPS----------EEDRLNDlaGFINRLRVTWAFLTPSV-ARLL------DPE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 384 QqsassfaAKQLRLMMCGSSALPSPLMKRWEEVTghRLLERYGMTEF-VMALSNPLHGARKEGTVGKPLPCVeAKIIMED 462
Cdd:cd05918 213 D-------VPSLRTLVLGGEALTQSDVDTWADRV--RLINAYGPAECtIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 463 --------GAettseVGELCIRSPSLFKEYWRKPEVTAESFID-------------GGFFKTGDTVTVDDEGYFIILGRT 521
Cdd:cd05918 283 nhdrlvpiGA-----VGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsgrgRRLYRTGDLVRYNPDGSLEYVGRK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 522 NADImKVGGYKLSALEIESVLLQH--EIVLECAVLGLP-DEAYGEIICAIIVPKEDSKKRAELDSKPAL-------TLEA 591
Cdd:cd05918 358 DTQV-KIRGQRVELGEIEHHLRQSlpGAKEVVVEVVKPkDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEpsdefraLVAE 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1002235085 592 LTSWSKDKLAPYKIPTrlyLW---DSLPRNAMGKVNKKELKKLLGA 634
Cdd:cd05918 437 LRSKLRQRLPSYMVPS---VFlplSHLPLTASGKIDRRALRELAES 479
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
261-631 |
6.29e-30 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 124.75 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVefmpkfSVRG 340
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSV------CMRH 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRwrESYPNNGSKNdeaITVFTGVPTMYTRLLQGydgmDPEQQSASSFAAKqlrlMMCGSSALPSPLMKRWEEVtGHR 420
Cdd:PLN03102 261 VTAP--EIYKNIEMHN---VTHMCCVPTVFNILLKG----NSLDLSPRSGPVH----VLTGGSPPPAALVKKVQRL-GFQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 421 LLERYGMTEFV--------------MALSNPLHGARKEGTVGKPLPCVEAK--IIMEDGAETTSEVGELCIRSPSLFKEY 484
Cdd:PLN03102 327 VMHAYGLTEATgpvlfcewqdewnrLPENQQMELKARQGVSILGLADVDVKnkETQESVPRDGKTMGEIVIKGSSIMKGY 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 485 WRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEI 564
Cdd:PLN03102 407 LKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSK-DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 565 ICAIIVPKEDSKKRAELDSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PLN03102 485 PCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
145-606 |
1.20e-29 |
|
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: 124.10 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQD-----IMENIST-------- 211
Cdd:cd17632 93 GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDlaveaVLEGGTPprlvvfdh 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 212 --KCSAHCSLLPSVTSIPVNIDCQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKgIVSQV 289
Cdd:cd17632 173 rpEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 290 QILSEAWGYRSEDQ--FLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGIWQRWRESYPnngskndeaiTVFTGVP 367
Cdd:cd17632 252 WLKVSSIQDIRPPAsiTLNFMPMSHIAGR-ISLYGTLARGGTAYFAAASDMSTLFDDLALVRP----------TELFLVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 368 TMYTRLLQGY---------DGMDPEQQSASsfAAKQLR---------LMMCGSSALpSPLMKRW-EEVTGHRLLERYGMT 428
Cdd:cd17632 321 RVCDMLFQRYqaeldrrsvAGADAETLAER--VKAELRervlggrllAAVCGSAPL-SAEMKAFmESLLDLDLHDGYGST 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 429 EFVMALSNplhgarkeGTVGKPlPCVEAKII--MEDGAETTSEV---GELCIRSPSLFKEYWRKPEVTAESFIDGGFFKT 503
Cdd:cd17632 398 EAGAVILD--------GVIVRP-PVLDYKLVdvPELGYFRTDRPhprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 504 GDTVTVDDEGYFIILGRTNADImkvggyKLSALE------IESVLLQHEIVLECAVLGLPDEAYgeiICAIIVPKEDSKK 577
Cdd:cd17632 469 GDVMAELGPDRLVYVDRRNNVL------KLSQGEfvtvarLEAVFAASPLVRQIFVYGNSERAY---LLAVVVPTQDALA 539
|
490 500 510
....*....|....*....|....*....|...
gi 1002235085 578 R---AELdsKPALtLEALTSWSKDK-LAPYKIP 606
Cdd:cd17632 540 GedtARL--RAAL-AESLQRIAREAgLQSYEIP 569
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
260-631 |
1.91e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 122.93 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGlFNALFAPLYSGSVVEFMPKFSVR 339
Cdd:PRK06164 181 DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAPLVCEPVFDAA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 GIWQRWRESYPNNGSKNDEaitvftgvptMYTRLLQGYDGMDPeqqsassFAAkqLRLMMCGSSALPSPLMKRWEEVTGH 419
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDE----------MLRRILDTAGERAD-------FPS--ARLFGFASFAPALGELAALARARGV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 RLLERYGMTEfVMAL-----SNPLHGARKE--GTVGKPLPCVEAKIIMEDGAETTSEVGELCIRSPSLFKEYWRKPEVTA 492
Cdd:PRK06164 321 PLTGLYGSSE-VQALvalqpATDPVSVRIEggGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESFIDGGFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIIcAIIVPK 572
Cdd:PRK06164 400 RALTDDGYFRTGDLGYTRGDGQFVYQTRM-GDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPT 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 573 EDskkrAELDSkpaltlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMG---KVNKKELKKL 631
Cdd:PRK06164 478 DG----ASPDE------AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
143-628 |
1.94e-29 |
|
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: 121.81 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 143 LGGAR---IGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkehqdimenistkcsahcsl 219
Cdd:cd17650 32 LGVAPgsvVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT--------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 lpsvtsipvnidcqEPsstevtssissliaeidsskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQilseAWGYR 299
Cdd:cd17650 91 --------------QP------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH----AWRRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 300 SEdqfLHCLPLHHVH------GLFNALFA-PLYSGSVVEFMP---KFSVRGIWQRWREsypnngskndEAITVFTGVPTM 369
Cdd:cd17650 129 YE---LDSFPVRLLQmasfsfDVFAGDFArSLLNGGTLVICPdevKLDPAALYDLILK----------SRITLMESTPAL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 370 YTRLLQ--GYDGMDPEQqsassfaakqLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTEFVMALSNPLHGARKEG 445
Cdd:cd17650 196 IRPVMAyvYRNGLDLSA----------MRLLIVGSDGCKAQDFKTLAARFGQgmRIINSYGVTEATIDSTYYEEGRDPLG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 446 T-----VGKPLPCVEAKIIME-DGAETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEG 513
Cdd:cd17650 266 DsanvpIGRPLPNTAMYVLDErLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 514 YFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEdskkraeldskpALTLEALT 593
Cdd:cd17650 346 NVELLGR-VDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA------------TLNTAELR 412
|
490 500 510
....*....|....*....|....*....|....*
gi 1002235085 594 SWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17650 413 AFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
267-629 |
2.05e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 123.03 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 267 YTSGTTGKPKGVVHTHKGivSQVQILSEA--WGYRSEDQFLHCLPLHHVHG-LFNALFAPLYSGSVVefMPKFSVRGIWQ 343
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNAliWGMNEGAVYLWTLPMFHCNGwCFTWTLAALCGTNIC--LRQVTAKAIYS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 344 RWResypNNGskndeaITVFTGVPTMYTRLLQGydgmdPEQQSASSFAaKQLRLMMCGSSALPSPLMKRWEEvtGHRLLE 423
Cdd:PLN02479 278 AIA----NYG------VTHFCAAPVVLNTIVNA-----PKSETILPLP-RVVHVMTAGAAPPPSVLFAMSEK--GFRVTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 424 RYGMTE-------------------FVMALSNPLHGARKEGTVGkpLPCVEAKIIMEDGAETTSeVGELCIRSPSLFKEY 484
Cdd:PLN02479 340 TYGLSEtygpstvcawkpewdslppEEQARLNARQGVRYIGLEG--LDVVDTKTMKPVPADGKT-MGEIVMRGNMVMKGY 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 485 WRKPEVTAESFiDGGFFKTGDTVTVDDEGYFIILGRtNADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEI 564
Cdd:PLN02479 417 LKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR-SKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGES 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 565 ICAIIVPKEDSKKraeldSKPALTLEALTSWSKDKLAPYKIPtRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PLN02479 495 PCAFVTLKPGVDK-----SDEAALAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVLR 553
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
261-631 |
5.74e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 119.09 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQiLSEAW--GYRSEDQFLhClplhhvhglfNA-----------LFAPLYSG 327
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLHTTGGYLVYAA-MTMKYvfDYKDGDVYW-C----------TAdvgwvtghsyiVYGPLANG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 328 S---VVEFMPKFSVRGIWqrWR--ESYpnngskndeaitvftGVPTMYT-----RLLQGYDGMDPEQQSASSfaakqLRL 397
Cdd:PRK00174 314 AttlMFEGVPNYPDPGRF--WEviDKH---------------KVTIFYTaptaiRALMKEGDEHPKKYDLSS-----LRL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 398 MmcGSSALP-SPlmKRWE---EVTGHrllER------YGMTEFVMALSNPLHGAR--KEGTVGKPLPCVEAKIIMEDGAE 465
Cdd:PRK00174 372 L--GSVGEPiNP--EAWEwyyKVVGG---ERcpivdtWWQTETGGIMITPLPGATplKPGSATRPLPGIQPAVVDEEGNP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 466 TTSEV-GELCIRS--PSLFKEYWRKPEVTAESF---IDGGFFkTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIE 539
Cdd:PRK00174 445 LEGGEgGNLVIKDpwPGMMRTIYGDHERFVKTYfstFKGMYF-TGDGARRDEDGYYWITGRVD-DVLNVSGHRLGTAEIE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 540 SVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKIPTRLYLWDSLPRNA 619
Cdd:PRK00174 523 SALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDEL-------RKELRNWVRKEIGPIAKPDVIQFAPGLPKTR 595
|
410
....*....|..
gi 1002235085 620 MGKVNKKELKKL 631
Cdd:PRK00174 596 SGKIMRRILRKI 607
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
257-601 |
7.25e-28 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 118.83 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 257 IRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQ--FLHCLPLHHVHG---LFNALfapLYSGS--- 328
Cdd:PRK08180 206 VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGgnhNLGIV---LYNGGtly 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 ------VVEFMPKfSVRGIwqrwRESYPnngskndeaiTVFTGVPTMYTRLLqgyDGMDPEQQSASSFAAKqLRLMMCGS 402
Cdd:PRK08180 283 iddgkpTPGGFDE-TLRNL----REISP----------TVYFNVPKGWEMLV---PALERDAALRRRFFSR-LKLLFYAG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALPSPLMKRWEEV----TGHR--LLERYGMTE---FVMALSNPLHGArkeGTVGKPLPCVEAKIIMEDGAEttsevgEL 473
Cdd:PRK08180 344 AALSQDVWDRLDRVaeatCGERirMMTGLGMTEtapSATFTTGPLSRA---GNIGLPAPGCEVKLVPVGGKL------EV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 474 CIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGY----FIILGRTNADimkvggYKLSALEIESV-LLQHEIV 548
Cdd:PRK08180 415 RVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADpergLMFDGRIAED------FKLSSGTWVSVgPLRARAV 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 549 LECA------VLGLPDEAYgeiICAIIVPKEDSKKR-----AELDSKPALTLEALTSWSKDKLA 601
Cdd:PRK08180 489 SAGAplvqdvVITGHDRDE---IGLLVFPNLDACRRlagllADASLAEVLAHPAVRAAFRERLA 549
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
146-628 |
1.39e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.50 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 146 ARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkeHQDIMENistkcsahcslLPSVTS 225
Cdd:PRK05691 1182 VCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT---QSHLLER-----------LPQAEG 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 226 I-PVNIDCQEPSSTEVTSSISSLiaeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:PRK05691 1248 VsAIALDSLHLDSWPSQAPGLHL----------HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVL 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHHVHGLFNAlFAPLYSGSvvefmpKFSVRGIWQRwRESYPNNGSKNDEAITVFTGVPTMYTRLLQgydgmDPEQ 384
Cdd:PRK05691 1318 MQKAPISFDVSVWEC-FWPLITGC------RLVLAGPGEH-RDPQRIAELVQQYGVTTLHFVPPLLQLFID-----EPLA 1384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSASSfaakqLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMalsNPLH-------GARKegTVGKPLPCVEA 456
Cdd:PRK05691 1385 AACTS-----LRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAI---NVTHwqcqaedGERS--PIGRPLGNVLC 1454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEDGAETTSEV-GELCIRSPSLFKEYWRKPEVTAESFI------DGG-FFKTGDTVTVDDEGYFIILGRTNADImKV 528
Cdd:PRK05691 1455 RVLDAELNLLPPGVaGELCIGGAGLARGYLGRPALTAERFVpdplgeDGArLYRTGDRARWNADGALEYLGRLDQQV-KL 1533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 529 GGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELdsKPALTLEaltswskdkLAPYKIPTR 608
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERL--KAALAAE---------LPEYMVPAQ 1602
|
490 500
....*....|....*....|
gi 1002235085 609 LYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK05691 1603 LIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
145-630 |
5.01e-27 |
|
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: 114.33 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKehqdimenistkcsahcsllpsvt 224
Cdd:cd17653 47 GDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD------------------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 sipvnidcqepsstevtssissliaeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQF 304
Cdd:cd17653 103 ---------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 305 LHCLPLHhvhglFNA----LFAPL-YSGSVVefmpkfsvrgiwqrWRESYPNNGSKNDEaITVFTGVPTMYTRL-LQGYD 378
Cdd:cd17653 150 AQVLSIA-----FDAcigeIFSTLcNGGTLV--------------LADPSDPFAHVART-VDALMSTPSILSTLsPQDFP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmdpeqqsassfaakQLRLMMCGSSALPSPLMKRWEEvtGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKI 458
Cdd:cd17653 210 ---------------NLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 459 IMEDGAETT-SEVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNADImKVGGY 531
Cdd:cd17653 273 LDADLQPVPeGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQV-KVRGF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 532 KLSALEIESVLLQHEIVLECAVLGLPDEAygeiICAIIVPkedskkrAELDskpaltLEALTSWSKDKLAPYKIPTRLYL 611
Cdd:cd17653 352 RINLEEIEEVVLQSQPEVTQAAAIVVNGR----LVAFVTP-------ETVD------VDGLRSELAKHLPSYAVPDRIIA 414
|
490
....*....|....*....
gi 1002235085 612 WDSLPRNAMGKVNKKELKK 630
Cdd:cd17653 415 LDSFPLTANGKVDRKALRE 433
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
260-631 |
7.34e-27 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 115.77 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKG-IVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPk 335
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVlvfEGAP- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 336 fsvrgiwqrwreSYPNNGSKND----EAITVFTGVPTMYTRLLQgyDGMDPeqqsASSFAAKQLRLMmcGSSALP-SPLM 410
Cdd:PLN02654 354 ------------NYPDSGRCWDivdkYKVTIFYTAPTLVRSLMR--DGDEY----VTRHSRKSLRVL--GSVGEPiNPSA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 411 KRW-EEVTGHR---LLERYGMTEFVMALSNPLHGA--RKEGTVGKPLPCVEAKIIMEDGAETTSEV-GELCIRS--PSLF 481
Cdd:PLN02654 414 WRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKEIEGECsGYLCVKKswPGAF 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 482 KEYWRKPEVTAESFID--GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDE 559
Cdd:PLN02654 494 RTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 560 AYGEIICAIIVPKEDSKKRAELDSKPALTLealtswsKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 631
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLILTV-------RNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
235-574 |
7.38e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.97 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 235 PSSTEVT-SSISSLIAEIDSSKEI----RGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLP 309
Cdd:PLN02736 191 PSGTGVEiVTYSKLLAQGRSSPQPfrppKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLP 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 310 LHHVHGLFNALfAPLYSGSVVEFmpkfsvrgiwqrwresYPNNGSK--NDEAI---TVFTGVPTMYTRLlqgYDGMDPEQ 384
Cdd:PLN02736 271 LAHIYERVNQI-VMLHYGVAVGF----------------YQGDNLKlmDDLAAlrpTIFCSVPRLYNRI---YDGITNAV 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 385 QSAS---------SFAAKQ----------------------------LRLMMCGSSALPSPLMKRWEEVTGHRLLERYGM 427
Cdd:PLN02736 331 KESGglkerlfnaAYNAKKqalengknpspmwdrlvfnkikaklggrVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGM 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 428 TEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTSE-----VGELCIRSPSLFKEYWRKPEVTAESFIDGGFFK 502
Cdd:PLN02736 411 TETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEdqpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 503 TGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALE-IESVLLQHEIVLECAVLGlpdEAYGEIICAIIVPKED 574
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKK-NIFKLAQGEYIAPEkIENVYAKCKFVAQCFVYG---DSLNSSLVAVVVVDPE 559
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
145-628 |
3.65e-26 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 112.79 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILstkehqdIMENISTKCSAHCSLLPSVT 224
Cdd:PRK05857 66 GSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAL-------VAPGSKMASSAVPEALHSIP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEvTSSISSLIAEIDSSkeirGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSE---AW-GYRS 300
Cdd:PRK05857 139 VIAVDIAAVTRESEH-SLDAASLAGNADQG----SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKeglNWvTWVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK-FSVRGIWqrwresypnngskNDEAITVFTGVPTMYTRLLQgydg 379
Cdd:PRK05857 214 GETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENtTSLLEIL-------------TTNAVATTCLVPTLLSKLVS---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 380 mdpEQQSASSfAAKQLRLMMCGSS-ALPSPLmkRWEEVTGHRLLERYGMTEF-VMALSNPLHG---ARKE-GTVGKPLPC 453
Cdd:PRK05857 277 ---ELKSANA-TVPSLRLVGYGGSrAIAADV--RFIEATGVRTAQVYGLSETgCTALCLPTDDgsiVKIEaGAVGRPYPG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 454 VEAKIIMEDGAETT-------SEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTNADIM 526
Cdd:PRK05857 351 VDVYLAATDGIGPTapgagpsASFGTLWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMII 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 527 KvGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKedskkrAELDSKPALTLE-ALTSWSKDKLAPYKI 605
Cdd:PRK05857 430 C-GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAS------AELDESAARALKhTIAARFRRESEPMAR 502
|
490 500
....*....|....*....|...
gi 1002235085 606 PTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK05857 503 PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
145-622 |
6.63e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 111.90 E-value: 6.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENIstkcsahcslLPSVT 224
Cdd:PRK07798 53 GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEV----------LPRLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNIDCQEPSSTEVTS---SISSLIAEIDSSKEI--RGDDPALILYTSGTTGKPKGVVHTHKGI-------------- 285
Cdd:PRK07798 123 KLRTLVVVEDGSGNDLLPgavDYEDALAAGSPERDFgeRSPDDLYLLYTGGTTGMPKGVMWRQEDIfrvllggrdfatge 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 286 -----VSQVQILSEAWGYRsedqFLHCLPLHHVHGLFNAlFAPLYSGSVVEFMP--KFSVRGIWQrwresypnngSKNDE 358
Cdd:PRK07798 203 piedeEELAKRAAAGPGMR----RFPAPPLMHGAGQWAA-FAALFSGQTVVLLPdvRFDADEVWR----------TIERE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 359 AITVFTGVPTMYTR-LLQGYDgmDPEQQSASSFAAkqlrlmmCGSSALP-SPLMK-RWEEVTGHR-LLERYGMTE----- 429
Cdd:PRK07798 268 KVNVITIVGDAMARpLLDALE--ARGPYDLSSLFA-------IASGGALfSPSVKeALLELLPNVvLTDSIGSSEtgfgg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 430 FVMALSNPLHGARKEGTVGKplpcvEAKIIMEDGAETTSEVGELCI--RSPSLFKEYWRKPEVTAESF--IDGGFFK-TG 504
Cdd:PRK07798 339 SGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFptIDGVRYAiPG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 505 DTVTVDDEGYFIILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSkkraeldsk 584
Cdd:PRK07798 414 DRARVEADGTITLLGRGSVCI-NTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGA--------- 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 1002235085 585 pALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGK 622
Cdd:PRK07798 484 -RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
155-630 |
6.74e-26 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 111.91 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 155 SPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdimenistkcsahcsLLPSVTSIPVnidcqe 234
Cdd:PRK04813 62 SPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEE-----------------LPLEILGIPV------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 235 pSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHhvh 314
Cdd:PRK04813 119 -ITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYS--- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 315 glFN----ALFAPLYSGSVVEFMPKFSVRGIWQRWRE--SYPnngskndeaITVFTGVPTMYTRLLqgydgMDPeqqsas 388
Cdd:PRK04813 195 --FDlsvmDLYPTLASGGTLVALPKDMTANFKQLFETlpQLP---------INVWVSTPSFADMCL-----LDP------ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 389 SFAAKQL----RLMMCGssalpsplmkrwEEVTgHR----LLER---------YGMTEFVMALS------------NPLh 439
Cdd:PRK04813 253 SFNEEHLpnltHFLFCG------------EELP-HKtakkLLERfpsatiyntYGPTEATVAVTsieitdemldqyKRL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 440 garkegTVGKPLPCVEAKIIMEDGAE-TTSEVGELCIRSPSLFKEYWRKPEVTAESF--IDG-GFFKTGDTVTVDDeGYF 515
Cdd:PRK04813 319 ------PIGYAKPDSPLLIIDEEGTKlPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGqPAYHTGDAGYLED-GLL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 516 IILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGL-PDEAYGEIIcAIIVPKEDSKKRaELDskpaLTlEALTS 594
Cdd:PRK04813 392 FYQGRIDFQI-KLNGYRIELEEIEQNLRQSSYVESAVVVPYnKDHKVQYLI-AYVVPKEEDFER-EFE----LT-KAIKK 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002235085 595 WSKDKLAPYKIPTRlYLW-DSLPRNAMGKVNKKELKK 630
Cdd:PRK04813 464 ELKERLMEYMIPRK-FIYrDSLPLTPNGKIDRKALIE 499
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
260-626 |
1.50e-25 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 111.37 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSED--QFLHCLPLHHVHGLFNALFAPLYSGSVVEF----- 332
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 333 MPkfsvrgiwQRWRESYPNngsKNDEAITVFTGVPTMYTRLLQGydgMDPEQQSASSFAAKqLRLMMCGSSALPSPLMKR 412
Cdd:cd05921 245 MP--------GGFEETLRN---LREISPTVYFNVPAGWEMLVAA---LEKDEALRRRFFKR-LKLMFYAGAGLSQDVWDR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 413 WEEV----TGHR--LLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAEttsevgELCIRSPSLFKEYWR 486
Cdd:cd05921 310 LQALavatVGERipMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKY------EVRVKGPNVTPGYWR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 487 KPEVTAESFIDGGFFKTGDTVTV----DDEGYFIILGRTNADimkvggYKLSALEIESV-LLQHEIVLEC------AVLG 555
Cdd:cd05921 384 QPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAED------FKLASGTWVSVgPLRARAVAACaplvhdAVVA 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 556 LPDeayGEIICAIIVPKEDSKKR----AELDSKPALTLEALTSWSKDKLAPYK--------IPTRLYLWDSLPRNAMGKV 623
Cdd:cd05921 458 GED---RAEVGALVFPDLLACRRlvglQEASDAEVLRHAKVRAAFRDRLAALNgeatgsssRIARALLLDEPPSIDKGEI 534
|
...
gi 1002235085 624 NKK 626
Cdd:cd05921 535 TDK 537
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
147-628 |
1.66e-25 |
|
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: 109.80 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPeaellhvmnDSDISLILSTKEHQDIMENIStkcsahcsllpsvtsi 226
Cdd:cd17648 40 LVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYP---------DERIQFILEDTGARVVITNST---------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 pvnidcqepsstevtssissliaeidsskeirgdDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQflh 306
Cdd:cd17648 95 ----------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 307 clplHHVHGLFNALFAP--------LYSGSVVeFMPKFSVRGIWQRWresYPnngSKNDEAITVFTGVPTmytrLLQGYD 378
Cdd:cd17648 138 ----EAVLFFSNYVFDFfveqmtlaLLNGQKL-VVPPDEMRFDPDRF---YA---YINREKVTYLSGTPS----VLQQYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmdpeQQSASSfaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHG-ARKEGTVGKPLPCVEA 456
Cdd:cd17648 203 -----LARLPH-----LKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETtVTNHKRFFPGdQRFDKSLGRPVRNTKC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMED------GAettseVGELCIRSPSLFKEYWRKPEVTAESFIDGGF--------------FKTGDTVTVDDEGYFI 516
Cdd:cd17648 273 YVLNDAmkrvpvGA-----VGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 517 ILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVLG--LPDEAYGEIICAII---VPKEDskkraeldskpALTLEA 591
Cdd:cd17648 348 YLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLVgyyLPEPG-----------HVPESD 415
|
490 500 510
....*....|....*....|....*....|....*..
gi 1002235085 592 LTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17648 416 LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
130-628 |
2.61e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 110.09 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 130 TGSSVKGINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEhqdIMENI 209
Cdd:PRK13383 70 TESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE---FAERI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 210 STKCSAHCSLLPSVtsipvnidcqepssteVTSSISSLIAEIDSSKEIrgddpalILYTSGTTGKPKGVVHTHK---GIV 286
Cdd:PRK13383 147 AGADDAVAVIDPAT----------------AGAEESGGRPAVAAPGRI-------VLLTSGTTGKPKGVPRAPQlrsAVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 287 SQVQILsEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEfmpkfsvrgiwQRWRESYPNNGSKNDEAITVFTGV 366
Cdd:PRK13383 204 VWVTIL-DRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT-----------HRHFDAEAALAQASLHRADAFTAV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 367 PTMYTRLLQGydgmdPEQQSASSfAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGARKEG 445
Cdd:PRK13383 272 PVVLARILEL-----PPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 446 TVGKPLPCVEAKIIMEDGaettSEVGelcirsPSLFKEYWRKPEVTAESFIDGG-------FFKTGDTVTVDDEGYFIIL 518
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNN----RPVG------PRVTGRIFVGGELAGTRYTDGGgkavvdgMTSTGDMGYLDNAGRLFIV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 519 GRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAeldskpaltlEALTSWSKD 598
Cdd:PRK13383 416 GRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA----------AQLRDYLKD 484
|
490 500 510
....*....|....*....|....*....|
gi 1002235085 599 KLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
260-580 |
5.10e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 109.60 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPlhhvhgLFnALFAP-LYSGSVVEFM----- 333
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFP------LF-ALFGPaLGMTSVIPDMdptrp 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 ----PKFSVRGIwqrwresypnngskNDEAITVFTGVPTMYTRLLQ-GydgmdpeQQSASSFAAkqLRLMMCGSSALPSP 408
Cdd:PRK09274 247 atvdPAKLFAAI--------------ERYGVTNLFGSPALLERLGRyG-------EANGIKLPS--LRRVISAGAPVPIA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 LMKRWEEVTGH--RLLERYGMTE----FVMALSNPLHGARK-----EGT-VGKPLPCVEAKII-MEDGAETTS------- 468
Cdd:PRK09274 304 VIERFRAMLPPdaEILTPYGATEalpiSSIESREILFATRAatdngAGIcVGRPVDGVEVRIIaISDAPIPEWddalrla 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 469 --EVGELCIRSPSLFKEYWRKPEVTAESFI---DGGFF-KTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVL 542
Cdd:PRK09274 384 tgEIGEIVVAGPMVTRSYYNRPEATRLAKIpdgQGDVWhRMGDLGYLDAQGRLWFCGRK-AHRVETAGGTLYTIPCERIF 462
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002235085 543 LQHEIVLECAVLGLPDEayGEIICAIIVPKEDSKKRAE 580
Cdd:PRK09274 463 NTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSK 498
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
136-566 |
7.74e-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: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 136 GINGTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQdimeniSTKCSA 215
Cdd:cd17641 27 GLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDEEQ------VDKLLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 216 HCSLLPSVTSIPV-------------------------NIDCQEPSSTEvtssissliAEIDsskEIRGDDPALILYTSG 270
Cdd:cd17641 101 IADRIPSVRYVIYcdprgmrkyddprlisfedvvalgrALDRRDPGLYE---------REVA---AGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 271 TTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM--------------PKF 336
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPeepetmmedlreigPTF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 ----------SVRGIWQRWRESYPNNGSKNDEAITVftgvptMYTRLLQGYDG--MDPEQQSASSFAAK----------- 393
Cdd:cd17641 249 vllpprvwegIAADVRARMMDATPFKRFMFELGMKL------GLRALDRGKRGrpVSLWLRLASWLADAllfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 394 --QLRLMMCGSSALpSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIimedgaettSEVG 471
Cdd:cd17641 323 fsRLRSAATGGAAL-GPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI---------DEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 472 ELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVG-GYKLSALEIESVLLQHEIVLE 550
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAK-DVGTTSdGTRFSPQFIENKLKFSPYIAE 471
|
490
....*....|....*.
gi 1002235085 551 CAVLGLPDEAYGEIIC 566
Cdd:cd17641 472 AVVLGAGRPYLTAFIC 487
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
145-571 |
1.48e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 105.69 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAHCSLLPSVT 224
Cdd:PLN02861 102 GDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPVNID------CQEPSSTEVTSSISSLIAEIDSSkeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQV----QILSE 294
Cdd:PLN02861 182 DVSSEQKeeaeelGVSCFSWEEFSLMGSLDCELPPK---QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstdHLLKV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 295 A-WGYRSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMpKFSVRGIWQRWRESYPnngskndeaiTVFTGVPTMYTRL 373
Cdd:PLN02861 259 TdRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFW-QGDIRYLMEDVQALKP----------TIFCGVPRVYDRI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LQGYD------GMDPE-------------------QQSASSFAAK------------QLRLMMCGSSALPSPLMKRWEEV 416
Cdd:PLN02861 327 YTGIMqkissgGMLRKklfdfaynyklgnlrkglkQEEASPRLDRlvfdkikeglggRVRLLLSGAAPLPRHVEEFLRVT 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 417 TGHRLLERYGMTEFVMALSNPLHGARKE-GTVGKPLPCVEAKI--IMEDGAETTSEV--GELCIRSPSLFKEYWRKPEVT 491
Cdd:PLN02861 407 SCSVLSQGYGLTESCGGCFTSIANVFSMvGTVGVPMTTIEARLesVPEMGYDALSDVprGEICLRGNTLFSGYHKRQDLT 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 492 AESFIDgGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALE-IESVLLQHEIVLECAVLGLPDEAYgeiICAIIV 570
Cdd:PLN02861 487 EEVLID-GWFHTGDIGEWQPNGAMKIIDRKK-NIFKLSQGEYVAVEnLENTYSRCPLIASIWVYGNSFESF---LVAVVV 561
|
.
gi 1002235085 571 P 571
Cdd:PLN02861 562 P 562
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
263-629 |
6.74e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 102.39 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 263 ALILYTSGTTGKPKGVVHTHKG-IVSQ-----VQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFM 333
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDLPGrDVDApgdpiVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVlakRFD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 PKFSVRGIwQRWResypnngskndeaITVFTGVPTMYTRLLQgydgMDPEQQSasSFAAKQLRLMMCGSSALPSPLMKRW 413
Cdd:PRK13390 231 AQATLGHV-ERYR-------------ITVTQMVPTMFVRLLK----LDADVRT--RYDVSSLRAVIHAAAPCPVDVKHAM 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 414 EEVTGHRLLERYGMTE-FVMALSNPLHGARKEGTVGKPLpCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEVT 491
Cdd:PRK13390 291 IDWLGPIVYEYYSSTEaHGMTFIDSPDWLAHPGSVGRSV-LGDLHICDDDGNELPAgRIGTVYFERDRLPFRYLNDPEKT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 492 AESFIDGGFFKT--GDTVTVDDEGYFIILGRTNADIMKvGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAII 569
Cdd:PRK13390 370 AAAQHPAHPFWTtvGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVI 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 570 VPKEDSKKRAELDSKpaltleaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK13390 449 QLVEGIRGSDELARE-------LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-624 |
1.11e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 100.15 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 258 RGDDPALILYTSGTTGKPKGVVHTH----------KGIVSQVQILSEAWGYRSEDQ----FLHCLPLHHVHGLFNALFAP 323
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAAagtvMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 324 LYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFTGVPTMYTR-LLQGYDGMDPeqqsassFAAKQLRLMMCGS 402
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEK----------HKVTSMTIVGDAMARpLIDALRDAGP-------YDLSSLFAISSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALPSPLMKRWEEVTGHRLL------ERYGMTEFVMALSNPlHGARKEGTVGkPLPCVeakiIMEDGAETT--SEVGELC 474
Cdd:cd05924 144 ALLSPEVKQGLLELVPNITLvdafgsSETGFTGSGHSAGSG-PETGPFTRAN-PDTVV----LDDDGRVVPpgSGGVGWI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 475 IRSPSLFKEYWRKPEVTAESF--IDGGFFK-TGDTVTVDDEGYFIILGRTNADImKVGGYKLSALEIESVLLQHEIVLEC 551
Cdd:cd05924 218 ARRGHIPLGYYGDEAKTAETFpeVDGVRYAvPGDRATVEADGTVTLLGRGSVCI-NTGGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 552 AVLGLPDEAYGEIICAIivpkedskkrAELDSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 624
Cdd:cd05924 297 LVVGRPDERWGQEVVAV----------VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
109-628 |
1.82e-22 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 100.62 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 109 IASALDVY-NILRNKNMTQNGStgssvkgingtgflggarIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHV 187
Cdd:cd17654 22 LAEKISNLsNFLRKKFQTEERA------------------IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 188 MNDSDISLILSTKEHqdimenistkcsahCSLLPSVTSIPVNIDCQEPSSTevtssissliaeidsskeirgddpALILY 267
Cdd:cd17654 84 MKKCHVSYLLQNKEL--------------DNAPLSFTPEHRHFNIRTDECL------------------------AYVIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 268 TSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHhvhglfnalFAPlysgSVVEFMPKFSVRGIWQRWRE 347
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLT---------FDP----SVVEIFLSLSSGATLLIVPT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 348 SYPNNGSKNDEA------ITVFTGVPTMYTRLLqgydgmdpeQQSASSF---AAKQLRLMMCGSSALPSP-LMKRW-EEV 416
Cdd:cd17654 193 SVKVLPSKLADIlfkrhrITVLQATPTLFRRFG---------SQSIKSTvlsATSSLRVLALGGEPFPSLvILSSWrGKG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 417 TGHRLLERYGMTEfVMALSNPLHGARKEGTVGKPLPCVEAKIIMEDgAETTSEVGELCIRSPSLFkeYWRKPEVTAesfI 496
Cdd:cd17654 264 NRTRIFNIYGITE-VSCWALAYKVPEEDSPVQLGSPLLGTVIEVRD-QNGSEGTGQVFLGGLNRV--CILDDEVTV---P 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 497 DGGFFKTGDTVTVDDEGYFiILGRTNADImKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEaygEIICAIIVPKEDSK 576
Cdd:cd17654 337 KGTMRATGDFVTVKDGELF-FLGRKDSQI-KRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ---RLIAFIVGESSSSR 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002235085 577 KRAELdskpaltlealtswSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17654 412 IHKEL--------------QLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
148-539 |
2.03e-22 |
|
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: 101.67 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 148 IGIVAKPSPEFVAGIFGTWLSGGVAVP-LALSYPEAeLLHVMNDSDISLIL--STKEHQDIMEnISTKcsahcslLPSVT 224
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGiYTTNSPEA-CQYVAETSEANILVveNQKQLQKILQ-IQDK-------LPHLK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIpvnIDCQEPSST------------EVTSSIS--SLIAEIDSskeIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQ 290
Cdd:cd05933 107 AI---IQYKEPLKEkepnlyswdefmELGRSIPdeQLDAIISS---QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 291 ILSEAWGYRSEDQ----FLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG-IWQRWRESYPnngskndeaiTVFTG 365
Cdd:cd05933 181 AASQHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGtLVKTLREVRP----------TAFMG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 366 VPTMYTRLLqgyDGMDPEQQSASSFAAK------------QLRLMMcGSSalPSPLMKRWEE------------------ 415
Cdd:cd05933 251 VPRVWEKIQ---EKMKAVGAKSGTLKRKiaswakgvgletNLKLMG-GES--PSPLFYRLAKklvfkkvrkalgldrcqk 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 416 -VTGH----------------RLLERYGMTEFVMA--LSNPlhGARKEGTVGKPLPCVEAKIIMEDgaetTSEVGELCIR 476
Cdd:cd05933 325 fFTGAapisretlefflslniPIMELYGMSETSGPhtISNP--QAYRLLSCGKALPGCKTKIHNPD----ADGIGEICFW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 477 SPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTNADIMKVGGYKLSALEIE 539
Cdd:cd05933 399 GRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIE 461
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
169-630 |
3.36e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 102.04 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 169 GGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENIstkcsahcsllPSVTSIPVNIDCQEPSSTEVTSSissli 248
Cdd:PRK10252 532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADV-----------PDLTSLCYNAPLAPQGAAPLQLS----- 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 249 aeidsskeiRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHhvhglFNA----LFAPL 324
Cdd:PRK10252 596 ---------QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCS-----FDVsvweFFWPF 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 325 YSGSVVEFMPKFSVRG-IW-QRWREsypnngsknDEAITVFTGVPTMYTRLLQgydgmDPEQQSASSfAAKQLRLMMCGS 402
Cdd:PRK10252 662 IAGAKLVMAEPEAHRDpLAmQQFFA---------EYGVTTTHFVPSMLAAFVA-----SLTPEGARQ-SCASLRQVFCSG 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGARKEGTVGKPLPcveakI----------IMED-------GA 464
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWyPAFGEELAAVRGSSVP-----IgypvwntglrILDArmrpvppGV 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 465 ettseVGELCIRSPSLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEI 538
Cdd:PRK10252 802 -----AGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSD-DQLKIRGQRIELGEI 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 539 ESVLLQHE-----IVLECaVLGLPDEAYGEI--ICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYL 611
Cdd:PRK10252 876 DRAMQALPdveqaVTHAC-VINQAAATGGDArqLVGYLVSQSGL----------PLDTSALQAQLRERLPPHMVPVVLLQ 944
|
490
....*....|....*....
gi 1002235085 612 WDSLPRNAMGKVNKKELKK 630
Cdd:PRK10252 945 LDQLPLSANGKLDRKALPL 963
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
260-630 |
5.18e-22 |
|
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: 99.43 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 339
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSAS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 GIWQRWRESYPNngskndeaITVFTGVPTMYtrLLQG----YDgmdpeqqsassfaaKQLRLMMCGSSALPSPLMKRWEE 415
Cdd:cd05937 167 QFWKDVRDSGAT--------IIQYVGELCRY--LLSTppspYD--------------RDHKVRVAWGNGLRPDIWERFRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 416 VTGHRLL-ERYGMTEFVMALSNPLHGARKEGTVGKPLPC---------VEAKIIMEDGAETTSEVGELCIRSP------- 478
Cdd:cd05937 223 RFNVPEIgEFYAATEGVFALTNHNVGDFGAGAIGHHGLIrrwkfenqvVLVKMDPETDDPIRDPKTGFCVRAPvgepgem 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 479 ---------SLFKEYWRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLL 543
Cdd:cd05937 303 lgrvpfknrEAFQGYLHNEDATESKLVRDVFrkgdiyFRTGDLLRQDADGRWYFLDRL-GDTFRWKSENVSTTEVADVLG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 544 QHEIVLECAVLGLPDEAY-GEIICAIIVPKEDSKKRAEldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGK 622
Cdd:cd05937 382 AHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAVPTE------FTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHK 455
|
....*...
gi 1002235085 623 VNKKELKK 630
Cdd:cd05937 456 QQKGVLRD 463
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
249-512 |
6.54e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.12 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 249 AEIDSSKEIRGDDP-ALILYTSGTTGKPKGVVHTHKGIVSQVQILSeawGYRSED------QFLHCLPLHHVHGlFNALF 321
Cdd:PRK12582 208 AAVAAAIAAITPDTvAKYLFTSGSTGMPKAVINTQRMMCANIAMQE---QLRPREpdppppVSLDWMPWNHTMG-GNANF 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 322 AP-LYSGSVVEFMPKFSVRGIW----QRWRESYPnngskndeaiTVFTGVPTMYTRLLqgyDGMDPEQQSASSFAaKQLR 396
Cdd:PRK12582 284 NGlLWGGGTLYIDDGKPLPGMFeetiRNLREISP----------TVYGNVPAGYAMLA---EAMEKDDALRRSFF-KNLR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 397 LMMCGSSALPSPLMKRWEEV----TGHR--LLERYGMTEFVMALSNPLHGARKEGTVGKPLPCVEAKIImedgaettsEV 470
Cdd:PRK12582 350 LMAYGGATLSDDLYERMQALavrtTGHRipFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLA---------PV 420
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002235085 471 G---ELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVT-VDDE 512
Cdd:PRK12582 421 GdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPD 466
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
250-629 |
1.70e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 94.33 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 250 EIDSSKEIRG----DDPALILYTSGTTGKPKGVVHT----HKGIVSQVQILSEAwgyRSEDQFLHClPLHHVHGLFNALF 321
Cdd:PRK08308 87 ESDFTKLEAVnylaEEPSLLQYSSGTTGEPKLIRRSwteiDREIEAYNEALNCE---QDETPIVAC-PVTHSYGLICGVL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 322 APLYSGSVVEFM----PKFsvrgIWQRWREsYPNNgskndeaitVFTGVPTMY---TRLLqgydgmdPEQQsassfaakQ 394
Cdd:PRK08308 163 AALTRGSKPVIItnknPKF----ALNILRN-TPQH---------ILYAVPLMLhilGRLL-------PGTF--------Q 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 395 LRLMMCGSSALPSPLMKRWEEVTGHrLLERYGMTEF-VMALSNPLhgaRKEGTVGKPLPCVEAKIIMEDGA--ETTSEVG 471
Cdd:PRK08308 214 FHAVMTSGTPLPEAWFYKLRERTTY-MMQQYGCSEAgCVSICPDM---KSHLDLGNPLPHVSVSAGSDENApeEIVVKMG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 472 ELCIRSPSLfkeywrkpevtaesfidgGFFktgdtvtvDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLEC 551
Cdd:PRK08308 290 DKEIFTKDL------------------GYK--------SERGTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEA 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002235085 552 AVLGLPDEAYGEIICAIIVpkedskkraeldSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PRK08308 343 VVYRGKDPVAGERVKAKVI------------SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-556 |
2.78e-20 |
|
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: 94.06 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 258 RGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHhvhglfnALFAPLYS-GSVVEFM--- 333
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGlTSVIPDMdpt 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 ------PKFSVRGIwQRWRESypnngskndeaiTVFtGVPTMYTRLlqGYDGMDPEQQSASsfaakqLRLMMCGSSALPS 407
Cdd:cd05910 156 rparadPQKLVGAI-RQYGVS------------IVF-GSPALLERV--ARYCAQHGITLPS------LRRVLSAGAPVPI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 408 PLMKRWEEVT--GHRLLERYGMTE---FVMALSNPLHGARKEGT-------VGKPLPCVEAKIIMEDGAETTS------- 468
Cdd:cd05910 214 ALAARLRKMLsdEAEILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIAEwddtlel 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 469 ---EVGELCIRSPSLFKEYWRKPEVTAESFI---DGGFF-KTGDTVTVDDEGYFIILGRTNADIMKVGGyKLSALEIESV 541
Cdd:cd05910 294 prgEIGEITVTGPTVTPTYVNRPVATALAKIddnSEGFWhRMGDLGYLDDEGRLWFCGRKAHRVITTGG-TLYTEPVERV 372
|
330
....*....|....*
gi 1002235085 542 LLQHEIVLECAVLGL 556
Cdd:cd05910 373 FNTHPGVRRSALVGV 387
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
219-616 |
3.23e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 90.70 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 LLPSVTSIPVNIDCQEPSSTEVTSSISSLIAEIDSSKeIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGY 298
Cdd:PRK09029 95 LLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA-WQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 299 RSEDQFLHCLPLHHVHGLfnalfaplysgsvvefmpkfsvrGIWQRW---------RESYPNngsknDEAITVFTG---V 366
Cdd:PRK09029 174 TAQDSWLLSLPLFHVSGQ-----------------------GIVWRWlyagatlvvRDKQPL-----EQALAGCTHaslV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 367 PTMYTRLLQgydgmdpeqQSASSFAAKQLRLmmcGSSALPSPLMKRWEEvTGHRLLERYGMTEF---VMAlsnplhgarK 443
Cdd:PRK09029 226 PTQLWRLLD---------NRSEPLSLKAVLL---GGAAIPVELTEQAEQ-QGIRCWCGYGLTEMastVCA---------K 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 444 E----GTVGKPLPCVEAKIIMedgaettsevGELCIRSPSLFKEYWRKPEVTaeSFIDG-GFFKTGDTVTVDDeGYFIIL 518
Cdd:PRK09029 284 RadglAGVGSPLPGREVKLVD----------GEIWLRGASLALGYWRQGQLV--PLVNDeGWFATRDRGEWQN-GELTIL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 519 GRtnADIMKV-GGYKLSALEIESVLLQHEIVLEcavlglpdeaygeiicAIIVPKEDSK--KR--AELDSKPALTLEALT 593
Cdd:PRK09029 351 GR--LDNLFFsGGEGIQPEEIERVINQHPLVQQ----------------VFVVPVADAEfgQRpvAVVESDSEAAVVNLA 412
|
410 420
....*....|....*....|...
gi 1002235085 594 SWSKDKLAPYKIPTRLYLwdsLP 616
Cdd:PRK09029 413 EWLQDKLARFQQPVAYYL---LP 432
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-631 |
3.44e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.92 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIV----SQVQIL--SEA-----WGYRSED----QFLHclplhhvhglfnalfAPL 324
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlSKVPYLalSEAdviaqTASQSFDisvwQFLA---------------APL 3933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 325 YsGSVVEFMPKFSVR---GIWQRWREsypnngskndEAITVFTGVPTMYTRLLQgydgmdPEQQSASSfaakqLRLMMCG 401
Cdd:PRK05691 3934 F-GARVEIVPNAIAHdpqGLLAHVQA----------QGITVLESVPSLIQGMLA------EDRQALDG-----LRWMLPT 3991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 402 SSALPSPLMKRWeevtghrlLERYGMTEFVMAL-----SNPLHGAR--KEGTVGKPLPC------------VEAKIIMED 462
Cdd:PRK05691 3992 GEAMPPELARQW--------LQRYPQIGLVNAYgpaecSDDVAFFRvdLASTRGSYLPIgsptdnnrlyllDEALELVPL 4063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 463 GAettseVGELCIRSPSLFKEYWRKPEVTAESFIDGGF-------FKTGDTVTVDDEGYFIILGRTNADImKVGGYKLSA 535
Cdd:PRK05691 4064 GA-----VGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQV-KIRGYRIEL 4137
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 536 LEIESVLLQHEIVLECAVlGLPDEAYGEIICAIIVPKEDSKKRAELdskpaltLEALTSWSKDKLAPYKIPTRLYLWDSL 615
Cdd:PRK05691 4138 GEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGAL-------LERIKQRLRAELPDYMVPLHWLWLDRL 4209
|
410
....*....|....*.
gi 1002235085 616 PRNAMGKVNKKELKKL 631
Cdd:PRK05691 4210 PLNANGKLDRKALPAL 4225
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
261-631 |
1.31e-18 |
|
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: 88.95 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG 340
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 341 IWQRWResypnngsKNDEAITVFTGVPTMYtrLLQgydgmDPEQQSASsfaAKQLRlMMCGSSALPSPlmkrWEEVTGH- 419
Cdd:cd05940 162 FWDDIR--------KYQATIFQYIGELCRY--LLN-----QPPKPTER---KHKVR-MIFGNGLRPDI----WEEFKERf 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 ---RLLERYGMTEFVMALSNPlhgARKEGTVGK---------PLPCVeaKIIMEDGAETTSEVGeLCIRSP--------- 478
Cdd:cd05940 219 gvpRIAEFYAATEGNSGFINF---FGKPGAIGRnpsllrkvaPLALV--KYDLESGEPIRDAEG-RCIKVPrgepgllis 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 479 -----SLFKEYWRKPEVTA----ESFIDG-GFFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIV 548
Cdd:cd05940 293 rinplEPFDGYTDPAATEKkilrDVFKKGdAWFNTGDLMRLDGEGFWYFVDRL-GDTFRWKGENVSTTEVAAVLGAFPGV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 549 LECAVLGLPDE-AYGEIICAIIVPKEDSkkraeldskpALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKE 627
Cdd:cd05940 372 EEANVYGVQVPgTDGRAGMAAIVLQPNE----------EFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVD 441
|
....
gi 1002235085 628 LKKL 631
Cdd:cd05940 442 LRNE 445
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
537-622 |
2.76e-18 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 79.51 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 537 EIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKkraeldskpaLTLEALTSWSKDKLAPYKIPTRLYLWDSLP 616
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE----------LLEEELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 1002235085 617 RNAMGK 622
Cdd:pfam13193 71 KTRSGK 76
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
143-630 |
3.55e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 87.87 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 143 LGGARIGIVAKPSPEFVAGI---FGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENistkcsaHCSL 219
Cdd:cd05915 44 LGVGVGDRVATLGFNHFRHLeayFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEA-------IRGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 LPSVTSIPVnidcQEPSSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGI---VSQVQILSEAW 296
Cdd:cd05915 117 LKTVQHFVV----MDEKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALvlhSLAASLVDGTA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 297 GyRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQrwresypnngSKNDEAITVFTGVPTMYTRLLQG 376
Cdd:cd05915 193 L-SEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVE----------LFDGEGVTFTAGVPTVWLALADY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 377 YDGMDpeqqsaSSFAAKqLRLMMCGSSalPSPLMKRWEEVTGHRLLERYGMTEfVMALSNPLHGARKEGTvgkpLPCVEA 456
Cdd:cd05915 262 LESTG------HRLKTL-RRLVVGGSA--APRSLIARFERMGVEVRQGYGLTE-TSPVVVQNFVKSHLES----LSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 -KIIMEDGAETTSEVGE------------------LCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFII 517
Cdd:cd05915 328 lTLKAKTGLPIPLVRLRvadeegrpvpkdgkalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 518 LGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRaeldskpaltlEALTSWSK 597
Cdd:cd05915 408 KDRLK-DLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP-----------EELNEHLL 475
|
490 500 510
....*....|....*....|....*....|....
gi 1002235085 598 DKLAPYK-IPTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:cd05915 476 KAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
265-578 |
6.07e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 87.95 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 265 ILYTSGTTGKPKGVVHTHKG---IVSQVQILSEAWGYR--SEDQFLHCLPLHHV-------------------HGLFNAL 320
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKmtHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 321 faplySGSVVEFMPkfsvrgiwqrwresypnngskndeaiTVFTGVPTMYTRLlqgYDGM-------DP----------- 382
Cdd:PLN02430 305 -----RDDLMELKP--------------------------TLLAGVPRVFERI---HEGIqkalqelNPrrrlifnalyk 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 383 ----------EQQSASSFA---------AK---QLRLMMCGSSALpSPLMKRWEEVTG-HRLLERYGMTEfvmALSNPLH 439
Cdd:PLN02430 351 yklawmnrgySHKKASPMAdflafrkvkAKlggRLRLLISGGAPL-STEIEEFLRVTScAFVVQGYGLTE---TLGPTTL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 440 GARKE----GTVGkpLPCVEAKIIMEDGAET------TSEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTV 509
Cdd:PLN02430 427 GFPDEmcmlGTVG--APAVYNELRLEEVPEMgydplgEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIGEI 503
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 510 DDEGYFIILGRTNaDIMKVGGYKLSALE-IESVLLQHEIVLECAVLGlpdEAYGEIICAIIVPKEDSKKR 578
Cdd:PLN02430 504 LPNGVLKIIDRKK-NLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTNK 569
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
219-630 |
6.14e-18 |
|
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: 87.16 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 LLPSVTSIPVNIDCQEPSSTEVTSSISSL-----IAEIDSSKEIRgDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILS 293
Cdd:cd05908 61 LLGGMIAVPVSIGSNEEHKLKLNKVWNTLknpylITEEEVLCELA-DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 294 EAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK--FSVRGI-WQRwresypnngsKNDEAITVFTGVPTMY 370
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTrlFIRRPIlWLK----------KASEHKATIVSSPNFG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 371 TRLLqgYDGMDPEQqsASSFAAKQLRLMMCGSSALPSPLMkrwEEVTGH---------RLLERYGMTEFVMALSNP---- 437
Cdd:cd05908 210 YKYF--LKTLKPEK--ANDWDLSSIRMILNGAEPIDYELC---HEFLDHmskyglkrnAILPVYGLAEASVGASLPkaqs 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 438 ------------LHGARKEGT------------VGKPLPCVEAKIIMEDGAETTSE-VGELCIRSPSLFKEYWRKPEVTA 492
Cdd:cd05908 283 pfktitlgrrhvTHGEPEPEVdkkdsecltfveVGKPIDETDIRICDEDNKILPDGyIGHIQIRGKNVTPGYYNNPEATA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 493 ESFIDGGFFKTGDTVTVDDeGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVL--ECAVLGLPD-EAYGEIICAII 569
Cdd:cd05908 363 KVFTDDGWLKTGDLGFIRN-GRLVITGREK-DIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNsNTRNEEIFCFI 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002235085 570 VPKEDSKKRAELDSKPALTLEALTSWSKDKLAPYKIptrlylwdsLPRNAMGKVNKKELKK 630
Cdd:cd05908 441 EHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLPIRR---------IPKTTSGKVKRYELAQ 492
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
262-632 |
1.06e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 87.10 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 262 PALILYTSGTTGKPKGVVHTHKG-IVSqvqiLSEAWGYRSEDQFLHCLPLHH------VHGLFNALFA-----PLYSGSV 329
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPhLVG----LKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLSlgntfVMFEGGI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 330 VEfmPKFSVRGIWqrwresypNNGSKNDeaITVFTGVPTMYTRLLQgydgMDPE-QQSASSFAAKQLRLMMCGSSALPSP 408
Cdd:PTZ00237 332 IK--NKHIEDDLW--------NTIEKHK--VTHTLTLPKTIRYLIK----TDPEaTIIRSKYDLSNLKEIWCGGEVIEES 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 LMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGARKEGTVGKPLPCVEAKIIMEDGAETTS-EVGELCIR---SPSLFKE 483
Cdd:PTZ00237 396 IPEYIENKLKIKSSRGYGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVnEIGEVAFKlpmPPSFATT 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 484 YWRKPEVTAESFID-GGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYG 562
Cdd:PTZ00237 476 FYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002235085 563 EIICAIIVPKEDskkraelDSKPALTLEALTS----WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 632
Cdd:PTZ00237 555 NVPIGLLVLKQD-------QSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFL 621
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
261-623 |
1.07e-17 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 86.93 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 261 DPALILYTSGTTGKPKGVVHTHKG-IVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSG--SVV-EFMPKF 336
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGVQRDTGGyAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGmaTIMyEGLPTR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 337 SVRGIWQRWRESYpnngskndeaitvftGVPTMYT-----RLLQGYDGMDPEQQSASSfaakqLRLMMCGSSALPSPlMK 411
Cdd:PRK10524 314 PDAGIWWRIVEKY---------------KVNRMFSaptaiRVLKKQDPALLRKHDLSS-----LRALFLAGEPLDEP-TA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 412 RW-EEVTGHRLLERYGMTEF---VMALSNPLHG-ARKEGTVGKPLPCVEAKIIME-DGAET-TSEVGELCIRSP------ 478
Cdd:PRK10524 373 SWiSEALGVPVIDNYWQTETgwpILAIARGVEDrPTRLGSPGVPMYGYNVKLLNEvTGEPCgPNEKGVLVIEGPlppgcm 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 479 --------SLFKEYWrkpevtaeSFIDGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVLE 550
Cdd:PRK10524 453 qtvwgdddRFVKTYW--------SLFGRQVYSTFDWGIRDADGYYFILGRTD-DVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002235085 551 CAVLGLPDEAYGEIICAIIVPKeDSKKRAELDSKPALTLEaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 623
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPK-DSDSLADREARLALEKE-IMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
139-632 |
1.56e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 86.21 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 139 GTGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYP----EA--ELLHVM-NDSDISLILSTKEHQDIMENIST 211
Cdd:PRK09192 68 ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggrESyiAQLRGMlASAQPAAIITPDELLPWVNEATH 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 212 KCSAHCSLLPSVTSIPVNIDCQEPsstevtssissliaeidsskEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQ- 290
Cdd:PRK09192 148 GNPLLHVLSHAWFKALPEADVALP--------------------RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRa 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 291 ILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP--KFSVRGI-WQRWResypnngSKNDEAITVftgVP 367
Cdd:PRK09192 208 ISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFARRPLqWLDLI-------SRNRGTISY---SP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 368 TMytrllqGYD--GMDPEQQSASSFAAKQLRLMMCGSSALPSPLMKRWEEVTGHR------LLERYGMTEFVMALSNPLH 439
Cdd:PRK09192 278 PF------GYElcARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSFSPL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 440 GA----------RKEGT------------------VGKPLPCVEAKIIMEDGAETTS-EVGELCIRSPSLFKEYWRKPEV 490
Cdd:PRK09192 352 GSgivveevdrdRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEAGMPLPErVVGHICVRGPSLMSGYFRDEES 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 491 TAESFIDgGFFKTGDTVTVDDeGYFIILGRTNaDIMKVGGYKLSALEIESVLLQHEIVL--ECAVLGLPDEAYGEIICAI 568
Cdd:PRK09192 432 QDVLAAD-GWLDTGDLGYLLD-GYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLV 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 569 IVPKEDSKKRAELDSKPALTLEALTSWSKD-KLAPYKiptrlylwdSLPRNAMGKVNKKELKKLL 632
Cdd:PRK09192 509 QCRISDEERRGQLIHALAALVRSEFGVEAAvELVPPH---------SLPRTSSGKLSRAKAKKRY 564
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
154-542 |
2.65e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 154 PS-PEFVAGIFGTWLSGGVAVPlalSYP--------EAELLHVMNDSDISLILSTKEHQDIMENISTKCSAHCSLLPSVT 224
Cdd:PRK05691 72 PSgPDYVAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 225 SIPvnidcqepsstevtssisSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWG--YRSED 302
Cdd:PRK05691 149 TLD------------------PALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 303 QFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWRESYPNNGSkndeaitVFTGVPTMYTRL--------- 373
Cdd:PRK05691 211 VIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGG-------TISGGPDFAYRLcservsesa 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 374 LQG---------YDGMDP-EQQSASSFAAKqlrLMMCG---SSALPSplmkrweevtghrllerYGMTEFVMALSNPLHG 440
Cdd:PRK05691 284 LERldlsrwrvaYSGSEPiRQDSLERFAEK---FAACGfdpDSFFAS-----------------YGLAEATLFVSGGRRG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 441 -------------ARK-----EGTV----GKPLPCVEAKIIMEDGAETTSE--VGELCIRSPSLFKEYWRKPEVTAESFI 496
Cdd:PRK05691 344 qgipaleldaealARNraepgTGSVlmscGRSQPGHAVLIVDPQSLEVLGDnrVGEIWASGPSIAHGYWRNPEASAKTFV 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1002235085 497 --DG-GFFKTGDtVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVL 542
Cdd:PRK05691 424 ehDGrTWLRTGD-LGFLRDGELFVTGRLK-DMLIVRGHNLYPQDIEKTV 470
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
256-539 |
1.19e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.51 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 256 EIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE-DQFLHCLPLHHVHGLFNALFAPLYSG-SVVEFM 333
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGaELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 334 PKFSVRG--IWqrwresyPNNGSKNDEAITVftgVP----TMYTRLLQGydGMDPEQQSASSfaakqLRLMMCGSSALPS 407
Cdd:PRK07768 228 PMDFLRDplLW-------AELISKYRGTMTA---APnfayALLARRLRR--QAKPGAFDLSS-----LRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 408 PLMKRWEEVtGHR-------LLERYGMTEFVMALSNP------------------LH--------GARKEGTVGKPLPCV 454
Cdd:PRK07768 291 ADVEDLLDA-GARfglrpeaILPAYGMAEATLAVSFSpcgaglvvdevdadllaaLRravpatkgNTRRLATLGPPLPGL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 455 EAKIIMEDGAET-TSEVGELCIRSPSLFKEYwrkpeVTAESFI----DGGFFKTGDTVTVDDEGYFIILGRTNaDIMKVG 529
Cdd:PRK07768 370 EVRVVDEDGQVLpPRGVGVIELRGESVTPGY-----LTMDGFIpaqdADGWLDTGDLGYLTEEGEVVVCGRVK-DVIIMA 443
|
330
....*....|
gi 1002235085 530 GYKLSALEIE 539
Cdd:PRK07768 444 GRNIYPTDIE 453
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
147-568 |
1.53e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 82.94 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 147 RIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILSTKEHQDIMENISTKCSAHCSLLPSVTSI 226
Cdd:PRK06334 69 HIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDAEYPFSLIYMEEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 227 PVNIDCQEPSSTEVTSSIS-SLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFL 305
Cdd:PRK06334 149 RKELSFWEKCRIGIYMSIPfEWLMRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 306 HCLPLHHVHGlFN--ALFaPLYSGSVVEF-----MPKFSVRGIwqrwresypnngskNDEAITVFTGVPTMYTRLLQGyd 378
Cdd:PRK06334 229 SFLPPFHAYG-FNscTLF-PLLSGVPVVFaynplYPKKIVEMI--------------DEAKVTFLGSTPVFFDYILKT-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 gmdpEQQSASSFAAkqLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEFVMALS-NPLHGARKEGTVGKPLPCVEA 456
Cdd:PRK06334 291 ----AKKQESCLPS--LRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 457 KIIMEdgaET-----TSEVGELCIRSPSLFKEYWRKPEvtAESFIDGG---FFKTGDTVTVDDEGYFIILGRTnADIMKV 528
Cdd:PRK06334 365 LIVSE---ETkvpvsSGETGLVLTRGTSLFSGYLGEDF--GQGFVELGgetWYVTGDLGYVDRHGELFLKGRL-SRFVKI 438
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002235085 529 GGYKLSALEIESVLLQHeivlecavLGLPDEAYGE--IICAI 568
Cdd:PRK06334 439 GAEMVSLEALESILMEG--------FGQNAADHAGplVVCGL 472
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
131-578 |
3.71e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 81.99 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 131 GSSVKGIngtGFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILStkEHQDIMENIS 210
Cdd:PLN02614 93 GNSLRSV---GVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFV--EEKKISELFK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 211 TkCSAHCSLLPSVtsipVNIDCQEPSSTEVTSSISSLIAEIDSSKEI-----------RGDDPALILYTSGTTGKPKGVV 279
Cdd:PLN02614 168 T-CPNSTEYMKTV----VSFGGVSREQKEEAETFGLVIYAWDEFLKLgegkqydlpikKKSDICTIMYTSGTTGDPKGVM 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 280 HTHKGIVS----QVQILSEAWGYRSE-DQFLHCLPLHHVhglFNALFAPLY--SGSVVEFMpKFSVRGIWQRWRESYPnn 352
Cdd:PLN02614 243 ISNESIVTliagVIRLLKSANAALTVkDVYLSYLPLAHI---FDRVIEECFiqHGAAIGFW-RGDVKLLIEDLGELKP-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 353 gskndeaiTVFTGVPTMYTRLLQG-----------------------YDGMDPEQQ--SASSFAAK------------QL 395
Cdd:PLN02614 317 --------TIFCAVPRVLDRVYSGlqkklsdggflkkfvfdsafsykFGNMKKGQShvEASPLCDKlvfnkvkqglggNV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 396 RLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE-----FVmALSNPLHGArkeGTVGKPLPCVEAKII----MEDGAET 466
Cdd:PLN02614 389 RIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscagtFV-SLPDELDML---GTVGPPVPNVDIRLEsvpeMEYDALA 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 467 TSEVGELCIRSPSLFKEYWRKPEVTAESFIDgGFFKTGDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALE-IESVLLQH 545
Cdd:PLN02614 465 STPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKK-NIFKLSQGEYVAVEnIENIYGEV 542
|
490 500 510
....*....|....*....|....*....|...
gi 1002235085 546 EIVLECAVLGLPDEAYgeiICAIIVPKEDSKKR 578
Cdd:PLN02614 543 QAVDSVWVYGNSFESF---LVAIANPNQQILER 572
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
252-606 |
1.34e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 80.30 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 252 DSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVE 331
Cdd:PRK08279 191 ASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 332 FMPKFSVRGIW---QRWResypnngskndeaITVFTGVPTMYTRLLQgydgmdpeQQSASSFAAKQLRLmMCGSSALPSP 408
Cdd:PRK08279 271 LRRKFSASRFWddvRRYR-------------ATAFQYIGELCRYLLN--------QPPKPTDRDHRLRL-MIGNGLRPDI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 409 lmkrWEEVTG----HRLLERYGMTEFVMALSNPLHgarKEGTVGK-PLPCVEAKIIMEDGAETTS--------------- 468
Cdd:PRK08279 329 ----WDEFQQrfgiPRILEFYAASEGNVGFINVFN---FDGTVGRvPLWLAHPYAIVKYDVDTGEpvrdadgrcikvkpg 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 469 EVGELC--IRSPSLFKEYwRKPEVTAESFIDGGF------FKTGDTVTVDDEGYFIILGRtnadimkVG------GYKLS 534
Cdd:PRK08279 402 EVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDR-------LGdtfrwkGENVA 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002235085 535 ALEIESVLLQHEIVLECAVLGLPdeaygeiicaiiVPKEDSkkRA-----ELDSKPALTLEALTSWSKDKLAPYKIP 606
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVE------------VPGTDG--RAgmaaiVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
141-631 |
2.52e-15 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 79.39 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 141 GFLGGARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDIS-LILSTKEHQDIMEnISTKcsahcsl 219
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTtVICDSKQLKKLID-ISSQ------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 220 LPSVTSIpVNIDCQEPSSTEVTSSISSLIAEIDSSKEIRG------------DDPALILYTSGTTGKPKGVVHTHKGIVS 287
Cdd:PLN02387 199 LETVKRV-IYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGkenpvdpdlpspNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 288 QVQ-ILSEAWGYRSEDQFLHCLPLHHVHGLF--NALFAplySGSVVEFMPKFSVRGIWQRWREsypnnGSKNDEAI---T 361
Cdd:PLN02387 278 TVAgVMTVVPKLGKNDVYLAYLPLAHILELAaeSVMAA---VGAAIGYGSPLTLTDTSNKIKK-----GTKGDASAlkpT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 362 VFTGVPTMYTRLLQG---------------YDGMDPEQQSA---SSFAA---------------------KQLRLMMCGS 402
Cdd:PLN02387 350 LMTAVPAILDRVRDGvrkkvdakgglakklFDIAYKRRLAAiegSWFGAwglekllwdalvfkkiravlgGRIRFMLSGG 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 403 SALpSPLMKRWEEVT-GHRLLERYGMTEFVMAlsnplhGARKE------GTVGKPLPCVEAKII-MEDGAETTSEV---- 470
Cdd:PLN02387 430 APL-SGDTQRFINIClGAPIGQGYGLTETCAG------ATFSEwddtsvGRVGPPLPCCYVKLVsWEEGGYLISDKpmpr 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 471 GELCIRSPSLFKEYWRKPEVTAESF-IDGG---FFKTGDTVTVDDEGYFIILGRTNaDIMKV--GGYkLSALEIESVLLQ 544
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVYkVDERgmrWFYTGDIGQFHPDGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSV 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 545 HEIVLECAVLGLPDEAYgeiiC-AIIVPKE------------DSKKRAELDSKPALTLEALTSWSKD----KLAPYKIPT 607
Cdd:PLN02387 581 SPYVDNIMVHADPFHSY----CvALVVPSQqalekwakkagiDYSNFAELCEKEEAVKEVQQSLSKAakaaRLEKFEIPA 656
|
570 580 590
....*....|....*....|....*....|....*...
gi 1002235085 608 RLYL----WD----------SLPRNAMGKVNKKELKKL 631
Cdd:PLN02387 657 KIKLlpepWTpesglvtaalKLKREQIRKKFKDDLKKL 694
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
145-615 |
2.41e-14 |
|
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: 76.18 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAgifgTWLsgGVA---VPLALSYPEAE---LLHVMNDSDISLILSTKEHQDIMENIstkcsahcs 218
Cdd:cd05938 31 GDTVALLLGNEPAFLW----IWL--GLAklgCPVAFLNTNIRsksLLHCFRCCGAKVLVVAPELQEAVEEV--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 lLPSVTSIpvNIDCQEPSSTEVTSSISSLIAEIDSS----------KEIRGDDPALILYTSGTTGKPKGVVHTHKGIVsQ 288
Cdd:cd05938 96 -LPALRAD--GVSVWYLSHTSNTEGVISLLDKVDAAsdepvpaslrAHVTIKSPALYIYTSGTTGLPKAARISHLRVL-Q 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 289 VQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWQRWREsypnngskndEAITVFtgvpt 368
Cdd:cd05938 172 CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRK----------HNVTVI----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 369 MYTRLLQGYDGMDPEQQSASsfaAKQLRLMMcGSSALPSPlmkrWEEVT---GH-RLLERYGMTEFVMALSNPlhgARKE 444
Cdd:cd05938 237 QYIGELLRYLCNQPQSPNDR---DHKVRLAI-GNGLRADV----WREFLrrfGPiRIREFYGSTEGNIGFFNY---TGKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 445 GTVGK----------------------PLP-----CVEAKiimedgaetTSEVGELC--IRSPSLFKEYWRKPEVT---- 491
Cdd:cd05938 306 GAVGRvsylykllfpfelikfdvekeePVRdaqgfCIPVA---------KGEPGLLVakITQQSPFLGYAGDKEQTekkl 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 492 -AESFIDGG-FFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAY-GEIICAI 568
Cdd:cd05938 377 lRDVFKKGDvYFNTGDLLVQDQQNFLYFHDRV-GDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAA 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1002235085 569 IVPKEDskkrAELDskpaltLEALTSWSKDKLAPYKIPTRLYLWDSL 615
Cdd:cd05938 456 VKLKPG----HEFD------GKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
260-632 |
9.74e-13 |
|
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: 71.15 E-value: 9.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVsqVQILSEawgyrsedQFLHClPLHHVHGLF----------NALFAPLYSG-S 328
Cdd:cd05943 249 DHPLYILYSSGTTGLPKCIVHGAGGTL--LQHLKE--------HILHC-DLRPGDRLFyyttcgwmmwNWLVSGLAVGaT 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 329 VV-----EFMPKFSVrgIWQRWREsypnngskndEAITVFTGVPTMYTRLLQGydGMDPeqqsASSFAAKQLRLMMCGSS 403
Cdd:cd05943 318 IVlydgsPFYPDTNA--LWDLADE----------EGITVFGTSAKYLDALEKA--GLKP----AETHDLSSLRTILSTGS 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 404 ALPsPLMKRW--EEVTGHRLLERY-GMTEFV--MALSNPLHGARKeGTVGKPLPCVEAKIIMEDGAETTSEVGELCIRS- 477
Cdd:cd05943 380 PLK-PESFDYvyDHIKPDVLLASIsGGTDIIscFVGGNPLLPVYR-GEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKp 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 478 -PSLFKEYWRKPEVTA--ESFID--GGFFKTGDTVTVDDEGYFIILGRTNADImKVGGYKLSALEIESVLLQHEIVLECA 552
Cdd:cd05943 458 fPSMPVGFWNDPDGSRyrAAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTL-NPGGVRIGTAEIYRVVEKIPEVEDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 553 VLGLPDEAYGEIICAIIVPKEDskkrAELDskPALtLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKvnKKEL--KK 630
Cdd:cd05943 537 VVGQEWKDGDERVILFVKLREG----VELD--DEL-RKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK--KVEVavKK 607
|
..
gi 1002235085 631 LL 632
Cdd:cd05943 608 II 609
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
257-543 |
2.99e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 69.75 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 257 IRGDDP---ALILYTSGTTGKPKGVVHTHKGIVSQVQILSEaWGYR---SEDQFLHCLPLHHVHGLFNALFAPLYSGSVv 330
Cdd:PTZ00342 298 IQNEDPdfiTSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK-HSIFkkyNPKTHLSYLPISHIYERVIAYLSFMLGGTI- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 331 efmpkfsvrGIWQRWRESYPNNGSKNDEAITVftGVPTMYTRLlqgYDGMDPEQQSASSFAakqlRLMMCGSSALPSPLM 410
Cdd:PTZ00342 376 ---------NIWSKDINYFSKDIYNSKGNILA--GVPKVFNRI---YTNIMTEINNLPPLK----RFLVKKILSLRKSNN 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 411 KRW-----EEVTGHR-------------------------------LL-----ERYGMTEfvmaLSNPLHGARKEGT--- 446
Cdd:PTZ00342 438 NGGfskflEGITHISskikdkvnpnlevilngggklspkiaeelsvLLnvnyyQGYGLTE----TTGPIFVQHADDNnte 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 447 -VGKPL-PCVEAKIIMED--GAETTSEVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEGYFIILGRTN 522
Cdd:PTZ00342 514 sIGGPIsPNTKYKVRTWEtyKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK 593
|
330 340
....*....|....*....|..
gi 1002235085 523 adimkvGGYKLSALE-IESVLL 543
Cdd:PTZ00342 594 ------GLVKLSQGEyIETDML 609
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
145-520 |
7.55e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 68.22 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPL-ALSYP-EAELLH-VMNDSDISLILSTkehqdimenisTKCSAHCSLLp 221
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPgHVGRLHaVLDDCTPSAILTT-----------TDSAEGVRKF- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 222 sVTSIPVNidcQEPSSTEVtSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSE 301
Cdd:PRK07769 147 -FRARPAK---ERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 302 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIWqRW-RESypnnGSKNDEAITVFTGVPTMytrllqGYD-- 378
Cdd:PRK07769 222 DRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPG-RWiREL----ARKPGGTGGTFSAAPNF------AFEha 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 379 ---GMDPEQQSA---SSFAAkqlrlMMCGSSALPSPLMKRWEEVTGHRLLER------YGMTEFVMALSNP--------L 438
Cdd:PRK07769 291 aarGLPKDGEPPldlSNVKG-----LLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptvI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 439 HGARKEGTVG----------KPLPCVEA-KIIMEDGA-----ETTSE-----VGELCIRSPSLFKEYWRKPEVTAESF-- 495
Cdd:PRK07769 366 YVDRDELNAGrfvevpadapNAVAQVSAgKVGVSEWAvivdpETASElpdgqIGEIWLHGNNIGTGYWGKPEETAATFqn 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1002235085 496 ---------------IDGGFFKTGDT-VTVDDEGYfiILGR 520
Cdd:PRK07769 446 ilksrlseshaegapDDALWVRTGDYgVYFDGELY--ITGR 484
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
260-631 |
3.88e-11 |
|
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: 65.52 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 339
Cdd:cd05939 104 RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 340 GIWqrwresypNNGSKNDEAITVFTGVPTMYTrLLQGYdgMDPEQQsassfaaKQLRLMMcGSSALPSPlmkrWEEVTGH 419
Cdd:cd05939 184 NFW--------DDCVKYNCTIVQYIGEICRYL-LAQPP--SEEEQK-------HNVRLAV-GNGLRPQI----WEQFVRR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 420 ----RLLERYGMTEFVMALSNplhgarKEGTVGK------------PLPCVEA-KIIME-----DG-------AETTSEV 470
Cdd:cd05939 241 fgipQIGEFYGATEGNSSLVN------IDNHVGAcgfnsrilpsvyPIRLIKVdEDTGElirdsDGlcipcqpGEPGLLV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 471 GELCIRSPSL-FKEYWRKPE----VTAESFIDGG-FFKTGDTVTVDDEGYFIILGRTnADIMKVGGYKLSALEIESVLLQ 544
Cdd:cd05939 315 GKIIQNDPLRrFDGYVNEGAtnkkIARDVFKKGDsAFLSGDVLVMDELGYLYFKDRT-GDTFRWKGENVSTTEVEGILSN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 545 heivlecaVLGLPDEA-YGeiicaIIVPKEDSKK--RAELDSKPALTLEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMG 621
Cdd:cd05939 394 --------VLGLEDVVvYG-----VEVPGVEGRAgmAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTF 460
|
410
....*....|
gi 1002235085 622 KVNKKELKKL 631
Cdd:cd05939 461 KLQKTDLQKE 470
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
145-553 |
2.88e-10 |
|
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: 63.14 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPLALSYPEAELLHVMNDSDISLILST----KEHQDIMENISTKCsahCSLL 220
Cdd:cd05905 40 GDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVeaclKGLPKKLLKSKTAA---EIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVtsIPVNIDcqepsSTEVTSSISSLIAEIDSSKEIRGDDPALILYTSGTTGKPKGVVHTHKGIVSQVQILSEAWGYRS 300
Cdd:cd05905 117 KKG--WPKILD-----FVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 301 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRgiwqrwresypNNGSKNDEAI------TVFTGVPTMYTRLL 374
Cdd:cd05905 190 SRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMK-----------TNPLLWLQTLsqykvrDAYVKLRTLHWCLK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 375 QgyDGMDPEQQSASSFAAKQLRlmMCGSSALPSP---LMKRWEEVTG-HRLLERYGMTEFvMALSNPLHGAR-------- 442
Cdd:cd05905 259 D--LSSTLASLKNRDVNLSSLR--MCMVPCENRPrisSCDSFLKLFQtLGLSPRAVSTEF-GTRVNPFICWQgtsgpeps 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 443 ---------KEGTV----------------GKPLPCVEAKIIMEDGAE--TTSEVGELCIRSPSLFKEYWR--------- 486
Cdd:cd05905 334 rvyldmralRHGVVrlderdkpnslplqdsGKVLPGAQVAIVNPETKGlcKDGEIGEIWVNSPANASGYFLldgetndtf 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 487 -KPEVTAESFIDGG--FFKTGD----------TVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIE-SVLLQHEIVLECA 552
Cdd:cd05905 414 kVFPSTRLSTGITNnsYARTGLlgflrptkctDLNVEEHDLLFVVGSID-ETLEVRGLRHHPSDIEaTVMRVHPYRGRCA 492
|
.
gi 1002235085 553 V 553
Cdd:cd05905 493 V 493
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
145-594 |
2.36e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 60.34 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPlaLSYPEAELLH-----VMNDSDISLILST-KEHQDIMENISTKCSAhcs 218
Cdd:PRK05850 59 GDRAVILAPQGLEYIVAFLGALQAGLIAVP--LSVPQGGAHDervsaVLRDTSPSVVLTTsAVVDDVTEYVAPQPGQ--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 219 llpSVTSIpVNIDcqepsSTEVTSSISSLIAEIDSSkeirgdDPALILYTSGTTGKPKGVVHTHKGIVSQV-QILSEAWG 297
Cdd:PRK05850 134 ---SAPPV-IEVD-----LLDLDSPRGSDARPRDLP------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 298 YR-----SEDQFLHCLPLHHVHGLFNALFAPLYSG------SVVEFMPKFSvrgiwqRWRESYPNNGSkndeaitVFTGV 366
Cdd:PRK05850 199 DTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGcpavltSPVAFLQRPA------RWMQLLASNPH-------AFSAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 367 PTMYTRL---------LQGYDgmdpeqqsassfaAKQLRLMMCGSsalpsplmKRWEEVTGHRLLER------------- 424
Cdd:PRK05850 266 PNFAFELavrktsdddMAGLD-------------LGGVLGIISGS--------ERVHPATLKRFADRfapfnlretairp 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 425 -YGMTE---FVMA----------------LSNPlHGARKEGTVGKPL--------PCVeaKIImeDGaETTSE-----VG 471
Cdd:PRK05850 325 sYGLAEatvYVATrepgqppesvrfdyekLSAG-HAKRCETGGGTPLvsygsprsPTV--RIV--DP-DTCIEcpagtVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 472 ELCIRSPSLFKEYWRKPEVTAESF-----------IDGGFFKTGDTVTVDDEGYFIIlGRTNaDIMKVGGYKLSALEIES 540
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPEGPWLRTGDLGFISEGELFIV-GRIK-DLLIVDGRNHYPDDIEA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1002235085 541 VLlqHEIVL-ECAVLGLPDEAyGEIICAIIvpkeDSKKRAELDSKPALTLEALTS 594
Cdd:PRK05850 477 TI--QEITGgRVAAISVPDDG-TEKLVAII----ELKKRGDSDEEAMDRLRTVKR 524
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
145-530 |
2.11e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.06 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 145 GARIGIVAKPSPEFVAGIFGTWLSGGVAVPL-ALSYP-EAELLH-VMNDSDISLILSTKEHQDIMEN-ISTKCSAHCSLL 220
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPgHAERLDtALRDAEPTVVLTTTAAAEAVEGfLRNLPRLRRPRV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 221 PSVTSIPvnidcqepssTEVTSSISSliAEIDSskeirgDDPALILYTSGTTGKPKGVVHTHKGIVSQV--QILSEA--- 295
Cdd:PRK12476 172 IAIDAIP----------DSAGESFVP--VELDT------DDVSHLQYTSGSTRPPVGVEITHRAVGTNLvqMILSIDlld 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 296 WGYRSedqfLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGIwQRWRESYpnngSKNDEAITVFTGVPTmYTRLLQ 375
Cdd:PRK12476 234 RNTHG----VSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRP-QRWIKAL----SEGSRTGRVVTAAPN-FAYEWA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 376 GYDGMDPEQQSASsfaakqLR--LMMCGSSALPSPLMKRWEEVTGHRLLER------YGMTEFVMALSNPLHGA------ 441
Cdd:PRK12476 304 AQRGLPAEGDDID------LSnvVLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATIAPDAepsvvy 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 442 --RKEGTVGKPLPCVEAK------------------IIMEDGAETT---SEVGELCIRSPSLFKEYWRKPEVTAESF--- 495
Cdd:PRK12476 378 ldREQLGAGRAVRVAADApnavahvscgqvarsqwaVIVDPDTGAElpdGEVGEIWLHGDNIGRGYWGRPEETERTFgak 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1002235085 496 ---------------IDGGFFKTGDT-VTVDDEGYfiILGRTnADIMKVGG 530
Cdd:PRK12476 458 lqsrlaegshadgaaDDGTWLRTGDLgVYLDGELY--ITGRI-ADLIVIDG 505
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
260-632 |
9.77e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 55.19 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 260 DDPALILYTSGTTGKPKGVVHTHKGIVsqVQILSEawgyrsedQFLHClPLH------------------HVHGLFNALF 321
Cdd:PRK03584 263 DHPLWILYSSGTTGLPKCIVHGHGGIL--LEHLKE--------LGLHC-DLGpgdrffwyttcgwmmwnwLVSGLLVGAT 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 322 APLYSGSvvefmPkfsvrgiwqrwreSYPNNGS----KNDEAITVFTGVPTMYTRLLQGydGMDPeqqsASSFAAKQLRL 397
Cdd:PRK03584 332 LVLYDGS-----P-------------FYPDPNVlwdlAAEEGVTVFGTSAKYLDACEKA--GLVP----GETHDLSALRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 398 MMCGSSALPsPLMKRW--EEVTGHRLLERY-GMTEFV--MALSNPLhgarkegtvgkpLP-------C----VEAKIIME 461
Cdd:PRK03584 388 IGSTGSPLP-PEGFDWvyEHVKADVWLASIsGGTDICscFVGGNPL------------LPvyrgeiqCrglgMAVEAWDE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 462 DGAETTSEVGELCIRS--PS--LFkeYWRKPevtaesfiDGG-----FFKT-------GDTVTVDDEGYFIILGRTNADI 525
Cdd:PRK03584 455 DGRPVVGEVGELVCTKpfPSmpLG--FWNDP--------DGSryrdaYFDTfpgvwrhGDWIEITEHGGVVIYGRSDATL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 MKvGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDskkrAELDskPALTlEALTSWSKDKLAPYKI 605
Cdd:PRK03584 525 NR-GGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEG----VTLD--DALR-ARIRTTIRTNLSPRHV 596
|
410 420
....*....|....*....|....*....
gi 1002235085 606 PTRLYLWDSLPRNAMGKvnKKEL--KKLL 632
Cdd:PRK03584 597 PDKIIAVPDIPRTLSGK--KVELpvKKLL 623
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
469-628 |
6.29e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 52.52 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 469 EVGELCIRSPSLFKEYWRKPEVTAESFIDGGFFKTGDTVTVDDEG-------YFII---------LGR--TNADI----- 525
Cdd:cd17647 314 EVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHWNYLDKDNnepwrqfWLGPrdrlyrtgdLGRylPNGDCeccgr 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 526 ----MKVGGYKLSALEIESVLLQHEIVLECAVLGLPDEAYGEIICAIIVPKEDSK---------KRAELDSKPAL-TLEA 591
Cdd:cd17647 394 addqVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqedVPKEVSTDPIVkGLIG 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002235085 592 LTSWSKD-------KLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 628
Cdd:cd17647 474 YRKLIKDireflkkRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
504-629 |
7.47e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 49.04 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 504 GDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQ-HEIVLECAVLGLPDEAYGEIICAIIVPKEDSKKRAELD 582
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRAD-DTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQA 440
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1002235085 583 SKPALTlEALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 629
Cdd:PLN03051 441 RPEALQ-KKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
504-630 |
1.46e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 48.15 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002235085 504 GDTVTVDDEGYFIILGRTNaDIMKVGGYKLSALEIESVLLQ-HEIVLECAVLGLPDEAYG-EIICAIIVPKEDSKKRAEL 581
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRAD-DTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL 672
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1002235085 582 DskpaLTLEALTSWSKDKLAP-YKIpTRLYLWDSLPRNAMGKVNKKELKK 630
Cdd:PLN03052 673 N----ELKKIFNSAIQKKLNPlFKV-SAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| |
