|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
55-568 |
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: 685.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRlqgcKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLA----LGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdRGAMIFYTSGTTGRPKGALS 214
Cdd:cd05941 77 EYVITDSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWekfLSSEAPQITVFMAVP 294
Cdd:cd05941 110 THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMGVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 295 TVYSKLLDYYDKHFTQPrvqDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVP 374
Cdd:cd05941 187 TIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 375 GSVGTPLPGVEVRIISENPQKgspyiihaegnergtkvtPGFEEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTG 454
Cdd:cd05941 264 GTVGMPLPGVQARIVDEETGE------------------PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 455 DTAVFK-DARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEG-HSLSHRDLK 532
Cdd:cd05941 326 DLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELK 405
|
490 500 510
....*....|....*....|....*....|....*.
gi 1195733688 533 EWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELL 568
Cdd:cd05941 406 EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-567 |
1.29e-147 |
|
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: 433.08 E-value: 1.29e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGD----RVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGR 208
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQIT 288
Cdd:COG0318 115 PKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELI---ERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKLLDYYDKHFTqprvqDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPL 368
Cdd:COG0318 192 VLFGVPTMLARLLRHPEFARY-----DL------SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 369 TE--ARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFt 446
Cdd:COG0318 261 EDpgERRPGSVGRPLPGVEVRIV----------------DEDGRELPPG---EVGEIVVRGPNVMKGYWNDPEATAEAF- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 447 SDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHS 525
Cdd:COG0318 321 RDGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1195733688 526 LSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:COG0318 400 LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-567 |
2.79e-118 |
|
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: 358.41 E-value: 2.79e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 53 FGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQ--GCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHP 130
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELDALAEAFAA---GLQnlGVQPGD----RVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 131 EAQLEYFIQDSRSSLVVVGQEYLERLSPLAqrlgvpLLPLTPAIYRGATekpteqpvkesgwrdrgAMIFYTSGTTGRPK 210
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAAGA------PLGERVALTPEDV-----------------AVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 211 GALSTHRNLAAVVTGlvhSWAWTK-----NDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAP 285
Cdd:cd05936 142 GAMLTHRNLVANALQ---IKAWLEdllegDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI---RKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 286 QITVFMAVPTVYSKLLDYYDKHFTQPRvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MAL 364
Cdd:cd05936 216 RVTIFPGVPTMYIALLNAPEFKKRDFS-----------SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 365 SNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd05936 285 VNPLDGPRKPGSIGIPLPGTEVKIVDD------------DGEE----LPPG---EVGELWVRGPQVMKGYWNRPEETAEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FTsDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEG 523
Cdd:cd05936 346 FV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1195733688 524 HSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05936 424 ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
50-567 |
3.99e-114 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 349.17 E-value: 3.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYG-HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07514 12 AFADRDAPFIETPDGlRYTYGDLDAASARLANLLVAL-GVKPGD----RVAVQVEKSPEALALYLATLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVP-LLPLTPA-----IYRGATEKPTEQPVKESGwrDRGAMIFYT 202
Cdd:PRK07514 87 YTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPhVETLDADgtgslLEAAAAAPDDFETVPRGA--DDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 203 SGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlss 282
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALM--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 283 eaPQITVFMAVPTVYSKLLDyydkhftQPRvqdFVRAVCKeRIRLMVSGSAalpvPLL----EKWRSATGHTLLERYGMT 358
Cdd:PRK07514 242 --PRATVMMGVPTFYTRLLQ-------EPR---LTREAAA-HMRLFISGSA----PLLaethREFQERTGHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 359 EIGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaeGNERGTKVTPGfeeKEGELLVRGPSVFREYWDKP 438
Cdd:PRK07514 305 ETNMNTSNPYDGERRAGTVGFPLPGVSLRVT---------------DPETGAELPPG---EIGMIEVKGPNVFKGYWRMP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 439 EETKSAFTSDGWFRTGDTAVFkDAR--YWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA 516
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKI-DERgyVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 517 VVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07514 445 VVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
30-569 |
1.07e-111 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 341.58 E-value: 1.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 30 SLLPTAPEAHTDGSvpvfiRALAFGDRialidkygHHTYRELYDRSLCLAQEICRLQgckvgdlqeeRVSFLCSNDISYV 109
Cdd:PRK07787 3 SLNPAAVAAAADIA-----DAVRIGGR--------VLSRSDLAGAATAVAERVAGAR----------RVAVLATPTLATV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 110 VAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGqeylerlsPLAQRLGVPLLPLTPAIyRGATEKPTEQPvke 189
Cdd:PRK07787 60 LAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP--------APDDPAGLPHVPVRLHA-RSWHRYPEPDP--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 190 sgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE 269
Cdd:PRK07787 128 ----DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 FSAQQVWEkflsSEAPQITVFMAVPTVYSKLldyydkhftqPRVQDFVRAVckERIRLMVSGSAALPVPLLEKWRSATGH 349
Cdd:PRK07787 204 PTPEAYAQ----ALSEGGTLYFGVPTVWSRI----------AADPEAARAL--RGARLLVSGSAALPVPVFDRLAALTGH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 TLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkGSPyiIHAEGnergtkvtpgfeEKEGELLVRGPS 429
Cdd:PRK07787 268 RPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDED---GGP--VPHDG------------ETVGELQVRGPT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 430 VFREYWDKPEETKSAFTSDGWFRTGDTAVFkDARYWIR--GRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPD 507
Cdd:PRK07787 331 LFDGYLNRPDATAAAFTADGWFRTGDVAVV-DPDGMHRivGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 508 MTWGQRVTAVVALQEGhsLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLT 569
Cdd:PRK07787 410 DDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
49-564 |
2.01e-107 |
|
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: 329.57 E-value: 2.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRAL-GVAKGD----RVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrDRGAMIFYTSGTTGR 208
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF----------------------------------------------DDLALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQIT 288
Cdd:cd17631 113 PKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI---ERHRVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKLLDYYDkhFTQPRVQdfvravckeRIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIGM---ALS 365
Cdd:cd17631 190 SFFLVPTMIQALLQHPR--FATTDLS---------SLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSPgvtFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF 445
Cdd:cd17631 258 PEDHRRK-LGSAGRPVFFVEVRIVDPD----------------GREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 446 tSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH 524
Cdd:cd17631 318 -RDGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1195733688 525 SLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNK 564
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
52-567 |
6.32e-106 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 328.68 E-value: 6.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 52 AFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPE 131
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRLANAL-RALGVKKGD----RVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 132 AQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL----------GVPLLPLTPAIYRGAT---EKPTEQPVKESGWRDRGAM 198
Cdd:PRK06187 93 EEIAYILNDAEDRVVLVDSEFVPLLAAILPQLptvrtvivegDGPAAPLAPEVGEYEEllaAASDTFDFPDIDENDAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 iFYTSGTTGRPKGALSTHRNLAAVVTGlVHSW-AWTKNDVILHVLPLHHVHG----VVnkllcPLWVGATCVMLPEFSAQ 273
Cdd:PRK06187 173 -LYTSGTTGHPKGVVLSHRNLFLHSLA-VCAWlKLSRDDVYLVIVPMFHVHAwglpYL-----ALMAGAKQVIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 274 QVWEKFlssEAPQITVFMAVPTVYSKLLDYYDKHFtqprvQDFVRavckerIRLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:PRK06187 246 NLLDLI---ETERVTFFFAVPTIWQMLLKAPRAYF-----VDFSS------LRLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIGMALS-NPLTE-----ARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFEEKeGELLVRG 427
Cdd:PRK06187 312 GYGMTETSPVVSvLPPEDqlpgqWTKRRSAGRPLPGVEARIV----------------DDDGDELPPDGGEV-GEIIVRG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 428 PSVFREYWDKPEETKSAFTsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVP 506
Cdd:PRK06187 375 PWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYlYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 507 DMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK06187 453 DEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
197-562 |
9.13e-105 |
|
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: 319.23 E-value: 9.13e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQQVW 276
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 EKFlssEAPQITVFMAVPTVYSKLLDyydkhftQPRVQDFVRAvckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYG 356
Cdd:cd04433 82 ELI---EREKVTILLGVPTLLARLLK-------APESAGYDLS----SLRALVSGGAPLPPELLERFEEAPGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 357 MTEIG--MALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGFEekeGELLVRGPSVFREY 434
Cdd:cd04433 148 LTETGgtVATGPPDDDARKPGSVGRPVPGVEVRIVDPD----------------GGELPPGEI---GELVVRGPSVMKGY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 435 WDKPEETkSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQR 513
Cdd:cd04433 209 WNNPEAT-AAVDEDGWYRTGDLGRLDEDGYlYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGER 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1195733688 514 VTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:cd04433 287 VVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
50-567 |
5.41e-103 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 320.70 E-value: 5.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAL-GIGKGD----RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLgvpllPLTPAIYRGATEKPTEQPVKESGWRD---RG---------- 196
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRL-----PALEHVVICETEEDDPHTEKMKTFTDflaAGdpaerapevd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 ----AMIFYTSGTTGRPKGALSTHRNLaavvTGLVHSWA----WTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP 268
Cdd:PRK07656 165 pddvADILFTSGTTGRPKGAMLTHRQL----LSNAADWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 EFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLDYYDKhftqpRVQDFvravckERIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK07656 241 VFDPDEV---FRLIETERITVLPGPPTMYNSLLQHPDR-----SAEDL------SSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 -HTLLERYGMTE-IGMALSNPLTEAR--VPGSVGTPLPGVEVRIISENpqkgspyiihaeGNERGTKVTpgfeekeGELL 424
Cdd:PRK07656 307 vDIVLTGYGLSEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIVNEL------------GEEVPVGEV-------GELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYlYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 504 GVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07656 447 GVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
67-567 |
7.15e-98 |
|
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: 306.93 E-value: 7.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05926 16 TYADLAELVDDLARQLAAL-GIKKGD----RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLERLSPLAQRLGVPL------------------LPLTPAIYRGATEKPTEQPvkesgwrDRGAMIFYTSGTTGR 208
Cdd:cd05926 91 LTPKGELGPASRAASKLGLAIlelaldvgvlirapsaesLSNLLADKKNAKSEGVPLP-------DDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQIT 288
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDV---RDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKLLDYYDKHFTQPRVqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG--MAlSN 366
Cdd:cd05926 241 WYTAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 PL-TEARVPGSVGTPLpGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF 445
Cdd:cd05926 310 PLpPGPRKPGSVGKPV-GVEVRIL----------------DEDGEILPPG---VVGEICLRGPNVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 446 TSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH 524
Cdd:cd05926 370 FKDGWFRTGDLGYLDADGYlFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1195733688 525 SLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
49-478 |
7.57e-92 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 288.44 E-value: 7.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIAL-IDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:pfam00501 4 QAARTPDKTALeVGEGRRLTYRELDERANRLAAGL-RALGVGKGD----RVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQE-YLERLSPLAQRLGVP-------LLPLTPAIYRGATEKPTEQPVKESGWRDRG--A 197
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVklvlvldRDPVLKEEPLPEEAKPADVPPPPPPPPDPDdlA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGL----VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQ 273
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 274 QVWEKFLSSEAPQITVFMAVPTVYSKLLDyydkhftqprvQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIGMALSNPLTE---ARVPGSVGTPLPGVEVRIISENpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSV 430
Cdd:pfam00501 308 GYGLTETTGVVTTPLPLdedLRSLGSVGRPLPGTEVKIVDDE-----------TGEP----VPPG---EPGELCVRGPGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1195733688 431 FREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTG 478
Cdd:pfam00501 370 MKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
40-566 |
5.46e-91 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 291.52 E-value: 5.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 40 TDGS-VPVFIRALA-FGDRIALiDKYGHH-TYRELyDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASW 116
Cdd:PRK05605 30 GDTTlVDLYDNAVArFGDRPAL-DFFGATtTYAEL-GKQVRRAAAGLRALGVRPGD----RVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 117 MSGGVAV---PLYWKHpeaQLEYFIQDSRSSLVVV---GQEYLERLS-----------------PLAQRLGVPLlPLTPA 173
Cdd:PRK05605 104 RLGAVVVehnPLYTAH---ELEHPFEDHGARVAIVwdkVAPTVERLRrttpletivsvnmiaamPLLQRLALRL-PIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 174 iyRGATEK---------PTEQPVKESGWRDRG------------AMIFYTSGTTGRPKGALSTHRNLAAvvtGLVHSWAW 232
Cdd:PRK05605 180 --RKARAAltgpapgtvPWETLVDAAIGGDGSdvshprptpddvALILYTSGTTGKPKGAQLTHRNLFA---NAAQGKAW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 233 T-----KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWeKFLSSEAPqiTVFMAVPTVYSKLLDYYDKH 307
Cdd:PRK05605 255 VpglgdGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLIL-DAMKKHPP--TWLPGVPPLYEKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 308 ftqprvqdfvrAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEV 386
Cdd:PRK05605 332 -----------GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 387 RIIS-ENPQKGSPyiihaegnergtkvtPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDTAVFkDARYW 465
Cdd:PRK05605 401 RIVDpEDPDETMP---------------DG---EEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVM-EEDGF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 466 IRgrtSVDIIK----TGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAP 541
Cdd:PRK05605 461 IR---IVDRIKeliiTGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTR 537
|
570 580
....*....|....*....|....*
gi 1195733688 542 YAVPSELLLLEEIPRNQMGKVNKKE 566
Cdd:PRK05605 538 YKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
54-568 |
1.31e-89 |
|
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: 285.80 E-value: 1.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 54 GDRIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRAL-----GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 134 LEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLL---------PLTPAIYRgATEKPTEQPVKESG--WRDRGAMIFYT 202
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVvlivsggagPEAGALLL-AELVAAEAEQLKPAatHADDPAFWLYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 203 SGTTGRPKGALSTHRNLAAV-------VTGLvhswawTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQV 275
Cdd:cd05959 172 SGSTGRPKGVVHLHADIYWTaelyarnVLGI------REDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEKFLSSEAPqiTVFMAVPTVYSKLLdyydkhfTQPRVQ--DFVRavckerIRLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:cd05959 246 VFKRIRRYRP--TVFFGVPTLYAAML-------AAPNLPsrDLSS------LRLCVSAGEALPAEVGERWKARFGLDILD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIG-MALSNpLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFR 432
Cdd:cd05959 311 GIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELR----------------DEDGGDVADG---EPGELYVRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 433 EYWDKPEETKSAFTSdGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWG 511
Cdd:cd05959 371 MYWNNRDKTRDTFQG-EWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 512 QRVTAVVAL---QEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELL 568
Cdd:cd05959 449 TKPKAFVVLrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-562 |
5.03e-85 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 275.45 E-value: 5.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 54 GDRIALI--DKYGHH---TYRELYDRSlclaqeiCRL------QGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVA 122
Cdd:COG0365 23 GDKVALIweGEDGEErtlTYAELRREV-------NRFanalraLGVKKGD----RVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 123 VPLYwkH---PEAqLEYFIQDSRSSLVVVGQEYLERLSPlaqrlgVPLLPLTPAIYRGATE-------KPTEQPVKESGW 192
Cdd:COG0365 92 SPVF--PgfgAEA-LADRIEDAEAKVLITADGGLRGGKV------IDLKEKVDEALEELPSlehvivvGRTGADVPMEGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 193 --------------------RDRGAMIFYTSGTTGRPKGALSTHRN-LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVV 251
Cdd:COG0365 163 ldwdellaaasaefepeptdADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 252 NKLLCPLWVGATCVML---PEF-SAQQVW---EKFlsseapQITVFMAVPTVYSKLLDYYDKHFTQPRVqdfvravckER 324
Cdd:COG0365 243 YIVYGPLLNGATVVLYegrPDFpDPGRLWeliEKY------GVTVFFTAPTAIRALMKAGDEPLKKYDL---------SS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 325 IRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMA-LSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiiha 403
Cdd:COG0365 308 LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVDE------------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 404 EGNErgtkVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAF--TSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKT 477
Cdd:COG0365 376 DGNP----VPPG---EEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGAR-RDEDgyFWILGRSD-DVINV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 478 GGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS---HRDLKEWARGVLAPYAVPSELLLLEEI 554
Cdd:COG0365 447 SGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDEL 526
|
....*...
gi 1195733688 555 PRNQMGKV 562
Cdd:COG0365 527 PKTRSGKI 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
67-563 |
1.42e-84 |
|
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: 271.78 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAqeiCRLQgcKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05911 12 TYAQLRTLSRRLA---AGLR--KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLERLSPLAQRLG----VPLLPLTPAiYRGATEKPTEQPVKESGWR---------DRGAMIFYTSGTTGRPKGAL 213
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGpkdkIIVLDDKPD-GVLSIEDLLSPTLGEEDEDlppplkdgkDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 214 STHRNLAAVV--TGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVF 290
Cdd:cd05911 166 LSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDS----ELFLDLiEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 MAVPTVYSKLLdyydKHftqPRVQDFVRAvckeRIRLMVSGSAALP---VPLLEKWRSATghTLLERYGMTEIGMALS-N 366
Cdd:cd05911 241 YLVPPIAAALA----KS---PLLDKYDLS----SLRVILSGGAPLSkelQELLAKRFPNA--TIKQGYGMTETGGILTvN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 PLTEArVPGSVGTPLPGVEVRIISENPQKGSPYiihaegNERGtkvtpgfeekegELLVRGPSVFREYWDKPEETKSAFT 446
Cdd:cd05911 308 PDGDD-KPGSVGRLLPNVEAKIVDDDGKDSLGP------NEPG------------EICVRGPQVMKGYYNNPEATKETFD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 447 SDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHS 525
Cdd:cd05911 369 EDGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1195733688 526 LSHRDLKEWARGVLAPYavpSEL----LLLEEIPRNQMGKVN 563
Cdd:cd05911 448 LTEKEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-567 |
7.93e-81 |
|
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: 7.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 65 HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:cd05934 3 RWTYAELLRESARIAAALAAL-GIRPGD----RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVgqeylerlSPlaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVT 224
Cdd:cd05934 78 LVVV--------DP--------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 225 GLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDyy 304
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGA---TVTNYLGAMLSYLLA-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 305 dkhfTQPRVQDfvravCKERIRlmVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGV 384
Cdd:cd05934 187 ----QPPSPDD-----RAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGY 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 385 EVRIISENPQKgspyiihaegNERGTKvtpgfeekeGELLVR---GPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFkD 461
Cdd:cd05934 256 EVRIVDDDGQE----------LPAGEP---------GELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYR-D 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 462 ARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVL 539
Cdd:cd05934 315 ADGFFYfvDRKK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQL 393
|
490 500
....*....|....*....|....*...
gi 1195733688 540 APYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05934 394 AYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
53-567 |
2.65e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 256.78 E-value: 2.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDL-GLKKGD----RVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAiyrgatEKPTEQPvkeSGWRDRGAM-------------- 198
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLV------LGGREAP---GGWLDFADWaeagsvaepdvela 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 ------IFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSA 272
Cdd:PRK08316 170 dddlaqILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 273 QQVWEKFlssEAPQITVFMAVPTVYSKLLDYYDkhFTQPRVQDFVRAVckerirlmvSGSAALPVPLLEKwrsatghtLL 352
Cdd:PRK08316 250 ELILRTI---EAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRKGY---------YGASIMPVEVLKE--------LR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 353 ER---------YGMTEIG---MALsNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKE 420
Cdd:PRK08316 308 ERlpglrfyncYGQTEIAplaTVL-GPEEHLRRPGSAGRPVLNVETRVV----------------DDDGNDVAPG---EV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 421 GELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIAD 499
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYiTVVDRKK-DMIKTGGENVASREVEEALYTHPAVAE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK08316 446 VAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
48-567 |
1.46e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 255.27 E-value: 1.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 48 IRALAFGDRIALIdKYGHH-TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLY 126
Cdd:PRK08314 18 VSARRYPDKTAIV-FYGRAiSYRELLEEAERLAGYLQQECGVRKGD----RVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 127 WKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVP---------LLPLTP--AIYRGATEKPTEQPVKESGW--- 192
Cdd:PRK08314 93 PMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvivaqysdYLPAEPeiAVPAWLRAEPPLQALAPGGVvaw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 193 ----------------RDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLC 256
Cdd:PRK08314 173 kealaaglappphtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 257 PLWVGATCVMLPEfsaqqvWEKFLSSEA---PQITVFMAVPTVyskLLDYydkhFTQPRVQDFvravCKERIRLMVSGSA 333
Cdd:PRK08314 253 PIYAGATVVLMPR------WDREAAARLierYRVTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 334 ALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARvPGSVGTPLPGVEVRIIseNPqkgspyiihaegnERGTKV 412
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVI--DP-------------ETLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 413 TPGfeeKEGELLVRGPSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIE 488
Cdd:PRK08314 380 PPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLGrMDEEGYFFITDRLK-RMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 489 RHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH--SLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKE 566
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
.
gi 1195733688 567 L 567
Cdd:PRK08314 536 L 536
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
46-565 |
2.20e-76 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 253.48 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 46 VFIRALAFGDRIALIDKYG----HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGV 121
Cdd:COG1022 17 LRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLAL-GVKPGD----RVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 122 AVPLYWKHPEAQLEYFIQDSRSSLVVVG-QEYLERLSPLAQRLGvpllPLTPAIY---RGATEKPTEQPVKEsgWRDRG- 196
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELP----SLRHIVVldpRGLRDDPRLLSLDE--LLALGr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 --------------------AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLC 256
Cdd:COG1022 166 evadpaelearraavkpddlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 257 pLWVGATCVMLPefSAQQVWEKfLSSEAPqiTVFMAVPTVYSKLLDY-YDKHFTQPRVQ----DFVRAVCKE-------- 323
Cdd:COG1022 246 -LAAGATVAFAE--SPDTLAED-LREVKP--TFMLAVPRVWEKVYAGiQAKAEEAGGLKrklfRWALAVGRRyararlag 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 324 ----------------------------RIRLMVSGSAALPVPLLEKWRSAtGHTLLERYGMTEI-GMALSNPLTEARvP 374
Cdd:COG1022 320 kspslllrlkhaladklvfsklrealggRLRFAVSGGAALGPELARFFRAL-GIPVLEGYGLTETsPVITVNRPGDNR-I 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 375 GSVGTPLPGVEVRIisenpqkgspyiihAEgnergtkvtpgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTG 454
Cdd:COG1022 398 GTVGPPLPGVEVKI--------------AE---------------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 455 DTAVFKDARY-WIRGRTSvDIIKT-GGYKVSALEIERHLLAHPSIADVAVIGvpDmtwgQR--VTAVVALQEGHslshrd 530
Cdd:COG1022 449 DIGELDEDGFlRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG--D----GRpfLAALIVPDFEA------ 515
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1195733688 531 LKEWA--RGVlaPYAVPSELL----LLEEIpRNQMGKVNKK 565
Cdd:COG1022 516 LGEWAeeNGL--PYTSYAELAqdpeVRALI-QEEVDRANAG 553
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
67-567 |
1.69e-75 |
|
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: 246.62 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGD----RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEyLERLsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05935 78 VVGSE-LDDL----------------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyydk 306
Cdd:cd05935 117 AVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLL----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 307 hfTQPRVQDFvravCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPgSVGTPLPGVE 385
Cdd:cd05935 189 --ATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPPLRPKLQ-CLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 386 VRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDG---WFRTGDTAVFKDA 462
Cdd:cd05935 262 ARVIDI---------------ETGRELPPN---EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 463 RYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH--SLSHRDLKEWARGVLA 540
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMA 403
|
490 500
....*....|....*....|....*..
gi 1195733688 541 PYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05935 404 AYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-567 |
2.67e-75 |
|
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: 248.30 E-value: 2.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 32 LPTAPEAHtdgsVPVFIRALAFGDRIALIDKYG--HHTYRELYDRSLCLAQEICRLQGCKvGDLqeerVSFLCSNDISYV 109
Cdd:cd05904 1 LPTDLPLD----SVSFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRK-GDV----VLLLSPNSIEFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 110 VAQWASwMSGGVAV----PLYwkhPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV-------PLLPLTPAIYRGA 178
Cdd:cd05904 72 VAFLAV-LSLGAVVttanPLS---TPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLldsaefdSLSFSDLLFEADE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 179 TEKPTEQpVKEsgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWT--KNDVILHVLPLHHVHGVVNKLLC 256
Cdd:cd05904 148 AEPPVVV-IKQ----DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 257 PLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLLDyydkhftQPRVQDFVRAvckeRIRLMVSGSAAL 335
Cdd:cd05904 223 LLRLGATVVVMPRFDL----EELLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 336 PVPLLEKWRSATGHT-LLERYGMTE---IGMALSNPLTEARVPGSVGTPLPGVEVRIIseNPQKGSPyiihaegnergtk 411
Cdd:cd05904 288 GKELIEAFRAKFPNVdLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIV--DPETGES------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 412 VTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERH 490
Cdd:cd05904 353 LPPN---QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYlFIVDRLK-ELIKYKGFQVAPAELEAL 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 491 LLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05904 429 LLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
49-571 |
1.37e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 243.61 E-value: 1.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGE----RIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV-PLLPLTpaiyrGATEKPTEQPVK-ESGWRDRGAMIFYTSGTT 206
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVqRVISIT-----SLKEIEDRKIDNfVEKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 207 GRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLP-EFSAQQVWEKFlssEAP 285
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMI---EKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 286 QITVFMAVPTVYSKLLDYYDkhFTQPRVQDfvravckerIRLMVSGSAALPVPLLEKWRSaTGHTLLERYGMTEIGMALS 365
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSK--FETTNLQS---------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NPLTE--ARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:PRK06839 306 MLSEEdaRRKVGSIGKPVLFCDYELIDEN----------------KNKVEVG---EVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 444 AFtSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQE 522
Cdd:PRK06839 367 TI-QDGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1195733688 523 GHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK06839 445 SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
67-567 |
4.20e-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: 240.36 E-value: 4.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGD----VVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVgqeylerlsplaqrlgvpllpltPAIYRGatEKPTEQPvkesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05903 78 VV-----------------------PERFRQ--FDPAAMP-------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEkFLSSEapQITVFMAVPTVYSKLLDYYDK 306
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA-LMREH--GVTFMMGATPFLTDLLNAVEE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 307 HFTQPRvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSN--PLTEARVPGSVGTPLPGV 384
Cdd:cd05903 203 AGEPLS-----------RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSitPAPEDRRLYTDGRPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 385 EVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY 464
Cdd:cd05903 272 EIKVV----------------DDTGATLAPG---VEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 465 W-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGV-LAPY 542
Cdd:cd05903 332 LrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQ 410
|
490 500
....*....|....*....|....*
gi 1195733688 543 AVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
33-567 |
3.72e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 237.58 E-value: 3.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 33 PTAPEAHTDGSVP-VFIRALA-FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVV 110
Cdd:PRK06188 3 TMADLLHSGATYGhLLVSALKrYPDRPALVLGDTRLTYGQLADRISRYIQAFEAL-GLGTGD----AVALLSLNRPEVLM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 111 AQWASWMSGGVAVPLywkHPEAQLE---YFIQDSR-SSLVVVGQEYLERLSPLAQRlgVP----LLPLTPAIY----RGA 178
Cdd:PRK06188 78 AIGAAQLAGLRRTAL---HPLGSLDdhaYVLEDAGiSTLIVDPAPFVERALALLAR--VPslkhVLTLGPVPDgvdlLAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 179 TEKPTEQPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvnKLLCPL 258
Cdd:PRK06188 153 AAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 259 WVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLLDYYDkhftqPRVQDFvravckERIRLMVSGSAAL-P 336
Cdd:PRK06188 231 LRGGTVIVLAKFDP----AEVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPMsP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 337 VPLLEKWRsATGHTLLERYGMTEIGMALS------NPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaeGNErgt 410
Cdd:PRK06188 296 VRLAEAIE-RFGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALLDED------------GRE--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 411 kVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKTGGYKVSALEIE 488
Cdd:PRK06188 360 -VAQG---EVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAR-EDEDgfYYIVDRKK-DMIVTGGFNVFPREVE 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 489 RHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK06188 433 DVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
67-565 |
2.91e-69 |
|
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: 230.56 E-value: 2.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05907 7 TWAEFAEEVRALAKGL-IALGVEPGD----RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVgqeylerlsplaqrlgvpllpltpaiyrgatEKPTEQpvkesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05907 82 FV-------------------------------EDPDDL-----------ATIIYTSGTTGRPKGVMLSHRNILSNALAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEfsaqqvwEKFLSSEAPQI--TVFMAVPTVYSKLldyY 304
Cdd:cd05907 120 AERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS-------AETLLDDLSEVrpTVFLAVPRVWEKV---Y 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 305 D--KHFTQPRVQDFVRAVCK-ERIRLMVSGSAALPVPLLEKWRSAtGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPL 381
Cdd:cd05907 190 AaiKVKAVPGLKRKLFDLAVgGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 382 PGVEVRIisenpqkgspyiihAEgnergtkvtpgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFK- 460
Cdd:cd05907 269 PGVEVRI--------------AD---------------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDe 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 461 DARYWIRGRtSVDIIKT-GGYKVSALEIERHLLAHPSIADVAVIGvpDmtwgQR--VTAVVALQEGhslshrDLKEWARG 537
Cdd:cd05907 320 DGFLHITGR-KKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRpfLVALIVPDPE------ALEAWAEE 386
|
490 500 510
....*....|....*....|....*....|..
gi 1195733688 538 VLAPYAVPSELL----LLEEIpRNQMGKVNKK 565
Cdd:cd05907 387 HGIAYTDVAELAanpaVRAEI-EAAVEAANAR 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
67-567 |
8.82e-68 |
|
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: 226.06 E-value: 8.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05972 2 SFRELKRESAKAANVLAKL-GLRKGD----RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALSTHRNL------A 220
Cdd:cd05972 77 VTDAEDP-------------------------------------------ALIYFTSGTTGLPKGVLHTHSYPlghiptA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 221 AVVTGL--------VHSWAWTKndvilhvlplhhvhGVVNKLLCPLWVGATCVM--LPEFSAQQVWEKfLSSEapQITVF 290
Cdd:cd05972 114 AYWLGLrpddihwnIADPGWAK--------------GAWSSFFGPWLLGATVFVyeGPRFDAERILEL-LERY--GVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 MAVPTVYsklldyydKHFTQPRVQDFVRavckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTE 370
Cdd:cd05972 177 CGPPTAY--------RMLIKQDLSSYKF----SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 371 ARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVR--GPSVFREYWDKPEETKSAFtSD 448
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAIIDD------------DGRE----LPPG---EEGDIAIKlpPPGLFLGYVGDPEKTEASI-RG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 449 GWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS 527
Cdd:cd05972 305 DYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPS 383
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1195733688 528 H---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05972 384 EelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
55-567 |
3.22e-67 |
|
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: 225.10 E-value: 3.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLAR---YLRERGVG--PGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDL-------------------------------------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPE---FSAQQVWEKFlssEAPQITVFM 291
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLL---AEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 292 AVPTVYSKLLDY-YDKHFTQPRVqdfvravckerirLMVSGSAaLPVPLLEKWRSA-TGHTLLERYGMTEIGMA------ 363
Cdd:cd05930 190 LTPSLLRLLLQElELAALPSLRL-------------VLVGGEA-LPPDLVRRWRELlPGARLVNLYGPTEATVDatyyrv 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 364 LSNPLTEARVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:cd05930 256 PPDDEEDGRVP--IGRPIPNTRVYVL----------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPELTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 444 AFTSDGWF------RTGDTAVFKDAR---YwiRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRV 514
Cdd:cd05930 315 RFVPNPFGpgermyRTGDLVRWLPDGnleF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRL 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 515 TAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05930 392 VAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
67-581 |
2.08e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 226.07 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAV---PLYwkhPEAQLEYFIQDSRS 143
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGD----RVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLY---TERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 144 SLVVVGQEYLERLSP--------------LAQRLGVPLLPLTPAIYRGATEKPTEqpVKESG----W------RDRG--- 196
Cdd:PRK06710 123 KVILCLDLVFPRVTNvqsatkiehvivtrIADFLPFPKNLLYPFVQKKQSNLVVK--VSESEtihlWnsvekeVNTGvev 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 --------AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHswaWTKN-----DVILHVLPLHHVHGVVNKLLCPLWVGAT 263
Cdd:PRK06710 201 pcdpendlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ---WLYNckegeEVVLGVLPFFHVYGMTAVMNLSIMQGYK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 264 CVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhftQPRVQDFVRAvckeRIRLMVSGSAALPVPLLEKW 343
Cdd:PRK06710 278 MVLIPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 344 RSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGE 422
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL---------------ETGEALPPG---EIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGPSVFREYWDKPEETkSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVA 501
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVGYMdEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 502 VIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLYPSGQRSQPG 581
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDEQTG 563
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-567 |
2.12e-66 |
|
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: 224.82 E-value: 2.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 65 HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:cd12119 25 RYTYAEVAERARRLANALRRL-GVKPGD----RVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYLERLSPLAQRL----------GVPLLPLTPAIYRGATEKPTEQPVKESGWRD----RGAMIFYTSGTTGRPK 210
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLptvehvvvmtDDAAMPEPAGVGVLAYEELLAAESPEYDWPDfdenTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 211 GALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVH--GVvnkllcP---LWVGATCV-----MLPEFSAQQVwek 278
Cdd:cd12119 180 GVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPMFHVNawGL------PyaaAMVGAKLVlpgpyLDPASLAELI--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 279 flssEAPQITVFMAVPTVYSKLLDYYDKHftqPRVQDFVRAVckerirlmVSGSAALPVPLLEKWRSAtGHTLLERYGMT 358
Cdd:cd12119 251 ----EREGVTFAAGVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWGMT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 359 EI-----------GMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnergTKVTPGFEEKEGELLVRG 427
Cdd:cd12119 315 ETsplgtvarppsEHSNLSEDEQLALRAKQGRPVPGVELRIVDDD-----------------GRELPWDGKAVGELQVRG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 428 PSVFREYWdKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVP 506
Cdd:cd12119 378 PWVTKSYY-KNDEESEALTEDGWLRTGDVATIDEDGYLtITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 507 DMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12119 456 HPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
49-571 |
6.82e-66 |
|
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: 223.87 E-value: 6.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGgvAVPLY-- 126
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGD----RVVVQLPNVAEFVIVFFALFRAG--AIPVFal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 127 WKHPEAQLEYFIQDSRSSLVVVGQEYLE-RLSPLAQRL--GVPLL----------PLTP--AIYRGATEKPTEQPvkesg 191
Cdd:COG1021 107 PAHRRAEISHFAEQSEAVAYIIPDRHRGfDYRALARELqaEVPSLrhvlvvgdagEFTSldALLAAPADLSEPRP----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wrDRGAMIFY--TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHH--------VHGVvnkllcpLWVG 261
Cdd:COG1021 182 --DPDDVAFFqlSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfplsspgVLGV-------LYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 262 ATCVMLPEFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPrvqdfvravckERIRLMVSGSAALPVPLLE 341
Cdd:COG1021 253 GTVVLAPDPSPDTA---FPLIERERVTVTALVPPLALLWLDAAERSRYDL-----------SSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 342 KWRSATGHTLLERYGMTEiGMALSNPL--TEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfee 418
Cdd:COG1021 319 RVRPALGCTLQQVFGMAE-GLVNYTRLddPEEVILTTQGRPIsPDDEVRIVDE------------DGNP----VPPG--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 419 KEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRtSVDIIKTGGYKVSALEIERHLLAHPSI 497
Cdd:COG1021 379 EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYlVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 498 ADVAVIGVPDMTWGQRVTAVVALQeGHSLSHRDLKEW--ARGVlAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:COG1021 458 HDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFlrERGL-AAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-567 |
1.65e-64 |
|
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: 217.71 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 56 RIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLE 135
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNL-----GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 136 YFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALST 215
Cdd:cd05919 76 YIARDCEARLVVTSADDI-------------------------------------------AYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 216 HRNLAAVVTGL-VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SAQQVWEKfLSSEAPqiTVFMAV 293
Cdd:cd05919 113 HRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLAT-LARFRP--TVLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 294 PTVYSKLLDYYDKHftqprvQDFVRAvckerIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEAR 372
Cdd:cd05919 190 PTFYANLLDSCAGS------PDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPGAWR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 373 vPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFR 452
Cdd:cd05919 259 -LGSTGRPVPGYEIRLV----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 453 TGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH--- 528
Cdd:cd05919 318 TGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEsla 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 1195733688 529 RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05919 397 RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-567 |
6.04e-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: 213.29 E-value: 6.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTHRNLA--AVVTGlvHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML-PEFSAQQV 275
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 wekFLSSEAPQITVFMAVPTVYSKLLDyydkhftQPRVQDFVRAvckeRIRLMVSGSAALPVPLLEKWRSATGHT-LLER 354
Cdd:cd05917 85 ---LEAIEKEKCTALHGVPTMFIAELE-------HPDFDKFDLS----SLRTGIMAGAPCPPELMKRVIEVMNMKdVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 355 YGMTE----IGMALSNPLTEARVpGSVGTPLPGVEVRIISEnpqkgspyiihaegnerGTKVTPGFEEKeGELLVRGPSV 430
Cdd:cd05917 151 YGMTEtspvSTQTRTDDSIEKRV-NTVGRIMPHTEAKIVDP-----------------EGGIVPPVGVP-GELCIRGYSV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 431 FREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:cd05917 212 MKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDER 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 510 WGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05917 291 YGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
55-573 |
3.66e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 212.74 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHH--TYRELyDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK09088 10 QRLAAVDLALGRrwTYAEL-DALVGRLAAVLRRRGCVDGE----RLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIQDSRSSLVVvGQEYLERLSPLaqrlGVPLLPLTPAIyRGATEKPTEqpvkeSGWRDRGAMIFYTSGTTGRPKGA 212
Cdd:PRK09088 85 ELDALLQDAEPRLLL-GDDAVAAGRTD----VEDLAAFIASA-DALEPADTP-----SIPPERVSLILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 213 LSTHRNLAAV-----VTGLVhswawTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWeKFLSSEAPQI 287
Cdd:PRK09088 154 MLSERNLQQTahnfgVLGRV-----DAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTL-GRLGDPALGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 288 TVFMAVPTVYSKLLDyydkhftQPrvqDFVRAVCKeRIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIGMALSNP 367
Cdd:PRK09088 228 THYFCVPQMAQAFRA-------QP---GFDAAALR-HLTALFTGGAPHAAEDILGWL-DDGIPMVDGFGMSEAGTVFGMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 368 LTEARVP---GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:PRK09088 296 VDCDVIRakaGAAGIPTPTVQTRVVDDQ----------------GNDCPAG---VPGELLLRGPNLSPGYWRRPQATARA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FTSDGWFRTGDTAVfKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQE 522
Cdd:PRK09088 357 FTGDGWFRTGDIAR-RDADgfFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 523 GHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLYP 573
Cdd:PRK09088 435 GAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
54-567 |
8.22e-62 |
|
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: 212.39 E-value: 8.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 54 GDRIALIDKYGHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRL-----GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 134 LEYFIQDSRSSLVVVGQEYLERLSPLAQRL---------GVPLLPLTPAIYRGATEKPTEQPVKESGwrDRGAMIFYTSG 204
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALGKSphlehrvvvGRPEAGEVQLAELLATESEQFKPAATQA--DDPAFWLYSSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 205 TTGRPKGALSTHRNLAAVV-TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SAQQVWEKFLSS 282
Cdd:TIGR02262 172 STGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 283 eapQITVFMAVPTVYSKLLdyydkhfTQPRVqdfvRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG- 361
Cdd:TIGR02262 252 ---QPTIFYGVPTLYAAML-------ADPNL----PSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLh 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 362 MALSNPLTEARVpGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEET 441
Cdd:TIGR02262 318 IFLSNLPGDVRY-GTSGKPVPGYRLRLV----------------GDGGQDVADG---EPGELLISGPSSATMYWNNRAKS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 442 KSAFTSdGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVAL 520
Cdd:TIGR02262 378 RDTFQG-EWTRSGDKYVRNdDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVL 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1195733688 521 QEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:TIGR02262 456 RPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKL 502
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
49-571 |
1.93e-61 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 210.97 E-value: 1.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQgcKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAG---KLA--ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQrlgvpllpltpAIYRGATEKPTEQPVKESGWR-DRGAMIFYTSGTTG 207
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGIS-----------VKFAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 208 RPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSeapQI 287
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTG---GV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 288 TVFMAVPTVYSKLLDYYDKHftqprvqdfvraVCKERIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIG---MAL 364
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETAsqiVTL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 365 SNPLTEARVpGSVGTPLPGVEVRIisenpqkgspyiihaegnERGTKVTPGFEEkeGELLVRGPSVFREYWDKPEETKSA 444
Cdd:PRK03640 298 SPEDALTKL-GSAGKPLFPCELKI------------------EKDGVVVPPFEE--GEIVVKGPNVTKGYLNREDATRET 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALqeG 523
Cdd:PRK03640 357 F-QDGWFKTGDIGYLDEEGFlYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--S 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1195733688 524 HSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK03640 433 GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
198-564 |
3.73e-61 |
|
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: 205.58 E-value: 3.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 KflsSEAPQITVFMAVPTVYSKLLDYYDKHFTQPRVqdfVRAVckerirlmvsgsAALPVP-LLEKWRSATGHTLLERYG 356
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSS---LRHV------------LGLDAPeTIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 357 MTEI-GMALSNPLTEArvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYW 435
Cdd:cd17637 145 QTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDN----------------DRPVPAG---ETGEIVVRGPLVFQGYW 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 436 DKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSV-DIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQR 513
Cdd:cd17637 204 NLPELTAYTF-RNGWHHTGDLGRFDEDGYlWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 514 VTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNK 564
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
53-583 |
1.08e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 209.90 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAALAA-RGVRKGD----RILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIQDSRSSLVVVGQEYLERLSplAQRLGVPLLPLTPAIYRGATEKPTEQPVKesgwRDRGAMI------------- 199
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFPEHAA--AVRAASPDLTHVVAIGGARAGLDYEALVA----RHLGARVanaavdhddpcwf 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 200 FYTSGTTGRPKGALSTHRNLAAVVT--------GLVHSwawtknDVILHVLPLHHVHGVvnKLLCPLWVGATCVMLP--E 269
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGQMAFVITnhladlmpGTTEQ------DASLVVAPLSHGAGI--HQLCQVARGAATVLLPseR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 FSAQQVWEKFlssEAPQITVFMAVPTVYsKLL------DYYDkHFTqprvqdfvravckerIRLMVSGSAALPVPLLEKW 343
Cdd:PRK07470 241 FDPAEVWALV---ERHRVTNLFTVPTIL-KMLvehpavDRYD-HSS---------------LRYVIYAGAPMYRADQKRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 344 RSATGHTLLERYGMTEI---------GMALSNPLTEARVpGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTP 414
Cdd:PRK07470 301 LAKLGKVLVQYFGLGEVtgnitvlppALHDAEDGPDARI-GTCGFERTGMEVQIQ----------------DDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLL 492
Cdd:PRK07470 364 G---ETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLG-HLDARgfLYITGRAS-DMYISGGSNVYPREIEEKLL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 493 AHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLY 572
Cdd:PRK07470 438 THPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELE 517
|
570
....*....|.
gi 1195733688 573 PSGQRSQPGQG 583
Cdd:PRK07470 518 ERGLLDLERAP 528
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
199-564 |
1.64e-60 |
|
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: 203.89 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTHRNlaavVTGLVHSWA----WTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQ 274
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQ----TLRAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 275 VWEKFlssEAPQITVFMAVPTVYSKLLDYydkhftqPRVQDFVRAvckeRIRLMVSGSAALPVPLLEKWRSATG-HTLLE 353
Cdd:cd17638 81 ILEAI---ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIGMA-LSNPLTEAR-VPGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELLVRGPSVF 431
Cdd:cd17638 147 AYGLTEAGVAtMCRPGDDAEtVATTCGRACPGFEVRI-----------------------------ADDGEVLVRGYNVM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 REYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTW 510
Cdd:cd17638 198 QGYLDDPEATAEAIDADGWLHTGDVGELDERGYLrITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 511 GQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNK 564
Cdd:cd17638 277 GEVGKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
49-571 |
3.51e-60 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 209.22 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGH-HTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK06087 32 TARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLA-KGIEPGD----RVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQRL-------GV-PLLPLTPAIYRG---ATEKPTEQPVKESG 191
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLpqlqqivGVdKLAPATSSLSLSqiiADYEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFS 271
Cdd:PRK06087 187 --DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 272 AQQVWEKFlssEAPQITVFM-AVPTVYSkLLDYYDKHftQPRVqdfvravckERIRLMVSGSAALPVPLLekwRSATGH- 349
Cdd:PRK06087 265 PDACLALL---EQQRCTCMLgATPFIYD-LLNLLEKQ--PADL---------SALRFFLCGGTTIPKKVA---RECQQRg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 -TLLERYGMTE----IGMALSNPLTeaRVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGfeeKEGELL 424
Cdd:PRK06087 327 iKLLSVYGSTEssphAVVNLDDPLS--RFMHTDGYAAAGVEIKVVDEARKT----------------LPPG---CEGEEA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:PRK06087 386 SRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIkITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 504 GVPDMTWGQRVTAVVALQEG-HSLSHRDLKEW-ARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
50-567 |
9.61e-60 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 206.38 E-value: 9.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIdkYGH--HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:cd12118 14 AAVYPDRTSIV--YGDrrYTWRQTYDRCRRLASALAAL-GISRGD----TVAVLAPNTPAMYELHFGVPMAGAVLNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQEYL-ERLsplaqrlgvpllpltpaIYRGATEKPTEQPVKEsgwRDRGAmIFYTSGTT 206
Cdd:cd12118 87 RLDAEEIAFILRHSEAKVLFVDREFEyEDL-----------------LAEGDPDFEWIPPADE---WDPIA-LNYTSGTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 207 GRPKGALSTHRN--LAAVVTGLvhSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VGATCVMLPEFSAQQVWEkfl 280
Cdd:cd12118 146 GRPKGVVYHHRGayLNALANIL--EWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYD--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 281 SSEAPQITVFMAVPTVYSKLLDYydkhftqprvQDFVRAVCKERIRLMVSGSAAlPVPLLEKwRSATGHTLLERYGMTEI 360
Cdd:cd12118 216 LIEKHKVTHFCGAPTVLNMLANA----------PPSDARPLPHRVHVMTAGAPP-PAAVLAK-MEELGFDVTHVYGLTET 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 -GMALSNPLTearvPGSVGTPLPgVEVRIISenpQKGSPYIIHAE---GNERGTKVTPGFEEKEGELLVRGPSVFREYWD 436
Cdd:cd12118 284 yGPATVCAWK----PEWDELPTE-ERARLKA---RQGVRYVGLEEvdvLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 437 KPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVT 515
Cdd:cd12118 356 NPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 516 AVVALQEGHSLSHRDLKEWARGVLAPYAVPSElLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12118 434 AFVELKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKIQKFVL 484
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
55-567 |
1.02e-59 |
|
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: 206.59 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHH--TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:cd05923 16 DACAIADPARGLrlTYSELRARIEAVAARLHAR-GLRPGQ----RVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIQ--DSRSSLVVVGQEYLE-------RLSPLAQRLGVPllplTPAIYRGATEKPTEQPvKESGWrdrgamIFYTS 203
Cdd:cd05923 91 ELAELIErgEMTAAVIAVDAQVMDaifqsgvRVLALSDLVGLG----EPESAGPLIEDPPREP-EQPAF------VFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 204 GTTGRPKGALSTHRNLA------AVVTGLVHSwawtKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd05923 160 GTTGLPKGAVIPQRAAEsrvlfmSTQAGLRHG----RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 KFlssEAPQITVFMAVPTVYSKLLdyYDKHFTQPRVqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGM 357
Cdd:cd05923 236 LI---EQERVTSLFATPTHLDALA--AAAEFAGLKL---------SSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 358 TEIGMALSNPltEARvPGSVGTPLPGVEVRIIsenPQKGSPYIIHAEGnergtkvtpgfeeKEGELLVR--GPSVFREYW 435
Cdd:cd05923 302 TEAMNSLYMR--DAR-TGTEMRPGFFSEVRIV---RIGGSPDEALANG-------------EEGELIVAaaADAAFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 436 DKPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRV 514
Cdd:cd05923 363 NQPEATAKKL-QDGWYRTGDVGYVDpSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 515 TAVVALQEGhSLSHRDLKEWARGV-LAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05923 441 TACVVPREG-TLSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
49-567 |
1.21e-59 |
|
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: 206.02 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAqeiCRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLA---AGLRGLGIR--PGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYlERLSPLAqrLGVPLLPLTPAIyrgatekpteqpvkesgwrdrgAMIFYTSGTTGR 208
Cdd:cd05920 99 HRRSELSAFCAHAEAVAYIVPDRH-AGFDHRA--LARELAESIPEV----------------------ALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHvhgvvN-KLLCP-----LWVGATCVMLPEFSAQQVwekFLSS 282
Cdd:cd05920 154 PKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDAA---FPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 283 EAPQITVFMAVPTVYSKLLDYYDKHFTQPrvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEiGM 362
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADL-----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 363 ----ALSNPltEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDK 437
Cdd:cd05920 294 lnytRLDDP--DEVIIHTQGRPMsPDDEIRVVDE------------EGNP----VPPG---EEGELLTRGPYTIRGYYRA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 438 PEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA 516
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 517 VVALQeGHSLSHRDLKEWARGV-LAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05920 432 FVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
56-567 |
1.66e-58 |
|
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: 201.94 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 56 RIALIDKYGHHTYRELydrsLCLAQEICRLQGCKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLE 135
Cdd:cd05958 1 RTCLRSPEREWTYRDL----LALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 136 YFIQDSRSSLVVVGqeylERLSPlaqrlgvpllpltpaiyrgatekpteqpvkesgwRDRGAMIFYTSGTTGRPKGALST 215
Cdd:cd05958 77 YILDKARITVALCA----HALTA----------------------------------SDDICILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 216 HRNLAAVVTGL-VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVwekfLSSEAPQ-ITVFMAV 293
Cdd:cd05958 119 HRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL----LSAIARYkPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 294 PTVYSKLLDYYDkhFTQPRVQDfvravckerIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEAR 372
Cdd:cd05958 195 PTAYRAMLAHPD--AAGPDLSS---------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmFHIFISARPGDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 373 vPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETksaFTSDGWFR 452
Cdd:cd05958 264 -PGATGKPVPGYEAKVVDD------------EGNP----VPDG---TIGRLAVRGPTGCRYLADKRQRT---YVQGGWNI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 453 TGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH--- 528
Cdd:cd05958 321 TGDTYSRDpDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvla 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 1195733688 529 RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05958 400 RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
67-567 |
1.86e-58 |
|
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: 200.65 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQeicRLQgcKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLv 146
Cdd:cd05912 3 TFAELFEEVSRLAE---HLA--ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 vvgqeylerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05912 77 -----------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVFMAVPTVYSKLLDYYDK 306
Cdd:cd05912 110 ALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSGK---VTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 307 HftqprvqdfvravCKERIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTEIG--MALSNPLTEARVPGSVGTPLPGV 384
Cdd:cd05912 186 G-------------YPNNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 385 EVRIISENpqkgspyiihaegnergtkvtpGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY 464
Cdd:cd05912 252 ELKIEDDG----------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 465 -WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEghSLSHRDLKEWARGVLAPYA 543
Cdd:cd05912 309 lYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYK 385
|
490 500
....*....|....*....|....
gi 1195733688 544 VPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05912 386 VPKKIYFVDELPRTASGKLLRHEL 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-567 |
2.83e-58 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 202.99 E-value: 2.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALI--DKYG---HHTYRELYdrslclaQEICRL------QGCKVGDlqeeRVSFLCSNDISYVVAQWASWM 117
Cdd:PRK08008 16 LADVYGHKTALIfeSSGGvvrRYSYLELN-------EEINRTanlfysLGIRKGD----KVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 118 SGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPL---------LPLTPAI---YRGATEKPTE- 184
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLrhicltrvaLPADDGVssfTQLKAQQPATl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 185 --QPVKESgwrDRGAMIFYTSGTTGRPKGALSTHRNLaaVVTGLVHSW--AWTKNDVILHVLPLHHVHGVVNKLLCPLWV 260
Cdd:PRK08008 165 cyAPPLST---DDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 261 GATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLdyydkhfTQPrVQDFVRAVCkerIRLMVsgsAALPVPLL 340
Cdd:PRK08008 240 GATFVLLEKYSARAFWGQVCKYRA---TITECIPMMIRTLM-------VQP-PSANDRQHC---LREVM---FYLNLSDQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 341 EK--WRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfe 417
Cdd:PRK08008 303 EKdaFEERFGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDH----------------NRPLPAG-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 418 eKEGELLVRG---PSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAH 494
Cdd:PRK08008 365 -EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 495 PSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
194-567 |
4.57e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 205.19 E-value: 4.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAMIFYTSGTTGRPKGALSTHRN------LAAVVTGLVHswawtkNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML 267
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHGNevanawLGALLLGLGP------GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 PE--FSAQQVWEKFLS-SEAPQITVFMAVPTVYSKLLDyydkhftQPrvqdfVRAVCKERIRLMVSGSAALPVPLLEKWR 344
Cdd:PRK07529 287 TPqgYRGPGVIANFWKiVERYRINFLSGVPTVYAALLQ-------VP-----VDGHDISSLRYALCGAAPLPVEVFRRFE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 345 SATGHTLLERYGMTEiGMALS--NPLTEARVPGSVGTPLPGVEVRIISENPQkgSPYIIHAEGNErgtkvtpgfeekEGE 422
Cdd:PRK07529 355 AATGVRIVEGYGLTE-ATCVSsvNPPDGERRIGSVGLRLPYQRVRVVILDDA--GRYLRDCAVDE------------VGV 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGPSVFREYWDkPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVA 501
Cdd:PRK07529 420 LCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 502 VIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARG-VLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07529 498 AVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDhIAERAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
54-567 |
8.62e-58 |
|
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: 200.60 E-value: 8.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 54 GDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAA---RLRARGVG--PGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 134 LEYFIQDSRSSLVVVGQEYLERLSplaqrLGVPLLPLTPAIYRGATEKPTEQPVKesgwrDRGAMIFYTSGTTGRPKGAL 213
Cdd:cd12116 76 LRYILEDAEPALVLTDDALPDRLP-----AGLPVLLLALAAAAAAPAAPRTPVSP-----DDLAYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 214 STHRNLAAVVTGLVHSWAWTKNDVILHVLP-------LhhvhgvvnKLLCPLWVGATCVMLPEFSAQQVwEKFLSS-EAP 285
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAVTTyafdislL--------ELLLPLLAGARVVIAPRETQRDP-EALARLiEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 286 QITVFMAVPTVYSKLLDyydkhfTQPRVQDFVRAVCkerirlmvsGSAALPVPLLEKWRSATGhTLLERYGMTEIGM-AL 364
Cdd:cd12116 217 SITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 365 SNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd12116 281 AARVTAAAGPIPIGRPLANTQVYVL----------------DAALRPVPPGV---PGELYIGGDGVAQGYLGRPALTAER 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FTSDG-------WFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTwGQRVTA 516
Cdd:cd12116 342 FVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVA 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 517 VVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12116 420 YVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-571 |
5.75e-57 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 200.28 E-value: 5.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHH------TYRELYDRSLCLAQEICRLqGCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK13295 39 DKTAVTAVRLGTgaprrfTYRELAALVDRVAVGLARL-GVGRGDV----VSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYleR---LSPLAQRLGvPLLPLTPAIY--RGATEKPTEQPVKESGW----------- 192
Cdd:PRK13295 114 FRERELSFMLKHAESKVLVVPKTF--RgfdHAAMARRLR-PELPALRHVVvvGGDGADSFEALLITPAWeqepdapaila 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 193 RDRG-----AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMl 267
Cdd:PRK13295 191 RLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVL- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 pefsaQQVWEKFLSSEAPQ---ITVFMAvptvysklldyydkhfTQPRVQDFVRAVcKER------IRLMVSGSAALPVP 338
Cdd:PRK13295 270 -----QDIWDPARAAELIRtegVTFTMA----------------STPFLTDLTRAV-KESgrpvssLRTFLCAGAPIPGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 339 LLEKWRSATGHTLLERYGMTEIGMALSNPLTEA--RVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGf 416
Cdd:PRK13295 328 LVERARAALGAKIVSAWGMTENGAVTLTKLDDPdeRASTTDGCPLPGVEVRVVDAD----------------GAPLPAG- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 eeKEGELLVRGPSVFREYWDKPEETKSAFtsDGWFRTGDTAvFKDARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAH 494
Cdd:PRK13295 391 --QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLA-RIDADGYIRisGRSK-DVIIRGGENIPVVEIEALLYRH 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 495 PSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEW--ARGVLAPYaVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK13295 465 PAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkAQKVAKQY-IPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
67-567 |
1.03e-56 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 196.90 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:TIGR01923 1 TWQDLDCEAAHLAKAL-KAQGIRSGS----RVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLERLSplaqrlgvpllpLTPAIYRGATEKPTEQPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:TIGR01923 76 LTDSLLEEKDF------------QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSaqQVWEKFLSSEapqITVFMAVPTVYSKLLDyydk 306
Cdd:TIGR01923 144 KENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLEMIANER---VTHISLVPTQLNRLLD---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 307 hftqprvqdfvRAVCKERIRLMVSGSAALPVPLLEKWRSaTGHTLLERYGMTEIG---MALSNPLTEARvpGSVGTPLPG 383
Cdd:TIGR01923 214 -----------EGGHNENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvTTATPEMLHAR--PDVGRPLAG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 384 VEVRIISENpqkgspyiihaegnergtkvtpgfEEKEGELLVRGPSVFREYWDkPEETKSAFTSDGWFRTGDTAVFK-DA 462
Cdd:TIGR01923 280 REIKIKVDN------------------------KEGHGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDgEG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 463 RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEghSLSHRDLKEWARGVLAPY 542
Cdd:TIGR01923 335 FLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 1195733688 543 AVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
50-567 |
2.48e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 198.46 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSR-RGVGFGD----RVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGqeylERLSPLAQ--RLGVPLLPlTPAIYRGATEKPT---EQPVKESGW--------RDRG 196
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTE----AALAPVATavRDIVPLLS-TVVVAGGSSDDSVlgyEDLLAEAGPahapvdipNDSP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAA-VVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLP--EFSAQ 273
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 274 QVWEKFlssEAPQITVFMAVPTVYSKLLDyydKHFTQPRvqdfvravcKERIRLMVSGSAALPVPLLEKWrSAT--GHTL 351
Cdd:PRK07786 256 QLLDVL---EAEKVTGIFLVPAQWQAVCA---EQQARPR---------DLALRVLSWGAAPASDTLLRQM-AATfpEAQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 352 LERYGMTEIgmalsNPLT-------EARVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGfeeKEGELL 424
Cdd:PRK07786 320 LAAFGQTEM-----SPVTcmllgedAIRKLGSVGKVIPTVAARVVDENMND----------------VPVG---EVGEIV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:PRK07786 376 YRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYvWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVI 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 504 GVPDMTWGQRVTAVVALQ-EGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07786 454 GRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
91-575 |
5.29e-56 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 197.42 E-value: 5.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 91 GDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQleyfiQDSRSSLVVVGQEYLERLSPLAQRLG-VPLLP 169
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE-----QRVRSQAAGARVVLIDADGPHDRAEPtTRWWP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 170 L-------------TPAIYRGATEKPTEQPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND 236
Cdd:PRK05852 139 LtvnvggdsgpsggTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 237 VILHVLPLHHVHGVVNKLLCPLWVGATcVMLP---EFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDyydkhftQPRV 313
Cdd:PRK05852 219 ATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAVGA---TWYTAVPTIHQILLE-------RAAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 314 QDFVRAvcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIgmalSNPLTEARVPGSVGTPLPGVEVRIISenp 393
Cdd:PRK05852 288 EPSGRK--PAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTTQIEGIGQTENPVVSTGLVG--- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 394 QKGSPYIIHAEGNerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDT-AVFKDARYWIRGRTSv 472
Cdd:PRK05852 359 RSTGAQIRIVGSD--GLPLPAG---AVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 473 DIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLE 552
Cdd:PRK05852 432 ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEAS 511
|
490 500
....*....|....*....|...
gi 1195733688 553 EIPRNQMGKVNKKELLTQLYPSG 575
Cdd:PRK05852 512 GLPHTAKGSLDRRAVAEQFGHSV 534
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
32-571 |
1.02e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.57 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 32 LPTAPE-AHTDGSVPVFIRALAF--GDRIAlIDKYGHH-TYRELYDRSLCLAqEICRLQGCKVGDlqeeRVSFLCSNDIS 107
Cdd:PRK06178 22 IPREPEyPHGERPLTEYLRAWARerPQRPA-IIFYGHViTYAELDELSDRFA-ALLRQRGVGAGD----RVAVFLPNCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 108 YVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVgqeyLERLSPLAQRL-------------------GVPLL 168
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA----LDQLAPVVEQVraetslrhvivtsladvlpAEPTL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 169 PLtPAIYRGATEKP-------------TEQPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNL---AAVVTGLVHswAW 232
Cdd:PRK06178 172 PL-PDSLRAPRLAAagaidllpalracTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMvytAAAAYAVAV--VG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 233 TKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQqvwekflsseapqiTVFMAVP----TVYSKLLDYYDKHF 308
Cdd:PRK06178 249 GEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAV--------------AFMAAVEryrvTRTVMLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 309 TQPRVQDF-------VRAVckerirlmvSGSAALPVPLLEKWRSATGHTLLE-RYGMTEIGMalSNPLTEA--------- 371
Cdd:PRK06178 315 DHPRFAEYdlsslrqVRVV---------SFVKKLNPDYRQRWRALTGSVLAEaAWGMTETHT--CDTFTAGfqdddfdll 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 372 RVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWF 451
Cdd:PRK06178 384 SQPVFVGLPVPGTEFKICDF---------------ETGELLPLG---AEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 452 RTGDTAVFKDA---RYWIRGRtsvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH 528
Cdd:PRK06178 445 HTGDIGKIDEQgflHYLGRRK---EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA 521
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1195733688 529 RDLKEWARGVLAPYAVPsELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK06178 522 AALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALA 563
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
65-503 |
1.82e-55 |
|
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: 194.20 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 65 HHTYRELYDRSLCLAQ--EICRLQgckVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSR 142
Cdd:cd05914 7 PLTYKDLADNIAKFALllKINGVG---TGD----RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 143 SSLVVVGQEylerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:cd05914 80 AKAIFVSDE------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 223 VTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAqqvwEKFLSSEAPQITVFMAVPTVYsKLLD 302
Cdd:cd05914 118 VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS----AKIIALAFAQVTPTLGVPVPL-VIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 303 YYdKHFTQPRV---------------QDFVRAVCKE-------RIRLMVSGSAALPVPLLEKWRSAtGHTLLERYGMTEI 360
Cdd:cd05914 193 IF-KMDIIPKLtlkkfkfklakkinnRKIRKLAFKKvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTET 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 GMALS-NPLTEARVpGSVGTPLPGVEVRIISENPQKGspyiihaegnergtkvtpgfeekEGELLVRGPSVFREYWDKPE 439
Cdd:cd05914 271 APIISySPPNRIRL-GSAGKVIDGVEVRIDSPDPATG-----------------------EGEIIVRGPNVMKGYYKNPE 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 440 ETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:cd05914 327 ATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV 391
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
49-567 |
1.97e-55 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 196.13 E-value: 1.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYV-VAQWASWMsGGVAVPLYW 127
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHAL-AAAGVKRGD----RVALMCGNRIEFLdVFLGCAWL-GAIAVPINT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQR---------LGVPLLPLTPAIYRGATEKPTEQPVKESGWR--DRG 196
Cdd:PRK06155 104 ALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdlplpavwlLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQpgDTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AmIFYTSGTTGRPKGALSTH-------RNLAAVVtGLvhswawTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPE 269
Cdd:PRK06155 184 A-ILYTSGTTGPSKGVCCPHaqfywwgRNSAEDL-EI------GADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 FSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDyydkhfTQPRVQDFVRAVckeRIRLMVSGSAALPVPLLEKwrsaTGH 349
Cdd:PRK06155 255 FSASGFWPAVRRHGA---TVTYLLGAMVSILLS------QPARESDRAHRV---RVALGPGVPAALHAAFRER----FGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 TLLERYGMTEIGMALSNPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRG-- 427
Cdd:PRK06155 319 DLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVVDEH----------------DQELPDG---EPGELLLRAde 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 428 PSVFRE-YWDKPEETKSAFtSDGWFRTGDTaVFKDARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:PRK06155 379 PFAFATgYFGMPEKTVEAW-RNLWFHTGDR-VVRDADGWFRfvDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 505 VPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
67-502 |
2.08e-54 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 189.78 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGD----RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKEsgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGP----DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPEfSAQQVWEKFLSS--EAPQITVFMAVPTVYSKLLDyy 304
Cdd:TIGR01733 153 ARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAALLAAliAEHPVTVLNLTPSLLALLAA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 305 dkhftqprvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE--IG-MALSNPLTEARVPGSV--G 378
Cdd:TIGR01733 229 ------------ALPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTEttVWsTATLVDPDDAPRESPVpiG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 379 TPLPGVEVriisenpqkgspYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDG--------W 450
Cdd:TIGR01733 297 RPLANTRL------------YVLDDDLRPVPVGVV-------GELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 451 FRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAV 502
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLeFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
50-567 |
3.60e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 192.83 E-value: 3.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLAL-GVRAGD----GVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVpllpltpaiYRGATEKPTEQPVKESGWRD--------------- 194
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGR---------LRAWGGNPDDDEPSGSTDETlddliagsstaplpk 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 195 ---RGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFS 271
Cdd:PRK07788 205 ppkPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 272 AQQVWEkflSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPRVQdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHTL 351
Cdd:PRK07788 284 PEATLE---DIAKHKATALVVVPVMLSRILDLGPEVLAKYDTS---------SLKIIFVSGSALSPELATRALEAFGPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 352 LERYGMTEIGMA-LSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSV 430
Cdd:PRK07788 352 YNLYGSTEVAFAtIATPEDLAEAPGTVGRPPKGVTVKILDEN----------------GNEVPRG---VVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 431 FREYWDkpeeTKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:PRK07788 413 FEGYTD----GRDKQIIDGLLSSGDVGYFDEDGLLfVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEE 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 510 WGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07788 488 FGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
66-567 |
9.03e-54 |
|
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: 189.25 E-value: 9.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 66 HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSL 145
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGD----RVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 146 VVVGQEYLERLSPlaqrlgvpllpltpaiyrgatEKPTeqpvkesgwrdrgaMIFYTSGTTGRPKGALSTHRNLAAVVTG 225
Cdd:cd05969 76 LITTEELYERTDP---------------------EDPT--------------LLHYTSGTTGTPKGVLHVHDAMIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 226 LVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQQvWEKFLSSEapQITVFMAVPTVYSKLLDYY 304
Cdd:cd05969 121 GKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERV--KVTVWYTAPTAIRMLMKEG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 305 DkhftqprvqDFVRAVCKERIRLMVSGSAALPvPLLEKW-RSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLP 382
Cdd:cd05969 198 D---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 383 GVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAFTsDGWFRTGDTAvFK 460
Cdd:cd05969 268 GVKAAVVDEN----------------GNELPPG---TKGILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLA-YR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 461 DAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWA 535
Cdd:cd05969 327 DEDgyFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFV 405
|
490 500 510
....*....|....*....|....*....|..
gi 1195733688 536 RGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-567 |
1.52e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 183.45 E-value: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 -EFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyydkhfTQPRVQDFvravckERIRLMVSGSAALPVPLLEKWRSAT 347
Cdd:cd05944 82 nPGLFDNFWKLV---ERYRITSLSTVPTVYAALL-------QVPVNADI------SSLRFAMSGAAPLPVELRARFEDAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 348 GHTLLERYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISENPQkgSPYIIHAEGNErgtkvtpgfeekEGELLVR 426
Cdd:cd05944 146 GLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGV--GRLLRDCAPDE------------VGEICVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 427 GPSVFREYWDKpEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV 505
Cdd:cd05944 212 GPGVFGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 506 PDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPY-AVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05944 290 PDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
195-567 |
2.52e-52 |
|
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: 181.76 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 195 RGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAqq 274
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 275 vwekFLSSEAPQITVFMA-VPTVYSKLLDYydkHFTQPRVqdfvravckERIRLMVSGSAALPVPLLEKWrSATGHTLLE 353
Cdd:cd17630 78 ----LAEDLAPPGVTHVSlVPTQLQRLLDS---GQGPAAL---------KSLRAVLLGGAPIPPELLERA-ADRGIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIG--MALSNPLTEARvpGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELLVRGPSVF 431
Cdd:cd17630 141 TYGMTETAsqVATKRPDGFGR--GGVGVLLPGRELRI-----------------------------VEDGEIWVGGASLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 REYWDKPEEtkSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTW 510
Cdd:cd17630 190 MGYLRGQLV--PEFNEDGWFTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEEL 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 511 GQRVTAVVALQEGHSLShrDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17630 267 GQRPVAVIVGRGPADPA--ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
65-577 |
2.97e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 186.65 E-value: 2.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 65 HHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSS 144
Cdd:PRK08276 11 VVTYGELEARSNRLAHGL-RALGLREGD----VVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYLERLSPLAQRL--GVPLLPL---TPAIYRGATEKPTEQPVKESGWRDRGAMIFYTSGTTGRPKG---ALSTH 216
Cdd:PRK08276 86 VLIVSAALADTAAELAAELpaGVPLLLVvagPVPGFRSYEEALAAQPDTPIADETAGADMLYSSGTTGRPKGikrPLPGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 217 RNLAA--VVTGLVHSWAWTKND-VILHVLPLHHV-----HGVVNKLlcplwvGATCVMLPEFSAqqvwEKFLSS-EAPQI 287
Cdd:PRK08276 166 DPDEApgMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDA----EEALALiERYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 288 TVFMAVPTVYSKLLdyydkhftqpRVQDFVRAvckeR-----IRLMVSGSAALPVP----LLEKWrsatGHTLLERYGMT 358
Cdd:PRK08276 236 THSQLVPTMFVRML----------KLPEEVRA----RydvssLRVAIHAAAPCPVEvkraMIDWW----GPIIHEYYASS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 359 E-IGMALSNPLTEARVPGSVGTPLPGvEVRIISENpqkgspyiihaeGNErgtkVTPGfeeKEGELLVRGPSVFREYWDK 437
Cdd:PRK08276 298 EgGGVTVITSEDWLAHPGSVGKAVLG-EVRILDED------------GNE----LPPG---EIGTVYFEMDGYPFEYHND 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 438 PEETKSAFTSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA 516
Cdd:PRK08276 358 PEKTAAARNPHGWVTVGDVGYLDEDGYlYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 517 VVALQEGHSLS---HRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLYPSGQR 577
Cdd:PRK08276 437 VVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQR 500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
55-567 |
3.78e-52 |
|
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: 184.76 E-value: 3.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAAL-ASLGLDAGD----PVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpaiyrgATEKPTeqpvkesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd05945 81 REILDAAKPALLI------------------------------ADGDDN-------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLH---HVHGvvnkLLCPLWVGATCVMLPEfsAQQVWEKFLSSEAPQ--ITV 289
Cdd:cd05945 118 SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD----LYPALASGATLVPVPR--DATADPKQLFRFLAEhgITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 290 FMAVPTVYSKLLdyYDKHFTQPRVqdfvravckERIRLMVSGSAALPVPLLEKWRSAT-GHTLLERYGMTEIGMALS--- 365
Cdd:cd05945 192 WVSTPSFAAMCL--LSPTFTPESL---------PSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTyie 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 ---NPLTEA-RVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEET 441
Cdd:cd05945 261 vtpEVLDGYdRLP--IGYAKPGAKLVIL----------------DEDGRPVPPG---EKGELVISGPSVSKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 442 KSAFTSD---GWFRTGDtAVFKDA--RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA 516
Cdd:cd05945 320 AAAFFPDegqRAYRTGD-LVRLEAdgLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIA 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 517 VVALQEGHSLSH-RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05945 398 FVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
44-567 |
1.51e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 185.64 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 44 VPVFIRALA-FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVA 122
Cdd:PRK08974 26 VDMFEQAVArYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGD----RVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 123 V---PLYwkHPEaQLEYFIQDSRSSLVVVGQEY---LERL-------SPLAQRLG---------------------VPLL 168
Cdd:PRK08974 102 VnvnPLY--TPR-ELEHQLNDSGAKAIVIVSNFahtLEKVvfktpvkHVILTRMGdqlstakgtlvnfvvkyikrlVPKY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 169 PLTPAI-YRGATEKPTE-QPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVtgLVHSWAW-----TKNDVILHV 241
Cdd:PRK08974 179 HLPDAIsFRSALHKGRRmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 242 LPLHHVHGV-VNKLLCpLWVGATCVM------LPEFSAQQVWEKFlsseapqiTVFMAVPTVYSKLLDyyDKHFTQprvQ 314
Cdd:PRK08974 257 LPLYHIFALtVNCLLF-IELGGQNLLitnprdIPGFVKELKKYPF--------TAITGVNTLFNALLN--NEEFQE---L 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 315 DFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISEnp 393
Cdd:PRK08974 323 DF------SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLVDD-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 394 qkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFkDARYWIR--GRTS 471
Cdd:PRK08974 395 ----------DGNE----VPPG---EPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVM-DEEGFLRivDRKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 472 vDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEgHSLSHRDLKEWARGVLAPYAVPSELLLL 551
Cdd:PRK08974 456 -DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFR 533
|
570
....*....|....*.
gi 1195733688 552 EEIPRNQMGKVNKKEL 567
Cdd:PRK08974 534 DELPKSNVGKILRREL 549
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
55-571 |
3.11e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 183.55 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGML-HARGIGQGDV----VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEY-----LER----LSPLAQ----RLGVPLLPLTPAiyrgATEKPTEQpvkesgwrdrgAMIFY 201
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFdaivaLETpkivIDAAAQadsrRLAQGGLEIPPQ----AAVAPTDL-----------VRLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEkflS 281
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA---A 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 282 SEAPQITVFMAVPTVYSKLL-----DYYDKhftqprvqdfvravckERIRLMVSGSAALPVPLLEKWRSA-TGHTLLERY 355
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLtvpdrDRFDL----------------DSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 GMTEI--GMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFRE 433
Cdd:PRK06145 298 GLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGA----------------GRWLPPN---MKGEICMRGPKVTKG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 434 YWDKPEETKSAFTsDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQR 513
Cdd:PRK06145 359 YWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGER 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 514 VTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK06145 438 ITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-567 |
3.93e-51 |
|
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: 181.86 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05971 8 TFKELKTASNRFANVLKEI-GLEKGD----RVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VvgqeylerlsplaqrlgvpllpltpaiyrgatekpTEQPvkesgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05971 83 V-----------------------------------TDGS-------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHS----------------WAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVwekFLSSEAPQITVF 290
Cdd:cd05971 121 QFPfnlfprdgdlywtpadWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTA---FLPPTALKMMRQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 MAVPTvysklldyydKHFtqprvqdfvravcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTE 370
Cdd:cd05971 198 QGEQL----------KHA-------------QVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 371 ARV-PGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPS--VFREYWDKPEETKSAFTS 447
Cdd:cd05971 255 FPIkPGSMGKPIPGHRVAIVDDN----------------GTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 448 DgWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSL 526
Cdd:cd05971 316 D-WLLTGDLGRKdSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1195733688 527 SH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05971 394 SDalaREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
34-580 |
2.79e-50 |
|
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: 187.37 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 34 TAPEAHTDGSVP--VFIRALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVA 111
Cdd:COG1020 468 TAAPYPADATLHelFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAH---HLRALGVG--PGDLVGVCLERSLEMVVA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 112 QWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLaqrlGVPLLPLTPAIYRGATEKPTEQPVKEsg 191
Cdd:COG1020 543 LLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPEL----GVPVLALDALALAAEPATNPPVPVTP-- 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFS 271
Cdd:COG1020 617 --DDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWE-IFGALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 272 AQ--QVWEKFLSSEapQITVFMAVPTVYSKLLDYYDKHFTQPRvqdfvravckeriRLMVSGSaALPVPLLEKWRSATGH 349
Cdd:COG1020 694 RRdpAALAELLARH--RVTVLNLTPSLLRALLDAAPEALPSLR-------------LVLVGGE-ALPPELVRRWRARLPG 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 T-LLERYGMTE------IGMALSNPLTEARVPgsVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGE 422
Cdd:COG1020 758 ArLVNLYGPTEttvdstYYEVTPPDADGGSVP--IGRPIANTRVYVL----------------DAHLQPVPVGV---PGE 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGPSVFREYWDKPEETKSAFTSDG-------WFRTGDTavfkdARYW----------------IRG-RtsvdiIKTG 478
Cdd:COG1020 817 LYIGGAGLARGYLNRPELTAERFVADPfgfpgarLYRTGDL-----ARWLpdgnleflgraddqvkIRGfR-----IELG 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 479 gykvsalEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQ 558
Cdd:COG1020 887 -------EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959
|
570 580
....*....|....*....|..
gi 1195733688 559 MGKVNKKELLTQLYPSGQRSQP 580
Cdd:COG1020 960 NGKLDRLALPAPAAAAAAAAAA 981
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
52-564 |
2.10e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 179.97 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 52 AFGDRIALIdkYGHH----TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK12583 30 RFPDREALV--VRHQalryTWRQLADAVDRLARGLLAL-GVQPGD----RVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQRLGV--------PLLP-LTPAIYRGATEKP----------- 182
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEgqpgalacERLPeLRGVVSLAPAPPPgflawhelqar 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 183 ----TEQPVKE---SGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLL 255
Cdd:PRK12583 183 getvSREALAErqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 256 CPLWVGAtCVMLP--EFSAQQVWEkflSSEAPQITVFMAVPTVYSKLLDYydkhftqPRVQDFVRAvckeRIRLMVSGSA 333
Cdd:PRK12583 263 GCMTVGA-CLVYPneAFDPLATLQ---AVEEERCTALYGVPTMFIAELDH-------PQRGNFDLS----SLRTGIMAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 334 ALPVPLLEKwrsatghtLLERYGMTEI----GMALSNPLT---------EARVPgSVGTPLPGVEVRiisenpqkgspyI 400
Cdd:PRK12583 328 PCPIEVMRR--------VMDEMHMAEVqiayGMTETSPVSlqttaaddlERRVE-TVGRTQPHLEVK------------V 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 401 IHAEGNergtKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRtSVDIIKTGG 479
Cdd:PRK12583 387 VDPDGA----TVPRG---EIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVrIVGR-SKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 480 YKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQM 559
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVT 538
|
....*
gi 1195733688 560 GKVNK 564
Cdd:PRK12583 539 GKVQK 543
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
55-567 |
3.11e-49 |
|
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: 178.44 E-value: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRLqGCKVGdlqeERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGL-GLARG----ERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLERLSPlaqrlGVPLLP-LTPAIYRGATEKPTEQPVKESG--WR----------------DR 195
Cdd:TIGR03098 90 AHILADCNVRLLVTSSERLDLLHP-----ALPGCHdLRTLIIVGDPAHASEGHPGEEPasWPkllalgdadpphpvidSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 196 GAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSAQQV 275
Cdd:TIGR03098 165 MAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLPRDV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEkflSSEAPQITVFMAVPTVYSKL--LDYYDKHFtqprvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGHT-LL 352
Cdd:TIGR03098 244 LK---ALEKHGITGLAAVPPLWAQLaqLDWPESAA--------------PSLRYLTNSGGAMPRATLSRLRSFLPNArLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 353 ERYGMTEIGMALSNPLTEA-RVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVF 431
Cdd:TIGR03098 307 LMYGLTEAFRSTYLPPEEVdRRPDSIGKAIPNAEVLVL----------------REDGSECAPG---EEGELVHRGALVA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 REYWDKPEETKSAFTSDGWFRTG----DTAVFKDARYW--------IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIAD 499
Cdd:TIGR03098 368 MGYWNDPEKTAERFRPLPPFPGElhlpELAVWSGDTVRrdeegflyFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLVAE 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:TIGR03098 447 AVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-561 |
4.63e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 178.54 E-value: 4.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 52 AFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPE 131
Cdd:PRK07798 15 AVPDRVALVCGDRRLTYAELEERANRLAHYL-IAQGLGPGD----HVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 132 AQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL-------------GVPLLPLTPAIYRGATEKPTEQPVKESGWRDRgaM 198
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREFAPRVAEVLPRLpklrtlvvvedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDL--Y 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTHRNL-------AAVVTG--------LVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGAT 263
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGepiedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAA-LFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 264 CVMLP--EFSAQQVWEkflSSEAPQITVFMAVPTVYSK-LLDYYDkhftQPRVQDFvravckERIRLMVSGSAALPVPLL 340
Cdd:PRK07798 247 VVLLPdvRFDADEVWR---TIEREKVNVITIVGDAMARpLLDALE----ARGPYDL------SSLFAIASGGALFSPSVK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 341 EKWRSATGH-TLLERYGMTEIG-MALSnplTEARVPGSVGTPL--PGVEVRIISENpqkgspyiihaegnerGTKVTPGf 416
Cdd:PRK07798 314 EALLELLPNvVLTDSIGSSETGfGGSG---TVAKGAVHTGGPRftIGPRTVVLDED----------------GNPVEPG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 EEKEGeLLVRGPSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSVdIIKTGGYKVSALEIERHLL 492
Cdd:PRK07798 374 SGEIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRArVEADGTITLLGRGSV-CINTGGEKVFPEEVEEALK 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 493 AHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGK 561
Cdd:PRK07798 452 AHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
67-567 |
4.78e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 178.80 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAV---PLYwkhPEAQLEYFIQDSRS 143
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGD----RIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY---TAREMEHQFNDSGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 144 SLVVV-------GQEYLER--------------LSPLAQRL----------GVPLLPLTPAI-YRGATEKPTEQPVKE-S 190
Cdd:PRK05677 124 KALVClanmahlAEKVLPKtgvkhvivtevadmLPPLKRLLinavvkhvkkMVPAYHLPQAVkFNDALAKGAGQPVTEaN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 GWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVT---GLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML 267
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqcrALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 PEFSAQQVWEKFLSSEapQITVFMAVPTVYSKLLDyyDKHFtqpRVQDFvravckERIRLMVSGSAALPVPLLEKWRSAT 347
Cdd:PRK05677 284 SNPRDLPAMVKELGKW--KFSGFVGLNTLFVALCN--NEAF---RKLDF------SALKLTLSGGMALQLATAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 348 GHTLLERYGMTEIG-MALSNPLtEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVR 426
Cdd:PRK05677 351 GCAICEGYGMTETSpVVSVNPS-QAIQVGTIGIPVPSTLCKVIDD------------DGNE----LPLG---EVGELCVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 427 GPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV 505
Cdd:PRK05677 411 GPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMrIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGV 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 506 PDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK05677 490 PDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
50-567 |
1.01e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 172.30 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGH--HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAV---P 124
Cdd:PRK08315 26 AARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLAL-GIEKGD----RVGIWAPNVPEWVLTQFATAKIGAILVtinP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 125 LYWKHpeaQLEYFIQDSRSSLVVV-----GQEYLERLSPLA--------QRLGVPLLP-LTPAIYRGATEKPTEQPVKEs 190
Cdd:PRK08315 101 AYRLS---ELEYALNQSGCKALIAadgfkDSDYVAMLYELApelatcepGQLQSARLPeLRRVIFLGDEKHPGMLNFDE- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 gWRDRGAM--------------------IFYTSGTTGRPKGALSTHRNL---AAVVTGLVHswaWTKNDVILHVLPLHHV 247
Cdd:PRK08315 177 -LLALGRAvddaelaarqatldpddpinIQYTSGTTGFPKGATLTHRNIlnnGYFIGEAMK---LTEEDRLCIPVPLYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 248 HGVVNKLLCPLWVGATCV-MLPEFSAQQVWEkflSSEAPQITVFMAVPTVYSKLLDyydkhftQPRVQDF----VR---- 318
Cdd:PRK08315 253 FGMVLGNLACVTHGATMVyPGEGFDPLATLA---AVEEERCTALYGVPTMFIAELD-------HPDFARFdlssLRtgim 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 319 --AVCkerirlmvsgsaalPVPLLEKwrsatghtLLERYGMTEI----GMALSNPLT---------EARVpGSVGTPLPG 383
Cdd:PRK08315 323 agSPC--------------PIEVMKR--------VIDKMHMSEVtiayGMTETSPVStqtrtddplEKRV-TTVGRALPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 384 VEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDAR 463
Cdd:PRK08315 380 LEVKIVDP---------------ETGETVPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 464 YW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPY 542
Cdd:PRK08315 442 YVnIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHY 520
|
570 580
....*....|....*....|....*
gi 1195733688 543 AVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK08315 521 KIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
185-567 |
4.48e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 170.77 E-value: 4.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 185 QPVKESgwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND----------VILHVLPLHHVHGVVNKL 254
Cdd:PRK12492 200 KPVPVG--LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFTANC 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 255 LCPLWVGATCVML------PEFSAQ-QVWekflsseapQITVFMAVPTVYSKLLDYydkhfTQPRVQDFvravckERIRL 327
Cdd:PRK12492 278 MCMMVSGNHNVLItnprdiPGFIKElGKW---------RFSALLGLNTLFVALMDH-----PGFKDLDF------SALKL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 328 MVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGN 406
Cdd:PRK12492 338 TNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDD------------DGN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 407 ERGtkvtpgFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSAL 485
Cdd:PRK12492 406 ELP------LGER-GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKK-DLIIVSGFNVYPN 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 486 EIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGhSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKK 565
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556
|
..
gi 1195733688 566 EL 567
Cdd:PRK12492 557 EL 558
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
55-567 |
1.09e-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: 167.10 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLAR---TLRAEGVG--PGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpaiyrgatekpteQPvkesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17643 77 AFILADSGPSLLLT------------------------------------DP-------DDLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVilhVLPLHH---------VHGvvnkllcPLWVGATCVMLPEFSAQQVWEKFLSSEAP 285
Cdd:cd17643 114 SHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPYEVARSPEDFARLLRDE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 286 QITVFMAVPTVYSKLLDYYDKHFTQPrvqdfvravckERIRLMVSGSAALPVPLLEKWRSATGH---TLLERYGMTEIGM 362
Cdd:cd17643 184 GVTVLNQTPSAFYQLVEAADRDGRDP-----------LALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 363 ALS-NPLTEARVPGS----VGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDK 437
Cdd:cd17643 253 HVTfRPLDAADLPAAaaspIGRPLPGLRVYVLDAD----------------GRPVPPG---VVGELYVSGAGVARGYLGR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 438 PEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:cd17643 314 PELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEP 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 510 WGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17643 393 GDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
49-567 |
3.83e-45 |
|
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: 166.61 E-value: 3.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLAR---RLRAAGVG--PGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVgqeylerLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESgwrDRGAMIFYTSGTTGR 208
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLT-------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSP---DDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNlaavVTGLVHSWAW---TKNDVILHVLPL------HHVHGvvnkllcPLWVGATCVMLPE---FSAQQVw 276
Cdd:cd12117 151 PKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPKgtlLDPDAL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 EKFLssEAPQITVFMAVPTVYSKLLDyydkhftqprvqdfVRAVCKERIRLMVSGSAALPVPLLEKWRSATGH-TLLERY 355
Cdd:cd12117 219 GALI--AEEGVTVLWLTAALFNQLAD--------------EDPECFAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 GMTE-IGMALSNPLTE-ARVPGSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVF 431
Cdd:cd12117 283 GPTEnTTFTTSHVVTElDEVAGSIpiGRPIANTRVYVL----------------DEDGRPVPPG---VPGELYVGGDGLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 REYWDKPEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:cd12117 344 LGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 505 VPDMTWGQRVTA-VVAlqeGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12117 423 REDAGGDKRLVAyVVA---EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
46-571 |
6.05e-45 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 167.08 E-value: 6.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 46 VFIRALAFGDRIALID-KYGH-HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGV-- 121
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADVELLSRRVAAGLHKL-GIRQGD----VVMLLLPNCPEFVLAFLGASRRGAVtt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 122 -AVPLYwkhPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPL--TPAIYRGATE----KPTEQPVKESGWRD 194
Cdd:PLN02246 104 tANPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIddPPEGCLHFSEltqaDENELPEVEISPDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 195 RGAMIfYTSGTTGRPKGALSTHRNL----AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:PLN02246 181 VVALP-YSSGTTGLPKGVMLTHKGLvtsvAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 SAQQVWEKFlssEAPQITVFMAVPTVY-----SKLLDYYDKhftqprvqdfvravckERIRLMVSGSAALPVPLLEKWRS 345
Cdd:PLN02246 260 EIGALLELI---QRHKVTIAPFVPPIVlaiakSPVVEKYDL----------------SSIRMVLSGAAPLGKELEDAFRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 346 A-TGHTLLERYGMTEIGMALSNPLTEARVP-----GSVGTPLPGVEVRIIseNPQKGS--PYiihaegnergtkvtpgfe 417
Cdd:PLN02246 321 KlPNAVLGQGYGMTEAGPVLAMCLAFAKEPfpvksGSCGTVVRNAELKIV--DPETGAslPR------------------ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 418 EKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPS 496
Cdd:PLN02246 381 NQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGyIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPS 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 497 IADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PLN02246 460 IADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
67-567 |
7.76e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 167.28 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVvaQW--ASWMSGGVAVPL-Y-WKHPEAQLEyfIQDSR 142
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRL-GLRNGD----VVAIAALNSDLYL--EWllAVACAGGIVAPLnYrWSFEEAKSA--MLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 143 SSLVVVGQE----YLE----RLSPLaqRLGVPLLPLTPAIYRGATEKPTEQPVKESG---------WR-DRGAMIFYTSG 204
Cdd:PLN02860 105 PVMLVTDETcsswYEElqndRLPSL--MWQVFLESPSSSVFIFLNSFLTTEMLKQRAlgtteldyaWApDDAVLICFTSG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 205 TTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWEKFlssEA 284
Cdd:PLN02860 183 TTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLPKFDAKAALQAI---KQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 285 PQITVFMAVPTVYSKLLDYYDKHFTQPrvqdfvravCKERIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGMA 363
Cdd:PLN02860 259 HNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACSS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 364 LS-NPLTEARVPGSVGTPLPGVEVRIISENPQKGS------PyiiHAEgnergTKVTPGFEEKEGELLVRGPSVFREYWD 436
Cdd:PLN02860 330 LTfMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVcvgkpaP---HVE-----LKIGLDESSRVGRILTRGPHVMLGYWG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 437 KPEETKSAFTSDGWFRTGDTAVFKDA-RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVT 515
Cdd:PLN02860 402 QNSETASVLSNDGWLDTGDIGWIDKAgNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 516 AVVALQEG--------------HSLSHRDLKEWARGV-LAPYAVPSELLLLEE-IPRNQMGKVNKKEL 567
Cdd:PLN02860 481 ACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEV 548
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
197-567 |
1.31e-44 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 166.59 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGlVHSWAWTKN------DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGGCNHLISNP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 SAQQVWEKFLssEAPQITVFMAVPTVYSKLLDyyDKHFTQprvQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHT 350
Cdd:PRK08751 290 RDMPGFVKEL--KKTRFTAFTGVNTLFNGLLN--TPGFDQ---IDF------SSLKMTLGGGMAVQRSVAERWKQVTGLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 351 LLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPS 429
Cdd:PRK08751 357 LVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDA----------------GTVLAIG---EIGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 430 VFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 509 TWGQrVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK08751 497 KSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
55-567 |
1.66e-44 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 165.70 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCkvgdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQALPIG-----EPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLERLS------PLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESGwrDRGAMIFYTSGTTGR 208
Cdd:PRK13382 133 AEVVTREGVDTVIYDEEFSATVDraladcPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTG--RKGRVILLTSGTTGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQIT 288
Cdd:PRK13382 211 PKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLDLIDRHRATGLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VfmaVPTVYSKLLDYYDKHFTQ--PRVQDFVRAvckerirlmvSGSAaLPVPLLEKWRSATGHTLLERYGMTEIGM-ALS 365
Cdd:PRK13382 290 V---VPVMFDRIMDLPAEVRNRysGRSLRFAAA----------SGSR-MRPDVVIAFMDQFGDVIYNNYNATEAGMiATA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYwdKPEETKSaf 445
Cdd:PRK13382 356 TPADLRAAPDTAGRPAEGTEIRILDQ------------DFRE----VPTG---EVGTIFVRNDTQFDGY--TSGSTKD-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 446 TSDGWFRTGDTAVFKDA-RYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH 524
Cdd:PRK13382 413 FHDGFMASGDVGYLDENgRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1195733688 525 SLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK13382 492 SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
91-568 |
2.05e-44 |
|
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: 163.77 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 91 GDLQEERVSFLCSNDISYVVAQWASWMSGG----VAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLsplaqRLGVP 166
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL-----RDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 167 LLPLTPAIYRG----ATEKPTEQPVKEsgwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVL 242
Cdd:cd05922 89 ASPDPGTVLDAdgirAARASAPAHEVS---HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 243 PLHHVHGVvNKLLCPLWVGATCVMLPEFS-AQQVWEKFLSSeapQITVFMAVPTVYSKLLDYYDKHFTQPRvqdfvravc 321
Cdd:cd05922 166 PLSYDYGL-SVLNTHLLRGATLVLTNDGVlDDAFWEDLREH---GATGLAGVPSTYAMLTRLGFDPAKLPS--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 322 kerIRLMVSGSAALPVPLLEKWRSA-TGHTLLERYGMTEI--GMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgsp 398
Cdd:cd05922 233 ---LRYLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEIL--------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 399 yiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKT 477
Cdd:cd05922 301 -------DDDGTPTPPG---EPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRD-RMIKL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 478 GGYKVSALEIERHLLAHPSIADVAVIGVPDmTWGQRVTAVVALQEGHSLShrDLKEWARGVLAPYAVPSELLLLEEIPRN 557
Cdd:cd05922 370 FGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLT 446
|
490
....*....|.
gi 1195733688 558 QMGKVNKKELL 568
Cdd:cd05922 447 ASGKVDYAALR 457
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
49-567 |
2.11e-44 |
|
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: 164.76 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLL-RARGVGPED----RVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAqrlGVPLLPltPAIYRGATEKPTEQPVKesgwRDRGAMIFYTSGTTGR 208
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAGG---DVALLG--DEALAAPPATPPLVPPR----PDNLAYVIYTSGSTGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhhvhGV---VNKLLCPLWVGATCVML-------PEFSAQQVWEK 278
Cdd:cd17646 153 PKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 279 flsseapQITVFMAVPTVYSKLLDyydkhftQPRVQDFVravckeRIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMT 358
Cdd:cd17646 229 -------GVTTCHFVPSMLRVFLA-------EPAAGSCA------SLRRVFCSGEALPPELAARFLALPGAELHNLYGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 359 EIGMALSNPLTEARVPG---SVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYW 435
Cdd:cd17646 289 EAAIDVTHWPVRGPAETpsvPIGRPVPNTRLYVL----------------DDALRPVPVGV---PGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 436 DKPEETKSAFTSDgWF-------RTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPD 507
Cdd:cd17646 350 GRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 508 MTWGQRVTAVVALQEGHS-LSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17646 428 PAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
87-567 |
2.21e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 164.87 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 87 GCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSlVVVGQEYLerLSPLAQRL--G 164
Cdd:PRK12406 32 GVRPGDC----VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR-VLIAHADL--LHGLASALpaG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 165 VPLL--PLTPAI---YR----------GA--------TEKPTEQPVKESgwrdRGAMIfYTSGTTGRPKG---ALSTHRN 218
Cdd:PRK12406 105 VTVLsvPTPPEIaaaYRispalltppaGAidwegwlaQQEPYDGPPVPQ----PQSMI-YTSGTTGHPKGvrrAAPTPEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 219 LAAVVTGLVHSWAWTKNDVILHVLPLHH----VHGvvnklLCPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAV 293
Cdd:PRK12406 180 AAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYG-----LRAGRLGGVLVLQPRFDP----EELLQLiERHRITHMHMV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 294 PTVYSKLLDYYDKhftqprvqdfVRAVCK-ERIRLMVSGSAALPVP----LLEKWrsatGHTLLERYGMTEIG-MALSNP 367
Cdd:PRK12406 251 PTMFIRLLKLPEE----------VRAKYDvSSLRHVIHAAAPCPADvkraMIEWW----GPVIYEYYGSTESGaVTFATS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 368 LTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSV--FrEYWDKPEEtKSAF 445
Cdd:PRK12406 317 EDALSHPGTVGKAAPGAELRFVDED----------------GRPLPQG---EIGEIYSRIAGNpdF-TYHNKPEK-RAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 446 TSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGH 524
Cdd:PRK12406 376 DRGGFITSGDVGYLdADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1195733688 525 SLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12406 455 TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
53-567 |
6.39e-44 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 164.42 E-value: 6.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 53 FGDRIALIDKYGHHTYRELYDRSLCLAqeiCRLQ--GCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAV---PLYW 127
Cdd:PRK07059 36 YADRPAFICMGKAITYGELDELSRALA---AWLQsrGLAKGA----RVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHpeaQLEYFIQDSRSSLVVVgqeyLERLSPLAQR------------------LG----------------VPL--LP-- 169
Cdd:PRK07059 109 PR---ELEHQLKDSGAEAIVV----LENFATTVQQvlaktavkhvvvasmgdlLGfkghivnfvvrrvkkmVPAwsLPgh 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 170 --LTPAIYRGAteKPTEQPVKESGwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLvHSW---AWTKND-----VIL 239
Cdd:PRK07059 182 vrFNDALAEGA--RQTFKPVKLGP--DDVAFLQYTGGTTGVSKGATLLHRNIVANVLQM-EAWlqpAFEKKPrpdqlNFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 240 HVLPLHHVHGV-VNKLLcPLWVGATCVMLPEFSAQQVWEKFLSSEapQITVFMAVPTVYSKLLDYYDkhFTQprvQDFvr 318
Cdd:PRK07059 257 CALPLYHIFALtVCGLL-GMRTGGRNILIPNPRDIPGFIKELKKY--QVHIFPAVNTLYNALLNNPD--FDK---LDF-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 319 avckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISEnpqkgs 397
Cdd:PRK07059 327 ----SKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDD------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 398 pyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDarywiRGRTSV----- 472
Cdd:PRK07059 397 ------DGND----LPLG---EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDE-----RGYTKIvdrkk 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 473 DIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVaLQEGHSLSHRDLKEWARGVLAPYAVPSELLLLE 552
Cdd:PRK07059 459 DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRT 537
|
570
....*....|....*
gi 1195733688 553 EIPRNQMGKVNKKEL 567
Cdd:PRK07059 538 ELPKTNVGKILRREL 552
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
33-567 |
1.17e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 163.38 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 33 PTAPEAHTDGSVPVFIRALAFG--DRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVV 110
Cdd:PRK06164 1 TPHDAAPRADTLASLLDAHARArpDAVALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGD----RVAVWLPNCIEWVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 111 AQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVV-----GQEYLERLSPLAQ--RLGVPLL-------PLTPAIYR 176
Cdd:PRK06164 76 LFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPdaLPPLRAIavvddaaDATPAPAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 177 GATEKPTEQP--------VKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVH 248
Cdd:PRK06164 156 GARVQLFALPdpappaaaGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 249 GVvNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVFMAVPTVYSKLLDyydkhfTQPRVQDFVRAvckeriRLM 328
Cdd:PRK06164 236 GF-STLLGALAGGAPLVCEPVFDAARTARALRRHR---VTHTFGNDEMLRRILD------TAGERADFPSA------RLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 329 VSGSAALPVPLLEKWRSATGHTLLERYGMTEI-----GMALSNPLTEARVPGsvGTPL-PGVEVRIIseNPQKGSpyiIH 402
Cdd:PRK06164 300 GFASFAPALGELAALARARGVPLTGLYGSSEVqalvaLQPATDPVSVRIEGG--GRPAsPEARVRAR--DPQDGA---LL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 403 AEGnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYK 481
Cdd:PRK06164 373 PDG-------------ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGFL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 482 VSALEIERHLLAHPSIADVAVIGVpDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMG- 560
Cdd:PRK06164 439 VNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAn 517
|
....*....
gi 1195733688 561 --KVNKKEL 567
Cdd:PRK06164 518 gaKIQKHRL 526
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
50-567 |
1.28e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 163.58 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIdkYG--HHTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:PRK08162 28 AEVYPDRPAVI--HGdrRRTWAETYARCRRLASALARR-GIGRGD----TVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPL--------TPAIYRGATE--------KPT---EQPVK 188
Cdd:PRK08162 101 RLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeyPGGRFIGALDyeaflasgDPDfawTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 189 EsgWrDRGAmIFYTSGTTGRPKGALSTHRN--LAAVVTGLvhSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VGA 262
Cdd:PRK08162 181 E--W-DAIA-LNYTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 263 TCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDYYDKHftqprvqdfvRAVCKERIRLMVSGsAALPVPLLEK 342
Cdd:PRK08162 250 TNVCLRKVDPKLIFDLI---REHGVTHYCGAPIVLSALINAPAEW----------RAGIDHPVHAMVAG-AAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 343 WRSAtGHTLLERYGMTEI-GMALSN---------PLTE-ARVPGSVGTPLPGVE-VRIIseNPQKGSPyiIHAEGnergt 410
Cdd:PRK08162 316 MEEI-GFDLTHVYGLTETyGPATVCawqpewdalPLDErAQLKARQGVRYPLQEgVTVL--DPDTMQP--VPADG----- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 411 kvtpgfeEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIER 489
Cdd:PRK08162 386 -------ETIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLhPDGYIKIKDR-SKDIIISGGENISSIEVED 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSElLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK08162 457 VLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVL 533
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
50-567 |
2.11e-43 |
|
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: 161.00 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRiALidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:cd17649 5 ALVFGDQ-SL-------SYAELDARANRLAH---RLRALGVG--PEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVvvgqeylerlspLAQRlgvpllpltpaiyrgatekpTEQPvkesgwrdrgAMIFYTSGTTGRP 209
Cdd:cd17649 72 PAERLRYMLEDSGAGLL------------LTHH--------------------PRQL----------AYVIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQITV 289
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 290 fMAVPTVY-SKLLDYYDKHftQPRVQdfvravckERIRLMVSGSAALPVPLLEKWRsATGHTLLERYGMTE---IGMALS 365
Cdd:cd17649 189 -LDLPPAYlQQLAEEADRT--GDGRP--------PSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEatvTPLVWK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NPLTEARVPGSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKS 443
Cdd:cd17649 257 CEAGAARAGASMpiGRPLGGRSAYIL----------------DADLNPVPVG---VTGELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 444 AFTSDG-------WFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVpDMTWGQRVT 515
Cdd:cd17649 318 RFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLV 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 516 AVVALQEGHSLSHRD--LKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17649 396 AYVVLRAAAAQPELRaqLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
55-567 |
2.36e-43 |
|
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: 161.74 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGDlqEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAH---RLRARGVGP--GDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEylerlspLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESGwRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17651 85 AFMLADAGPVLVLTHPA-------LAGELAVELVAVTLLDQPGAAAGADAEPDPALD-ADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLA----------AVVTGL-VHSWAWTKNDVILHvlplhhvhgvvnKLLCPLWVGATCVMLPE---FSAQQVWEkFL 280
Cdd:cd17651 157 PHRSLAnlvawqarasSLGPGArTLQFAGLGFDVSVQ------------EIFSTLCAGATLVLPPEevrTDPPALAA-WL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 281 SSEAPQItVFMavPTVYSKLLdyydkhFTQPRVQDFVRAvckeRIRLMVSGSAALPV-PLLEKW-RSATGHTLLERYGMT 358
Cdd:cd17651 224 DEQRISR-VFL--PTVALRAL------AEHGRPLGVRLA----ALRYLLTGGEQLVLtEDLREFcAGLPGLRLHNHYGPT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 359 E----IGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREY 434
Cdd:cd17651 291 EthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL----------------DAALRPVPPG---VPGELYIGGAGLARGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 435 WDKPEETKSAFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPD 507
Cdd:cd17651 352 LNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREAVVLARED 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 508 MTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17651 431 RPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
61-504 |
2.42e-43 |
|
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: 161.37 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 61 DKYGHHTYRELYDRSLCLAqeiCRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQD 140
Cdd:cd17640 1 KPPKRITYKDLYQEILDFA---AGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 141 SRSSLVVVgqeylerlsplaqrlgvpllpltpaiyrgatekpteqpvkESGWRDRgAMIFYTSGTTGRPKGALSTHRNLa 220
Cdd:cd17640 76 SESVALVV----------------------------------------ENDSDDL-ATIIYTSGTTGNPKGVMLTHANL- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 221 avVTGLVHSWAWTK---NDVILHVLPLHHVHGVVNKLLCPLWvGATCVmlpeFSAQQVWEKFLSSEAPQitVFMAVPTVY 297
Cdd:cd17640 114 --LHQIRSLSDIVPpqpGDRFLSILPIWHSYERSAEYFIFAC-GCSQA----YTSIRTLKDDLKRVKPH--YIVSVPRLW 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 298 SKLLD-YYDKHFTQPRVQDFV--RAVCKERIRLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVP 374
Cdd:cd17640 185 ESLYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 375 GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPgFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTG 454
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPE----------------GNVVLP-PGEK-GIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTG 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 455 DTAVF-KDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:cd17640 326 DLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
49-567 |
3.25e-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: 162.31 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYG--HHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLY 126
Cdd:cd17642 26 RYASVPGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKY-----GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 127 WKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL----GVPLLPLTPAiYRG--ATEKPTEQP----------VKES 190
Cdd:cd17642 101 DIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiikTIIILDSKED-YKGyqCLYTFITQNlppgfneydfKPPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 GWRDRG-AMIFYTSGTTGRPKGALSTHRNLAAVVTGL---VHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVM 266
Cdd:cd17642 180 FDRDEQvALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpIFGNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 267 LPEFSAqqvwEKFLSS-EAPQITVFMAVPTVY-----SKLLDYYDKHftqprvqdfvravckeriRLMVSGSAALPvplL 340
Cdd:cd17642 259 MYKFEE----ELFLRSlQDYKVQSALLVPTLFaffakSTLVDKYDLS------------------NLHEIASGGAP---L 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 341 EKwrsATGHTLLER---------YGMTEIGMA-LSNPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnergT 410
Cdd:cd17642 314 SK---EVGEAVAKRfklpgirqgYGLTETTSAiLITPEGDDK-PGAVGKVVPFFYAKVVDLD-----------------T 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 411 KVTPGFEEKeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:cd17642 373 GKTLGPNER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELES 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWargvLAPYAVPSELL-----LLEEIPRNQMGKVNK 564
Cdd:cd17642 451 ILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDY----VASQVSTAKRLrggvkFVDEVPKGLTGKIDR 526
|
...
gi 1195733688 565 KEL 567
Cdd:cd17642 527 RKI 529
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
29-567 |
3.67e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 162.32 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 29 HSLLPTAPEAHTDGSVPVFIRALAFGDRiALIDKYGHH--TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDI 106
Cdd:PLN02574 29 HPPVPLPSDPNLDAVSFIFSHHNHNGDT-ALIDSSTGFsiSYSELQPLVKSMAAGLYHVMGVRQGDV----VLLLLPNSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 107 SYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLaqrlGVPLLPLTPAIY--RGATEKPT- 183
Cdd:PLN02574 104 YFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL----GVPVIGVPENYDfdSKRIEFPKf 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 184 EQPVKESG--------WRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLV------HSWAWTKNdVILHVLPLHHVHG 249
Cdd:PLN02574 180 YELIKEDFdfvpkpviKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeasqYEYPGSDN-VYLAALPMFHIYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 250 VVNKLLCPLWVGATCVMLPEFSAQ---QVWEKFlsseapQITVFMAVPTVYSKLLdyydkHFTQPrvqdfVRAVCKERIR 326
Cdd:PLN02574 259 LSLFVVGLLSLGSTIVVMRRFDASdmvKVIDRF------KVTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 327 LMVSGSAALPVPLLEKWRSATGHT-LLERYGMTE---IGMALSNPlTEARVPGSVGTPLPGVEVRIISEnpqkgspyiih 402
Cdd:PLN02574 323 QVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEstaVGTRGFNT-EKLSKYSSVGLLAPNMQAKVVDW----------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 403 aegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYK 481
Cdd:PLN02574 391 ----STGCLLPPG---NCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 482 VSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGK 561
Cdd:PLN02574 463 IAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGK 542
|
....*.
gi 1195733688 562 VNKKEL 567
Cdd:PLN02574 543 ILRREL 548
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-562 |
4.44e-43 |
|
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: 156.80 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 KfLSSEapQITVFMAVPTVYSKLLDYYDKHFTqprvqdfvravckerIRLMVSGSAALPVPLLEKWRSATGHT-LLERYG 356
Cdd:cd17633 83 K-INQY--NATVIYLVPTMLQALARTLEPESK---------------IKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 357 MTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqkgspyiihAEGNERGTkvtpgfeekegeLLVRGPSVFREYWD 436
Cdd:cd17633 145 TSELSFITYNFNQESRPPNSVGRPFPNVEIEIRN------------ADGGEIGK------------IFVKSEMVFSGYVR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 437 KPEETKsaftsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQrvt 515
Cdd:cd17633 201 GGFSNP-----DGWMSVGDIGYVDEEGYlYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE--- 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1195733688 516 AVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:cd17633 272 IAVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
55-567 |
7.25e-43 |
|
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: 160.13 E-value: 7.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGD----LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPaiyrgatekPTEQPVKESGwRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAA---------PAPPPPVDVA-PDDLAYVIFTSGSTGTPKGVMI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSAQQV--WEKFLSSEapQITVFMA 292
Cdd:cd12114 147 SHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEARRRDPahWAELIERH--GVTLWNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 293 VPTVYSKLLDYYDKHFTQPRVQdfvRAVckerirlMVSGSaALPVPLLEKWRSATGH-TLLERYGMTEiGMALSNPLTEA 371
Cdd:cd12114 224 VPALLEMLLDVLEAAQALLPSL---RLV-------LLSGD-WIPLDLPARLRALAPDaRLISLGGATE-ASIWSIYHPID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 372 RVP---GSV--GTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEETKSAFT 446
Cdd:cd12114 292 EVPpdwRSIpyGRPLANQRYRVL----------------DPRGRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 447 SDG----WFRTGDTavfkdARYW------IRGRtsVDI-IKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVT 515
Cdd:cd12114 353 THPdgerLYRTGDL-----GRYRpdgtleFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 516 AVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12114 426 FVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
199-570 |
8.91e-43 |
|
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: 160.71 E-value: 8.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTHRNLAAVVTGLVHSW-AWTKNDVILHVLPLHHVHGVVNKLLCPlWVGATCVM---LPEFSAQQ 274
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPRFDPLV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 275 VWEKFlsSEAPqITVFMAVPTVYSKLLDyydkhftqprvQDFVRAVCKeRIRLMVSGSAALPVPLLEKWRSATGHTLLER 354
Cdd:cd05928 258 ILKTL--SSYP-ITTFCGAPTVYRMLVQ-----------QDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 355 YGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVR-GP----S 429
Cdd:cd05928 323 YGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDN----------------GNVLPPG---TEGDIGIRvKPirpfG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 430 VFREYWDKPEETKSAFTSDGWFrTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:cd05928 384 LFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 509 TWGQRVTAVVALQEGHsLSH------RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQ 570
Cdd:cd05928 462 IRGEVVKAFVVLAPQF-LSHdpeqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
193-562 |
6.74e-42 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 158.91 E-value: 6.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 193 RDRGAMIFYTSGTTGRPKGALSTHRnlaAVVTglvHsWAWTKndvilHVLPLHH------------VHGVVNKLLCPLWV 260
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLHVHN---AMLQ---H-YQTGK-----YVLDLHEddvywctadpgwVTGTSYGIFAPWLN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 261 GATCVML-PEFSAQQvWEKFLSSEapQITVFMAVPTVYSKLLDYYDkhftqprvqDFVRAVCKERIRLMVSGSAALPvPL 339
Cdd:PRK04319 272 GATNVIDgGRFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGD---------DLVKKYDLSSLRHILSVGEPLN-PE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 340 LEKW-RSATGHTLLERYGMTEIG-MALSNPLTEARVPGSVGTPLPGVEVRIISENPQKGSPYiihaegnergtkvtpgfe 417
Cdd:PRK04319 339 VVRWgMKVFGLPIHDNWWMTETGgIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPN------------------ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 418 eKEGELLVRG--PSVFREYWDKPEETKSAFtSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLA 493
Cdd:PRK04319 401 -RMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSA-YMDEDgyFWFQGRVD-DVIKTSGERVGPFEVESKLME 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 494 HPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:PRK04319 477 HPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
198-556 |
7.68e-42 |
|
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: 153.61 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSAQQVWE 277
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 kFLSSEAPQITvFMAVPTVysklldyydkhftqprvqDFVRAVCKERI----RLMVSGSAALPVPLLEKWRSATGHTLLE 353
Cdd:cd17636 83 -LIEAERCTHA-FLLPPTI------------------DQIVELNADGLydlsSLRSSPAAPEWNDMATVDTSPWGRKPGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 rYGMTEI-GMALSNPLTEARVpGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEGELLVRGPSVFR 432
Cdd:cd17636 143 -YGQTEVmGLATFAALGGGAI-GGAGRPSPLVQVRILDE------------DGRE----VPDG---EVGEIVARGPTVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 433 EYWDKPEETkSAFTSDGWFRTGDTavfkdarywirGRTSVD-----------IIKTGGYKVSALEIERHLLAHPSIADVA 501
Cdd:cd17636 202 GYWNRPEVN-ARRTRGGWHHTNDL-----------GRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAA 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 502 VIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPR 556
Cdd:cd17636 270 VIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
31-567 |
1.12e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 157.47 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 31 LLPTAPEAHTDGSVPVFIRALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGdlqeERVSFLCSNDISYVV 110
Cdd:PRK13383 26 LLREASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTR-DGVAPG----RAVGVMCRNGRGFVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 111 AQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVpllpLTPAIYrGATEKPTEQPVKES 190
Cdd:PRK13383 101 AVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAV----IDPATA-GAEESGGRPAVAAP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 GwrdrgAMIFYTSGTTGRPKGALSTHRNLAAV---VTGLVHSWAWTKNDVILhVLPLHHVHGVvNKLLCPLWVGATCVML 267
Cdd:PRK13383 176 G-----RIVLLTSGTTGKPKGVPRAPQLRSAVgvwVTILDRTRLRTGSRISV-AMPMFHGLGL-GMLMLTIALGGTVLTH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 PEFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLDYYDKhftqprvqdfVRAVCK-ERIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PRK13383 249 RHFDAEAA---LAQASLHRADAFTAVPVVLARILELPPR----------VRARNPlPQLRVVMSSGDRLDPTLGQRFMDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 TGHTLLERYGMTEIGM-ALSNPLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaeGNERGTKVTpgfeekeGELLV 425
Cdd:PRK13383 316 YGDILYNGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRN------------NRPVGPRVT-------GRIFV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 426 RGPSVFREYWDKPEETksafTSDGWFRTGDTAVFKDA-RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:PRK13383 377 GGELAGTRYTDGGGKA----VVDGMTSTGDMGYLDNAgRLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIG 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 505 VPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK13383 452 VPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
197-564 |
1.68e-41 |
|
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: 153.19 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLV-HSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSAQQV 275
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEKFLSSEAPQITVFmaVPTVYSKLLDYYdkhftqprvQDFVRAVckERIRLMVSGSaALPVPLLEKWRSATGHT-LLER 354
Cdd:cd17635 83 LFKILTTNAVTTTCL--VPTLLSKLVSEL---------KSANATV--PSLRLIGYGG-SRAIAADVRFIEATGLTnTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 355 YGMTEIGMAL----SNPLTEArvpGSVGTPLPGVEVRIISenpqkgspyiihaegnergTKVTPGFEEKEGELLVRGPSV 430
Cdd:cd17635 149 YGLSETGTALclptDDDSIEI---NAVGRPYPGVDVYLAA-------------------TDGIAGPSASFGTIWIKSPAN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 431 FREYWDKPEETKSAFTsDGWFRTGDTA-VFKDARYWIRGRTSVDIIKtGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:cd17635 207 MLGYWNNPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 510 WGQRV-TAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNK 564
Cdd:cd17635 285 FGELVgLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
55-567 |
1.90e-41 |
|
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: 155.10 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLAR---LLAARGVG--PERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVgqeylerlsplaqrlgvpllpltpaiyrgatekpteQPvkesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17652 77 AYMLADARPALLLT------------------------------------TP-------DNLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLPEFSAQ--QVWEKFLSSEApqITVFMA 292
Cdd:cd17652 114 THRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHR--ITHVTL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 293 VPTVYSKLldyydkhftqprvqdfvRAVCKERIRLMVSGSAALPVPLLEKWrsATGHTLLERYGMTE--IGMALSNPLTE 370
Cdd:cd17652 191 PPAALAAL-----------------PPDDLPDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTEttVCATMAGPLPG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 371 ARVPgSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGFEekeGELLVRGPSVFREYWDKPEETKSAFTSDGW 450
Cdd:cd17652 252 GGVP-PIGRPVPGTRVYVLDARLRP----------------VPPGVP---GELYIAGAGLARGYLNRPGLTAERFVADPF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 451 -------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQE 522
Cdd:cd17652 312 gapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1195733688 523 GHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17652 391 GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
62-539 |
1.14e-40 |
|
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: 154.55 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 62 KYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDS 141
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAAL-RALGLEPGS----KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 142 RSSLVVVGQ--EYLERLSPLAQRLG---VPLLPLTPAIYRGATEKPTEQPVKESGWR--DRGAMIFYTSGTTGRPKGALS 214
Cdd:cd05932 78 ESKALFVGKldDWKAMAPGVPEGLIsisLPPPSAANCQYQWDDLIAQHPPLEERPTRfpEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATcVMLPE----FSAQqvwekfLSSEAPqiTVF 290
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL-VAFAEsldtFVED------VQRARP--TLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 MAVPTVYSKLldyydkhftQPRVQD--------------FVRAVCKERI---------RLMVSGSAALPVPLLEKWRSaT 347
Cdd:cd05932 229 FSVPRLWTKF---------QQGVQDkipqqklnlllkipVVNSLVKRKVlkglgldqcRLAGCGSAPVPPALLEWYRS-L 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 348 GHTLLERYGMTEiGMALSN---PLTeaRVPGSVGTPLPGVEVRIisenpqkgspyiihaegnergtkvtpgfeEKEGELL 424
Cdd:cd05932 299 GLNILEAYGMTE-NFAYSHlnyPGR--DKIGTVGNAGPGVEVRI-----------------------------SEDGEIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWDKPEETKSAFTSDGWFRTGDT-AVFKDARYWIRGRTSvDIIKTG-GYKVSALEIERHLLAHPSIADVAV 502
Cdd:cd05932 347 VRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLTITGRVK-DIFKTSkGKYVAPAPIENKLAEHDRVEMVCV 425
|
490 500 510
....*....|....*....|....*....|....*..
gi 1195733688 503 IgvpdmtwGQRVTAVVALQEGHSLSHRDLKEWARGVL 539
Cdd:cd05932 426 I-------GSGLPAPLALVVLSEEARLRADAFARAEL 455
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
67-571 |
1.38e-40 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 154.91 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRlQGCKVGDlqeeRVSFLCSNDISYVVAqWASWMS-GGVAVPLYWK-HPEaQLEYFIQDSRSS 144
Cdd:PRK06018 41 TYAQIHDRALKVSQALDR-DGIKLGD----RVATIAWNTWRHLEA-WYGIMGiGAICHTVNPRlFPE-QIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYLERLSPLAQRLG-------------VPLLPLTPAIyrgATEKPTEQPVKESGWRD----RGAMIFYTSGTTG 207
Cdd:PRK06018 114 VVITDLTFVPILEKIADKLPsveryvvltdaahMPQTTLKNAV---AYEEWIAEADGDFAWKTfdenTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 208 RPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQQVWEkFLSSEa 284
Cdd:PRK06018 191 DPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYE-LLDTE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 285 pQITVFMAVPTVYSKLLDYYDKH-FTQPRvqdfvravckerIRLMVSGSAALPVPLLEKWrSATGHTLLERYGMTE---I 360
Cdd:PRK06018 268 -KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEmspL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 GM--ALSNPLTEARVPGSV------GTPLPGVEVRIISEnpqkgspyiihaEGNErgtkvTPGFEEKEGELLVRGPSVFR 432
Cdd:PRK06018 334 GTlaALKPPFSKLPGDARLdvlqkqGYPPFGVEMKITDD------------AGKE-----LPWDGKTFGRLKVRGPAVAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 433 EYWdkpEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWG 511
Cdd:PRK06018 397 AYY---RVDGEILDDDGFFDTGDVAtIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWD 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 512 QRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK06018 473 ERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
67-571 |
1.59e-40 |
|
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: 154.75 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPL-------YWKHPEAQLEYFIQ 139
Cdd:cd05906 41 SYQDLLEDARRLAAGL-RQLGLRPGD----SVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 140 DSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESgwrDRGAMIFYTSGTTGRPKGALSTHRNL 219
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRP---DDLALLMLTSGSTGFPKAVPLTHRNI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 220 AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGAtcvmlpefsaQQVwekflsseapqitvfmAVPTVY-- 297
Cdd:cd05906 193 LARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGC----------QQV----------------HVPTEEil 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 298 ---SKLLDYYDKH---------FTQPRVQDFVRAVCKER-----IRLMVSGSAALPVPLLEKWRSatghtLLERY----- 355
Cdd:cd05906 247 adpLRWLDLIDRYrvtitwapnFAFALLNDLLEEIEDGTwdlssLRYLVNAGEAVVAKTIRRLLR-----LLEPYglppd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 ------GMTEI--GMALSNPLTEARVPG-----SVGTPLPGVEVRIISENpqkgspyiihaegnergTKVTPgfEEKEGE 422
Cdd:cd05906 322 airpafGMTETcsGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDE-----------------GQLLP--EGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIAD--V 500
Cdd:cd05906 383 LQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIEAAVEEVPGVEPsfT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 501 AVIGVPDMTWGQRVTAVV-----ALQEGHSLSHRDLKEWAR---GVLAPYAVPselLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:cd05906 462 AAFAVRDPGAETEELAIFfvpeyDLQDALSETLRAIRSVVSrevGVSPAYLIP---LPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
67-455 |
1.85e-40 |
|
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: 154.68 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeERVSFLCSNDISYVVAQWASWMSGGVAVPLYwkH---PEAqLEYFIQDSRS 143
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPA---SFVGIYSINRPEWIISELACYAYSLVTVPLY--DtlgPEA-IEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 144 SLVVVGQeylerlsplaqrlGVPLLPLTPAIYRGATEK-PTEQPVKESGwrdrgAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:cd05927 81 SIVFCDA-------------GVKVYSLEEFEKLGKKNKvPPPPPKPEDL-----ATICYTSGTTGNPKGVMLTHGNIVSN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 223 VTGLVHSW----AWTKNDVILHVLPLHHV--HGVVNKLLC-----PLWVGATCVMLPEFSAQQvwekflsseaPqiTVFM 291
Cdd:cd05927 143 VAGVFKILeilnKINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRLLLDDIKALK----------P--TVFP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 292 AVPTVYSKLldyYDKHFT----QPRVQDFV--------------RAVCKE-----------------RIRLMVSGSAALP 336
Cdd:cd05927 211 GVPRVLNRI---YDKIFNkvqaKGPLKRKLfnfalnyklaelrsGVVRASpfwdklvfnkikqalggNVRLMLTGSAPLS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 337 VPLLEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPGVEVRIISEnPQKGspYiiHAEGNErgtkvtp 414
Cdd:cd05927 288 PEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKLVDV-PEMN--Y--DAKDPN------- 353
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1195733688 415 gfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:cd05927 354 ----PRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
55-567 |
2.73e-40 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 152.09 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKvgdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARL-RAAGVG----PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd12115 89 RFILEDAQARLVLTDPDDL-------------------------------------------AYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVtglvhSWAwtkndviLHVLPLHHVHGV-----------VNKLLCPLWVGATCVMlpefsAQQVWEKFLSSE 283
Cdd:cd12115 126 EHRNAAAFL-----QWA-------AAAFSAEELAGVlastsicfdlsVFELFGPLATGGKVVL-----ADNVLALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 284 APQITVFMAVPTVYSKLLdyydKHFTQPRVqdfVRAVCkerirlmVSGSAaLPVPLLEK-WRSATGHTLLERYGMTE--- 359
Cdd:cd12115 189 AAEVTLINTVPSAAAELL----RHDALPAS---VRVVN-------LAGEP-LPRDLVQRlYARLQVERVVNLYGPSEdtt 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 360 --IGMALSnplTEARVPGSVGTPLPGVEVriisenpqkgspYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDK 437
Cdd:cd12115 254 ysTVAPVP---PGASGEVSIGRPLANTQA------------YVLDRALQPVPLGVP-------GELYIGGAGVARGYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 438 PEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTW 510
Cdd:cd12115 312 PGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 511 GQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
197-567 |
3.26e-40 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 152.87 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE-FSAQQV 275
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEkfLSSEApQITVFMAVPTvyskLLDYYDKhftqprvqdFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERY 355
Cdd:cd05909 230 PE--LIYDK-KATILLGTPT----FLRGYAR---------AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 GMTEIG--MALSNPLTeARVPGSVGTPLPGVEVRIISEnpqkgspyiihaEGNErgtkvtPGFEEKEGELLVRGPSVFRE 433
Cdd:cd05909 294 GTTECSpvISVNTPQS-PNKEGTVGRPLPGMEVKIVSV------------ETHE------EVPIGEGGLLLVRGPNVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 434 YWDKPEETKSAFtSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAH-PSIADVAVIGVPDMTWG 511
Cdd:cd05909 355 YLNEPELTSFAF-GDGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 512 QRvtaVVALQEGHSLSHRDLKEWARGVLAP-YAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05909 433 EK---IVLLTTTTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-562 |
6.33e-40 |
|
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: 153.16 E-value: 6.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIA---LIDKYG---HHTYRELYDRSLCLAQEIcrLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVA 122
Cdd:cd05931 2 RAAARPDRPAytfLDDEGGreeTLTYAELDRRARAIAARL--QAVGKPGD----RVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 123 VPLYWKHPEAQLEYF---IQDSRSSLVVVGQEYLERLSPLA---------QRLGVPLLPLTPAiyrGATEKPTEQPvkes 190
Cdd:cd05931 76 VPLPPPTPGRHAERLaaiLADAGPRVVLTTAAALAAVRAFAasrpaagtpRLLVVDLLPDTSA---ADWPPPSPDP---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 gwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:cd05931 149 ---DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 SaqqvwekflsseapqitvFMAVPTVYSKLLDYYDKHFTQprVQDFVRAVCKERIR-----------LMVSGSAALPVpl 339
Cdd:cd05931 226 A------------------FLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVRdedlegldlssWRVALNGAEPV-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 340 lekwRSATGHTLLER--------------YGMTE-------------------IGMALSNPLTEARVPG-------SVGT 379
Cdd:cd05931 284 ----RPATLRRFAEAfapfgfrpeafrpsYGLAEatlfvsggppgtgpvvlrvDRDALAGRAVAVAADDpaarelvSCGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 380 PLPGVEVRIIseNPqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF------TSDGWFRT 453
Cdd:cd05931 360 PLPDQEVRIV--DP-------------ETGRELPDG---EVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 454 GDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPS---IADVAVIGVPDmtwGQRVTAVVALQEGHSLSHRD 530
Cdd:cd05931 422 GDLGFLHDGELYITGRLK-DLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPD---DGEERLVVVAEVERGADPAD 497
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1195733688 531 LKEWARGVLApyAV-------PSELLLLE--EIPRNQMGKV 562
Cdd:cd05931 498 LAAIAAAIRA--AVarehgvaPADVVLVRpgSIPRTSSGKI 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
55-579 |
1.69e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 150.70 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYdRSLCLAQEICRLQGCKvgdlqEERVSFLCSNDISYVVAQWASWMSGGVAVPL--YWKHPEA 132
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWF-ESVCKVANWLNEKESK-----NKTIAILLENRIEFLQLFAGAAMAGWTCVPLdiKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIqdSRSSLVVVGQEYLERLSPLAQRLgVPLLPLTPAIYRgatEKPTEQPVKesgwrDRGAMIFY---TSGTTGRP 209
Cdd:PRK07638 90 KERLAI--SNADMIVTERYKLNDLPDEEGRV-IEIDEWKRMIEK---YLPTYAPIE-----NVQNAPFYmgfTSGSTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVH---GVVNKLlcplWVGATCVMLPEFSAQQVWEKfLSSEapQ 286
Cdd:PRK07638 159 KAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLDK-LETE--N 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 287 ITVFMAVPTVYSKLLDyydkhftqprvqdfVRAVCKERIRLMVSGsAALPVPLLEKWRSATGH-TLLERYGMTEIG-MAL 364
Cdd:PRK07638 232 ISVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYGASELSfVTA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 365 SNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSa 444
Cdd:PRK07638 297 LVDEESERRPNSVGRPFHNVQVRIC----------------NEAGEEVQKG---EIGTVYVKSPQFFMGYIIGGVLARE- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVValqEG 523
Cdd:PRK07638 357 LNADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KG 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 524 HSLShRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLYPSGQRSQ 579
Cdd:PRK07638 433 SATK-QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
197-567 |
2.65e-39 |
|
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: 151.11 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKgaLSTHRN---LAAVVTGLVhsWAWTK-NDVILHVLPLHHVHGVVNKLLCPlWVGATCVMLPE--- 269
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEHDFtypLGHIVTAKY--WQNVReGGLHLTVADTGWGKAVWGKIYGQ-WIAGAAVFVYDydk 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 FSAQQVWEKFlssEAPQITVFMAVPTVYSKL----LDYYDKhftqprvqdfvravckERIRLMVSGSAALPVPLLEKWRS 345
Cdd:cd05970 263 FDPKALLEKL---SKYGVTTFCAPPTIYRFLiredLSRYDL----------------SSLRYCTTAGEALNPEVFNTFKE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 346 ATGHTLLERYGMTEIGMALSN-PLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELL 424
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEIDLIDRE----------------GRSCEAG---EEGEIV 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VR---GPSV--FREYWDKPEETKSAFtSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIA 498
Cdd:cd05970 384 IRtskGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVL 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 499 DVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05970 462 ECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
72-568 |
7.90e-39 |
|
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: 148.68 E-value: 7.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 72 YDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVgqe 151
Cdd:cd05929 23 YSIALNRNARAAAAEGVWIAD----GVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 152 ylerlsplaqRLGVPLLPLTPAIY-RGATEKPTEQPVKESgwrdRGAMIFYTSGTTGRPKGALsthRNLAAVV--TGLVH 228
Cdd:cd05929 96 ----------LFTGGGALDGLEDYeAAEGGSPETPIEDEA----AGWKMLYSGGTTGRPKGIK---RGLPGGPpdNDTLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 229 SWA----WTKNDVILHVLPLHHV--HGVVNKllcPLWVGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLL 301
Cdd:cd05929 159 AAAlgfgPGADSVYLSPAPLYHAapFRWSMT---ALFMGGTLVLMEKFDP----EEFLRLiERYRVTFAQFVPTMFVRLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 302 DYYDKhftQPRVQDFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTP 380
Cdd:cd05929 232 KLPEA---VRNAYDL------SSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEEWLTHPGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 381 LPGvEVRIISENpqkgspyiihaeGNErgtkVTPGfeeKEGELLVRGPSVFrEYWDKPEETKSAFTSDGWFRTGDTAVFK 460
Cdd:cd05929 303 VLG-KVHILDED------------GNE----VPPG---EIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 461 DARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVV----------ALQEGhslshrd 530
Cdd:cd05929 362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgadagtALAEE------- 434
|
490 500 510
....*....|....*....|....*....|....*...
gi 1195733688 531 LKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELL 568
Cdd:cd05929 435 LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
66-571 |
7.76e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 147.16 E-value: 7.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 66 HTYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK-HPEaQLEYFIQDSRSS 144
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAAL-GVEPGD----RVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFPE-QIAYIVNHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYLerlsPLAQRLGvPLLP-------LTPAIYRGATEKPT---EQPVK-ESG---W----RDRGAMIFYTSGTT 206
Cdd:PRK07008 114 YVLFDLTFL----PLVDALA-PQCPnvkgwvaMTDAAHLPAGSTPLlcyETLVGaQDGdydWprfdENQASSLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 207 GRPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSAQQVWEKFlssE 283
Cdd:PRK07008 189 GNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYELI---E 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 284 APQITVFMAVPTVYSKLLDYYDKhfTQPRVQDFVRAVckerirlmVSGSAAlPVPLLEKWRSATGHTLLERYGMTEI--- 360
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLNHMRE--AGLRFSTLRRTV--------IGGSAC-PPAMIRTFEDEYGVEVIHAWGMTEMspl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 -------GMALSNPLTEAR-VPGSVGTPLPGVEVRIISEN----PQKGSPYiihaegnergtkvtpgfeekeGELLVRGP 428
Cdd:PRK07008 334 gtlcklkWKHSQLPLDEQRkLLEKQGRVIYGVDMKIVGDDgrelPWDGKAF---------------------GDLQVRGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 429 SVFREYWDKPEETksafTSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPD 507
Cdd:PRK07008 393 WVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAH 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 508 MTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK07008 468 PKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
50-567 |
1.10e-37 |
|
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: 145.55 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeICRLQGCKvgdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:cd17655 15 AVVFEDQTL--------TYRELNERANQLAR-TLREKGVG----PDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVgQEYLErlSPLAQRLGVPLLPL-TPAIYRGATEKPTEQPvkesgwrDRGAMIFYTSGTTGR 208
Cdd:cd17655 82 PEERIQYILEDSGADILLT-QSHLQ--PPIAFIGLIDLLDEdTIYHEESENLEPVSKS-------DDLAYVIYTSGSTGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLP--EFSAQQVWEKFLSSEapQ 286
Cdd:cd17655 152 PKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVRkeTVLDGQALTQYIRQN--R 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 287 ITVFMAVPTVYsKLLDYYDKHFTQPrvqdfvravckerIRLMVSGSAALPVPLLEKWRSATGH--TLLERYGMTE----- 359
Cdd:cd17655 229 ITIIDLTPAHL-KLLDAADDSEGLS-------------LKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTEttvda 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 360 -IGMALSNPLTEARVPgsVGTPLPGVEVRIISEN--PQK-GSPyiihaegnergtkvtpgfeekeGELLVRGPSVFREYW 435
Cdd:cd17655 295 sIYQYEPETDQQVSVP--IGKPLGNTRIYILDQYgrPQPvGVA----------------------GELYIGGEGVARGYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 436 DKPEETKSAFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:cd17655 351 NRPELTAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 509 TWGQRVTAVVALQEghSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17655 430 QGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-567 |
1.93e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 149.16 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 33 PTAPEAHTDGSVPVFIRALAFG-DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVA 111
Cdd:PRK12467 504 APATEYAPDCVHQLIEAQARQHpERPALVFGEQVLSYAELNRQANRLAH---VLIAAGVG--PDVLVGIAVERSIEMVVG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 112 QWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVvGQEYLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKEsg 191
Cdd:PRK12467 579 LLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL-TQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDP-- 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFS 271
Cdd:PRK12467 656 --DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 272 AQQVWEKFLSSEAPQITVFMAVPTVYSKLLdyydkhftqprvQDFVRAVCKERIRLMVSGSaALPVPLLEKWRS-ATGHT 350
Cdd:PRK12467 733 ARDAEAFAALMADQGVTVLKIVPSHLQALL------------QASRVALPRPQRALVCGGE-ALQVDLLARVRAlGPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 351 LLERYGMTE--IGMALSNPLTEARVPGSV--GTPLPGVEVRII--SENPqkgspyiihaegnergtkVTPGFeekEGELL 424
Cdd:PRK12467 800 LINHYGPTEttVGVSTYELSDEERDFGNVpiGQPLANLGLYILdhYLNP------------------VPVGV---VGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWDKPEETKSAFTSDGW-------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPS 496
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPG 937
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 497 IADVAVIGVPDMTWGQRVTAVVALQEGHSLSHR----DLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 938 VREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
38-567 |
8.46e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 143.68 E-value: 8.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 38 AHTDGSVPVFIRAlAFGDRIalidkyghhTYRELYDRSLCLAQeICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWM 117
Cdd:PRK13391 7 AQTTPDKPAVIMA-STGEVV---------TYRELDERSNRLAH-LFRSLGLKRGD----HVAIFMENNLRYLEVCWAAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 118 SGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLtpaIYRGATEKPTEQPVKE-----SGW 192
Cdd:PRK13391 72 SGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL---VLDGDGELEGFVGYAEavaglPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 193 R----DRGAMIFYTSGTTGRPKGAL--------STHRNLAAVVTGLvhsWAWTKNDVILHVLPLHHVH-----GVVNKLl 255
Cdd:PRK13391 149 PiadeSLGTDMLYSSGTTGRPKGIKrplpeqppDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 256 cplwvGATCVMLPEFSAqqvwEKFLSS-EAPQITVFMAVPTVYSKLL-------DYYDkhftqprVQDFVRAVckerirl 327
Cdd:PRK13391 225 -----GGTVIVMEHFDA----EQYLALiEEYGVTHTQLVPTMFSRMLklpeevrDKYD-------LSSLEVAI------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 328 mvsgSAALPVP------LLEKWrsatGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVeVRIIsenpqkgspyi 400
Cdd:PRK13391 282 ----HAAAPCPpqvkeqMIDWW----GPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHIL----------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 401 ihaegNERGTKVTPGfeeKEGELLVRGPSVFrEYWDKPEETKSAFTSDG-WFRTGDTAVFKDARYWIRGRTSVDIIKTGG 479
Cdd:PRK13391 342 -----DDDGAELPPG---EPGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 480 YKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS---HRDLKEWARGVLAPYAVPSELLLLEEIPR 556
Cdd:PRK13391 413 VNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPR 492
|
570
....*....|.
gi 1195733688 557 NQMGKVNKKEL 567
Cdd:PRK13391 493 LPTGKLYKRLL 503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-567 |
2.01e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 146.26 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 23 PRRHRGHSLLptapeAHTDGSVPVFIrALAFGDRialidkygHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLC 102
Cdd:PRK12316 2000 PRGPGVHQRI-----AEQAARAPEAI-AVVFGDQ--------HLSYAELDSRANRLAH---RLRARGVG--PEVRVAIAA 2060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 103 SNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPAIYrgATEKP 182
Cdd:PRK12316 2061 ERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL-PLPA--GVARLPLDRDAE--WADYP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 183 TEQPVKESGwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGA 262
Cdd:PRK12316 2136 DTAPAVQLA-GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 263 TCVM------LPEFSAQQVWEKflsseapQITVfMAVPTVYSKLLdyydkhftqprVQDFVRAVCKERIRLMVSGSAALP 336
Cdd:PRK12316 2214 RVLIrddelwDPEQLYDEMERH-------GVTI-LDFPPVYLQQL-----------AEHAERDGRPPAVRVYCFGGEAVP 2274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 337 VPLLEK-WRSATGHTLLERYGMTEIGMALS-------NPLTEARVPgsVGTPLPGVevriisenpqkgSPYIIHAEGNER 408
Cdd:PRK12316 2275 AASLRLaWEALRPVYLFNGYGPTEAVVTPLlwkcrpqDPCGAAYVP--IGRALGNR------------RAYILDADLNLL 2340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 409 GTKVTpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGG 479
Cdd:PRK12316 2341 APGMA-------GELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRG 2411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 480 YKVSALEIERHLLAHPSIADVAVIGVpDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQM 559
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
....*...
gi 1195733688 560 GKVNKKEL 567
Cdd:PRK12316 2491 GKLDRKAL 2498
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-564 |
2.40e-36 |
|
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: 141.12 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGD----VVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGqeylerlspLAQRlgvpllpltpaiyrgatEKPTEQPVkesgwrdrgaMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05973 77 VTD---------AANR-----------------HKLDSDPF----------VMMFTSGTTGLPKGVPVPLRALAAFGAYL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLdyyd 305
Cdd:cd05973 121 RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRVI---ERLGVTNLAGSPTAYRLLM---- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 306 khftqprvQDFVRAVCKERIRLMVSGSAALPV-PLLEKWRSAT-GHTLLERYGMTEIGMALSNPLTEARV--PGSVGTPL 381
Cdd:cd05973 194 --------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHALEHPvhAGSAGRAM 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 382 PGVEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLV---RGPSV-FREYWDKPEETKSAftsdGWFRTGDTA 457
Cdd:cd05973 266 PGWRVAVLDDD----------------GDELGPG---EPGRLAIdiaNSPLMwFRGYQLPDTPAIDG----GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 458 VFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWAR 536
Cdd:cd05973 323 EFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQL 401
|
490 500 510
....*....|....*....|....*....|.
gi 1195733688 537 GV---LAPYAVPSELLLLEEIPRNQMGKVNK 564
Cdd:cd05973 402 HVkkrLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
197-571 |
9.11e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 137.48 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVT------GLVHSWawtkndviLHVLPLHHVHGVvNKLLCPLWVGATCVMLpef 270
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADathdrlGGPGQW--------LLALPAHHIAGL-QVLVRSVIAGSEPVEL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 saqQVWEKFLSSEAPQITVFMAVPTVYSKLLDY-YDKHFTQPRVQDFVRavckeRIRLMVSGSAALPVPLLEKWRSAtGH 349
Cdd:PRK07824 106 ---DVSAGFDPTALPRAVAELGGGRRYTSLVPMqLAKALDDPAATAALA-----ELDAVLVGGGPAPAPVLDAAAAA-GI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 TLLERYGMTEIGmalsnpltearvPGSV--GTPLPGVEVRIIsenpqkgspyiihaegnergtkvtpgfeekEGELLVRG 427
Cdd:PRK07824 177 NVVRTYGMSETS------------GGCVydGVPLDGVRVRVE------------------------------DGRIALGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 428 PSVFREYWDKPEEtkSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPD 507
Cdd:PRK07824 215 PTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPD 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 508 MTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PRK07824 292 DRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
197-536 |
1.15e-35 |
|
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: 140.04 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVH--SWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP------ 268
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPrtltdk 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 ----------EF------SAQQVWE---KFLSSEAPQI-----TVFMavpTVYS----KLLDYYDKHFTQPRVQDFVRAV 320
Cdd:cd17639 171 skrgckgdltEFkptlmvGVPAIWDtirKGVLAKLNPMgglkrTLFW---TAYQsklkALKEGPGTPLLDELVFKKVRAA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 321 CKERIRLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPGVEVRIISEnpqkgsp 398
Cdd:cd17639 248 LGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKLVDW------- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 399 yiihAEGNERGTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARYWIRGRTSvDIIKT 477
Cdd:cd17639 318 ----EEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDRKK-DLVKL 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 478 --GGYkvSALE-IERHLLAHPSIADVAVIGVPDMTwgqRVTAVVALQEGHslshrdLKEWAR 536
Cdd:cd17639 388 qnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAE 438
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
54-562 |
1.29e-34 |
|
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: 138.48 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 54 GDRIALI------DKYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTL-LDLGVKKGD----RVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQEYLE--RLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESG-----WRDRGA--- 197
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGGVRagRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEgrdlwWRDLIAkas 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 --------------MIFYTSGTTGRPKGALSTHRNLA-AVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGA 262
Cdd:cd17634 222 pehqpeamnaedplFILYTSGTTGKPKGVLHTTGGYLvYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 263 TCVMlpeFSAQQVWekflsseapqitvfmavPTVySKLLDYYDKH-----FTQPRVqdfVRAVCKE---------RIRLM 328
Cdd:cd17634 302 TTLL---YEGVPNW-----------------PTP-ARMWQVVDKHgvnilYTAPTA---IRALMAAgddaiegtdRSSLR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 329 VSGSAALPV-PllEKWRSATGHTLLER------YGMTEIGMALSNPL--TEARVPGSVGTPLPGVEVRIIsenpqkgspy 399
Cdd:cd17634 358 ILGSVGEPInP--EAYEWYWKKIGKEKcpvvdtWWQTETGGFMITPLpgAIELKAGSATRPVFGVQPAVV---------- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 400 iihaegNERGTKVTPGfeeKEGELLVRG--PSVFREYWDKPEETKSAF--TSDGWFRTGDTA-VFKDARYWIRGRtSVDI 474
Cdd:cd17634 426 ------DNEGHPQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQTYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 475 IKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS---HRDLKEWARGVLAPYAVPSELLLL 551
Cdd:cd17634 496 INVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWV 575
|
570
....*....|.
gi 1195733688 552 EEIPRNQMGKV 562
Cdd:cd17634 576 DSLPKTRSGKI 586
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
36-581 |
2.10e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 137.06 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 36 PEA----HTDGSvpvfiRALAFGDRIALIDKYGHHTYrelydrslclAQEICrlqgckvgdlQEERVSFLCSNDISYVVA 111
Cdd:PRK05857 28 PEAialrRCDGT-----SALRYRELVAEVGGLAADLR----------AQSVS----------RGSRVLVISDNGPETYLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 112 QWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRL-GVPLLPL------TPAIYRGATEKPTE 184
Cdd:PRK05857 83 VLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALhSIPVIAVdiaavtRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 185 QPvkESGWRDRGAMIFyTSGTTGRPKGALSTHRNLAAV-----VTGLvhSWA-WTKNDVILHVLPLHHVHGVVNKLLCpL 258
Cdd:PRK05857 163 NA--DQGSEDPLAMIF-TSGTTGEPKAVLLANRTFFAVpdilqKEGL--NWVtWVVGETTYSPLPATHIGGLWWILTC-L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 259 WVGATCVMLPEFSAQqvWEKFLSSEAPQITVFmaVPTVYSKLLdyYDKHFTqprvqdfvrAVCKERIRLMVSGSA---AL 335
Cdd:PRK05857 237 MHGGLCVTGGENTTS--LLEILTTNAVATTCL--VPTLLSKLV--SELKSA---------NATVPSLRLVGYGGSraiAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 336 PVPLLEkwrsATGHTLLERYGMTEIG-MALSNPLTEARVP----GSVGTPLPGVEVRIISENpqKGSPyiihaegNERGT 410
Cdd:PRK05857 302 DVRFIE----ATGVRTAQVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAATD--GIGP-------TAPGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 411 KVTPGFeekeGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:PRK05857 369 GPSASF----GTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTWGQRV-TAVVALQEGHSLSHRDLKewaRGVLAPY-------AVPSELLLLEEIPRNQMGK 561
Cdd:PRK05857 443 IAEGVSGVREAACYEIPDEEFGALVgLAVVASAELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGK 519
|
570 580
....*....|....*....|
gi 1195733688 562 VNKKELLTQLYPSGQRSQPG 581
Cdd:PRK05857 520 VMRASLAAAATADKARVVVR 539
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-567 |
2.75e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.53 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRialidkygHHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12467 1592 ALVFGEQ--------ELTYGELNRRANRLAHRLIAL-----GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPAIYRGATEKPTEQPVKESGwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTQSHLQARL-PLPD--GLRSLVLDQEDDWLEGYSDSNPAVNLAP--QNLAYVIYTSGSTGRP 1733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPlHHVHGVVNKLLCPLWVGATCVMLPeFSAQQVWEKFLSS-EAPQIT 288
Cdd:PRK12467 1734 KGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQLIQLiERQQVT 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKLLDyYDKHFTQPRvqdfvravckeRIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGM----- 362
Cdd:PRK12467 1812 TLHFVPSMLQQLLQ-MDEQVEHPL-----------SLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVdvthw 1879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 363 ALSNPLTEARVPGSVGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETK 442
Cdd:PRK12467 1880 TCRRKDLEGRDSVPIGQPIANL------------STYILDASLNPVPIGVA-------GELYLGGVGLARGYLNRPALTA 1940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 443 SAFTSDGW-------FRTGDTavfkdARYwiRGRTSVDI-------IKTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:PRK12467 1941 ERFVADPFgtvgsrlYRTGDL-----ARY--RADGVIEYlgridhqVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA 2013
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 509 TWGQRVTAVVALQEG-------HSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 2014 NGKQLVAYVVPTDPGlvdddeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
197-567 |
3.02e-34 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 137.22 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGL--VHSWAWTKNDVILHVLPLHHV--HGVvnkllcPL--WVGATCVMLP-- 268
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 EFSAQQVwEKFLSSEAPQitVFMAVPTVYSKLLDYYDKHftQPRvqdfvravcKERIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK05620 258 DLSAPTL-AKIIATAMPR--VAHGVPTLWIQLMVHYLKN--PPE---------RMSLQEIYVGGSAVPPILIKAWEERYG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 HTLLERYGMTEIGMAlsnpltearvpGSVGTPLPGV--EVRIISENPQKGSP----YIIHAEGNergtkVTPGFEEKEGE 422
Cdd:PRK05620 324 VDVVHVWGMTETSPV-----------GTVARPPSGVsgEARWAYRVSQGRFPasleYRIVNDGQ-----VMESTDRNEGE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGPSVFREYWDKP----------------EETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSAL 485
Cdd:PRK05620 388 IQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGsVTRDGFLTIHDRAR-DVIRSGGEWIYSA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 486 EIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*
gi 1195733688 563 NKKEL 567
Cdd:PRK05620 547 DKKDL 551
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
49-567 |
3.83e-34 |
|
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: 134.74 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKvGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVP-GD----VVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpaiyrgatekPTEQPvkesgwrDRGAMIFYTSGTTGR 208
Cdd:cd17653 81 LPSARIQAILRTSGATLLL----------------------------------TTDSP-------DDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVT---GLVHSwawTKNDVILHVLPLHHVHGVvNKLLCPLWVGATCVmLPEFSAQqvwekfLSSEAP 285
Cdd:cd17653 120 PKGVMVPHRGVLNYVSqppARLDV---GPGSRVAQVLSIAFDACI-GEIFSTLCNGGTLV-LADPSDP------FAHVAR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 286 QITVFMAVPTVYSKLldyydkhftqpRVQDFvravckERIRLMVSGSAALPVPLLEKWRSatGHTLLERYGMTEIGMALS 365
Cdd:cd17653 189 TVDALMSTPSILSTL-----------SPQDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NPLTEARVPGSVGTPLPGVEVRIISENPQkgspyiihaegnergtkvtPGFEEKEGELLVRGPSVFREYWDKPEETKSAF 445
Cdd:cd17653 250 MTELLPGQPVTIGKPIPNSTCYILDADLQ-------------------PVPEGVVGEICISGVQVARGYLGNPALTASKF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 446 TSDGW------FRTGDTAVF-KDARYWIRGRTSVDIiKTGGYKVSALEIERHLLA-HPSIADVAVIGVPDmtwgqrvtAV 517
Cdd:cd17653 311 VPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNG--------RL 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1195733688 518 VALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17653 382 VAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
49-567 |
1.14e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.81 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRelydRSLCLAQEICRLQGCKVGDLQEervsflcsNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07867 20 RGLYFEDSFTSWREHIRGSAA----RAAALRARLDPTRPPHVGVLLD--------NTPEFSLLLGAAALSGIVPVGLNPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQrlGVPLLPL-TP------AIYRGATEKPTE-QPvkesgwrDRGAMIF 200
Cdd:PRK07867 88 RRGAALARDIAHADCQLVLTESAHAELLDGLDP--GVRVINVdSPawadelAAHRDAEPPFRVaDP-------DDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 201 YTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQvwekFL 280
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASG----FL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 281 sseaPQITVFMAVPTVY-SKLLDYYDKhfTQPRVQDfvravcKERIRLMVSGSAALPVPLlEKWRSATGHTLLERYGMTE 359
Cdd:PRK07867 235 ----PDVRRYGATYANYvGKPLSYVLA--TPERPDD------ADNPLRIVYGNEGAPGDI-ARFARRFGCVVVDGFGSTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 360 IGMALSNplTEARVPGSVGTPLPGVEVRiiseNPQKGS---PYIIHAEGNERGTKVTpgfeekeGELL-VRGPSVFREYW 435
Cdd:PRK07867 302 GGVAITR--TPDTPPGALGPLPPGVAIV----DPDTGTecpPAEDADGRLLNADEAI-------GELVnTAGPGGFEGYY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 436 DKPEETkSAFTSDGWFRTGDTAvFKDAR--YWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQR 513
Cdd:PRK07867 369 NDPEAD-AERMRGGVYWSGDLA-YRDADgyAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQ 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 514 VTAVVALQEGHSLSHRDLKEW--ARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07867 446 VMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
67-567 |
1.50e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 133.98 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQeICRLQGCKVGDLqeerVSFLCSNDISYVVAQWASWMSG--GVAVPLYWKHPEAqlEYFIQDSRSS 144
Cdd:PRK13390 26 SYRQLDDDSAALAR-VLYDAGLRTGDV----VALLSDNSPEALVVLWAALRSGlyITAINHHLTAPEA--DYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEylerLSPLAQRLGVPLlPLT-------------PAIYRGATEKPTEQPVkesgwrdrGAMIFYTSGTTGRPKG 211
Cdd:PRK13390 99 VLVASAA----LDGLAAKVGADL-PLRlsfggeidgfgsfEAALAGAGPRLTEQPC--------GAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 212 ALST--HRN-------LAAVVTGLvhsWAWTKNDVILHVLPLHHVH-----GVVNKLlcplwvGATCVMLPEFSAQQVW- 276
Cdd:PRK13390 166 IQPDlpGRDvdapgdpIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVVLAKRFDAQATLg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 --EKFlsseapQITVFMAVPTVYSKLLDYYDKHFTQPRVQDfvravckerIRLMVSGSAALPVPLLEKWRSATGHTLLER 354
Cdd:PRK13390 237 hvERY------RITVTQMVPTMFVRLLKLDADVRTRYDVSS---------LRAVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 355 YGMTEI-GMALSNPLTEARVPGSVGTPLpgvevriisenpqKGSPYIIHAEGNE--RGTKVTPGFEekegellvRGPSVF 431
Cdd:PRK13390 302 YSSTEAhGMTFIDSPDWLAHPGSVGRSV-------------LGDLHICDDDGNElpAGRIGTVYFE--------RDRLPF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 ReYWDKPEETKSAF--TSDGWFRTGDTAVFKDARY-WIRGRTSVDIIkTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:PRK13390 361 R-YLNDPEKTAAAQhpAHPFWTTVGDLGSVDEDGYlYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 509 TWGQRVTAVVALQEGHSLSH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK13390 439 EMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-583 |
3.49e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 136.24 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12316 529 ALAFGEETL--------DYAELNRRANRLAH---ALIERGVG--PDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVvGQEYLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKEsgwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLL-SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNP----ENLAYVIYTSGSTGKP 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVMLPE---FSAQQVWEkflSSEAPQ 286
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPgdhRDPAKLVE---LINREG 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 287 ITVFMAVPTVYSKLLDyydkhftQPRVQDFVravckeRIRLMVSGSAALPVPLLEK--WRSATGHtLLERYGMTE--IGM 362
Cdd:PRK12316 747 VDTLHFVPSMLQAFLQ-------DEDVASCT------SLRRIVCSGEALPADAQEQvfAKLPQAG-LYNLYGPTEaaIDV 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 363 ALSNPLTEARVPGSVGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKPEETK 442
Cdd:PRK12316 813 THWTCVEEGGDSVPIGRPIANL------------ACYILDANLEPVPVGVL-------GELYLAGRGLARGYHGRPGLTA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 443 SAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPdmtwGQRVT 515
Cdd:PRK12316 874 ERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLV 948
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 516 AVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELltqlyPSGQRSQPGQG 583
Cdd:PRK12316 949 GYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL-----PAPEASVAQQG 1011
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
53-567 |
1.87e-32 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 131.68 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 53 FGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKvgdlqEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEA 132
Cdd:PLN03102 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITK-----NDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 133 QLEYFIQDSRSSLVVVGQEYlerlSPLAQRLgVPLLPLT------PAIYRGATEKPTEQPVKESGWR---DRG------- 196
Cdd:PLN03102 102 SIAAILRHAKPKILFVDRSF----EPLAREV-LHLLSSEdsnlnlPVIFIHEIDFPKRPSSEELDYEcliQRGeptpslv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIF------------YTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnkllcplWV---- 260
Cdd:PLN03102 177 ARMFriqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 261 ----GATCVMLPEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLL--DYYDKHFTQPRVQdfvravckerirlMVSGSAA 334
Cdd:PLN03102 248 taarGGTSVCMRHVTAPEIYKNI---EMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVH-------------VLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 335 LPVPLLEKWRSaTGHTLLERYGMTE-IGMALSNPLTEA--RVPgsvgtplpgvEVRIISENPQKGSPYIIHAEGNERGTK 411
Cdd:PLN03102 312 PPAALVKKVQR-LGFQVMHAYGLTEaTGPVLFCEWQDEwnRLP----------ENQQMELKARQGVSILGLADVDVKNKE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 412 V---TPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVFK-DARYWIRGRtSVDIIKTGGYKVSALEI 487
Cdd:PLN03102 381 TqesVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDR-SKDIIISGGENISSVEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 488 ERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHS----------LSHRDLKEWARGVLAPYAVPSELLLLEEIPRN 557
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKN 538
|
570
....*....|
gi 1195733688 558 QMGKVNKKEL 567
Cdd:PLN03102 539 GNGKILKPKL 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-567 |
2.36e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.54 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAH---ALIARGVG--PEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLsPLAQrlGVPLLPLTPAiyRGATEKPTEQP-VKESGwrDRGAMIFYTSGTTG 207
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRL-PIPD--GLASLALDRD--EDWEGFPAHDPaVRLHP--DNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 208 RPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVM------LPEFSAQQVWEKfls 281
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLYAEIHEH--- 4783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 282 seapQITVFMAVPTVYSKLLdyydkhftqprvQDFVRAVCKERIRLMVSGSAALPVPLLEK-WRSATGHTLLERYGMTEi 360
Cdd:PRK12316 4784 ----RVTVLVFPPVYLQQLA------------EHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTE- 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 gmALSNPLTEARVPGS--------VGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFR 432
Cdd:PRK12316 4847 --TTVTVLLWKARDGDacgaaympIGTPLGNR------------SGYVLDGQLNPLPVGVA-------GELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 433 EYWDKPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:PRK12316 4906 GYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 504 GVPDMTWGQRVTAVVAlQEGHSLSH-------RD-LKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12316 4984 AQEGAVGKQLVGYVVP-QDPALADAdeaqaelRDeLKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-563 |
6.64e-32 |
|
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: 126.73 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTH----------RNLAAVV----TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATC 264
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 265 VMLPEFSAQQVWEkflSSEAPQITVFMAVPTVYSK-LLDYYDKhftqPRVQDFvravckERIRLMVSGSAALPVPLLEKW 343
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 344 RSATGH-TLLERYGMTEIGMALSnpltearvpGSVGTPLPGVEVRIiseNPQKGSPYIihaegNERGTKVTPGfEEKEGE 422
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFTGS---------GHSAGSGPETGPFT---RANPDTVVL-----DDDGRVVPPG-SGGVGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 423 LLVRGpSVFREYWDKPEETKSAF-TSDG--WFRTGDTA-VFKDARYWIRGRTSVdIIKTGGYKVSALEIERHLLAHPSIA 498
Cdd:cd05924 217 IARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRAtVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAVY 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 499 DVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVN 563
Cdd:cd05924 295 DVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
67-570 |
7.80e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 130.92 E-value: 7.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAqEICRLQGCKVGDlqeeRVsFLCSNDISYVVAQWASWMSGGVAVplYWKHPEAQLEYFI---QDSRS 143
Cdd:PRK06060 32 THGQIHDGAARLG-EVLRNRGLSSGD----RV-LLCLPDSPDLVQLLLACLARGVMA--FLANPELHRDDHAlaaRNTEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 144 SLVVVGQEYLERLSPLAQRLGVPLLPltpaiyRGATEKPTE-QPVkeSGwrDRGAMIFYTSGTTGRPKGALSTHRNLAAV 222
Cdd:PRK06060 104 ALVVTSDALRDRFQPSRVAEAAELMS------EAARVAPGGyEPM--GG--DALAYATYTSGTTGPPKAAIHRHADPLTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 223 VTGLV-HSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPqiTVFMAVPTVYSKLL 301
Cdd:PRK06060 174 VDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGP--SVLYGVPNFFARVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 302 DYYDKhftqprvqDFVRAVckeriRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEIGMA-LSNPLTEARvPGSVGT 379
Cdd:PRK06060 252 DSCSP--------DSFRSL-----RCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTfVSNRVDEWR-LGTLGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 380 PLPGVEVRIISENpqkgspyiihaegnerGTKVTPGFEekeGELLVRGPSVFREYWDKPEetkSAFTSDGWFRTGDTAVF 459
Cdd:PRK06060 318 VLPPYEIRVVAPD----------------GTTAGPGVE---GDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 460 KDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA--VVALQEGHSLS-HRDLKEWAR 536
Cdd:PRK06060 376 DSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAflVATSGATIDGSvMRDLHRGLL 455
|
490 500 510
....*....|....*....|....*....|....
gi 1195733688 537 GVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQ 570
Cdd:PRK06060 456 NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
55-567 |
2.75e-31 |
|
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: 126.43 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLAR---TLRGLGVA--PGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSrsslvvvgqeylerlsplaqrlGVPLLPLTPaiyrgatekpteqpvkesgwrDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17650 77 QYMLEDS----------------------GAKLLLTQP---------------------EDLAYVIYTSGTTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVvtglVHSWawtKNDVILHVLPLHHVHGV-------VNKLLCPLWVGATCVMLPE---FSAQQVWEKFLSSEa 284
Cdd:cd17650 114 EHRNVAHA----AHAW---RREYELDSFPVRLLQMAsfsfdvfAGDFARSLLNGGTLVICPDevkLDPAALYDLILKSR- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 285 pqITVFMAVPTVYSKLLDYYDKHFTQPrvqdfvravckERIRLMVSGS----AALPVPLLEKWRSATghTLLERYGMTEI 360
Cdd:cd17650 186 --ITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSdgckAQDFKTLAARFGQGM--RIINSYGVTEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 GMALS------NPLTEAR-VPgsVGTPLPGVEVRIISE--NPQKGSPYiihaegnergtkvtpgfeekeGELLVRGPSVF 431
Cdd:cd17650 251 TIDSTyyeegrDPLGDSAnVP--IGRPLPNTAMYVLDErlQPQPVGVA---------------------GELYIGGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 432 REYWDKPEETKSAFTSDGW------FRTGDTAVFK-DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:cd17650 308 RGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDEAVVAV 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 505 VPDMTWGQRVTA-VVAlqeGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17650 387 REDKGGEARLCAyVVA---AATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
145-570 |
3.50e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.45 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYLERLSPLAQRlGVPLLPLTPAIYRGATEKPTE-QPVKESGWRDRGAMIFyTSGTTGRPKGALSTHRNLAAVV 223
Cdd:PRK13388 102 LLVTDAEHRPLLDGLDLP-GVRVLDVDTPAYAELVAAAGAlTPHREVDAMDPFMLIF-TSGTTGAPKAVRCSHGRLAFAG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 224 TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQqvweKFLsseaPQITVFMAVPTVY-SKLLD 302
Cdd:PRK13388 180 RALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSAS----GFL----DDVRRYGATYFNYvGKPLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 303 YY-------DKHFTQPRVQdFvravckerirlmvsGSAALPVPLlEKWRSATGHTLLERYGMTEIGMALSNPltEARVPG 375
Cdd:PRK13388 252 YIlatperpDDADNPLRVA-F--------------GNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVVRE--PGTPPG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 376 SVGTPLPGVEVRiiseNPQKGSPYIIhAEGNERGTKVTPgfEEKEGELLVR-GPSVFREYWDKPEETKSAFtSDGWFRTG 454
Cdd:PRK13388 314 SIGRGAPGVAIY----NPETLTECAV-ARFDAHGALLNA--DEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 455 DTAvFKDARYWI--RGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLK 532
Cdd:PRK13388 386 DLA-YRDADGWIyfAGRTA-DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFA 463
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1195733688 533 EW--ARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQ 570
Cdd:PRK13388 464 AFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
55-567 |
4.01e-31 |
|
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: 126.40 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGDlqEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAH---YLQSLGVKS--ESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd17644 90 TYILEDAQISVLLTQPENL-------------------------------------------AYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILHVLPLhhVHGVVNKLLCPLWV-GATCVMLPE---FSAQQVWEKflsSEAPQITVF 290
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTLLsGATLVLRPEemrSSLEDFVQY---IQQWQLTVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 mAVPTVYSKLLdyydkhftqprVQDFVRAVCK--ERIRLMVSGSAALPVPLLEKWRSATGH--TLLERYGMTEIGMA--- 363
Cdd:cd17644 202 -SLPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAatv 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 364 --LSNPLTEARVPGSVGTPLPGVEVRIISENPQKgspyiihaegnergtkVTPGFEekeGELLVRGPSVFREYWDKPEET 441
Cdd:cd17644 270 crLTQLTERNITSVPIGRPIANTQVYILDENLQP----------------VPVGVP---GELHIGGVGLARGYLNRPELT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 442 KSAFTSDGW--------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQ 512
Cdd:cd17644 331 AEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 513 RVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17644 410 RLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
50-570 |
8.86e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 123.80 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PLN02479 30 AVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAK-RSIGPGST----VAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYL----ERLSPLAQRLG----VPLL-----------PLTPAIYRGATE--KPTEQPVK 188
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFtlaeEALKILAEKKKssfkPPLLivigdptcdpkSLQYALGKGAIEyeKFLETGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 189 ESGWR---DRGAMIF--YTSGTTGRPKGALSTHRN--LAAVVTGLVhsWAWTKNDVILHVLPLHHVHGvvnklLCPLWVG 261
Cdd:PLN02479 185 EFAWKppaDEWQSIAlgYTSGTTASPKGVVLHHRGayLMALSNALI--WGMNEGAVYLWTLPMFHCNG-----WCFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 262 A----TCVMLPEFSAQQVWEKFLSSeapQITVFMAVPTVYSKLLDY--YDKHFTQPRVqdfvravckerIRLMVSGSAal 335
Cdd:PLN02479 258 AalcgTNICLRQVTAKAIYSAIANY---GVTHFCAAPVVLNTIVNApkSETILPLPRV-----------VHVMTAGAA-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 336 PVPLLEKWRSATGHTLLERYGMTEIgmalSNPLTE-ARVPGSVGTPlPGVEVRIiseNPQKGSPYiIHAEG----NERGT 410
Cdd:PLN02479 322 PPPSVLFAMSEKGFRVTHTYGLSET----YGPSTVcAWKPEWDSLP-PEEQARL---NARQGVRY-IGLEGldvvDTKTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 411 KVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTAV-FKDARYWIRGRtSVDIIKTGGYKVSALEIER 489
Cdd:PLN02479 393 KPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVkHPDGYIEIKDR-SKDIIISGGENISSLEVEN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH-----RDLKEWARGVLAPYAVPSElLLLEEIPRNQMGKVNK 564
Cdd:PLN02479 471 VVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaalaEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQK 549
|
....*.
gi 1195733688 565 KELLTQ 570
Cdd:PLN02479 550 HVLRAK 555
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-567 |
9.94e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.45 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAH---RLIERGVG--PDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSsLVVVGQEYLErlspLAQRLGVPLLPLTPAIYRGATEKPTEQPVKESGwrdrgAMIFYTSGTTGR 208
Cdd:PRK12316 3141 YPEERLAYMLEDSGA-QLLLSQSHLR----LPLAQGVQVLDLDRGDENYAEANPAIRTMPENL-----AYVIYTSGSTGK 3210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMlpefSAQQVWEKFLSSEAPQIT 288
Cdd:PRK12316 3211 PKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVL----AGPEDWRDPALLVELINS 3285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKLLdyyDKHFTQPRVQDFVravckeRIRLMVSGSAALPVPLLEKWRSatGHTLLERYGMTE--IGMALSN 366
Cdd:PRK12316 3286 EGVDVLHAYPSML---QAFLEEEDAHRCT------SLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEatITVTHWQ 3354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 PLTEARVPGSVGTPLPGVEVRIISENpqkgspyiihaegnergtkVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFT 446
Cdd:PRK12316 3355 CVEEGKDAVPIGRPIANRACYILDGS-------------------LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFV 3415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 447 SDGW------FRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPdmtwGQRVTAVVAL 520
Cdd:PRK12316 3416 PDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVP 3491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1195733688 521 QEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12316 3492 EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
130-536 |
2.32e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 122.31 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFI----QDSRSSLVVVGQeyleRLSPLAQRLGVPLLPLTPAIYRGATEKPTEQpvkesgwrdrgAMIFYTSGT 205
Cdd:PRK09274 121 PKAHLARRLfgwgKPSVRRLVTVGG----RLLWGGTTLATLLRDGAAAPFPMADLAPDDM-----------AAILFTSGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 206 TGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnkllcplwVGATCVmLPEFSA--------QQVW- 276
Cdd:PRK09274 186 TGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMDPtrpatvdpAKLFa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 --EKFlsseapQITVFMAVPTVYSKLLDYydkhftqprvqdfvravCKER------IRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK09274 257 aiERY------GVTNLFGSPALLERLGRY-----------------GEANgiklpsLRRVISAGAPVPIAVIERFRAMLP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 HT--LLERYGMTE------IGM-ALSNPLTEARVPGS---VGTPLPGVEVRII--SENPqkgspyIIHAEGNERgtkVTP 414
Cdd:PRK09274 314 PDaeILTPYGATEalpissIESrEILFATRAATDNGAgicVGRPVDGVEVRIIaiSDAP------IPEWDDALR---LAT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAVFKD-ARYWIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:PRK09274 385 G---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKA-HRVETAGGTLYTIPCER 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTwGQRVTAVVALQEGHSLS----HRDLKEWAR 536
Cdd:PRK09274 461 IFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSksalYQELRALAA 510
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
194-565 |
4.16e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.11 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdptda 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 EFSAQQVwEKFlsseapQITVFMAVPTvyskLLDYYDKHftqPRVQ--DFvravckERIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PRK08633 862 LGIAKLV-AKH------RATILLGTPT----FLRLYLRN---KKLHplMF------ASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 TGHTLLERYGMTEIG--MALSNPLTEAR--------VPGSVGTPLPGVEVRIIseNPqkgspyiihaegnERGTKVTPGf 416
Cdd:PRK08633 922 FGIRILEGYGATETSpvASVNLPDVLAAdfkrqtgsKEGSVGMPLPGVAVRIV--DP-------------ETFEELPPG- 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 eeKEGELLVRGPSVFREYWDKPEETKSAFT---SDGWFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVS--ALEIERH 490
Cdd:PRK08633 986 --EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLdEDGFLTITDRYS-RFAKIGGEMVPlgAVEEELA 1062
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 491 LLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS-HRDLKEwarGVLAPYAVPSELLLLEEIPRNQMGKVNKK 565
Cdd:PRK08633 1063 KALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEElKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
201-567 |
5.39e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.24 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 201 YTSGTTGRPKGALSTHRNLAAvvtGLVHSWAWTKNDVI-----LHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQV 275
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVA---NLCSSLFSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEKFLSSEapqITVFMAVPTVYSKLLdyydkhfTQPRVQDFvrAVCKERIRLMVSGSAALPVPLLEKWRSA-TGHTLLER 354
Cdd:PLN02330 268 LNALITQE---VSFAPIVPPIILNLV-------KNPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEAKfPGVQVQEA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 355 YGMTE---IGMALSNPLTEARVP--GSVGTPLPGVEVRIIseNPQKGSPYiihaegnergTKVTPGfeekegELLVRGPS 429
Cdd:PLN02330 336 YGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKFI--DPDTGRSL----------PKNTPG------ELCVRSQC 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 430 VFREYWDKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDM 508
Cdd:PLN02330 398 VMQGYYNNKEETDRTIDEDGWLHTGDIGyIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 509 TWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
67-504 |
8.16e-29 |
|
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: 120.99 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd17641 13 TWADYADRVRAFALGLLAL-GVGRGD----VVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVG-QEYLERLSPLAQRlgVPLLPLTpaIY---RG--------------ATEKPTEQPVKESGWRDRG---------AMI 199
Cdd:cd17641 88 IAEdEEQVDKLLEIADR--IPSVRYV--IYcdpRGmrkyddprlisfedVVALGRALDRRDPGLYEREvaagkgedvAVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 200 FYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGaTCVMLPE---------- 269
Cdd:cd17641 164 CTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 -------FSAQQVWEKFLS------SEAPQITVFM--AVPTVYSKLLDYYDKHFTQPRVQDFVRAVCKE----------- 323
Cdd:cd17641 243 eigptfvLLPPRVWEGIAAdvrarmMDATPFKRFMfeLGMKLGLRALDRGKRGRPVSLWLRLASWLADAllfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 324 --RIRLMVSGSAALPvPLLEKWRSATGHTLLERYGMTEI-GMALSNPLTEARvPGSVGTPLPGVEVRIIsenpqkgspyi 400
Cdd:cd17641 323 fsRLRSAATGGAALG-PDTFRFFHAIGVPLKQLYGQTELaGAYTVHRDGDVD-PDTVGVPFPGTEVRID----------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 401 ihaegnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYW-IRGRTSvDIIKTG- 478
Cdd:cd17641 390 ------------------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLvVIDRAK-DVGTTSd 450
|
490 500
....*....|....*....|....*.
gi 1195733688 479 GYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
145-455 |
9.36e-29 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 121.36 E-value: 9.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 145 LVVVGQEYlERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPVKEsgwrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVT 224
Cdd:PLN02736 177 IVVVGGAD-EPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKP----EDVATICYTSGTTGTPKGVVLTHGNLIANVA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 225 GLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpEFSAQQVWEKFLSSEAPQITVFMAVPTVYSKLldyY 304
Cdd:PLN02736 252 GSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNLKLMDDLAALRPTIFCSVPRLYNRI---Y 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 305 DKHFTQPR----------------------------------VQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHT 350
Cdd:PLN02736 324 DGITNAVKesgglkerlfnaaynakkqalengknpspmwdrlVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGR 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 351 LLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIIS----ENPQKGSPYiihaegnergtkvtpgfeeKEGELLVR 426
Cdd:PLN02736 404 VLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemNYTSEDQPY-------------------PRGEICVR 464
|
330 340
....*....|....*....|....*....
gi 1195733688 427 GPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
199-562 |
1.20e-28 |
|
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: 120.74 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSThrnlaavvTG--LVHSWAWTKNdvilhVLPLH----------------HVHGVVNKLLCplwv 260
Cdd:cd05966 236 ILYTSGSTGKPKGVVHT--------TGgyLLYAATTFKY-----VFDYHpddiywctadigwitgHSYIVYGPLAN---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 261 GATCVML------PEFSaqQVWEKFlssEAPQITVFMAVPTVYSKLLDYYDKHFTQprvqdfvravcKERIRLMVSGSAA 334
Cdd:cd05966 299 GATTVMFegtptyPDPG--RYWDIV---EKHKVTIFYTAPTAIRALMKFGDEWVKK-----------HDLSSLRVLGSVG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 335 LPV-PllEKWRSATGHTLLER------YGMTEIGMALSNPL---TEARvPGSVGTPLPGVEvriisenpqkgsPYIIHAE 404
Cdd:cd05966 363 EPInP--EAWMWYYEVIGKERcpivdtWWQTETGGIMITPLpgaTPLK-PGSATRPFFGIE------------PAILDEE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 405 GNERGTkvtpgfeEKEGELLVRG--PSVFREYWDKPEETKSAFTSD--GWFRTGDTAVF-KDARYWIRGRTSvDIIKTGG 479
Cdd:cd05966 428 GNEVEG-------EVEGYLVIKRpwPGMARTIYGDHERYEDTYFSKfpGYYFTGDGARRdEDGYYWITGRVD-DVINVSG 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 480 YKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHR---DLKEWARGVLAPYAVPSELLLLEEIPR 556
Cdd:cd05966 500 HRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPK 579
|
....*.
gi 1195733688 557 NQMGKV 562
Cdd:cd05966 580 TRSGKI 585
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
55-567 |
2.27e-28 |
|
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: 118.35 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKvgdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFL-REKGVK----KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSlVVVGQEYLErlSPLAQRlGVPLLPLTPAIYRGATEKpteqpVKESGWRDRGAMIFYTSGTTGRPKGALS 214
Cdd:cd17656 78 IYIMLDSGVR-VVLTQRHLK--SKLSFN-KSTILLEDPSISQEDTSN-----IDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVT-GLVHSWAWTKNDVILHVLPLHHV--HGVVNKLLcplwVGATCVMLPEFSAQQVWE--KFLSSEAPQITV 289
Cdd:cd17656 149 EHKNMVNLLHfEREKTNINFSDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQlfDLVKRHNIEVVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 290 FmavPTVYSKLLdyYDKHFTQPRVQDFVRAVCKERIRLMVSGsaalpvPLLEKWRSATGHtLLERYGMTE---IGMALSN 366
Cdd:cd17656 225 L---PVAFLKFI--FSEREFINRFPTCVKHIITAGEQLVITN------EFKEMLHEHNVH-LHNHYGPSEthvVTTYTIN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 PLTEARVPGSVGTPLPGVEVRIISENPQ---KGSPyiihaegnergtkvtpgfeekeGELLVRGPSVFREYWDKPEETKS 443
Cdd:cd17656 293 PEAEIPELPPIGKPISNTWIYILDQEQQlqpQGIV----------------------GELYISGASVARGYLNRQELTAE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 444 AFTSDGW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTA 516
Cdd:cd17656 351 KFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 517 -VVALQEghsLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17656 430 yFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
49-567 |
2.70e-28 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 118.41 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRL---QGCKVGdlqeerVSFLCSndISYVVAQWASWMSGGVAVPL 125
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLgvgPGVFVP------LCFEKS--KWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 126 YWKHPEAQLEYFIQDSRSSLVVvgqeylerlsplaqrlgvpllpltpaiyrgatekpTEQPvkesgwrDRGAMIFYTSGT 205
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVL-----------------------------------TSSP-------SDAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 206 TGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLplHHVHGV-VNKLLCPLWVGAT-CVM--------LPEFSAQQv 275
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYTFDVsILEIFTTLAAGGClCIPseedrlndLAGFINRL- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 wekflsseapQITVFMAVPTVySKLLDyydkhftqPrvQDFVRavckerIRLMVSGSAALPVPLLEKWrsATGHTLLERY 355
Cdd:cd05918 195 ----------RVTWAFLTPSV-ARLLD--------P--EDVPS------LRTLVLGGEALTQSDVDTW--ADRVRLINAY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 GMTE--IGMALSNPLTEARvPGSVGTPLPGVevriisenpqkgsPYIIHAEGNERgtKVTPGFEekeGELLVRGPSVFRE 433
Cdd:cd05918 246 GPAEctIAATVSPVVPSTD-PRNIGRPLGAT-------------CWVVDPDNHDR--LVPIGAV---GELLIEGPILARG 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 434 YWDKPEETKSAFTSD-GW------------FRTGD--------TAVF---KDARYWIRG-RtsVDIiktggykvsaLEIE 488
Cdd:cd05918 307 YLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDlvrynpdgSLEYvgrKDTQVKIRGqR--VEL----------GEIE 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 489 RHLLAHPSIADVAVIGV---PDMTWGQRVTAVVALQEGHSLSH-----------------RDLKEWARGVLAPYAVPSEL 548
Cdd:cd05918 375 HHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefralvAELRSKLRQRLPSYMVPSVF 454
|
570
....*....|....*....
gi 1195733688 549 LLLEEIPRNQMGKVNKKEL 567
Cdd:cd05918 455 LPLSHLPLTASGKIDRRAL 473
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
202-567 |
7.08e-28 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 116.63 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRNLAAVVTGL--------VHSwawtkndviLHVLPLHHVHGVVnKLLCPLWVGATCVMLPefsaq 273
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFqryfqlqqVNS---------FCVLPLYHVSGLM-QFMRSFLTGGKLVILP----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 274 qvWEKFLSSEAPQITV---FMA-VPTVYSKLLdyydkhftQPRVQ---DFvRAVckerirlMVSGSAALPvPLLEKWRSA 346
Cdd:PRK07445 193 --YKRLKSGQELPPNPsdfFLSlVPTQLQRLL--------QLRPQwlaQF-RTI-------LLGGAPAWP-SLLEQARQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 tGHTLLERYGMTEIGMALSNPLTEARVPG--SVGTPLPGVEVRIisENPQKGspyIIHaegnergtkvtpgfeekegell 424
Cdd:PRK07445 254 -QLRLAPTYGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITI--PANQTG---NIT---------------------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 VRGPSVFREYWdkPEetksAFTSDGWFRTGDTAVF-KDARYWIRGRTSVDIIkTGGYKVSALEIERHLLAHPSIADVAVI 503
Cdd:PRK07445 306 IQAQSLALGYY--PQ----ILDSQGIFETDDLGYLdAQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLVQDVCVL 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 504 GVPDMTWGQRVTAVVALQEGhSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK07445 379 GLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
58-567 |
9.23e-27 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 115.91 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 58 ALIDKYGHHTYRELYDRSLCLAQEIcRLQGCKVGD---LQEERVSFLcsndisyVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLL-RERGVKPGDsvaVALPRSVFL-------TLALHAIVEAGAAWLPLDTGYPDDRL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLERLSplaqrlGVPLLplTPAIYRGATEKPTEQPVKESGWRDrGAMIFYTSGTTGRPKGALS 214
Cdd:PRK10252 548 KMMLEDARPSLLITTADQLPRFA------DVPDL--TSLCYNAPLAPQGAAPLQLSQPHH-TAYIIFTSGSTGRPKGVMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRnlaAVVTGLV---HSWAWTKNDVILHVLPL-HHVHgvVNKLLCPLWVGATCVML-PEFSAQQVW-EKFLSSEApqIT 288
Cdd:PRK10252 619 GQT---AIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAePEAHRDPLAmQQFFAEYG--VT 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 289 VFMAVPTVYSKlldyydkhFTQPRVQDFVRAVCKERIRLMVSGSaALPVPLLEKWRSATGHTLLERYGMTEIGMALS--- 365
Cdd:PRK10252 692 TTHFVPSMLAA--------FVASLTPEGARQSCASLRQVFCSGE-ALPADLCREWQQLTGAPLHNLYGPTEAAVDVSwyp 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 -NPLTEARVPGS---VGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPGFeekEGELLVRGPSVFREYWDKPEET 441
Cdd:PRK10252 763 aFGEELAAVRGSsvpIGYPVWNTGLRIL----------------DARMRPVPPGV---AGDLYLTGIQLAQGYLGRPDLT 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 442 KSAFTSDGW------FRTGDTAVFKD---ARYWirGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVA----VIGVPDM 508
Cdd:PRK10252 824 ASRFIADPFapgermYRTGDVARWLDdgaVEYL--GR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAA 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 509 TWG---QRVTAVVAlQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK10252 901 TGGdarQLVGYLVS-QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
67-570 |
3.32e-26 |
|
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: 111.76 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLGVQAGDF----VAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALSTHRNLAAVVTGL 226
Cdd:cd05937 83 IVDPDDP-------------------------------------------AILIYTSGTTGLPKAAAISWRRTLVTSNLL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 227 VHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVPTVYSKLLDY--- 303
Cdd:cd05937 120 SHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGA---TIIQYVGELCRYLLSTpps 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 304 -YDKhftQPRVQdfvravckerirlMVSGSAALPvPLLEKWRsatghtllERYGMTEIG---------MALSNPLTEARV 373
Cdd:cd05937 197 pYDR---DHKVR-------------VAWGNGLRP-DIWERFR--------ERFNVPEIGefyaategvFALTNHNVGDFG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 374 PGSVGtpLPGVEVRIISEN--------PQKGSPYiihaEGNERGTKVTPGFEEkEGELLVRGP----SVFREYWDKPEET 441
Cdd:cd05937 252 AGAIG--HHGLIRRWKFENqvvlvkmdPETDDPI----RDPKTGFCVRAPVGE-PGEMLGRVPfknrEAFQGYLHNEDAT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 442 KSAFTS------DGWFRTGDtAVFKDA--RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV--PDMTwG 511
Cdd:cd05937 325 ESKLVRdvfrkgDIYFRTGD-LLRQDAdgRWYFLDRLG-DTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvPGHD-G 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 512 QRVTAVVALQEGHS----LSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQ 570
Cdd:cd05937 402 RAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
67-562 |
1.44e-25 |
|
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: 111.04 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd05968 93 TYGELLYEVKRLANGLRAL-GVGKGD----RVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLER---LSPLA------------------QRLGVPLLPlTPAIYRGATE-KPTEQPVKESGWRDRGAMIFYTSG 204
Cdd:cd05968 168 ITADGFTRRgreVNLKEeadkacaqcptvekvvvvRHLGNDFTP-AKGRDLSYDEeKETAGDGAERTESEDPLMIIYTSG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 205 TTGRPKGALSTHRNL---AAVvtGLVHSWAWTKNDVILHVLPLHHVHGVVnKLLCPLWVGATCVM---LPEF-SAQQVWE 277
Cdd:cd05968 247 TTGKPKGTVHVHAGFplkAAQ--DMYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHpKADRLWR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 kflSSEAPQITVFMAVPTVYSKLldyydkhftQPRVQDFVRAvcKERIRLMVSGSAALPVPLlEKWRSATGHTLLERY-- 355
Cdd:cd05968 324 ---MVEDHEITHLGLSPTLIRAL---------KPRGDAPVNA--HDLSSLRVLGSTGEPWNP-EPWNWLFETVGKGRNpi 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 ----GMTEI-GMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgspyiihaegNERGTKVTPgfeeKEGELLVRGP-- 428
Cdd:cd05968 389 inysGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL----------------DESGKPARP----EVGELVLLAPwp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 429 SVFREYWDKPEETKSAFTS--DGWFRTGDTAVFKDARYW-IRGRtSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV 505
Cdd:cd05968 449 GMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFyILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 506 PDMTWGQRVTAVVALQEGHSLSHRDLKEWARGV---LAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:cd05968 528 PHPVKGEAIVCFVVLKPGVTPTEALAEELMERVadeLGKPLSPERILFVKDLPKTRNAKV 587
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
67-469 |
2.25e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 110.84 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRL---QGCKVGDLQEERVSFLCSndisyvvaQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRS 143
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELgltKGSNVAIYEETRWEWLAS--------IYGIWSQSMVAATVYANLGEDALAYALRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 144 SLVVVGQE--------------------YLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEqPVKESGWRDRGAMIFYTS 203
Cdd:PTZ00216 195 KAIVCNGKnvpnllrlmksggmpnttiiYLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHH-PLNIPENNDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 204 GTTGRPKGALSTHRNLAAVVTGLVHSWawtkNDVI---------LHVLPLHHV--HGVVNKLL---CPLWVGAT------ 263
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEDRL----NDLIgppeedetyCSYLPLAHImeFGVTNIFLargALIGFGSPrtltdt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 264 ----CVMLPEFSaqqvwekflsseaPqiTVFMAVPTVY--------SKL----------------------LDYYDKHFT 309
Cdd:PTZ00216 350 farpHGDLTEFR-------------P--VFLIGVPRIFdtikkaveAKLppvgslkrrvfdhayqsrlralKEGKDTPYW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 310 QPRVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGhTLLERYGMTEI----GMALSNPLTearvPGSVGTPLPGVE 385
Cdd:PTZ00216 415 NEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTETvccgGIQRTGDLE----PNAVGQLLKGVE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 386 VRIISENPQKgspyiiHAEgnergtkvTPgfeEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVF-KDARY 464
Cdd:PTZ00216 490 MKLLDTEEYK------HTD--------TP---EPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTL 552
|
....*
gi 1195733688 465 WIRGR 469
Cdd:PTZ00216 553 RIIGR 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
50-567 |
4.98e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.03 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK05691 1141 ARQTPERIALVWDGGSLDYAELHAQANRLAH---YLRDKGVG--PDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAIYrgatekPTEQP-VKESGwrDRGAMIFYTSGTTGR 208
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSW------PSQAPgLHLHG--DNLAYVIYTSGSTGQ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 209 PKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVML-------PEFSAQQVwekfls 281
Cdd:PRK05691 1288 PKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI-SFDVSVWECFWPLITGCRLVLAgpgehrdPQRIAELV------ 1360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 282 sEAPQITVFMAVPTVYSKLLDyydkhftQPRVQDfvravCKeRIRLMVSGSAALPVPLLEKWRSA-TGHTLLERYGMTEI 360
Cdd:PRK05691 1361 -QQYGVTTLHFVPPLLQLFID-------EPLAAA-----CT-SLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTET 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 361 GMALSNPLTEA----RVPgsVGTPLPGVEVRIISenpqkgspyiihAEGNErgtkVTPGFeekEGELLVRGPSVFREYWD 436
Cdd:PRK05691 1427 AINVTHWQCQAedgeRSP--IGRPLGNVLCRVLD------------AELNL----LPPGV---AGELCIGGAGLARGYLG 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 437 KPEETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRTSVDiIKTGGYKVSALEIERHLLAHPSIADVAVIgVPDM 508
Cdd:PRK05691 1486 RPALTAERFVPDPLgedgarlYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREG 1563
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 509 TWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK05691 1564 AAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
62-576 |
7.18e-25 |
|
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: 108.34 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 62 KYGHHTYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPlywkhpeaqleyfiqds 141
Cdd:cd05908 12 KEKFVSYRHLREEALGYLGAL-QELGIKPGQ----EVVFQITHNNKFLYLFWACLLGGMIAVP----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 142 rsslVVVG--QEYLERLSPLAQRLGVPLLPltpaiyrgATEKPTEQpvkesgWRDRGAMIFYTSGTTGRPKGALSTHRNL 219
Cdd:cd05908 70 ----VSIGsnEEHKLKLNKVWNTLKNPYLI--------TEEEVLCE------LADELAFIQFSSGSTGDPKGVMLTHENL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 220 AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP--EFSAQQV-WEKFLSSEAPQITvfmAVPTV 296
Cdd:cd05908 132 VHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPtrLFIRRPIlWLKKASEHKATIV---SSPNF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 297 YSKlldYYDKHFTQPRVQDfvraVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSNP--- 367
Cdd:cd05908 209 GYK---YFLKTLKPEKAND----WDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRnailpvYGLAEASVGASLPkaq 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 368 -------------LTEARVPG------------SVGTPLPGVEVRIISE-NPQKGSPYIIHAEgnERGTKVTPGfeekeg 421
Cdd:cd05908 282 spfktitlgrrhvTHGEPEPEvdkkdsecltfvEVGKPIDETDIRICDEdNKILPDGYIGHIQ--IRGKNVTPG------ 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 422 ellvrgpsvfreYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHL--LAHPSIAD 499
Cdd:cd05908 354 ------------YYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREK-DIIFVNGQNVYPHDIERIAeeLEGVELGR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALqegHSLSHRDLKEWARGV------LAPYAVpSELLLLEEIPRNQMGKVNKKElLTQLYP 573
Cdd:cd05908 421 VVACGVNNSNTRNEEIFCFIE---HRKSEDDFYPLGKKIkkhlnkRGGWQI-NEVLPIRRIPKTTSGKVKRYE-LAQRYQ 495
|
...
gi 1195733688 574 SGQ 576
Cdd:cd05908 496 SGE 498
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
49-545 |
1.00e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 108.42 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRslclAQEICRL---QGCKVGDLqeerVSFLCSNDISYVVAqWASWMSGGVAVPL 125
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNAR----ANRYAHWaaaRGVGKGDV----VALLMENRPEYLAA-WLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 126 YWKHPEAQ-LEYFIQDSRSSLVVVGQEYLERLSPLAQ--RLGVPLLPLTPAIY----------RGATEKPTEQPVKESG- 191
Cdd:PRK08279 117 LNTQQRGAvLAHSLNLVDAKHLIVGEELVEAFEEARAdlARPPRLWVAGGDTLddpegyedlaAAAAGAPTTNPASRSGv 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 -WRDRgAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF 270
Cdd:PRK08279 197 tAKDT-AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 SAQQVWEKFlssEAPQITVFMAVPTVYSKLLDYydkhftQPRVQDfvRAvckERIRLMVsgSAALPVPLLEKWRSATG-H 349
Cdd:PRK08279 276 SASRFWDDV---RRYRATAFQYIGELCRYLLNQ------PPKPTD--RD---HRLRLMI--GNGLRPDIWDEFQQRFGiP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 TLLERYGMTEIGMALSNPLTearVPGSVG-TPLPGVE-VRIISENPQKGSPyIIHAEGneRGTKVTPGfeekE-GELLV- 425
Cdd:PRK08279 340 RILEFYAASEGNVGFINVFN---FDGTVGrVPLWLAHpYAIVKYDVDTGEP-VRDADG--RCIKVKPG----EvGLLIGr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 426 ---RGPsvFREYWDkPEETKS-----AFT-SDGWFRTGDTAVFKDARYWirgrTSVDII------KtgGYKVSALEIERH 490
Cdd:PRK08279 410 itdRGP--FDGYTD-PEASEKkilrdVFKkGDAWFNTGDLMRDDGFGHA----QFVDRLgdtfrwK--GENVATTEVENA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 491 LLAHPSIADVAVIGV--PDMTwGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVP 545
Cdd:PRK08279 481 LSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
199-562 |
1.19e-24 |
|
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: 108.56 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKG----------ALS-THRNLAAVVTGlvHSWaWTKNDVILHVLPLHHVHGvvnkllcPLWVGATCVM- 266
Cdd:cd05967 235 ILYTSGTTGKPKGvvrdngghavALNwSMRNIYGIKPG--DVW-WAASDVGWVVGHSYIVYG-------PLLHGATTVLy 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 267 --LPEFS--AQQVW---EKFlsseapQITVFMAVPTVYsKLLDYYDKHftqprvQDFVRAVCKERIRLMVSGSAALPVPL 339
Cdd:cd05967 305 egKPVGTpdPGAFWrviEKY------QVNALFTAPTAI-RAIRKEDPD------GKYIKKYDLSSLRTLFLAGERLDPPT 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 340 LEKWRSATGHTLLERYGMTEIGMALS-NPLTEARVP---GSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTPG 415
Cdd:cd05967 372 LEWAENTLGVPVIDHWWQTETGWPITaNPVGLEPLPikaGSPGKPVPGYQVQVLDED----------------GEPVGPN 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 416 feeKEGELLVRGP---SVFREYWDKPEETKSAF--TSDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIER 489
Cdd:cd05967 436 ---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYlFIMGRTD-DVINVAGHRLSTGEMEE 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 490 HLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS----HRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-567 |
1.33e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.48 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRIAlidkyghhTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH 129
Cdd:PRK12467 3113 ALVFGDQQL--------SYAELNRRANRLAH---RLIAIGVG--PDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 130 PEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAIYRGATEKPTEQPvkesgwrDRGAMIFYTSGTTGRP 209
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMG-------ENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 210 KGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHhVHGVVNKLLCPLWVGATCVMLP--EFSAQQVWEKFLsseAPQI 287
Cdd:PRK12467 3253 KGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS-FDGAQERFLWTLICGGCLVVRDndLWDPEELWQAIH---AHRI 3328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 288 TVFMAVPTvysklldyydkhFTQPRVQDFVRAVCKeRIRLMVSGSAALPVPLLEKWRSATGHT-LLERYGMTEigmALSN 366
Cdd:PRK12467 3329 SIACFPPA------------YLQQFAEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTE---AVVT 3392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 PL----TEARVPGS----VGTPLPGVevriisenpqkgSPYIIHAEGNERGTKVTpgfeekeGELLVRGPSVFREYWDKP 438
Cdd:PRK12467 3393 VTlwkcGGDAVCEApyapIGRPVAGR------------SIYVLDGQLNPVPVGVA-------GELYIGGVGLARGYHQRP 3453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 439 EETKSAFTSDGW-------FRTGDTAVFK-DARYWIRGRtsVD-IIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:PRK12467 3454 SLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG 3531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 510 WGQRVTAVVALQEGhslshRDLKEWARGVLAP----YAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK12467 3532 GKQLVAYVVPADPQ-----GDWRETLRDHLAAslpdYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
160-567 |
2.44e-24 |
|
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: 105.73 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 160 AQRLGVPLLP----LTPAIYRGATE--KPTEQPVKESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAvvtGLVHSWAWT 233
Cdd:cd05974 45 AMKLGAVVIPattlLTPDDLRDRVDrgGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPV---GHLSTMYWI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 234 ---KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML--PEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhf 308
Cdd:cd05974 122 glkPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAAL---VRYGVTTLCAPPTVWRMLIQ------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 309 tqprvQDFVRAvcKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRI 388
Cdd:cd05974 193 -----QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 389 ISenpqkgspyiihAEGNErgtkvtpgfeEKEGELLV-----RGPSVFREYWDKPEETKSAFtSDGWFRTGDTAVF-KDA 462
Cdd:cd05974 266 LD------------PDGAP----------ATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRdEDG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 463 RYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWARGVL 539
Cdd:cd05974 323 YLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPetaLEIFRFSRERL 401
|
410 420
....*....|....*....|....*...
gi 1195733688 540 APYAVPSELLLLeEIPRNQMGKVNKKEL 567
Cdd:cd05974 402 APYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
67-455 |
5.12e-24 |
|
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: 106.39 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLV 146
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQPVRPGD----FVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 VVGQEYLerlsPLAQRL------------------------------------GVPLLPLTPAIYRGATEKPTEQPVKES 190
Cdd:cd17632 145 AVSAEHL----DLAVEAvleggtpprlvvfdhrpevdahraalesarerlaavGIPVTTLTLIAVRGRDLPPAPLFRPEP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 191 GwRDRGAMIFYTSGTTGRPKGALSTHRNLAAvvtglvhswAWTKND----------VILHVLPLHHVHGvVNKLLCPLWV 260
Cdd:cd17632 221 D-DDPLALLIYTSGSTGTPKGAMYTERLVAT---------FWLKVSsiqdirppasITLNFMPMSHIAG-RISLYGTLAR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 261 GATCVMLPEFSAQQVWEKFlsSEAPQITVFMaVPTVYSKLLDYY----DKHFTQPRVQDF----VRAVCKERI---RLM- 328
Cdd:cd17632 290 GGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCDMLFQRYqaelDRRSVAGADAETlaerVKAELRERVlggRLLa 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 329 -VSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNpltearvpGSVGTPlPGVEVRIIsENPQKG-----SPYiih 402
Cdd:cd17632 367 aVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILD--------GVIVRP-PVLDYKLV-DVPELGyfrtdRPH--- 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1195733688 403 aegnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:cd17632 434 ----------------PRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD 470
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
197-504 |
1.80e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 104.74 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVL---PLHHVHGVvNKLLCP-LWVGATCVM-----L 267
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMGG-NANFNGlLWGGGTLYIddgkpL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 PEFSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqprvQDFVRAVCKERIRLMVSGSAALPVPLLEKWR--- 344
Cdd:PRK12582 302 PGMFEETI--RNLREISP--TVYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQala 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 345 -SATGH--TLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqKGSPYiihaegnergtkvtpgfeekeg 421
Cdd:PRK12582 371 vRTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP----VGDKY---------------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 422 ELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIR-----GRTSVDIIKTGGYKVSALEIERHLLA--H 494
Cdd:PRK12582 425 EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDFKLSTGTWVSVGTLRPDAVAacS 504
|
330
....*....|
gi 1195733688 495 PSIADVAVIG 504
Cdd:PRK12582 505 PVIHDAVVAG 514
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
61-504 |
1.91e-23 |
|
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: 104.36 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 61 DKYGHHTYRELYDRslclaqeiCRLQG---CKVGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKH-PEAqLEY 136
Cdd:cd05933 4 DKWHTLTYKEYYEA--------CRQAAkafLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNsPEA-CQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 137 FIQDSRSSLVVVG-----------QEYLERLSPLAQrLGVPLLPLTPAIY------RGATEKPTEQ--PVKESGWRDRGA 197
Cdd:cd05933 75 VAETSEANILVVEnqkqlqkilqiQDKLPHLKAIIQ-YKEPLKEKEPNLYswdefmELGRSIPDEQldAIISSQKPNQCC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNL----AAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGAtCVMLPEFSAQ 273
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYFAQPDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 274 QvWEKFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQP---RVQDFVRA---VCKERIRLMVSGSaalPVPL-------- 339
Cdd:cd05933 233 K-GTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSgtlKRKIASWAkgvGLETNLKLMGGES---PSPLfyrlakkl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 340 -LEKWRSATG----HTLL----------------------ERYGMTEIGMA--LSNPltEARVPGSVGTPLPGVEVRIIS 390
Cdd:cd05933 309 vFKKVRKALGldrcQKFFtgaapisretlefflslnipimELYGMSETSGPhtISNP--QAYRLLSCGKALPGCKTKIHN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 391 ENpqkgspyiihAEGNergtkvtpgfeekeGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARY-WIRGR 469
Cdd:cd05933 387 PD----------ADGI--------------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFlYITGR 442
|
490 500 510
....*....|....*....|....*....|....*.
gi 1195733688 470 TSVDIIKTGGYKVSALEIERHLLAH-PSIADVAVIG 504
Cdd:cd05933 443 IKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
55-567 |
4.99e-23 |
|
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: 101.86 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQL 134
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLAR---HLRGKGVK--PDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 135 EYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGALS 214
Cdd:cd17645 88 AYMLADSSAKILLTNPDDL-------------------------------------------AYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 215 THRNLAAVVTGLVHSWAWTKNDVILhVLPLHHVHGVVNKLLCPLWVGATCVMLPEfsaqqvwEKFLSSEapqitvfmavp 294
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSL-VYASFSFDASAWEIFPHLTAGAALHVVPS-------ERRLDLD----------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 295 tvysKLLDYYDKH-----FTQPRVQDFVRAVCKERIRLMVSGSAALPVpLLEKwrsatGHTLLERYGMTEIG-MALSNPL 368
Cdd:cd17645 186 ----ALNDYFNQEgitisFLPTGAAEQFMQLDNQSLRVLLTGGDKLKK-IERK-----GYKLVNNYGPTENTvVATSFEI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 369 TEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnerGTKVTPgfEEKEGELLVRGPSVFREYWDKPEETKSAFTSD 448
Cdd:cd17645 256 DKPYANIPIGKPIDNTRVYILDE-----------------ALQLQP--IGVAGELCIAGEGLARGYLNRPELTAEKFIVH 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 449 GW------FRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQ 521
Cdd:cd17645 317 PFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1195733688 522 EghSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17645 396 E--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
67-570 |
8.55e-23 |
|
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: 101.28 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEIcRLQGCKVGDLqeerVSFLCSNDISYVVAQWASWMSGGVAvplywkhpeAQLEYFIqdsrsslv 146
Cdd:cd05940 5 TYAELDAMANRYARWL-KSLGLKPGDV----VALFMENRPEYVLLWLGLVKIGAVA---------ALINYNL-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 vvgqeyleRLSPLAQRLGVP---LLPLTPAIYrgatekpteqpvkesgwrdrgamiFYTSGTTGRPKGALSTHRNLAAVV 223
Cdd:cd05940 63 --------RGESLAHCLNVSsakHLVVDAALY------------------------IYTSGTTGLPKAAIISHRRAWRGG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 224 TGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLsseAPQITVFMAVPTVYSKLLDy 303
Cdd:cd05940 111 AFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR---KYQATIFQYIGELCRYLLN- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 304 ydkhftQPRVQDFVravcKERIRlMVSGSAALPvpllEKWRSATGH----TLLERYGMTEIGMALSNpltEARVPGSVG- 378
Cdd:cd05940 187 ------QPPKPTER----KHKVR-MIFGNGLRP----DIWEEFKERfgvpRIAEFYAATEGNSGFIN---FFGKPGAIGr 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 379 ---TPLPGVEVRIISENPQKGSPyIIHAEGneRGTKVTPGfeeKEGELLVR--GPSVFREYWDKPEETKSAFTS-----D 448
Cdd:cd05940 249 npsLLRKVAPLALVKYDLESGEP-IRDAEG--RCIKVPRG---EPGLLISRinPLEPFDGYTDPAATEKKILRDvfkkgD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 449 GWFRTGDTAVFKDARYW-IRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV--PDmTWGQRVTAVVALQEGHS 525
Cdd:cd05940 323 AWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvPG-TDGRAGMAAIVLQPNEE 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1195733688 526 LSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQ 570
Cdd:cd05940 401 FDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
196-569 |
1.61e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 100.11 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 196 GAMIFYTSGTTGRPK----GALSTHRNLAAVVTglvhswAWTKNDVILHVL--PLHHVHGVVNKLLCPLWVGATCVML-- 267
Cdd:PRK08308 103 PSLLQYSSGTTGEPKlirrSWTEIDREIEAYNE------ALNCEQDETPIVacPVTHSYGLICGVLAALTRGSKPVIItn 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 --PEFSAQQVwekflsSEAPQITVFmAVPTVYSKLldyydKHFTQPRVQDFvravckeriRLMVSGsAALPVPLLEKWRS 345
Cdd:PRK08308 177 knPKFALNIL------RNTPQHILY-AVPLMLHIL-----GRLLPGTFQFH---------AVMTSG-TPLPEAWFYKLRE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 346 ATGHtLLERYGMTEIG-MALSNPLTEarvPGSVGTPLPGVEVRIiSENPQKGSPYIIHAEGNERGTKvTPGFEEKEGELl 424
Cdd:PRK08308 235 RTTY-MMQQYGCSEAGcVSICPDMKS---HLDLGNPLPHVSVSA-GSDENAPEEIVVKMGDKEIFTK-DLGYKSERGTL- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 425 vrgpsVFREYWDkpeetksaftsdgwfrtgdtavfkdarywirgrtsvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:PRK08308 308 -----HFMGRMD------------------------------------DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYR 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195733688 505 VPDMTWGQRVTAVVALQegHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLT 569
Cdd:PRK08308 347 GKDPVAGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
197-565 |
2.17e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 101.49 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND--VILHVLPLHHVHGVVNKLLCPLWVGATCVM-----LPE 269
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 FSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqprvQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGH 349
Cdd:PRK08180 292 GFDETL--RNLREISP--TVYFNVPKGWEMLVPALER-------DAALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 350 TLLER------YGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIIsenpqkgsPYiihaegnerGTKVtpgfeekegEL 423
Cdd:PRK08180 361 TCGERirmmtgLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV--------PV---------GGKL---------EV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 424 LVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIR-----GRTSVDIIKTGGYKVSALEIERHLLAH--PS 496
Cdd:PRK08180 415 RVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPADPERglmfdGRIAEDFKLSSGTWVSVGPLRARAVSAgaPL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 497 IADVAVIG----------VPDMTWGQRvtaVVALQEGHS----LSHRDLKEWARGVLAPY--------AVPSELLLLEEI 554
Cdd:PRK08180 495 VQDVVITGhdrdeigllvFPNLDACRR---LAGLLADASlaevLAHPAVRAAFRERLARLnaqatgssTRVARALLLDEP 571
|
410
....*....|.
gi 1195733688 555 PRNQMGKVNKK 565
Cdd:PRK08180 572 PSLDAGEITDK 582
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-462 |
2.98e-22 |
|
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: 100.58 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHH-----TYRELYDRSLCLAQEICRLqgckvgDLQEER-VSFLCSNDISYVVAQWASwMSGGVAV----P 124
Cdd:cd05921 10 DRTWLAEREGNGgwrrvTYAEALRQVRAIAQGLLDL------GLSAERpLLILSGNSIEHALMALAA-MYAGVPAapvsP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 125 LY--WKHPEAQLEYFIQdsrssLVVVGQEYLERLSPLAQRLGVPLLPLTPAIY-------RGATEKPT--EQPVKESGWR 193
Cdd:cd05921 83 AYslMSQDLAKLKHLFE-----LLKPGLVFAQDAAPFARALAAIFPLGTPLVVsrnavagRGAISFAElaATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAM-------IFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKND--VILHVLPLHHVHGVVNKLLCPLWVGATC 264
Cdd:cd05921 158 AFAAVgpdtvakFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 265 VM-----LPEFSAQQVweKFLSSEAPqiTVFMAVPTVYSKLLDYYDKhftqprvQDFVRAVCKERIRLMVSGSAALPVPL 339
Cdd:cd05921 238 YIddgkpMPGGFEETL--RNLREISP--TVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 340 LEKWR----SATGH--TLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqKGSPYiihaEGNERGTKVT 413
Cdd:cd05921 307 WDRLQalavATVGEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP----SGGKY----EVRVKGPNVT 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1195733688 414 PGfeekegellvrgpsvfreYWDKPEETKSAFTSDGWFRTGDTAVFKDA 462
Cdd:cd05921 379 PG------------------YWRQPELTAQAFDEEGFYCLGDAAKLADP 409
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
67-455 |
8.24e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.53 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEIcRLQGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLY-----------WKHPEAQLE 135
Cdd:PLN02861 79 TYKEVYDAAIRIGSAI-RSRGVNPGD----RCGIYGSNCPEWIIAMEACNSQGITYVPLYdtlganavefiINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 136 yFIQDSRSSLVVVGQE----YLERLSPL----------AQRLGVPLLPLTPAIYRGATEkpTEQPVKEsgwRDRGAMIFY 201
Cdd:PLN02861 154 -FVQESKISSILSCLPkcssNLKTIVSFgdvsseqkeeAEELGVSCFSWEEFSLMGSLD--CELPPKQ---KTDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRNLAAVVTGLVH-----SWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefsaqQVW 276
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVLSTDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI---------GFW 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 E---KFLSSEAPQI--TVFMAVPTVYSKL--------------------------LDYYDKHFTQ----PRVQDFVRAVC 321
Cdd:PLN02861 298 QgdiRYLMEDVQALkpTIFCGVPRVYDRIytgimqkissggmlrkklfdfaynykLGNLRKGLKQeeasPRLDRLVFDKI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 322 KE----RIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE-IGMALSNPLTEARVPGSVGTPLPGVEVRIISEnPQKG 396
Cdd:PLN02861 378 KEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLESV-PEMG 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1195733688 397 SPYIIHAegnergtkvtpgfeeKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGD 455
Cdd:PLN02861 457 YDALSDV---------------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGD 499
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
199-561 |
1.53e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 98.67 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKG-----------ALSTHRNL------------AAV--VTGlvHSWAwtkndvilhvlplhhVHGvvnk 253
Cdd:PRK00174 250 ILYTSGSTGKPKGvlhttggylvyAAMTMKYVfdykdgdvywctADVgwVTG--HSYI---------------VYG---- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 254 llcPLWVGATCVML---PEFSAQ----QVWEKFlsseapQITVFMAVPTVYSKLLDYYDkhftqprvqDFVRAVCKERIR 326
Cdd:PRK00174 309 ---PLANGATTLMFegvPNYPDPgrfwEVIDKH------KVTIFYTAPTAIRALMKEGD---------EHPKKYDLSSLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 327 LMvsGSAALPV-PllEKWR---SATGHtllER------YGMTEIGMALSNPLTEAR--VPGSVGTPLPGVEvriisenpq 394
Cdd:PRK00174 371 LL--GSVGEPInP--EAWEwyyKVVGG---ERcpivdtWWQTETGGIMITPLPGATplKPGSATRPLPGIQ--------- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 395 kgsPYIIHAEGNErgtkvTPGfeEKEGELLVRG--PSVFREYWDKPEETKSAFTSD--GWFRTGDTAVF-KDARYWIRGR 469
Cdd:PRK00174 435 ---PAVVDEEGNP-----LEG--GEGGNLVIKDpwPGMMRTIYGDHERFVKTYFSTfkGMYFTGDGARRdEDGYYWITGR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 470 TSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS---HRDLKEWARGVLAPYAVPS 546
Cdd:PRK00174 505 VD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAKPD 583
|
410
....*....|....*
gi 1195733688 547 ELLLLEEIPRNQMGK 561
Cdd:PRK00174 584 VIQFAPGLPKTRSGK 598
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-567 |
1.82e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIDKYGHHTYRELYDRSLCLAQEIcRLQGckVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK05691 2197 QAARTPQAPALTFAGQTLSYAELDARANRLARAL-RERG--VG--PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLG-------VPLLPLTPAIYRGATEKPTEQpvkesgwrdrgAMIFY 201
Cdd:PRK05691 2272 YPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwcleddAAALAAYSDAPLPFLSLPQHQ-----------AYLIY 2340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLhHVHGVVNKLLCPLWVGATCVMlpefSAQQVW--EKF 279
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVL----RAQGQWgaEEI 2415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 280 LS-SEAPQITVFMAVPTVYSKLLDYYDKHFTQPRVqdfvravckeriRLMVSGSAALPVPLLEKWRSATGHTLL-ERYGM 357
Cdd:PRK05691 2416 CQlIREQQVSILGFTPSYGSQLAQWLAGQGEQLPV------------RMCITGGEALTGEHLQRIRQAFAPQLFfNAYGP 2483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 358 TE-IGMALSNPLTEARVPGSVGTPLPgvevRIISENpqkgSPYIIHAEgnergtkVTPGFEEKEGELLVRGPSVFREYWD 436
Cdd:PRK05691 2484 TEtVVMPLACLAPEQLEEGAASVPIG----RVVGAR----VAYILDAD-------LALVPQGATGELYVGGAGLAQGYHD 2548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 437 KPEETKSAFTSDGW-------FRTGDTAVFKD---ARYWIRGRTSVdiiKTGGYKVSALEIERHLLAHPSIADVAVIGVP 506
Cdd:PRK05691 2549 RPGLTAERFVADPFaadggrlYRTGDLVRLRAdglVEYVGRIDHQV---KIRGFRIELGEIESRLLEHPAVREAVVLALD 2625
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 507 DMTWGQRVTAVVALQEGHSLSHRD-----LKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK05691 2626 TPSGKQLAGYLVSAVAGQDDEAQAalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
55-567 |
4.04e-21 |
|
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: 96.32 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICrlqgcKVGDLQ-EERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQ 133
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLL-----SVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 134 LEYFIQDSRSSLVVVGQEYLerlsplaqrlgvpllpltpaiyrgatekpteqpvkesgwrdrgAMIFYTSGTTGRPKGAL 213
Cdd:cd17648 77 IQFILEDTGARVVITNSTDL-------------------------------------------AYAIYTSGTTGKPKGVL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 214 STHRNLAAVVTGLVHSWAWTKND--VIL----HVLPLHhvhgvVNKLLCPLWVGATCVMLPEfSAQQVWEKFLS-SEAPQ 286
Cdd:cd17648 114 VEHGSVVNLRTSLSERYFGRDNGdeAVLffsnYVFDFF-----VEQMTLALLNGQKLVVPPD-EMRFDPDRFYAyINREK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 287 ITVFMAVPTVYSKLldyydkhftqprvqDFVRavCKERIRLMVSGSAaLPVPLLEKWRSATGHTLLERYGMTEIGM-ALS 365
Cdd:cd17648 188 VTYLSGTPSVLQQY--------------DLAR--LPHLKRVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVtNHK 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 366 NP-LTEARVPGSVGTPLPGVEVRIISENPQkgsPYIIHAegnergtkvtpgfeekEGELLVRGPSVFREYWDKPEETKSA 444
Cdd:cd17648 251 RFfPGDQRFDKSLGRPVRNTKCYVLNDAMK---RVPVGA----------------VGELYLGGDGVARGYLNRPELTAER 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 445 FTSDGW--------------FRTGDTAVFK-DARYWIRGRTSVDiIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMT 509
Cdd:cd17648 312 FLPNPFqteqerargrnarlYKTGDLVRWLpSGELEYLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAS 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 510 WGQ--RVTAVVA--LQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17648 391 QAQsrIQKYLVGyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
55-568 |
2.60e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 94.19 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKV------GDLQEER-VSFLcsndisyvvaqwASWMSGGVAVPLYW 127
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKspiivfGHMSPEMlATFL------------GAVKAGHAYIPVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVV-VGQEYLERLsplaqrlGVPLLPLT--PAIYRGATEKPTEQPVKEsgwrDRGAMIFYTSG 204
Cdd:PRK04813 85 SSPAERIEMIIEVAKPSLIIaTEELPLEIL-------GIPVITLDelKDIFATGNPYDFDHAVKG----DDNYYIIFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 205 TTGRPKGALSTHRNLAAVVtglvhSWAWTKNDVI-----------------------------LHVLPlhhvHGVVN--K 253
Cdd:PRK04813 154 TTGKPKGVQISHDNLVSFT-----NWMLEDFALPegpqflnqapysfdlsvmdlyptlasggtLVALP----KDMTAnfK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 254 LL------CPL--WVgAT------CVMLPEFSAQQVwekflsseaPQITVFMavptvysklldyydkhftqprvqdFvra 319
Cdd:PRK04813 225 QLfetlpqLPInvWV-STpsfadmCLLDPSFNEEHL---------PNLTHFL------------------------F--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 320 vCKErirlmvsgsaALPVpllekwrsATGHTLLER---------YGMTEIGMALSN-PLTEA------RVPgsVGTPLPG 383
Cdd:PRK04813 268 -CGE----------ELPH--------KTAKKLLERfpsatiyntYGPTEATVAVTSiEITDEmldqykRLP--IGYAKPD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 384 VEVRIISENpqkgspyiihaegnerGTKVTPGfeeKEGELLVRGPSVFREYWDKPEETKSAF-TSDGW--FRTGDTAVFK 460
Cdd:PRK04813 327 SPLLIIDEE----------------GTKLPDG---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLE 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 461 DARYWIRGRtsVDI-IKTGGYKVSALEIERHLLAHPSIAdVAVIgVPDMTwGQRVT---AVVALQEGHSLSHRDL----K 532
Cdd:PRK04813 388 DGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQSSYVE-SAVV-VPYNK-DHKVQyliAYVVPKEEDFEREFELtkaiK 462
|
570 580 590
....*....|....*....|....*....|....*.
gi 1195733688 533 EWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELL 568
Cdd:PRK04813 463 KELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-567 |
4.44e-20 |
|
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: 93.65 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 50 ALAFGDRialidKYG--HHTYRELYDRSLCLAQEICRLqgckvGDLQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYW 127
Cdd:cd05915 12 EVVSRLH-----TGEvhRTTYAEVYQRARRLMGGLRAL-----GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 128 KHPEAQLEYFIQDSRSSLVVVGQEYL----ERLSPLAQRLGVPLLPLTPAIYRG--ATEKPTEQPVKESGWRDRGAMIFy 201
Cdd:cd05915 82 RLSPKEIAYILNHAEDKVLLFDPNLLplveAIRGELKTVQHFVVMDEKAPEGYLayEEALGEEADPVRVPERAACGMAY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRN--LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnklLCPLWV----GATCVMLPEFSAQQV 275
Cdd:cd05915 161 TTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGPRLDPAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WekFLSSEAPQITVFMAVPTVYSKLLDyydkhftqprVQDFVRAVCKERIRLMVSGSAalPVPLLEKWRSATGHTLLERY 355
Cdd:cd05915 236 L--VELFDGEGVTFTAGVPTVWLALAD----------YLESTGHRLKTLRRLVVGGSA--APRSLIARFERMGVEVRQGY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 356 GMTEI---GMA-LSNPLTEArvpgsvgtpLPgvEVRIISENPQKGSPYIIHAEGNERGTKVTPGFEEKEGELL-VRGPSV 430
Cdd:cd05915 302 GLTETspvVVQnFVKSHLES---------LS--EEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVqLKGPWI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 431 FREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTW 510
Cdd:cd05915 371 TGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKW 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 511 GQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd05915 451 QERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
62-455 |
7.57e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 93.55 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 62 KYGHHTYRELYDRSLCLAQEicrLQGCKVGDlqEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDS 141
Cdd:PLN02614 76 KYVWQTYQEVYDIVIKLGNS---LRSVGVKD--EAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 142 RSSLVVVGQ--------------EYLERLSPL----------AQRLGVPLLPLTPAIYRGATeKPTEQPVKEsgwRDRGA 197
Cdd:PLN02614 151 EVSIVFVEEkkiselfktcpnstEYMKTVVSFggvsreqkeeAETFGLVIYAWDEFLKLGEG-KQYDLPIKK---KSDIC 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 198 MIFYTSGTTGRPKGALSTHRNLAAVVTGLVH-----SWAWTKNDVILHVLPLHHVHGVVNKLlCPLWVGAtcvmlpefsA 272
Cdd:PLN02614 227 TIMYTSGTTGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGA---------A 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 273 QQVWE---KFLSSEAPQI--TVFMAVPTV----YS----KLLD-------YYDKHFT---------------QPRVQDFV 317
Cdd:PLN02614 297 IGFWRgdvKLLIEDLGELkpTIFCAVPRVldrvYSglqkKLSDggflkkfVFDSAFSykfgnmkkgqshveaSPLCDKLV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 318 RAVCKE----RIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTE--IGMALSNPlTEARVPGSVGTPLPGVEVRIISE 391
Cdd:PLN02614 377 FNKVKQglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLP-DELDMLGTVGPPVPNVDIRLESV 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 392 npqkgspyiihAEGNERGTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTsDGWFRTGD 455
Cdd:PLN02614 456 -----------PEMEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGD 502
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
197-563 |
1.01e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 93.88 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE-FSAQQV 275
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSpLHYRII 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 276 WEKFLSSEApqiTVFMAVPTV---YSKLLDYYDkhftqprvqdFvravckERIRLMVSGSAALPVPLLEKWRSATGHTLL 352
Cdd:PRK06814 876 PELIYDTNA---TILFGTDTFlngYARYAHPYD----------F------RSLRYVFAGAEKVKEETRQTWMEKFGIRIL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 353 ERYGMTEIG--MALSNPLteARVPGSVGTPLPGVEVRIisenpqkgspyiihaegnergTKVtPGFEEKeGELLVRGPSV 430
Cdd:PRK06814 937 EGYGVTETApvIALNTPM--HNKAGTVGRLLPGIEYRL---------------------EPV-PGIDEG-GRLFVRGPNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 431 FREYW--DKP---EETKsaftsDGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIG 504
Cdd:PRK06814 992 MLGYLraENPgvlEPPA-----DGWYDTGDIVTIDEEGFiTIKGRAK-RFAKIAGEMISLAAVEELAAELWPDALHAAVS 1065
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 505 VPDMTWGQRvtaVVALQEGHSLSHRDLKEWARGVLAP-YAVPSELLLLEEIPRNQMGKVN 563
Cdd:PRK06814 1066 IPDARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-561 |
1.57e-19 |
|
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: 82.98 E-value: 1.57e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195733688 486 EIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGK 561
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
67-545 |
8.23e-19 |
|
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: 89.66 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLQGCKVGDLqeerVSFLCSNDISYVVAqWASWMSGGVAVPLYWKHPEAQ-LEYFIQDSRSSL 145
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDT----VALLLGNEPAFLWI-WLGLAKLGCPVAFLNTNIRSKsLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 146 VVVG---QEYLERLSPLAQRLGVPLLPLTP--------AIYRGATEKPTEQPVK----ESGWRDRgAMIFYTSGTTGRPK 210
Cdd:cd05938 82 LVVApelQEAVEEVLPALRADGVSVWYLSHtsntegviSLLDKVDAASDEPVPAslraHVTIKSP-ALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 211 GALSTHRNLAAVvTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEapqITVF 290
Cdd:cd05938 161 AARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHN---VTVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 291 MAVptvySKLLDYYDKhfTQPRVQDfvravCKERIRLMVsGSAALPvpllEKWRSAT---GHT-LLERYGMTEIGMALSN 366
Cdd:cd05938 237 QYI----GELLRYLCN--QPQSPND-----RDHKVRLAI-GNGLRA----DVWREFLrrfGPIrIREFYGSTEGNIGFFN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 367 pltEARVPGSVG---------TPLpgvevRIISENPQKGSPyIIHAEGneRGTKVTPGfeekEGELLV---RGPSVFREY 434
Cdd:cd05938 301 ---YTGKIGAVGrvsylykllFPF-----ELIKFDVEKEEP-VRDAQG--FCIPVAKG----EPGLLVakiTQQSPFLGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 435 WDKPEETKSAF------TSDGWFRTGDTAV--------FKDarywirgRTSvDIIKTGGYKVSALEIERHLLAHPSIADV 500
Cdd:cd05938 366 AGDKEQTEKKLlrdvfkKGDVYFNTGDLLVqdqqnflyFHD-------RVG-DTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1195733688 501 AVIGVPDMTWGQRV-TAVVALQEGHSLSHRDLKEWARGVLAPYAVP 545
Cdd:cd05938 438 NVYGVTVPGHEGRIgMAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
63-579 |
9.03e-19 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 90.26 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 63 YGHHTYRELYDRSLCLAQEIcRLQGCKVGdlqeERVSFLCSNDISYVVAQWASWMSGGVAVPLY-----------WKHPE 131
Cdd:PLN02430 74 YMWKTYKEVYEEVLQIGSAL-RASGAEPG----SRVGIYGSNCPQWIVAMEACAAHSLICVPLYdtlgpgavdyiVDHAE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 132 AQLeYFIQD--------------SRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAIYRGaTEKPTE-QPVKESGWrdrg 196
Cdd:PLN02430 149 IDF-VFVQDkkikellepdcksaKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMG-KENPSEtNPPKPLDI---- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGL-----VHSWAWTKNDVILHVLPLHHV-------------------HGVVN 252
Cdd:PLN02430 223 CTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 253 KL------LCP-LWVGATCVMlpefsaQQVWE---KFLSSEAP-QITVFMAVptvYSKLLDYYDKHFTQPRVQDF----- 316
Cdd:PLN02430 303 ALrddlmeLKPtLLAGVPRVF------ERIHEgiqKALQELNPrRRLIFNAL---YKYKLAWMNRGYSHKKASPMadfla 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 317 ---VRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI--GMALSNPlTEARVPGSVGTPLPGVEVRiISE 391
Cdd:PLN02430 374 frkVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFP-DEMCMLGTVGAPAVYNELR-LEE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 392 NPQKGspyiihaegnergtkVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFtSDGWFRTGDTA-VFKDARYWIRGRT 470
Cdd:PLN02430 452 VPEMG---------------YDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGeILPNGVLKIIDRK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 471 SvDIIKTGGYKVSALE-IERHLLAHPSIADVAVIGvpdMTWGQRVTAVVALQEghslshRDLKEWAR--GVLAPYavpSE 547
Cdd:PLN02430 516 K-NLIKLSQGEYVALEyLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNE------ENTNKWAKdnGFTGSF---EE 582
|
570 580 590
....*....|....*....|....*....|..
gi 1195733688 548 LLLLEEIprnqmgkvnKKELLTQLYPSGQRSQ 579
Cdd:PLN02430 583 LCSLPEL---------KEHILSELKSTAEKNK 605
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-505 |
1.39e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 88.67 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVnkllcplwVGATCV---MLPEF 270
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPA--------LGLTSVipdMDPTR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 271 SAQQVWEKFLSS-EAPQITVFMAVPTVYSKLLDYYDKH-FTQPRVqdfvravckeriRLMVSGSAALPVPLLEKWRSATG 348
Cdd:cd05910 157 PARADPQKLVGAiRQYGVSIVFGSPALLERVARYCAQHgITLPSL------------RRVLSAGAPVPIALAARLRKMLS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 HT--LLERYGMTE---IGMALSNPLTEARVPGS-------VGTPLPGVEVRIISENPQKgspyiIHAEGNERgtKVTPGf 416
Cdd:cd05910 225 DEaeILTPYGATEalpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEP-----IAEWDDTL--ELPRG- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 eeKEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAVFKDA-RYWIRGRTSVDIIKTGGyKVSALEIERHL 491
Cdd:cd05910 297 --EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEgRLWFCGRKAHRVITTGG-TLYTEPVERVF 373
|
330
....*....|....
gi 1195733688 492 LAHPSIADVAVIGV 505
Cdd:cd05910 374 NTHPGVRRSALVGV 387
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
182-567 |
2.36e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 88.80 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 182 PTEQPVKesgWRDRGAMIF--YTSGTTGRPKGALSTHRN-LAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPL 258
Cdd:PLN02654 264 PTKCEVE---WVDAEDPLFllYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 259 WVGATCVML---PEF-SAQQVWE---KFlsseapQITVFMAVPTVYSKLLDYYDKHFTQprvqdfvravcKERIRLMVSG 331
Cdd:PLN02654 341 LNGATVLVFegaPNYpDSGRCWDivdKY------KVTIFYTAPTLVRSLMRDGDEYVTR-----------HSRKSLRVLG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 332 SAALPV-PLLEKW-RSATGHT---LLERYGMTEIGMALSNPLTEA--RVPGSVGTPLPGVEVRIISENPQKgspyiihAE 404
Cdd:PLN02654 404 SVGEPInPSAWRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKE-------IE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 405 GnergtkvtpgfeEKEGELLVRG--PSVFRE-YWDKPEETKSAFTS-DGWFRTGD-TAVFKDARYWIRGRTSvDIIKTGG 479
Cdd:PLN02654 477 G------------ECSGYLCVKKswPGAFRTlYGDHERYETTYFKPfAGYYFSGDgCSRDKDGYYWLTGRVD-DVINVSG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 480 YKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS---HRDLKEWARGVLAPYAVPSELLLLEEIPR 556
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623
|
410
....*....|.
gi 1195733688 557 NQMGKVNKKEL 567
Cdd:PLN02654 624 TRSGKIMRRIL 634
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
194-555 |
2.76e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.61 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 194 DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLP----- 268
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 269 EFSAQQVWEKflsseapQITVFMAVPTvyskLLDYYDKhFTQPrvQDFVRavckerIRLMVSGSAALPVPLLEKWRSATG 348
Cdd:PRK08043 445 RIVPELVYDR-------NCTVLFGTST----FLGNYAR-FANP--YDFAR------LRYVVAGAEKLQESTKQLWQDKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 HTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISenpqkgspyiihaegnergtkvTPGFEEKeGELLVRGP 428
Cdd:PRK08043 505 LRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS----------------------VPGIEQG-GRLQLKGP 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 429 SVFREYW--DKPE--ETKSAFTSDG-----WFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIA 498
Cdd:PRK08043 562 NIMNGYLrvEKPGvlEVPTAENARGemergWYDTGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVSLEMVEQLALGVSPDK 640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 499 DVAVIGVPDMTWGQrvtAVVALQEGHSLSHRDLKEWARGVLAP-YAVPSELLLLEEIP 555
Cdd:PRK08043 641 QHATAIKSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-583 |
3.42e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.07 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIAL---IDKYGHH---TYRELYDRSLCLAQEICRLQGckVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVA 122
Cdd:PRK05691 18 RAAQTPDRLALrflADDPGEGvvlSYRDLDLRARTIAAALQARAS--FGD----RAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 123 VPLY-----WKHPEAQLEYFIQDSRSSLVVVG---QEYLERLSPLAQRLGVPLL---PLTPAIYRGaTEKPTEQPvkesg 191
Cdd:PRK05691 92 VPAYppesaRRHHQERLLSIIADAEPRLLLTVadlRDSLLQMEELAAANAPELLcvdTLDPALAEA-WQEPALQP----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wrDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKN--DVILHVLPLHHVHGVVNKLLCPLWVGATCVMLpe 269
Cdd:PRK05691 166 --DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 270 fsaqqvwekflsseAPQitVFMAVPTVYSKLLDYYDKhfTQPRVQDFVRAVCKERIrlmvsGSAALPVPLLEKWRSA--- 346
Cdd:PRK05691 242 --------------SPA--YFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERV-----SESALERLDLSRWRVAysg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 ---------------------TGHTLLERYGMTEIGMALSN-------PLTE------AR---VPG------SVGTPLPG 383
Cdd:PRK05691 299 sepirqdslerfaekfaacgfDPDSFFASYGLAEATLFVSGgrrgqgiPALEldaealARnraEPGtgsvlmSCGRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 384 VEVRIISENPQKGSPyiihaegnergtkvtpgfEEKEGELLVRGPSVFREYWDKPEETKSAFTS-DG--WFRTGDTAVFK 460
Cdd:PRK05691 379 HAVLIVDPQSLEVLG------------------DNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 461 DARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIA---DVAVIGVPDM-TWGQRVTAVVALQEGHSLSHRDLKEWAR 536
Cdd:PRK05691 441 DGELFVTGRLK-DMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAFAVNHQgEEGIGIAAEISRSVQKILPPQALIKSIR 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195733688 537 GVLAP--YAVPSELLLLE--EIPRNQMGKVNKKELLTQL----------YPSGQRSQPGQG 583
Cdd:PRK05691 520 QAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSACRLRLadgsldsyalFPALQAVEAAQT 580
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
55-567 |
3.92e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 87.74 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 55 DRIALIDKYGHHTYRELYDRSLCLAQEICRlQGCKVGD---LQEERVSFLcsndisYVVAqWASWMSGGVAVPLYWKHPE 131
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRR-QGIKPGDtalVQLGNVAEF------YITF-FALLKLGVAPVNALFSHQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 132 AQLEYFIQDSRSSLVVV--------GQEYLERLSPLAQRLGVPLL-------PLTPAIYRGATE-KPTEQPVKESGWrdr 195
Cdd:PRK10946 110 SELNAYASQIEPALLIAdrqhalfsDDDFLNTLVAEHSSLRVVLLlnddgehSLDDAINHPAEDfTATPSPADEVAF--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 196 gamiFYTSG-TTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHH--------VHGVvnkllcpLWVGATCVM 266
Cdd:PRK10946 187 ----FQLSGgSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypmsspgALGV-------FLAGGTVVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 267 LPEFSAQQVwekFLSSEAPQITVFMAVPTVYSKLLdyydKHFTQPRVQDFVRAvckerIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PRK10946 256 APDPSATLC---FPLIEKHQVNVTALVPPAVSLWL----QAIAEGGSRAQLAS-----LKLLQVGGARLSETLARRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 TGHTLLERYGMTEiGM----ALSNPltEARVPGSVGTPL-PGVEVRIISEnpqkgspyiihaEGNErgtkVTPGfeeKEG 421
Cdd:PRK10946 324 LGCQLQQVFGMAE-GLvnytRLDDS--DERIFTTQGRPMsPDDEVWVADA------------DGNP----LPQG---EVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 422 ELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTaVFKDARYWIR--GRTSvDIIKTGGYKVSALEIERHLLAHPSIAD 499
Cdd:PRK10946 382 RLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDL-VSIDPDGYITvvGREK-DQINRGGEKIAAEEIENLLLRHPAVIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALQEghSLSHRDLKEWAR--GVlAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:PRK10946 460 AALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLReqGI-AEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
192-573 |
2.57e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 84.54 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 WR-DRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnklLCPLW----VGATCVm 266
Cdd:PRK09029 132 WQpQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG-----QGIVWrwlyAGATLV- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 267 LPEFsaqqvwEKFLSSEApQITVFMAVPTVYSKLLDYydkhfTQPRVQdfVRAVckerirLMvsGSAALPVPL---LEKW 343
Cdd:PRK09029 206 VRDK------QPLEQALA-GCTHASLVPTQLWRLLDN-----RSEPLS--LKAV------LL--GGAAIPVELteqAEQQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 344 --RSATGhtllerYGMTEigMAlsNPLTEARVPGS--VGTPLPGVEVRIIsenpqkgspyiihaegnergtkvtpgfeek 419
Cdd:PRK09029 264 giRCWCG------YGLTE--MA--STVCAKRADGLagVGSPLPGREVKLV------------------------------ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 420 EGELLVRGPSVFREYWdKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIkTGGYKVSALEIERHLLAHPSIAD 499
Cdd:PRK09029 304 DGEIWLRGASLALGYW-RQGQLVPLVNDEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALQEGHSLShrDLKEWARGVLAPYAVPSELLLLEE--------IPRNQMgkvnkKELLTQL 571
Cdd:PRK09029 382 VFVVPVADAEFGQRPVAVVESDSEAAVV--NLAEWLQDKLARFQQPVAYYLLPPelknggikISRQAL-----KEWVAQQ 454
|
..
gi 1195733688 572 YP 573
Cdd:PRK09029 455 LG 456
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
49-489 |
4.18e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 84.66 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 49 RALAFGDRIALIdkygHHTYRELYDRSLCLAQeicRLQGCKVGdlQEERVSFLCSNDISYVVAQWASWMSGGVAVPLYWK 128
Cdd:PRK07768 17 RGMVTGEPDAPV----RHTWGEVHERARRIAG---GLAAAGVG--PGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 129 HPEAQLEYFIQDSR-------SSLVVVGQEYLErLSPLAQRLGVPLLPLTPAIyrgATEKPTEQPVKEsgwrDRGAMIFY 201
Cdd:PRK07768 88 TPRTDLAVWAEDTLrvigmigAKAVVVGEPFLA-AAPVLEEKGIRVLTVADLL---AADPIDPVETGE----DDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 202 TSGTTGRPKGALSTHRNLAAVVTGLVHSWAWT-KNDVILHVLPLHHVHGVVNKLLCPLWVGATCVML-P-EFSAQQ-VWE 277
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVtPmDFLRDPlLWA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 278 KFLSSEAPQITvfmAVP----TVYSKLLdyydkhftqpRVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATG----- 348
Cdd:PRK07768 240 ELISKYRGTMT---AAPnfayALLARRL----------RRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGArfglr 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 349 -HTLLERYGMTEIGMALSNP--------------LTEAR---VPG---------SVGTPLPGVEVRIISENPQkgspyii 401
Cdd:PRK07768 307 pEAILPAYGMAEATLAVSFSpcgaglvvdevdadLLAALrraVPAtkgntrrlaTLGPPLPGLEVRVVDEDGQ------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 402 haegnergtkVTPgfEEKEGELLVRGPSVFREYwDKPEETKSAFTSDGWFRTGDTAVFKDA-RYWIRGRTSvDIIKTGGY 480
Cdd:PRK07768 380 ----------VLP--PRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEgEVVVCGRVK-DVIIMAGR 445
|
....*....
gi 1195733688 481 KVSALEIER 489
Cdd:PRK07768 446 NIYPTDIER 454
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
68-518 |
1.05e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 83.52 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 68 YRELYDRSLCLAQEICRLqGCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPL-----------YwkhpEAQLEY 136
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGD----RVALIAETDGDFVEAFFACQYAGLVPVPLplpmgfggresY----IAQLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 137 FIQDSRSSLVVVGQEYLERLSPLAQRLGvPLLPLTPAIYR----GATEKPTEQPvkesgwrDRGAMIFYTSGTTGRPKGA 212
Cdd:PRK09192 123 MLASAQPAAIITPDELLPWVNEATHGNP-LLHVLSHAWFKalpeADVALPRPTP-------DDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 213 LSTHRNLAAVVTGLVH------------SWawtkndvilhvLPLHHVHGVVNKLLCPLwvgatcvmlpefsAQQVWEKFL 280
Cdd:PRK09192 195 IITHRALMANLRAISHdglkvrpgdrcvSW-----------LPFYHDMGLVGFLLTPV-------------ATQLSVDYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 281 SSEApqitvFMAVPTVYSKLLDyyDKHFTQPRVQDFVRAVCKERIRlmVSGSAALPvplLEKWRSA----------TGHT 350
Cdd:PRK09192 251 PTRD-----FARRPLQWLDLIS--RNRGTISYSPPFGYELCARRVN--SKDLAELD---LSCWRVAgigadmirpdVLHQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 351 LLER--------------YGMTEIGMALS-NPLTE-----------------ARVPGS----------VGTPLPGVEVRI 388
Cdd:PRK09192 319 FAEAfapagfddkafmpsYGLAEATLAVSfSPLGSgivveevdrdrleyqgkAVAPGAetrrvrtfvnCGKALPGHEIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 389 ISENPQkgspyiihaegnergtkVTPgfEEKEGELLVRGPSVFREYWDKpEETKSAFTSDGWFRTGDTAVFKDARYWIRG 468
Cdd:PRK09192 399 RNEAGM-----------------PLP--ERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLDGYLYITG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1195733688 469 RTSvDIIKTGGYKVSALEIERHLLAHPSI--ADVAVIGVPDMTwGQRVTAVV 518
Cdd:PRK09192 459 RAK-DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQEN-GEKIVLLV 508
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
197-567 |
5.81e-16 |
|
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: 80.59 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEfSAQQVW 276
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 EKFLSS--EAPQITVFMAVPTVYSKLLDYYDKHFTQPRVqdfvravckERIRLMVSGSAALPVP-LLEKWRSATGHT-LL 352
Cdd:cd17654 199 SKLADIlfKRHRITVLQATPTLFRRFGSQSIKSTVLSAT---------SSLRVLALGGEPFPSLvILSSWRGKGNRTrIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 353 ERYGMTEIGM-ALSNPLTEARVPGSVGTPLPG--VEVRIISENPQKGspyiihaegnergtkvtpgfeEKEGELLVRGpS 429
Cdd:cd17654 270 NIYGITEVSCwALAYKVPEEDSPVQLGSPLLGtvIEVRDQNGSEGTG---------------------QVFLGGLNRV-C 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 430 VFREYWDKPEETksaftsdgWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVigvpdmT 509
Cdd:cd17654 328 ILDDEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------T 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 510 W--GQRVTAVVALQEGHSLSHRDLKewaRGVLAPYAVPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17654 393 LsdQQRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
115-579 |
1.39e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.98 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 115 SWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGV---PLLPLTPAIYrgATEKPTEQPVKESG 191
Cdd:PRK05691 3790 SFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCanrPRLLVWEEVQ--AGEVASHNPGIYSG 3867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 192 wRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWvGATCVMLPEFS 271
Cdd:PRK05691 3868 -PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNAI 3945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 272 AQQVWEKFLSSEAPQITVFMAVPTVYSKLLdyydkhfTQPRVQdfvravcKERIRLMVSGSAALPVPLLEKWrsatghtl 351
Cdd:PRK05691 3946 AHDPQGLLAHVQAQGITVLESVPSLIQGML-------AEDRQA-------LDGLRWMLPTGEAMPPELARQW-------- 4003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 352 LERYgmTEIGmaLSNPLTEARVPGSV-----------GTPLPgvevriisenpqKGSP------YIIhaegNERGTKVTP 414
Cdd:PRK05691 4004 LQRY--PQIG--LVNAYGPAECSDDVaffrvdlastrGSYLP------------IGSPtdnnrlYLL----DEALELVPL 4063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 415 GfeeKEGELLVRGPSVFREYWDKPEETKSAFTSDGW-------FRTGDTA-VFKDARYWIRGRtsVD-IIKTGGYKVSAL 485
Cdd:PRK05691 4064 G---AVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLArRRSDGVLEYVGR--IDhQVKIRGYRIELG 4138
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 486 EIERHLLAHPSIADVAViGVPDMTWGQRVTA-VVALQEGHSLSHR--DLKEWARGVLAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:PRK05691 4139 EIEARLHEQAEVREAAV-AVQEGVNGKHLVGyLVPHQTVLAQGALleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
490
....*....|....*..
gi 1195733688 563 NKKELLTqLYPSGQRSQ 579
Cdd:PRK05691 4218 DRKALPA-LDIGQLQSQ 4233
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
65-572 |
8.13e-15 |
|
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: 77.08 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 65 HHTYRELydrsLCLAQEICRL---QGCKVGDLqeerVSFLCSNDISYVvAQWASWMSGGVAVPLY---WKHPeaQLEYFI 138
Cdd:cd05939 3 HWTFREL----NEYSNKVANFfqaQGYRSGDV----VALFMENRLEFV-ALWLGLAKIGVETALInsnLRLE--SLLHCI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 139 QDSRSSLVVVgqeylerlsplaqRLGVPLLPLTPaiyrgaTEKPTEQPVkesGWRDRGAMIfYTSGTTGRPKGALSTHRN 218
Cdd:cd05939 72 TVSKAKALIF-------------NLLDPLLTQSS------TEPPSQDDV---NFRDKLFYI-YTSGTTGLPKAAVIVHSR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 219 LAAVVTGLVHSWAWTKNDVILHVLPLHH----VHGVVNKLLcplwVGATCVMLPEFSAQQVWEKFLSSEApqiTVFMAVP 294
Cdd:cd05939 129 YYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNFWDDCVKYNC---TIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 295 TVYSKLLdyydkhfTQPRVQDfvraVCKERIRLMVsGSAALPvpllEKWRSATGH----TLLERYGMTEIGMALSNPLTE 370
Cdd:cd05939 202 EICRYLL-------AQPPSEE----EQKHNVRLAV-GNGLRP----QIWEQFVRRfgipQIGEFYGATEGNSSLVNIDNH 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 371 ARVPGSVGTPLPGV-EVRIISENPQKGSP------YIIHAEGNERGTKVtpgfeekeGELLVRGPSV-FREYWDKPEETK 442
Cdd:cd05939 266 VGACGFNSRILPSVyPIRLIKVDEDTGELirdsdgLCIPCQPGEPGLLV--------GKIIQNDPLRrFDGYVNEGATNK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 443 ----SAFTS-DGWFRTGDTAVFKDARY-WIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGV--PDMTwGQRV 514
Cdd:cd05939 338 kiarDVFKKgDSAFLSGDVLVMDELGYlYFKDRTG-DTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVE-GRAG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 515 TAVVALQEGHSLSHRdLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLY 572
Cdd:cd05939 416 MAAIVDPERKVDLDR-FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
84-469 |
1.35e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 76.69 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 84 RLQGC-KVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLYwkHPEA-----QLEYFIQDSRSSLVVVGQEYLE--- 154
Cdd:PRK07769 71 RLQQVtKPGD----RVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAEpghvgRLHAVLDDCTPSAILTTTDSAEgvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 155 ---RLSPLAQR---LGVPLLPLTPaiyrGATEKPTEQPvkesgwRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVH 228
Cdd:PRK07769 145 kffRARPAKERprvIAVDAVPDEV----GATWVPPEAN------EDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVID 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 229 SWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQV--WEKFLSSEAPQIT-VFMAVPtvyskllDYYD 305
Cdd:PRK07769 215 ALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPgrWIRELARKPGGTGgTFSAAP-------NFAF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 306 KHFTQprvqdfvRAVCKE--------RIRLMVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSNPL--T 369
Cdd:PRK07769 288 EHAAA-------RGLPKDgeppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTPmdE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 370 EARVPGSVGTPLPG---VEVRIISEN--PQKGSPYIIHAE-----GNERGTKVTPGfeeKEGELLVRGPSVFREYWDKPE 439
Cdd:PRK07769 361 EPTVIYVDRDELNAgrfVEVPADAPNavAQVSAGKVGVSEwavivDPETASELPDG---QIGEIWLHGNNIGTGYWGKPE 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1195733688 440 ETKSAF---------------TSDG--WFRTGDTAVFKDARYWIRGR 469
Cdd:PRK07769 438 ETAATFqnilksrlseshaegAPDDalWVRTGDYGVYFDGELYITGR 484
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
197-548 |
4.96e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 75.15 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSW-AWTKNDVILHVLPLHHVhgvvnkllcpLWVGATCVMLPEFSA--- 272
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHI----------LELAAESVMAAVGAAigy 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 273 ---------QQVWEKFLSSEAPQI--TVFMAVPTVY------------------SKLLD--YY----------------D 305
Cdd:PLN02387 323 gspltltdtSNKIKKGTKGDASALkpTLMTAVPAILdrvrdgvrkkvdakgglaKKLFDiaYKrrlaaiegswfgawglE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 306 KHFTQPRVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEI--GMALSNPltEARVPGSVGTPLPG 383
Cdd:PLN02387 403 KLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETcaGATFSEW--DDTSVGRVGPPLPC 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 384 VEVRIISenpqkgspyiiHAEGNERGT-KVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDG----WFRTGDTAV 458
Cdd:PLN02387 481 CYVKLVS-----------WEEGGYLISdKPMP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQ 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 459 FK-DARYWIRGRTSvDIIKT--GGYkVSALEIERHLLAHPSIADVAVIGVPDMTWGqrVTAVVAlqeghslSHRDLKEWA 535
Cdd:PLN02387 545 FHpDGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHADPFHSYC--VALVVP-------SQQALEKWA 613
|
410
....*....|...
gi 1195733688 536 RGVLAPYAVPSEL 548
Cdd:PLN02387 614 KKAGIDYSNFAEL 626
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-506 |
8.21e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.08 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 197 AMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpeFSAQQVW 276
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV----FAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 EKFLSS--EAPQITVFMAVPTVYSKLLDYYDKHFTqprvqdfvravCKERIRLMVSGSAALPVPLLEKWRSATGH-TLLE 353
Cdd:PRK06334 262 PKKIVEmiDEAKVTFLGSTPVFFDYILKTAKKQES-----------CLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 RYGMTEIGMALS-NPLTEARVPGSVGTPLPGVEVRIISEnpqkgspyiihaegnERGTKVTPGfeeKEGELLVRGPSVFR 432
Cdd:PRK06334 331 GYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSE---------------ETKVPVSSG---ETGLVLTRGTSLFS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 433 EYW-DKPEETKSAFTSDGWFRTGDTA-VFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAH------PSIADVAVIG 504
Cdd:PRK06334 393 GYLgEDFGQGFVELGGETWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCG 471
|
..
gi 1195733688 505 VP 506
Cdd:PRK06334 472 LP 473
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
199-562 |
4.23e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 65.92 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALsthRNLAAVVTGLVHSWAWTKNDVILHVLPLHH------VHGVVNKLLCplwVGATCVML----- 267
Cdd:PTZ00237 259 ILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS---LGNTFVMFeggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 268 -PEFSAQQVWEKFlssEAPQITVFMAVPTVYSKLLDyydkhfTQPRVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSA 346
Cdd:PTZ00237 333 kNKHIEDDLWNTI---EKHKVTHTLTLPKTIRYLIK------TDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 347 TGHTLLERYGMTEIGMALSNPLTEARVP-GSVGTPLPGVEVRIISEnpqkgspyiihaEGNERGtkvtpgfEEKEGEL-- 423
Cdd:PTZ00237 404 LKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSE------------DGKELN-------VNEIGEVaf 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 424 -LVRGPSVFREYWDKPEETKSAFTS-DGWFRTGDTAvFKDAR--YWIRGRtSVDIIKTGGYKVSALEIERHLLAHPSIAD 499
Cdd:PTZ00237 465 kLPMPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLG-FKDENgyYTIVSR-SDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 500 VAVIGVPDMTWGQRVTAVVALQEGHSLSHRDLKEWARGV-------LAPYAVPSELLLLEEIPRNQMGKV 562
Cdd:PTZ00237 543 CCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEInniitqdIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
96-469 |
6.79e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.15 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 96 ERVSFLCSNDISYVVAQWASWMSGGVAVPLYwkHPEAQ-----LEYFIQDSRSSLVVVGQ-------EYLERLSplaqRL 163
Cdd:PRK12476 93 DRVAILAPQGIDYVAGFFAAIKAGTIAVPLF--APELPghaerLDTALRDAEPTVVLTTTaaaeaveGFLRNLP----RL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 164 GVPLLPLTPAIYRGATEKPTEQPVKEsgwrDRGAMIFYTSGTTGRPKGALSTHRnlaAVVTGLV-------------HSW 230
Cdd:PRK12476 167 RRPRVIAIDAIPDSAGESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHR---AVGTNLVqmilsidlldrntHGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 231 AWtkndvilhvLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSAQ-QVWEKFLSSEAPQITVFMAVPtvysklldyydkhf 308
Cdd:PRK12476 240 SW---------LPLYHDMGLSMIGFPAVYGGHSTLMSPtAFVRRpQRWIKALSEGSRTGRVVTAAP-------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 309 tqprvqDFVRAVCKER--------IRL----MVSGSAALPVPLLEKWRSATGHTLLER------YGMTEIGMALSN--PL 368
Cdd:PRK12476 297 ------NFAYEWAAQRglpaegddIDLsnvvLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVATiaPD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 369 TEARVPGSVGTPL-PGVEVRIISENPQkGSPYII--HAEGNERGTKVTPGFEEKE-----GELLVRGPSVFREYWDKPEE 440
Cdd:PRK12476 371 AEPSVVYLDREQLgAGRAVRVAADAPN-AVAHVScgQVARSQWAVIVDPDTGAELpdgevGEIWLHGDNIGRGYWGRPEE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1195733688 441 TKSAF------------------TSDGWFRTGDTAVFKDARYWIRGR 469
Cdd:PRK12476 450 TERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLDGELYITGR 496
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
67-469 |
1.99e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 63.42 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 67 TYRELYDRSLCLAQEICRLqgCKVGDlqeeRVSFLCSNDISYVVAQWASWMSGGVAVPLywkhPEAQleYFIQDSRSSLV 146
Cdd:PRK05850 37 TWSQLYRRTLNVAEELRRH--GSTGD----RAVILAPQGLEYIVAFLGALQAGLIAVPL----SVPQ--GGAHDERVSAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 147 --------------VVGQ--EYLErlsplAQRLGVPllPLTPAIYRGATEKPTEqPVKESGWRDRGAMIFYTSGTTGRPK 210
Cdd:PRK05850 105 lrdtspsvvlttsaVVDDvtEYVA-----PQPGQSA--PPVIEVDLLDLDSPRG-SDARPRDLPSTAYLQYTSGSTRTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 211 GALSTHRNLAAVVTGLVHSW------AWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVmlpefsaqqvwekFLSSEA 284
Cdd:PRK05850 177 GVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAV-------------LTSPVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 285 pqitvFMAVPTVYSKLLDYYDKHFTQPRVQDFVRAVCKER-----------IRLMVSGSaalpvpllEKWRSATGHTLLE 353
Cdd:PRK05850 244 -----FLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSdddmagldlggVLGIISGS--------ERVHPATLKRFAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 354 R---YGMTEIGMALSNPLTEARVpgSVGTPLPGVEVRIISENPQKGSPYiiHAE--GNERGTKVT--------------- 413
Cdd:PRK05850 311 RfapFNLRETAIRPSYGLAEATV--YVATREPGQPPESVRFDYEKLSAG--HAKrcETGGGTPLVsygsprsptvrivdp 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195733688 414 -------PGfeeKEGELLVRGPSVFREYWDKPEETKSAF----------TSDG-WFRTGDTAVFKDARYWIRGR 469
Cdd:PRK05850 387 dtciecpAG---TVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
199-562 |
3.57e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 62.66 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKG----------ALSThrNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGvvnkllcPLWVGATCVM-- 266
Cdd:PRK10524 238 ILYTSGTTGKPKGvqrdtggyavALAT--SMDTIFGGKAGETFFCASDIGWVVGHSYIVYA-------PLLAGMATIMye 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 267 -LPEFSAQQVWEKFLssEAPQITVFMAVPTVYsKLLDYYDKHFTQPRVQDFVRAvckerirLMVSGSaalpvPLLE---K 342
Cdd:PRK10524 309 gLPTRPDAGIWWRIV--EKYKVNRMFSAPTAI-RVLKKQDPALLRKHDLSSLRA-------LFLAGE-----PLDEptaS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 343 WRS-ATGHTLLERYGMTEIG---MALSNPLtEARVP--GSVGTPLPGVEVRIISENPqkgspyiihaegnerGTKVTPGf 416
Cdd:PRK10524 374 WISeALGVPVIDNYWQTETGwpiLAIARGV-EDRPTrlGSPGVPMYGYNVKLLNEVT---------------GEPCGPN- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 eEKeGELLVRGP-------SVFReywDKPEETKSAFTSDG--WFRTGDTAVF-KDARYWIRGRTSvDIIKTGGYKVSALE 486
Cdd:PRK10524 437 -EK-GVLVIEGPlppgcmqTVWG---DDDRFVKTYWSLFGrqVYSTFDWGIRdADGYYFILGRTD-DVINVAGHRLGTRE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 487 IERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSHRDL-----KEWARGV---LAPYAVPSELLLLEEIPRNQ 558
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaleKEIMALVdsqLGAVARPARVWFVSALPKTR 590
|
....
gi 1195733688 559 MGKV 562
Cdd:PRK10524 591 SGKL 594
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
151-571 |
6.49e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 58.62 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 151 EYLERLSPLAQrlGVPLLPLTPAiyrGATEKPTEQPVKESGwrdRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLV-HS 229
Cdd:PRK05851 117 SHLERLRAVDS--SVTVHDLATA---AHTNRSASLTPPDSG---GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNaRV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 230 WAWTKNDVILHVLPLHHVHGVVNkLLCPLWVGATCVMLPE--FSAQQV-WEKFLSSEAPQITvfmAVPTVYSKLLDYYDK 306
Cdd:PRK05851 189 GLDAATDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTtaFSASPFrWLSWLSDSRATLT---AAPNFAYNLIGKYAR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 307 hftqpRVQDfvraVCKERIRLMVSGSAALPVPLLEKWRSATGH------TLLERYGMTEIGMALSNPltearVPGS---- 376
Cdd:PRK05851 265 -----RVSD----VDLGALRVALNGGEPVDCDGFERFATAMAPfgfdagAAAPSYGLAESTCAVTVP-----VPGIglrv 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 377 ----------------VGTPLPGVEVRIiseNPQKGSpyiihAEGNERGTkvtpgfeekeGELLVRGPSVFREYWDKPee 440
Cdd:PRK05851 331 devttddgsgarrhavLGNPIPGMEVRI---SPGDGA-----AGVAGREI----------GEIEIRGASMMSGYLGQA-- 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 441 tksAFTSDGWFRTGDTAVFKDARYWIRGRTSvDIIKTGGYKVSALEIERHLLAHPSIADVAVIGVPDMTWGQRVTAVVAL 520
Cdd:PRK05851 391 ---PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAA 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 521 QeghsLSHRDLKEWARGVLAPYA-----VPSELLLLE--EIPRNQMGKVNKKELLTQL 571
Cdd:PRK05851 467 E----FRGPDEAGARSEVVQRVAsecgvVPSDVVFVApgSLPRTSSGKLRRLAVKRSL 520
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
199-455 |
7.61e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 58.58 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGALSTHRNLAAVVTGLV-HSWAWTKN-DVILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefsaqQVW 276
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCkHSIFKKYNpKTHLSYLPISHIYERVIAYLS-FMLGGTI---------NIW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 277 EKFLSSEAPQI-----TVFMAVPTVYSKLldYYD-----------------------KHFTQPRVQDFVRAVCK--ERIR 326
Cdd:PTZ00342 379 SKDINYFSKDIynskgNILAGVPKVFNRI--YTNimteinnlpplkrflvkkilslrKSNNNGGFSKFLEGITHisSKIK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 327 --------LMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPL-PGVEVRIISENPQKGs 397
Cdd:PTZ00342 457 dkvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKA- 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 398 pyiihaegnergTKVTPgfeekEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGD 455
Cdd:PTZ00342 536 ------------TDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGD 576
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
417-567 |
4.30e-05 |
|
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: 46.36 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 417 EEKEGELLVRGPSVFREYWDKPEetksaftsDGWFRTGDTAvfkdaRYWIRGRTSV-----DIIKTGGYKVSALEIERHL 491
Cdd:cd17647 348 PDHWNYLDKDNNEPWRQFWLGPR--------DRLYRTGDLG-----RYLPNGDCECcgradDQVKIRGFRIELGEIDTHI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 492 LAHPSIAD---------------VAVIgVPDM----TWGQRVTA---------VVALQEGHSLSHRDLKEWARGVLAPYA 543
Cdd:cd17647 415 SQHPLVREnitlvrrdkdeeptlVSYI-VPRFdkpdDESFAQEDvpkevstdpIVKGLIGYRKLIKDIREFLKKRLASYA 493
|
170 180
....*....|....*....|....
gi 1195733688 544 VPSELLLLEEIPRNQMGKVNKKEL 567
Cdd:cd17647 494 IPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
199-561 |
2.43e-04 |
|
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: 44.18 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 199 IFYTSGTTGRPKGalsthrnlaavvtgLVHSWAWTkndvILHVLPLHHVHGVV-----------------NKLLCPLWVG 261
Cdd:cd05943 254 ILYSSGTTGLPKC--------------IVHGAGGT----LLQHLKEHILHCDLrpgdrlfyyttcgwmmwNWLVSGLAVG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 262 ATCVML---PEFSAQQVWEKFLSSEapQITVFMAVPTVYSKLLDyydKHFTQPRVQDFvravckERIRLMVSGSAALPVP 338
Cdd:cd05943 316 ATIVLYdgsPFYPDTNALWDLADEE--GITVFGTSAKYLDALEK---AGLKPAETHDL------SSLRTILSTGSPLKPE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 339 LLEKWRSATGHTLL--ERYGMTEI--GMALSNPLTEARvPGSVGTPLPGVEVRIISENpqkgspyiihaegnerGTKVTp 414
Cdd:cd05943 385 SFDYVYDHIKPDVLlaSISGGTDIisCFVGGNPLLPVY-RGEIQCRGLGMAVEAFDEE----------------GKPVW- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 415 gfEEKeGELLVRG--PSVFREYWDKPEETK--SAF--TSDGWFRTGDTAVF-KDARYWIRGRtSVDIIKTGGYKVSALEI 487
Cdd:cd05943 447 --GEK-GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIEItPRGGVVILGR-SDGTLNPGGVRIGTAEI 522
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195733688 488 ERHLLAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLSH---RDLKEWARGVLAPYAVPSELLLLEEIPRNQMGK 561
Cdd:cd05943 523 YRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
452-578 |
5.55e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 42.76 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 452 RTGDtaVFK---DARYWIRGRTSvDIIKTGGYKVSALEIERHL-LAHPSIADVAVIGVPDMTWGQRVTAVVALQEGHSLS 527
Cdd:PLN03052 592 RHGD--IFErtsGGYYRAHGRAD-DTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGS 668
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195733688 528 HRDLKEWARGV-------LAPYAVPSELLLLEEIPRNQMGKVNKKELLTQLYPSGQRS 578
Cdd:PLN03052 669 NPDLNELKKIFnsaiqkkLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQLAQELSRS 726
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
452-571 |
1.23e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 41.73 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195733688 452 RTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLL-AHPSIADVAVIGVPDMTWGQRVTAVVA----LQEGHSL 526
Cdd:PLN03051 360 RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLvlgeEKKGFDQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1195733688 527 S-----HRDLKEWARGVLAPYAVPSELLLLEEIPRNQMGKVNKKELLTQL 571
Cdd:PLN03051 440 ArpealQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQL 489
|
|
| |
