|
Name |
Accession |
Description |
Interval |
E-value |
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1-517 |
0e+00 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 1129.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 1 MDIIGGQHLRQMWDDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWF 80
Cdd:PRK08008 1 MDIVGGQHLRQMWDDLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 81 GLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQLKNQQ 160
Cdd:PRK08008 81 GLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 161 PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
Cdd:PRK08008 161 PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 241 ATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYG 320
Cdd:PRK08008 241 ATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATAKVLEADGWL 400
Cdd:PRK08008 321 MTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYYLDPKATAKVLEADGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEF 480
Cdd:PRK08008 401 HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEF 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 1629467165 481 FRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08008 481 FAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-517 |
0e+00 |
|
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: 661.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 35 VNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLV 114
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 115 TsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstdDTAEILFTSGTTSRPKGVVIT 194
Cdd:cd05934 81 V----------------------------------------------------------DPASILYTSGTTGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 195 HYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIR 274
Cdd:cd05934 103 HANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 275 TLMVQPPSANDRQHRLREVMFYLNLsEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGdKRRWPSIGRAGFCYEAEIR 354
Cdd:cd05934 183 YLLAQPPSPDDRAHRLRAAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDE-PRRPGSIGRPAPGYEVRIV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 355 DDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCV 434
Cdd:cd05934 261 DDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEATAEAMR-NGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 435 ELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRK 514
Cdd:cd05934 340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
...
gi 1629467165 515 NLK 517
Cdd:cd05934 420 QLR 422
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-517 |
1.27e-149 |
|
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: 435.78 E-value: 1.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 9 LRQMWDDLADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR-----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 89 MVPINARLLREESAWILQNSQACLLVTsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyap 168
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVT----------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 plstddtAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEK 248
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLReVMFYL--NLSEQEKDAFCERFGVRLLTSYGMTETIV 326
Cdd:COG0318 176 FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLR-LVVSGgaPLPPELLERFEERFGVRIVEGYGLTETSP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 327 GIIGdRPGDK--RRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLeADGWLHTGD 404
Cdd:COG0318 255 VVTV-NPEDPgeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGP---NVMKGYWNDPEATAEAF-RDGWLRTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC 484
Cdd:COG0318 330 LGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFL 409
|
490 500 510
....*....|....*....|....*....|...
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:COG0318 410 RERLARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
17-517 |
1.12e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 371.83 E-value: 1.12e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PRK06187 16 ARKHPDKEAVYFDGR-----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQIQqEDATQLRHICLID--VALPADDGVSSFTQLKNQQPATLCyAPPLSTDD 174
Cdd:PRK06187 91 KPEEIAYILNDAEDRVVLVDSEFVPLLAAIL-PQLPTVRTVIVEGdgPAAPLAPEVGEYEELLAAASDTFD-FPDIDEND 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 175 TAEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCA----LRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLVEKYS 250
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNL----FLHSLAVCawlkLSRDDVYLVIVPMFHVH-AWGLPYLALMAGAKQVIPRRFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 251 ARAFWGQVQKYRATVTECIPMMIrTLMVQPPSANDRQ-HRLREVMfY--LNLSEQEKDAFCERFGVRLLTSYGMTET--I 325
Cdd:PRK06187 244 PENLLDLIETERVTFFFAVPTIW-QMLLKAPRAYFVDfSSLRLVI-YggAALPPALLREFKEKFGIDLVQGYGMTETspV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 326 VGIIGDRPGDKRRWP---SIGRAGFCYEAEIRDDHNRPLPA--GEIGEICIKGvPgkTIFKEYFLNPKATAKVLEaDGWL 400
Cdd:PRK06187 322 VSVLPPEDQLPGQWTkrrSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRG-P--WLMQGYWNRPEATAETID-GGWL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEF 480
Cdd:PRK06187 398 HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKEL 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 1629467165 481 FRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK06187 478 RAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-517 |
8.20e-122 |
|
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: 365.35 E-value: 8.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 9 LRQMWDDLADVYGHKTALICessGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF---MGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 89 MVPINARLLREESAWILQNSQACLLVTSAQFypmyqqiqqEDATQlrhiclidvalpaddgvssftqlknqQPATLCYAP 168
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVSF---------TDLLA--------------------------AGAPLGERV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCA------LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGAT 242
Cdd:cd05936 121 ALTPEDVAVLQYTSGTTGVPKGAMLTHRNL----VANALQIKawledlLEGDDVVLAALPLFHVFGLTVALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 243 FVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPpsaNDRQHRLREVMFYLN----LSEQEKDAFCERFGVRLLTS 318
Cdd:cd05936 197 IVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAP---EFKKRDFSSLRLCISggapLPVEVAERFEELTGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEaDG 398
Cdd:cd05936 274 YGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRG-P--QVMKGYWNRPEETAEAFV-DG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 399 WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE 478
Cdd:cd05936 350 WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEE 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 1629467165 479 EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05936 430 EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
17-513 |
2.57e-116 |
|
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: 349.99 E-value: 2.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICessGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:cd17631 5 ARRHPDRTALVF---GGR--SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVtsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTA 176
Cdd:cd17631 80 TPPEVAYILADSGAKVLF----------------------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWG 256
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 257 QVQKYRATVTECIPMMIrTLMVQPPSANDRQH-RLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGD 335
Cdd:cd17631 182 LIERHRVTSFFLVPTMI-QALLQHPRFATTDLsSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPED 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 336 KRRWP-SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFF 414
Cdd:cd17631 261 HRRKLgSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG-P--HVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 415 YFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVP 494
Cdd:cd17631 337 YIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIP 416
|
490
....*....|....*....
gi 1629467165 495 SYLEIRKDLPRNCSGKIIR 513
Cdd:cd17631 417 KSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
7-517 |
8.57e-110 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 336.11 E-value: 8.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 7 QHLRQMWDDLADVYGHKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGD-----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 87 AIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATqLRH--ICLIDVALPADDGVSSFTQ-LKNQQPAT 163
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPA-LEHvvICETEEDDPHTEKMKTFTDfLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 164 lcYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAgyYSAWqCA---LRDDDVYLTVMPAFHIDCQCTAAMAAFSAG 240
Cdd:PRK07656 159 --RAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSN--AADW-AEylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 241 ATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLR------EVMfYLNLSEqekdAFCERFGVR 314
Cdd:PRK07656 234 ATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRlavtgaASM-PVALLE----RFESELGVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 315 -LLTSYGMTE-----TIvgiigDRPGDKRRWP--SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLN 386
Cdd:PRK07656 309 iVLTGYGLSEasgvtTF-----NRLDDDRKTVagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG---PNVMKGYYDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 387 PKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
Cdd:PRK07656 381 PEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 467 VVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07656 461 VVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
174-511 |
3.84e-107 |
|
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: 323.08 E-value: 3.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 174 DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGaTFVLVEKYSARA 253
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGG-TVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 FWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFY-LNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDR 332
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGgAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 PGDK-RRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEE 411
Cdd:cd04433 160 PDDDaRKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRG---PSVMKGYWNNPEATAAVDE-DGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKF 491
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|
gi 1629467165 492 KVPSYLEIRKDLPRNCSGKI 511
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKI 335
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
37-517 |
1.79e-106 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 328.26 E-value: 1.79e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQQIQqEDATQLRHICLID----VALPADDGVSSFTQLknQQPATlcyAPPLSTDDTAEILFTSGTTSRPKGVV 192
Cdd:PRK06155 126 AALLAALEAAD-PGDLPLPAVWLLDapasVSVPAGWSTAPLPPL--DAPAP---AAAVQPGDTAAILYTSGTTGPSKGVC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 193 ITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGaTFVLVEKYSARAFWGQVQKYRATVTECIPMM 272
Cdd:PRK06155 200 CPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGA-TYVLEPRFSASGFWPAVRRHGATVTYLLGAM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 273 IRTLMVQPPSANDRQHRLReVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVgIIGDRPGDKRrwP-SIGRAGFCYEA 351
Cdd:PRK06155 279 VSILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERFGVDLLDGYGSTETNF-VIAVTHGSQR--PgSMGRLAPGFEA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATakvLEA--DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGE 429
Cdd:PRK06155 355 RVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKT---VEAwrNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
Cdd:PRK06155 432 NISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENG 511
|
....*...
gi 1629467165 510 KIIRKNLK 517
Cdd:PRK06155 512 KVQKFVLR 519
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
14-517 |
2.06e-105 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 326.30 E-value: 2.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 14 DDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:COG0365 16 DRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAWILQNSQACLLVTSAQFY------PMYQQIQQ--EDATQLRHICLIDVALPAD--DGVSSFTQLKNQQPAT 163
Cdd:COG0365 96 PGFGAEALADRIEDAEAKVLITADGGLrggkviDLKEKVDEalEELPSLEHVIVVGRTGADVpmEGDLDWDELLAAASAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 164 lCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY------YSAWQCALRDDDVYLT-------------VMPAF 224
Cdd:COG0365 176 -FEPEPTDADDPLFILYTSGTTGKPKGVVHTH-----GGYlvhaatTAKYVLDLKPGDVFWCtadigwatghsyiVYGPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 225 HIDCqctaamaafsagaTFVLVEK----YSARAFWGQVQKYRATVTECIPMMIRTLM---VQPPSANDRQHrLREVM--- 294
Cdd:COG0365 250 LNGA-------------TVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMkagDEPLKKYDLSS-LRLLGsag 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 295 -------FylnlseqekDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRwP-SIGRAGFCYEAEIRDDHNRPLPAGEI 366
Cdd:COG0365 316 eplnpevW---------EWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVK-PgSMGKPVPGYDVAVVDEDGNPVPPGEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 367 GEICIKG-VPGktIFKEYFLNPKATAKVL--EADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH 443
Cdd:COG0365 386 GELVIKGpWPG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1629467165 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:COG0365 464 PAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-517 |
3.16e-99 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 308.09 E-value: 3.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVT-S 116
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQqiqqedATQLRHICLIDVALPADDGVSSF--TQLKNQQPATLCYAPPLST--DDTAEILFTSGTTSRPKGVV 192
Cdd:cd05926 95 GELGPASR------AASKLGLAILELALDVGVLIRAPsaESLSNLLADKKNAKSEGVPlpDDLALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 193 ITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMM 272
Cdd:cd05926 169 LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 273 IRT-LMVQPPSANDRQHRLRevmFYLN----LSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDR-PGDKRRWPSIGRaG 346
Cdd:cd05926 249 HQIlLNRPEPNPESPPPKLR---FIRScsasLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPlPPGPRKPGSVGK-P 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 347 FCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:cd05926 325 VGVEVRILDEDGEILPPGVVGEICLRG---PNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRN 506
Cdd:cd05926 402 GGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKT 481
|
490
....*....|.
gi 1629467165 507 CSGKIIRKNLK 517
Cdd:cd05926 482 ATGKIQRRKVA 492
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
17-516 |
9.29e-98 |
|
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: 304.54 E-value: 9.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSGgvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:cd05904 15 ASAHPSRPALIDAATG---RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPmyqQIQqedATQLRHICLIDvalpADDGVSSFTQLKNQQPATLCYAPPLSTDDTA 176
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELAE---KLA---SLALPVVLLDS----AEFDSLSFSDLLFEADEAEPPVVVIKQDDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYNL--RFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAF 254
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLiaMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 255 WGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMF-YLNLSEQEKDAFCERF-GVRLLTSYGMTET--IVGIIG 330
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSgAAPLGKELIEAFRAKFpNVDLGQGYGMTEStgVVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 331 DRPGDKRRWPSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEADGWLHTGDTGYCD 409
Cdd:cd05904 322 APEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG-P--SIMKGYLNNPEATAATIDKEGWLHTGDLCYID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 410 EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFceqnMA 489
Cdd:cd05904 399 EDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDF----VA 474
|
490 500 510
....*....|....*....|....*....|..
gi 1629467165 490 KfKVPSYLEIRK-----DLPRNCSGKIIRKNL 516
Cdd:cd05904 475 K-QVAPYKKVRKvafvdAIPKSPSGKILRKEL 505
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
17-427 |
1.57e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 293.45 E-value: 1.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICessgGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:pfam00501 5 AARTPDKTALEV----GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQLKnqQPATLCYAPPLSTDDTA 176
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP--ADVPPPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYNLrFAGYYSAWQC-----ALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSA 251
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNL-VANVLSIKRVrprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 R---AFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFyl-nLSEQEKDAFCERFGVRLLTSYGMTET--I 325
Cdd:pfam00501 238 LdpaALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSggapLPPELARRFRELFGGALVNGYGLTETtgV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 326 VGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDH-NRPLPAGEIGEICIKGvPGktIFKEYFLNPKATAKVLEADGWLHTGD 404
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRG-PG--VMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRG 427
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
20-517 |
1.40e-91 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 289.14 E-value: 1.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 20 YGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:PRK08316 24 YPDKTALVFGDR-----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSAQFYPmyqqiQQEDATQLRHICLIDVAL-----PADDGVSSFTQLKNQQPATLcYAPPLSTDD 174
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAP-----TAEAALALLPVDTLILSLvlggrEAPGGWLDFADWAEAGSVAE-PDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 175 TAEILFTSGTTSRPKGVVITHYNLrFAGYYSA-WQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARA 253
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRAL-IAEYVSCiVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 FWGQVQKYRATVTECIPMMIRTLMVQPPSAndrQHRLR--------------EVmfylnLSEQEkdafcERF-GVRLLTS 318
Cdd:PRK08316 252 ILRTIEAERITSFFAPPTVWISLLRHPDFD---TRDLSslrkgyygasimpvEV-----LKELR-----ERLpGLRFYNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTE-----TIVGiigdrPGD-KRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYFLNPKATAk 392
Cdd:PRK08316 319 YGQTEiaplaTVLG-----PEEhLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRS-PQLML--GYWDDPEKTA- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 393 vlEA--DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN 470
Cdd:PRK08316 390 --EAfrGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1629467165 471 EGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08316 468 AGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
25-511 |
1.76e-88 |
|
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: 279.87 E-value: 1.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESSGgvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
Cdd:cd05911 1 AQIDADTG---KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 LQNSQACLLVTSAQFYPMYQQIQQEdATQLRHICLIDVALPADDGVSSFTQLKNQQPATLCYAPP-LSTDDTAEILFTSG 183
Cdd:cd05911 78 LKISKPKVIFTDPDGLEKVKEAAKE-LGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLkDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 184 TTSRPKGVVITHYNL--RFAGYYSAWQCALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKY 261
Cdd:cd05911 157 TTGLPKGVCLSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPLYHI-YGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 262 RatVTECI---PMMIrtLMVQPPSANdrQHRLREVMFYL----NLSEQEKDAFCERFG-VRLLTSYGMTETiVGIIGDRP 333
Cdd:cd05911 236 K--ITFLYlvpPIAA--ALAKSPLLD--KYDLSSLRVILsggaPLSKELQELLAKRFPnATIKQGYGMTET-GGILTVNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 334 GDKRRWPSIGRAGFCYEAEIRDDH-NRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEG 412
Cdd:cd05911 309 DGDDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRG---PQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFK 492
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK 465
|
490 500
....*....|....*....|....*
gi 1629467165 493 vpsylEIR------KDLPRNCSGKI 511
Cdd:cd05911 466 -----QLRggvvfvDEIPKSASGKI 485
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
39-517 |
4.69e-87 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 276.07 E-value: 4.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQEDATQLrhiclidvalpaddgvssftQLKNQQPATLCYAPPLstDDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:PRK03640 109 FEAKLIPGISVKFAEL--------------------MNGPKEEAEIQEEFDL--DEVATIMYTSGTTGKPKGVIQTYGNH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 RFAGYYSAWQCALRDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMV 278
Cdd:PRK03640 167 WWSAVGSALNLGLTEDDCWLAAVPIFHIS-GLSILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 279 QPPSANDRQHrLREVMF-----YLNLSEQekdafCERFGVRLLTSYGMTETIVGIIGDRPGDKRRwpSIGRAG---FCYE 350
Cdd:PRK03640 246 RLGEGTYPSS-FRCMLLgggpaPKPLLEQ-----CKEKGIPVYQSYGMTETASQIVTLSPEDALT--KLGSAGkplFPCE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 351 AEIRDDhNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGEN 430
Cdd:PRK03640 318 LKIEKD-GVVVPPFEEGEIVVKG-P--NVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGEN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 431 VSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLneGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
Cdd:PRK03640 393 IYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGK 470
|
....*..
gi 1629467165 511 IIRKNLK 517
Cdd:PRK03640 471 LLRHELK 477
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
38-517 |
9.38e-80 |
|
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: 254.96 E-value: 9.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAcllvtsa 117
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 qfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplSTDDTAEILFTSGTTSRPKGVVITHYN 197
Cdd:cd05912 75 -----------------------------------------------------KLDDIATIMYTSGTTGKPKGVQQTFGN 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LrfagYYSAWQCAL----RDDDVYLTVMPAFHIDcQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMI 273
Cdd:cd05912 102 H----WWSAIGSALnlglTEDDNWLCALPLFHIS-GLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 274 RTLMVQPP---SANDRQHRLREVMFYLNLSEQekdafCERFGVRLLTSYGMTETIVGIIGDRPGDK-RRWPSIGRAGFCY 349
Cdd:cd05912 177 QRLLEILGegyPNNLRCILLGGGPAPKPLLEQ-----CKEKGIPVYQSYGMTETCSQIVTLSPEDAlNKIGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 EAEIRDDHNRPlpaGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGE 429
Cdd:cd05912 252 ELKIEDDGQPP---YEVGEILLKG---PNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
Cdd:cd05912 325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASG 402
|
....*...
gi 1629467165 510 KIIRKNLK 517
Cdd:cd05912 403 KLLRHELK 410
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-516 |
2.55e-79 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 256.71 E-value: 2.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLF-YTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQQIQQEDATQlRHICLIDVALPADDGVSSFTQLKNQQPATLCYapplstddtaeilfTSGTTSRPKGVVITHY 196
Cdd:PRK06839 108 KTFQNMALSMQKVSYVQ-RVISITSLKEIEDRKIDNFVEKNESASFIICY--------------TSGTTGKPKGAVLTQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:PRK06839 173 NMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDRQHRLRevMFYLN---LSEQEKDAFCERfGVRLLTSYGMTETIVGIIGDRPGDKRRWP-SIGR-AGFCyEA 351
Cdd:PRK06839 253 INCSKFETTNLQSVR--WFYNGgapCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDARRKVgSIGKpVLFC-DY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENV 431
Cdd:PRK06839 329 ELIDENKNKVEVGEVGELLIRG---PNVMKEYWNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKI 484
|
....*
gi 1629467165 512 IRKNL 516
Cdd:PRK06839 485 QKAQL 489
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-511 |
2.64e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 252.57 E-value: 2.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 12 MWDDL---ADVYGHKTALICESsggvvNRYSYLELNQEINRTAN-LFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
Cdd:PRK08314 12 LFHNLevsARRYPDKTAIVFYG-----RAISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 88 IMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEdaTQLRHICLIDV--ALPADDGVSSftqlknqqPATLC 165
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGN--LRLRHVIVAQYsdYLPAEPEIAV--------PAWLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 YAPPLST--------------------------DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLT 219
Cdd:PRK08314 157 AEPPLQAlapggvvawkealaaglappphtagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 220 VMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPpsaNDRQHRLREVMfYLN- 298
Cdd:PRK08314 237 VLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASP---GLAERDLSSLR-YIGg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 299 ----LSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDrPGDKRRWPSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKG 373
Cdd:PRK08314 313 ggaaMPEAVAERLKELTGLDYVEGYGLTETMAQTHSN-PPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 374 vPGktIFKEYFLNPKATAKV-LEADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
Cdd:PRK08314 392 -PQ--VFKGYWNRPEATAEAfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAC 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1629467165 451 VVGIKDSIRDEAIKAFVVLNEGE--TLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
Cdd:PRK08314 469 VIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
17-516 |
2.60e-75 |
|
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: 246.77 E-value: 2.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSGGVVnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:cd12119 6 ARLHGDREIVSRTHEGEVH-RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVA---LPADDGVSSFTQLKNQQPaTLCYAPPLSTD 173
Cdd:cd12119 85 FPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAampEPAGVGVLAYEELLAAES-PEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 174 DTAEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCALRD------DDVYLTVMPAFHIDCQCTAAMAAFSAGAtFVLVE 247
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSL----VLHAMAALLTDglglseSDVVLPVVPMFHVNAWGLPYAAAMVGAK-LVLPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 248 KYSARAFWGQ-VQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVmfYLNLSEQEKdAFCERF---GVRLLTSYGMTE 323
Cdd:cd12119 239 PYLDPASLAElIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRV--VIGGSAVPR-SLIEAFeerGVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TI-VGIIG-------DRPGDKR--RWPSIGRAGFCYEAEIRDDHNRPLPA--GEIGEICIKGvPgkTIFKEYFLNPKATA 391
Cdd:cd12119 316 TSpLGTVArppsehsNLSEDEQlaLRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRG-P--WVTKSYYKNDEESE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 392 KVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE 471
Cdd:cd12119 393 ALTE-DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1629467165 472 GETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd12119 472 GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
39-517 |
8.45e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 244.80 E-value: 8.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FypmyqqiqQEDATQLRHICLIDVALPADDGVSSftqlKNQQPATLCYapPLSTDDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:PRK06145 109 F--------DAIVALETPKIVIDAAAQADSRRLA----QGGLEIPPQA--AVAPTDLVRLMYTSGTTDRPKGVMHSYGNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 RFAGYYSAWQCALRDDDVYLTVMPAFHIDCqCTAAMAAFSAGATFVLVEK-YSARAFWGQVQKYRATVTECIPMMI-RTL 276
Cdd:PRK06145 175 HWKSIDHVIALGLTASERLLVVGPLYHVGA-FDLPGIAVLWVGGTLRIHReFDPEAVLAAIERHRLTCAWMAPVMLsRVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERF-GVRLLTSYGMTETIVGIIGDRPGDK-RRWPSIGRAGFCYEAEIR 354
Cdd:PRK06145 254 TVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGREiEKIGSTGRALAHVEIRIA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 355 DDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCV 434
Cdd:PRK06145 334 DGAGRWLPPNMKGEICMRG---PKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 435 ELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRK 514
Cdd:PRK06145 410 EVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKR 489
|
...
gi 1629467165 515 NLK 517
Cdd:PRK06145 490 VLR 492
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
13-503 |
1.07e-74 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 247.09 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 13 WDDLADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ-----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 93 NARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQLKNQQPATlcyaPPLST 172
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTT----NPASR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 -----DDTAEILFTSGTTSRPKGVVITHYnlRFAGYYSAWQ--CALRDDDVYLTVMPAFH----IDCQCTaamaAFSAGA 241
Cdd:PRK08279 194 sgvtaKDTAFYIYTSGTTGLPKAAVMSHM--RWLKAMGGFGglLRLTPDDVLYCCLPLYHntggTVAWSS----VLAAGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 242 TFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLReVMFYLNLSEQEKDAFCERFGV-RLLTSYG 320
Cdd:PRK08279 268 TLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLR-LMIGNGLRPDIWDEFQQRFGIpRILEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETIVGIIG--DRPGDKRRWPSIGRAGFCY-------EAEIRDD--HNRPLPAGEIGEiCIKGVPGKTIFKEYfLNPKA 389
Cdd:PRK08279 347 ASEGNVGFINvfNFDGTVGRVPLWLAHPYAIvkydvdtGEPVRDAdgRCIKVKPGEVGL-LIGRITDRGPFDGY-TDPEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 390 TAKVL------EADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkdSIRD--- 460
Cdd:PRK08279 425 SEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV--EVPGtdg 502
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1629467165 461 EAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDL 503
Cdd:PRK08279 503 RAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
39-516 |
1.28e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 243.40 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQedATQLRHICLIDVA--LP-ADDGVSSFTQLKN--------------------QQPATLCYAPPLSTDDT 175
Cdd:PRK06710 131 VFPRVTNVQS--ATKIEHVIVTRIAdfLPfPKNLLYPFVQKKQsnlvvkvsesetihlwnsveKEVNTGVEVPCDPENDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 176 AEILFTSGTTSRPKGVVITHYNL---RFAGYYSAWQCaLRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSAR 252
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLvsnTLMGVQWLYNC-KEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 253 AFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVM---FYLNLSEQEKdaFCERFGVRLLTSYGMTETIVGII 329
Cdd:PRK06710 288 MVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsgsAPLPVEVQEK--FETVTGGKLVEGYGLTESSPVTH 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 330 GDRPGDKRRWPSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYC 408
Cdd:PRK06710 366 SNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG---PQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNM 488
Cdd:PRK06710 442 DEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYL 521
|
490 500
....*....|....*....|....*...
gi 1629467165 489 AKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK06710 522 AAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
18-516 |
5.06e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 241.87 E-value: 5.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 18 DVYGHKTalicessggvvnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
Cdd:PRK06178 53 IFYGHVI--------------TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 98 REESAWILQNSQACLLVTSAQFYPMYQQIQQEdaTQLRHIC------------------LIDVALPADDGVSSFTQLKNQ 159
Cdd:PRK06178 119 EHELSYELNDAGAEVLLALDQLAPVVEQVRAE--TSLRHVIvtsladvlpaeptlplpdSLRAPRLAAAGAIDLLPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 160 QPAtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF--AGYYSAWQcALRDDDVYLTVMPAFHIDCQCTAAMAAF 237
Cdd:PRK06178 197 CTA-PVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYtaAAAYAVAV-VGGEDSVFLSFLPEFWIAGENFGLLFPL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 238 SAGATFVLVEKYSARAFWGQVQKYRATVTEcipMMIRT---LMVQPPSANDRQHRLREVM---FYLNLSEQEKDAFCERF 311
Cdd:PRK06178 275 FSGATLVLLARWDAVAFMAAVERYRVTRTV---MLVDNaveLMDHPRFAEYDLSSLRQVRvvsFVKKLNPDYRQRWRALT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLL-TSYGMTET------IVGIIGDrPGDKRRWPSigragFC------YEAEIRD-DHNRPLPAGEIGEICIKgVPgk 377
Cdd:PRK06178 352 GSVLAeAAWGMTEThtcdtfTAGFQDD-DFDLLSQPV-----FVglpvpgTEFKICDfETGELLPLGAEGEIVVR-TP-- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 378 TIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
Cdd:PRK06178 423 SLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 458 IRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSyLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK06178 502 DKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
11-511 |
1.09e-72 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 240.87 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 11 QMWDDLADVYGHKTALIcESSGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMV 90
Cdd:PRK08315 20 QLLDRTAARYPDREALV-YRDQGL--RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 91 PINARLLREESAWILQNSQACLLVTSAQF----YP-MYQQIQQEDATQ------------LRHICLIDVALPAddGVSSF 153
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAADGFkdsdYVaMLYELAPELATCepgqlqsarlpeLRRVIFLGDEKHP--GMLNF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 154 TQL----KNQQPATL-CYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDD-VYLTVmPAFHid 227
Cdd:PRK08315 175 DELlalgRAVDDAELaARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrLCIPV-PLYH-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 228 C--------QCTAAMAafsagaTFVL-VEKYSARAFWGQVQKYRATVTECIPMM-----------------IRT------ 275
Cdd:PRK08315 252 CfgmvlgnlACVTHGA------TMVYpGEGFDPLATLAAVEEERCTALYGVPTMfiaeldhpdfarfdlssLRTgimags 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 276 -----LMvqppsandrqhrlREVMFYLNLSEqekdafcerfgvrlLTS-YGMTETIVGIIGDRPGD--KRRWPSIGRAGF 347
Cdd:PRK08315 326 pcpieVM-------------KRVIDKMHMSE--------------VTIaYGMTETSPVSTQTRTDDplEKRVTTVGRALP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 348 CYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:PRK08315 379 HLEVKIVDpETGETVPRGEQGELCTRG---YSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRN 506
Cdd:PRK08315 456 GGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMT 535
|
....*
gi 1629467165 507 CSGKI 511
Cdd:PRK08315 536 VTGKI 540
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
37-511 |
1.12e-72 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 240.83 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQF-----YPMYQQIQQEDAT------------QLRHICLIDVALP-----------ADDGVSSftQLKNQQPATLcyap 168
Cdd:PRK12583 125 DAFktsdyHAMLQELLPGLAEgqpgalacerlpELRGVVSLAPAPPpgflawhelqaRGETVSR--EALAERQASL---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 plSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL-VE 247
Cdd:PRK12583 199 --DRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 248 KYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLR---------------EVMFYLNLSEqekdafcerfg 312
Cdd:PRK12583 277 AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRtgimagapcpievmrRVMDEMHMAE----------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 313 vrLLTSYGMTETIVGIIGDRPGD--KRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKAT 390
Cdd:PRK12583 346 --VQIAYGMTETSPVSLQTTAADdlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGY---SVMKGYWNNPEAT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 391 AKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN 470
Cdd:PRK12583 421 AESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLH 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1629467165 471 EGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
Cdd:PRK12583 501 PGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
38-517 |
2.26e-72 |
|
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: 236.46 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSA 117
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 qfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITH-Y 196
Cdd:cd05972 81 -------------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHsY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQcALRDDDVYLTVM-PAFHIDCQCTAAMAAFSAGATFV-LVEKYSARAFWGQVQKYRATVTECIPMMIR 274
Cdd:cd05972 106 PLGHIPTAAYWL-GLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVyEGPRFDAERILELLERYGVTSFCGPPTAYR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 275 TLMVQPPSANDRQHrLREVMFY---LNlsEQEKDAFCERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRAGFCYEA 351
Cdd:cd05972 185 MLIKQDLSSYKFSH-LRLVVSAgepLN--PEVIEWWRAATGLPIRDGYGQTETGL-TVGNFPDMPVKPGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENV 431
Cdd:cd05972 261 AIIDDDGRELPPGEEGDIAIK-LPPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCS 508
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTIS 418
|
....*....
gi 1629467165 509 GKIIRKNLK 517
Cdd:cd05972 419 GKIRRVELR 427
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
22-517 |
1.42e-71 |
|
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: 234.49 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALIceSSGGvvnRYSYLELNQEINRTANLFYTLG-IRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
Cdd:cd05941 1 DRIAIV--DDGD---SITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 101 SAWILQNSQACLLVtsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstdDTAEILF 180
Cdd:cd05941 76 LEYVITDSEPSLVL-----------------------------------------------------------DPALILY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 181 TSGTTSRPKGVVITHYNLRF--AGYYSAWQcaLRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQV 258
Cdd:cd05941 97 TSGTTGRPKGVVLTHANLAAnvRALVDAWR--WTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 QKYRATVTECIPMMIRTLMvQPPSANDRQ---------HRLRevmfyLN------LSEQEKDAFCERFGVRLLTSYGMTE 323
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLL-QYYEAHFTDpqfaraaaaERLR-----LMvsgsaaLPVPTLEEWEAITGHTLLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TivGIIGDRPGD-KRRWPSIGRAGFCYEAEIRDDH-NRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLH 401
Cdd:cd05941 249 I--GMALSNPLDgERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRG---PSVFKEYWNKPEATKEEFTDDGWFK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 402 TGDTGYCDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-ETLSEEE 479
Cdd:cd05941 324 TGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEE 403
|
490 500 510
....*....|....*....|....*....|....*...
gi 1629467165 480 FFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05941 404 LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
13-516 |
7.76e-71 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 235.80 E-value: 7.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 13 WDDLADVYGHKTALICESSGgvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
Cdd:PRK06087 29 WQQTARAMPDKIAVVDNHGA----SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 93 NARLLREESAWILQNSQACLLVTSAQFY-----PMYQQIQqEDATQLRHICLIDVALPADDGVSSFTQLKNQQPatLCYA 167
Cdd:PRK06087 105 LPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvDLILPLQ-NQLPQLQQIVGVDKLAPATSSLSLSQIIADYEP--LTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 168 PPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLtvMPA--------FHidcqctAAMAAFSA 239
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFM--MPAplghatgfLH------GVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 240 GATFVLVEKYSARAFWGQVQKYRAT----VTECIPMMIRTLMVQPPsandrqhRLREVMFYL--------NLSEQekdaf 307
Cdd:PRK06087 254 GARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDLLNLLEKQPA-------DLSALRFFLcggttipkKVARE----- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 308 CERFGVRLLTSYGMTETIVGIIGdRPGDKRRWpSIGRAGFCYEA-EIR--DDHNRPLPAGEIGEICIKGvpgKTIFKEYF 384
Cdd:PRK06087 322 CQQRGIKLLSVYGSTESSPHAVV-NLDDPLSR-FMHTDGYAAAGvEIKvvDEARKTLPPGCEGEEASRG---PNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 385 LNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
Cdd:PRK06087 397 DEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 465 AFVVLNEGE-TLSEEEFFRF-CEQNMAKFKVPSYLEIRKDLPRNCSGKiIRKNL 516
Cdd:PRK06087 477 AYVVLKAPHhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGK-IQKFL 529
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
14-517 |
1.79e-70 |
|
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: 233.80 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 14 DDLADVYGHKTALIcessgGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:cd05959 11 LNLNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVAlPADDGVSSFTQLknqqPATLC-YAPPLST 172
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGA-GPEAGALLLAEL----VAAEAeQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 --DDTAEILFTSGTTSRPKGVVITHYNLRF-AGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLV-EK 248
Cdd:cd05959 161 haDDPAFWLYSSGSTGRPKGVVHLHADIYWtAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMpER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLR------EVmfylnLSEQEKDAFCERFGVRLLTSYGMT 322
Cdd:cd05959 241 PTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRlcvsagEA-----LPAEVGERWKARFGLDILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 323 ETIVGIIGDRPGDKRrWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIFkeYFLNPKATAKVLEAdGWLHT 402
Cdd:cd05959 316 EMLHIFLSNRPGRVR-YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRG-PSSATM--YWNNRDKTRDTFQG-EWTRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 403 GDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG---ETLSEEE 479
Cdd:cd05959 391 GDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEE 470
|
490 500 510
....*....|....*....|....*....|....*...
gi 1629467165 480 FFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05959 471 LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
25-517 |
4.37e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 232.49 E-value: 4.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESSGGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
Cdd:PRK08276 2 AVIMAPSGEVV---TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 LQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVALPaddGVSSFTQLKNQQPATlcyaPPLSTDDTAEILFTSGT 184
Cdd:PRK08276 79 VDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVP---GFRSYEEALAAQPDT----PIADETAGADMLYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 185 TSRPKGVV-------ITHYNLRFAGYYSAWQCAlRDDDVYLTVMPAFHID----CQctaamAAFSAGATFVLVEKYSARA 253
Cdd:PRK08276 152 TGRPKGIKrplpgldPDEAPGMMLALLGFGMYG-GPDSVYLSPAPLYHTAplrfGM-----SALALGGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 FWGQVQKYRATVTECIPMMIRTLMVQPPSANDR----QHRLR---------EVmfylnlseqeKDAFCERFGVRLLTSYG 320
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFVRMLKLPEEVRARydvsSLRVAihaaapcpvEV----------KRAMIDWWGPIIHEYYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETI-VGIIG-----DRPGdkrrwpSIGRAGfcyEAEIR--DDHNRPLPAGEIGEICIK-GVPGktiFkEYFLNPKATA 391
Cdd:PRK08276 296 SSEGGgVTVITsedwlAHPG------SVGKAV---LGEVRilDEDGNELPPGEIGTVYFEmDGYP---F-EYHNDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 392 KVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE 471
Cdd:PRK08276 363 AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1629467165 472 GETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08276 443 GADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
23-517 |
8.84e-69 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 229.19 E-value: 8.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESSGGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFI-FCWFGLaKIGAIMVPINARLLREES 101
Cdd:PRK13391 13 KPAVIMASTGEVV---TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLeVCWAAE-RSGLYYTCVNSHLTPAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTSAQFYpmyqQIQQEDATQLRHI--CLIDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDdtaeIL 179
Cdd:PRK13391 89 AYIVDDSGARALITSAAKL----DVARALLKQCPGVrhRLVLDGDGELEGFVGYAEAVAGLPATPIADESLGTD----ML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 180 FTSGTTSRPKGVV-------------ITHYNLRFAGYysawqcalRDDDVYLTVMPAFHIDCQcTAAMAAFSAGATFVLV 246
Cdd:PRK13391 161 YSSGTTGRPKGIKrplpeqppdtplpLTAFLQRLWGF--------RSDMVYLSPAPLYHSAPQ-RAVMLVIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 247 EKYSARAFWGQVQKYRATVTECIP-MMIRtlMVQPPSANDRQHRLREVMFYLNLSE----QEKDAFCERFGVRLLTSYGM 321
Cdd:PRK13391 232 EHFDAEQYLALIEEYGVTHTQLVPtMFSR--MLKLPEEVRDKYDLSSLEVAIHAAApcppQVKEQMIDWWGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 322 TETiVGIIG-------DRPGdkrrwpSIGRAGFCyEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFkEYFLNPKATAKVL 394
Cdd:PRK13391 310 TEG-LGFTAcdseewlAHPG------TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG---GRPF-EYLNDPAKTAEAR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 395 EADG-WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE 473
Cdd:PRK13391 378 HPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1629467165 474 TLSE---EEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK13391 458 DPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
36-517 |
5.09e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 227.62 E-value: 5.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 36 NRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVT 115
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 SAQFyPMYQQIQQEDATQLRHICLIDVAlPADDGVSSFTQL---KNQQPATLCYapplstDDTAEILFTSGTTSRPKGVV 192
Cdd:PRK07470 111 HADF-PEHAAAVRAASPDLTHVVAIGGA-RAGLDYEALVARhlgARVANAAVDH------DDPCWFFFTSGTTGRPKAAV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 193 ITHYNLRF--AGYYSAWQCALRDDDVYLTVMP-----AFHIDCQctaamaaFSAGATFVLV--EKYSARAFWGQVQKYRA 263
Cdd:PRK07470 183 LTHGQMAFviTNHLADLMPGTTEQDASLVVAPlshgaGIHQLCQ-------VARGAATVLLpsERFDPAEVWALVERHRV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 264 TVTECIPMMIRtLMVQPPSANDRQH-RLREVMF-----YlnlSEQEKDAFcERFGVRLLTSYGMTEtIVGII-------- 329
Cdd:PRK07470 256 TNLFTVPTILK-MLVEHPAVDRYDHsSLRYVIYagapmY---RADQKRAL-AKLGKVLVQYFGLGE-VTGNItvlppalh 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 330 --GDRPGDKrrwpsIGRAGF---CYEAEIRDDHNRPLPAGEIGEICIKGVPgktIFKEYFLNPKATAKVLEaDGWLHTGD 404
Cdd:PRK07470 330 daEDGPDAR-----IGTCGFertGMEVQIQDDEGRELPPGETGEICVIGPA---VFAGYYNNPEANAKAFR-DGWFRTGD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC 484
Cdd:PRK07470 401 LGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWL 480
|
490 500 510
....*....|....*....|....*....|...
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07470 481 DGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
37-516 |
5.12e-68 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 225.05 E-value: 5.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd05935 81 SEL-----------------------------------------------------DDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDRQHRLREVMF-YLNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRwPSIGRAGFCYEAEIRD 355
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGgGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKL-QCLGIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 356 -DHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKV-LEADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENV 431
Cdd:cd05935 267 iETGRELPPNEVGEIVVR---GPQIFKGYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE--TLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
....*..
gi 1629467165 510 KIIRKNL 516
Cdd:cd05935 424 KILWRLL 430
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-453 |
6.58e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 229.22 E-value: 6.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 2 DIIGGQHLRQMWDDLADVYGHKTALIcESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFG 81
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 82 LAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFypMYQQIQ--QEDATQLRHICLID-VALPADDGVSSFTQL-- 156
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQE--QLDKLLevRDELPSLRHIVVLDpRGLRDDPRLLSLDELla 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 157 ---KNQQPATLCYAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMP---------- 222
Cdd:COG1022 163 lgrEVADPAELEARRaAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPlahvfertvs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 223 AFHIDCQCTAAMAAFSAGA---------TFVLV-----EKYSARAfWGQVQK--------YRATVTECIPMMIRTLMVQP 280
Cdd:COG1022 243 YYALAAGATVAFAESPDTLaedlrevkpTFMLAvprvwEKVYAGI-QAKAEEagglkrklFRWALAVGRRYARARLAGKS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 281 PSANDR-QHRL---------REVM--------------------FYLNLseqekdafcerfGVRLLTSYGMTETIVGIIG 330
Cdd:COG1022 322 PSLLLRlKHALadklvfsklREALggrlrfavsggaalgpelarFFRAL------------GIPVLEGYGLTETSPVITV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 331 DRPGDKRrwpsIGRAGfcyeaeirddhnRPLPAGEI-----GEICIKGvPGktIFKEYFLNPKATAKVLEADGWLHTGDT 405
Cdd:COG1022 390 NRPGDNR----IGTVG------------PPLPGVEVkiaedGEILVRG-PN--VMKGYYKNPEATAEAFDADGWLHTGDI 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1629467165 406 GYCDEEGFFYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVG 453
Cdd:COG1022 451 GELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
6-517 |
1.34e-67 |
|
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: 226.57 E-value: 1.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGHKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAImvPINA----RllREESAWILQNSQACLLVTSAQF----Y-PMYQQIQQEDATqLRHICLIDvalPADDGVsSFTQL 156
Cdd:COG1021 99 GAI--PVFAlpahR--RAEISHFAEQSEAVAYIIPDRHrgfdYrALARELQAEVPS-LRHVLVVG---DAGEFT-SLDAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 157 KNqQPATLcYAPPLSTDDTAEILFTSGTTSRPKGVVITH----YNLRfagyYSAWQCALRDDDVYLTVMPAFHidcqcta 232
Cdd:COG1021 170 LA-APADL-SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVR----ASAEICGLDADTVYLAALPAAH------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 233 amaafsagaTF-----------------VLVEKYSARAFWGQVQKYRATVTECIPMMIrTLMVQppSANDRQHRLREVMF 295
Cdd:COG1021 237 ---------NFplsspgvlgvlyaggtvVLAPDPSPDTAFPLIERERVTVTALVPPLA-LLWLD--AAERSRYDLSSLRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 296 YLN----LSEQEKDAFCERFGVRLLTSYGMTETIVgiIGDRPGD--KRRWPSIGRAgFCYEAEIR--DDHNRPLPAGEIG 367
Cdd:COG1021 305 LQVggakLSPELARRVRPALGCTLQQVFGMAEGLV--NYTRLDDpeEVILTTQGRP-ISPDDEVRivDEDGNPVPPGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 368 EICIKGvPGktIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQ 447
Cdd:COG1021 382 ELLTRG-PY--TIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVH 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1629467165 448 DIVVVGIKDSIRDEAIKAFVVLNeGETLSEEE---FFRfcEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:COG1021 459 DAAVVAMPDEYLGERSCAFVVPR-GEPLTLAElrrFLR--ERGLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
20-517 |
2.91e-67 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 226.02 E-value: 2.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 20 YGHKTALICESSGGVvnrYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:PLN02246 36 FSDRPCLIDGATGRV---YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQlrhICLIDvalPADDGVSSFTQLKNQQPATlCYAPPLSTDDTAEIL 179
Cdd:PLN02246 113 EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT---VVTID---DPPEGCLHFSELTQADENE-LPEVEISPDDVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 180 FTSGTTSRPKGVVITHYNLrfagYYSAWQCA--------LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSA 251
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGL----VTSVAQQVdgenpnlyFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMF-YLNLSEQEKDAFCERF-GVRLLTSYGMTETivgii 329
Cdd:PLN02246 262 GALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSgAAPLGKELEDAFRAKLpNAVLGQGYGMTEA----- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 330 gdrpGD---------KRRWPSigRAGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKV 393
Cdd:PLN02246 337 ----GPvlamclafaKEPFPV--KSGSCgtvvrnAELKIVDpETGASLPRNQPGEICIRG---PQIMKGYLNDPEATANT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 394 LEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE 473
Cdd:PLN02246 408 IDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1629467165 474 TLSEEEFfrfcEQNMAKfKVPSYLEIRK-----DLPRNCSGKIIRKNLK 517
Cdd:PLN02246 488 EITEDEI----KQFVAK-QVVFYKRIHKvffvdSIPKAPSGKILRKDLR 531
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
14-513 |
8.35e-66 |
|
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: 221.99 E-value: 8.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 14 DDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:cd05970 24 DAMAKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAWILQNSQACLLVTSAQfYPMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQL-KNQQPAtlcYAPP--- 169
Cdd:cd05970 104 HQLTAKDIVYRIESADIKMIVAIAE-DNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLiKNASPD---FERPtan 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 170 --LSTDDTAEILFTSGTTSRPKGVVITH-YNLRFAGYYSAWQcALRDDDVYLTVMPAFHIDCQCTAAMAA-FSAGATFVL 245
Cdd:cd05970 180 syPCGEDILLVYFSSGTTGMPKMVEHDFtYPLGHIVTAKYWQ-NVREGGLHLTVADTGWGKAVWGKIYGQwIAGAAVFVY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 246 -VEKYSARAFWGQVQKYRATvTECIPMMIRTLMVQPPSANDRQHRLRE-VMFYLNLSEQEKDAFCERFGVRLLTSYGMTE 323
Cdd:cd05970 259 dYDKFDPKALLEKLSKYGVT-TFCAPPTIYRFLIREDLSRYDLSSLRYcTTAGEALNPEVFNTFKEKTGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TIVgIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYFLNPKATAKVLEaDGWLH 401
Cdd:cd05970 338 TTL-TIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVglFGGYYKDAEKTAEVWH-DGYYH 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 402 TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE--- 478
Cdd:cd05970 416 TGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkk 495
|
490 500 510
....*....|....*....|....*....|....*
gi 1629467165 479 EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:cd05970 496 ELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
17-515 |
1.17e-65 |
|
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: 220.25 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:cd12118 14 AAVYPDRTSIVYGDR-----RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFypMYQQIQQEdatqlrhiclidvalpaddGVSSFTQLknqqpatlcyaPPLSTDDTA 176
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREF--EYEDLLAE-------------------GDPDFEWI-----------PPADEWDPI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCtAAMAAFSAGATFVLVEKYSARAFWG 256
Cdd:cd12118 137 ALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWC-FPWTVAAVGGTNVCLRKVDAKAIYD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 257 QVQKYRATVTECIPMMIRTLMVQPPSanDRQHRLREVMFY----------LNLSEQEkdafcerfGVRLLTSYGMTETI- 325
Cdd:cd12118 216 LIEKHKVTHFCGAPTVLNMLANAPPS--DARPLPHRVHVMtagapppaavLAKMEEL--------GFDVTHVYGLTETYg 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 326 VGIIG------DRPGDKRRWPSIGRAGFCY----EAEIRD-DHNRPLPA-GE-IGEICIKgvpGKTIFKEYFLNPKATAK 392
Cdd:cd12118 286 PATVCawkpewDELPTEERARLKARQGVRYvgleEVDVLDpETMKPVPRdGKtIGEIVFR---GNIVMKGYLKNPEATAE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 393 VLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
Cdd:cd12118 363 AFR-GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1629467165 473 ETLSEEEFFRFCEQNMAKFKVPSYLEIRkDLPRNCSGKiIRKN 515
Cdd:cd12118 442 AKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGK-IQKF 482
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
37-517 |
2.77e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 220.24 E-value: 2.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEfIFCWFGLAKI-GAIMVPINARLLREESAWILQNSQACLLVT 115
Cdd:PRK06188 37 RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE-VLMAIGAAQLaGLRRTALHPLGSLDDHAYVLEDAGISTLIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 SAQFYPMYQQIQQEDATQLRHICLIDvalPADDGVSSFTQLKNQQPATLcyAPPLSTDDTAEILFTSGTTSRPKGVVITH 195
Cdd:PRK06188 116 DPAPFVERALALLARVPSLKHVLTLG---PVPDGVDLLAAAAKFGPAPL--VAAALPPDIAGLAYTGGTTGKPKGVMGTH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 ynlRFAGYYSAWQCA---LRDDDVYLTVMPAFHIdcQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMM 272
Cdd:PRK06188 191 ---RSIATMAQIQLAeweWPADPRFLMCTPLSHA--GGAFFLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 273 IRTLMVQPPSAnDRQHRLREVMFY-------LNLSEQekdafCERFGVRLLTSYGMTE-----TIVGIIGDRPGDKRRWP 340
Cdd:PRK06188 266 IYALLDHPDLR-TRDLSSLETVYYgaspmspVRLAEA-----IERFGPIFAQYYGQTEapmviTYLRKRDHDPDDPKRLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 341 SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRR 420
Cdd:PRK06188 340 SCGRPTPGLRVALLDEDGREVAQGEVGEICVRG-PL--VMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIR 500
Cdd:PRK06188 416 KDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFV 495
|
490
....*....|....*..
gi 1629467165 501 KDLPRNCSGKIIRKNLK 517
Cdd:PRK06188 496 DSLPLTALGKPDKKALR 512
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
38-517 |
2.70e-64 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 215.44 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSA 117
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 QfypMYQQIQQEDATQLrhiclidvalpaddgvssftqlknqqpatlcyapplstddtaeiLFTSGTTSRPKGVVITHYN 197
Cdd:cd05969 81 E---LYERTDPEDPTLL--------------------------------------------HYTSGTTGTPKGVLHVHDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LRFAGYYSAWQCALRDDDVY-LTVMPAFhIDCQCTAAMAAFSAGATFVLVE-KYSARAFWGQVQKYRATVTECIPMMIRT 275
Cdd:cd05969 114 MIFYYFTGKYVLDLHPDDIYwCTADPGW-VTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 276 LM---VQPPSANDRQHrLREVMF---YLNlseqeKDAF---CERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAG 346
Cdd:cd05969 193 LMkegDELARKYDLSS-LRFIHSvgePLN-----PEAIrwgMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 347 FCYEAEIRDDHNRPLPAGEIGEICIK-GVPgkTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIK 425
Cdd:cd05969 267 PGVKAAVVDENGNELPPGTKGILALKpGWP--SMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 426 RGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKD 502
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*
gi 1629467165 503 LPRNCSGKIIRKNLK 517
Cdd:cd05969 424 LPKTRSGKIMRRVLK 438
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
37-511 |
3.63e-64 |
|
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: 214.94 E-value: 3.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFypmyqqiqqedaTQLRHiclidVALPaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd05903 81 ERF------------RQFDP-----AAMP---------------------------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:cd05903 117 TLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDRQHRLRevmFYL--------NLSEQEKdafcERFGVRLLTSYGMTE--TIVGIIGDRPGDkRRWPSIGRAG 346
Cdd:cd05903 197 LNAVEEAGEPLSRLR---TFVcggatvprSLARRAA----ELLGAKVCSAYGSTEcpGAVTSITPAPED-RRLYTDGRPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 347 FCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:cd05903 269 PGVEIKVVDDTGATLAPGVEGELLSRG---PSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCE-QNMAKFKVPSYLEIRKDLPR 505
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPR 424
|
....*.
gi 1629467165 506 NCSGKI 511
Cdd:cd05903 425 TPSGKV 430
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-517 |
2.73e-63 |
|
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: 210.21 E-value: 2.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEK-YSA 251
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLRE-VMFYLNLSEQEKDAFCERFGVRLLTS-YGMTETIVGII 329
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTgIMAGAPCPPELMKRVIEVMNMKDVTIaYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 330 GDRPGD--KRRWPSIGRAGFCYEAEIRDDHNRPLPA-GEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGWLHTGDTG 406
Cdd:cd05917 162 QTRTDDsiEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGY---SVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 407 YCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQ 486
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 1629467165 487 NMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
21-517 |
5.59e-63 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 215.53 E-value: 5.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICESSGGVVnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
Cdd:PRK04319 58 KDKVALRYLDASRKE-KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 101 SAWILQNSQACLLVTSAQfypMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQLKNQQPATlCYAPPLSTDDTAEILF 180
Cdd:PRK04319 137 VRDRLEDSEAKVLITTPA---LLERKPADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQASDE-FDIEWTDREDGAILHY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 181 TSGTTSRPKGV------VITHYnlrfagyYSA-WQCALRDDDVY--------LT------VMPAFHidcqctaamaafsa 239
Cdd:PRK04319 213 TSGSTGKPKGVlhvhnaMLQHY-------QTGkYVLDLHEDDVYwctadpgwVTgtsygiFAPWLN-------------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 240 GATFVLVE-KYSARAFWGQVQKYRATVTECIPMMIRTLMvqppSAND---RQHRLREVMFYLNLSEQ---E-----KDAF 307
Cdd:PRK04319 272 GATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRMLM----GAGDdlvKKYDLSSLRHILSVGEPlnpEvvrwgMKVF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 308 cerfGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIK-GVPgkTIFKEYFLN 386
Cdd:PRK04319 348 ----GLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKkGWP--SMMRGIWNN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 387 PKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
Cdd:PRK04319 422 PEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAF 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 467 VVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK04319 501 VALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
39-516 |
2.72e-62 |
|
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: 210.00 E-value: 2.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIqqedatqlrhICLIDVALPADDGVSSFTQLKNQQPATlcyapplstddtaeILFTSGTTSRPKGVVITHYNL 198
Cdd:TIGR01923 81 LEEKDFQA----------DSLDRIEAAGRYETSLSASFNMDQIAT--------------LMFTSGTTGKPKAVPHTFRNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 RFAGYYSAWQCALRDDDVYLTVMPAFHIDCQcTAAMAAFSAGATFVLVEKYSAraFWGQVQKYRATVTECIPMMIRTLMV 278
Cdd:TIGR01923 137 YASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 279 QP-PSANDRQHRLREVMFYLNLSEQekdafCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDH 357
Cdd:TIGR01923 214 EGgHNENLRKILLGGSAIPAPLIEE-----AQQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 358 NRplpagEIGEICIKGvpgKTIFKEYfLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
Cdd:TIGR01923 289 KE-----GHGEIMVKG---ANLMKGY-LYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:TIGR01923 360 TVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-517 |
4.34e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 212.94 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 5 GGQHLRQMWDDLADVYGHKTALicESSGGvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPAL--DFFGA---TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 85 IGAIMVPIN----ARLLREEsawiLQNSQACLLVTSAQFYPMYQQIQqeDATQLRHICLIDV----------AL------ 144
Cdd:PRK05605 105 LGAVVVEHNplytAHELEHP----FEDHGARVAIVWDKVAPTVERLR--RTTPLETIVSVNMiaampllqrlALrlpipa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 145 ----------PADDGVSSFTQLKNQQPATLCYA--PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR---FAGyySAWQC 209
Cdd:PRK05605 179 lrkaraaltgPAPGTVPWETLVDAAIGGDGSDVshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFanaAQG--KAWVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 210 ALRDDD-VYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVqppSANDRQH 288
Cdd:PRK05605 257 GLGDGPeRVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE---AAEERGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 289 RLREVMFYL----NLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGrAGFCyEAEIR----DDHNRP 360
Cdd:PRK05605 334 DLSGVRNAFsgamALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVG-VPFP-DTEVRivdpEDPDET 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 361 LPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENII 440
Cdd:PRK05605 412 MPDGEEGELLVRG---PQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1629467165 441 ATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK05605 488 REHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
42-517 |
6.33e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 211.94 E-value: 6.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 42 ELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYP 121
Cdd:PRK07786 47 ELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 122 MYQQIQQEDATQLrhiCLIDVALPADDGVSSFTQLKNQqpATLCYAPPLSTDDT-AEILFTSGTTSRPKGVVITHYNLR- 199
Cdd:PRK07786 127 VATAVRDIVPLLS---TVVVAGGSSDDSVLGYEDLLAE--AGPAHAPVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 200 --FAGYYsAWQcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL-VEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:PRK07786 202 qaMTCLR-TNG-ADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPpSANDRQHRLREVMF-YLNLSEQEKDAFCERF-GVRLLTSYGMTE-TIVGIIGDRPGDKRRWPSIGRAGFCYEAEI 353
Cdd:PRK07786 280 CAEQ-QARPRDLALRVLSWgAAPASDTLLRQMAATFpEAQILAAFGQTEmSPVTCMLLGEDAIRKLGSVGKVIPTVAARV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 354 RDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSC 433
Cdd:PRK07786 359 VDENMNDVPVGEVGEIVYRA---PTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYC 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 434 VELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL-NEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
Cdd:PRK07786 435 AEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVrNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVL 514
|
....*
gi 1629467165 513 RKNLK 517
Cdd:PRK07786 515 KTELR 519
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
37-517 |
8.21e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 210.43 E-value: 8.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFypmyqqiqqEDATqlrhicLIDVALPAddgvssFT-QLKNQQPATLCYAPPlstDDTAEILFTSGTTSRPKGVVITH 195
Cdd:PRK09088 102 DAV---------AAGR------TDVEDLAA------FIaSADALEPADTPSIPP---ERVSLILFTSGTSGQPKGVMLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTE--CIPMMI 273
Cdd:PRK09088 158 RNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHyfCVPQMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 274 RTLMVQP---PSANDR---------QHRLREVMFYLNLseqekdafcerfGVRLLTSYGMTE--TIVGIigdrPGDKRRW 339
Cdd:PRK09088 238 QAFRAQPgfdAAALRHltalftggaPHAAEDILGWLDD------------GIPMVDGFGMSEagTVFGM----SVDCDVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 340 PS-IGRAGFC---YEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFY 415
Cdd:PRK09088 302 RAkAGAAGIPtptVQTRVVDDQGNDCPAGVPGELLLRG---PNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 416 FVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPS 495
Cdd:PRK09088 379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPK 458
|
490 500
....*....|....*....|..
gi 1629467165 496 YLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK09088 459 HLRLVDALPRTASGKLQKARLR 480
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
23-517 |
4.24e-61 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 206.95 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALIcesSGGVvnRYSYLELNQEINRTAN-LFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:cd05958 1 RTCLR---SPER--EWTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNsqacllvtsaqfypmyqqiqqedatqlrhiCLIDVALPADDGVSSftqlknqqpatlcyapplstDDTAEILFT 181
Cdd:cd05958 76 AYILDK------------------------------ARITVALCAHALTAS--------------------DDICILAFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYN-LRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQK 260
Cdd:cd05958 106 SGTTGAPKATMHFHRDpLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIAR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 261 YRATVTECIPMMIRTLMVQPPSAndrQHRLREVMFYLNLSE----QEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDK 336
Cdd:cd05958 186 YKPTVLFTAPTAYRAMLAHPDAA---GPDLSSLRKCVSAGEalpaALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 337 RrwpsIGRAGFC---YEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKeYFLNPKATAKVleADGWLHTGDTGYCDEEGF 413
Cdd:cd05958 263 R----PGATGKPvpgYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 414 FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFRFCEQNMAK 490
Cdd:cd05958 333 FRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAP 412
|
490 500
....*....|....*....|....*..
gi 1629467165 491 FKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05958 413 YKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
37-503 |
9.79e-60 |
|
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: 203.74 E-value: 9.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYpmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstddtaeiLFTSGTTSRPKGVVITHY 196
Cdd:cd05940 83 AALY----------------------------------------------------------IYTSGTTGLPKAAIISHR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 N-LRFAGYYSAWQCALRDDDVYLTvMPAFH----IDCQCTAAMAAFsagaTFVLVEKYSARAFWGQVQKYRATVTECIPM 271
Cdd:cd05940 105 RaWRGGAFFAGSGGALPSDVLYTC-LPLYHstalIVGWSACLASGA----TLVIRKKFSASNFWDDIRKYQATIFQYIGE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 272 MIRTLMVQPPSANDRQHRLReVMFYLNLSEQEKDAFCERFGV-RLLTSYGMTETIVGIIG--DRPGDKRRWPSIGRAGFC 348
Cdd:cd05940 180 LCRYLLNQPPKPTERKHKVR-MIFGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINffGKPGAIGRNPSLLRKVAP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 349 YE---------AEIRDDHNR--PLPAGEIGEiCIKGVPGKTIFKEYFLNPKATAKVL-----EADGWLHTGDTGYCDEEG 412
Cdd:cd05940 259 LAlvkydlesgEPIRDAEGRciKVPRGEPGL-LISRINPLEPFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD-EAIKAFVVLNEGETLSEEEFFRFCEQNMAKF 491
Cdd:cd05940 338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDgRAGMAAIVLQPNEEFDLSALAAHLEKNLPGY 417
|
490
....*....|..
gi 1629467165 492 KVPSYLEIRKDL 503
Cdd:cd05940 418 ARPLFLRLQPEM 429
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-517 |
5.29e-58 |
|
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: 198.81 E-value: 5.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 33 GVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACL 112
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 113 LVTsaqfypmyqqiqqedatqlrhiclidvalpadDGvssftqlknqqpatlcyapplsTDDTAEILFTSGTTSRPKGVV 192
Cdd:cd05971 82 LVT--------------------------------DG----------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 193 ITHYNL--RFAGYYSAWQCALRDDDVYLT-------------VMPAFHIDCQCTAAMAafsagatfvlvEKYSARAFWGQ 257
Cdd:cd05971 108 HAHRVLlgHLPGVQFPFNLFPRDGDLYWTpadwawigglldvLLPSLYFGVPVLAHRM-----------TKFDPKAALDL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 258 VQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFY-LNLSEQEKDAFCERFGVRLLTSYGMTET--IVG---IIGD 331
Cdd:cd05971 177 MSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGgESLGEELLGWAREQFGVEVNEFYGQTECnlVIGncsALFP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 332 -RPGdkrrwpSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDE 410
Cdd:cd05971 257 iKPG------SMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE-LPDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQN 487
Cdd:cd05971 329 DGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTR 408
|
490 500 510
....*....|....*....|....*....|
gi 1629467165 488 MAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05971 409 LAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
23-517 |
3.88e-57 |
|
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: 196.53 E-value: 3.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESsgGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd05919 1 KTAFYAAD--RSV---TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTSAqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTS 182
Cdd:cd05919 76 YIARDCEARLVVTSA-------------------------------------------------------DDIAYLLYSS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 183 GTTSRPKGVVITHYN-LRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLV-EKYSARAFWGQVQK 260
Cdd:cd05919 101 GTTGPPKGVMHAHRDpLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNpGWPTAERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 261 YRATVTECIPMMIRTLMvqpPSANDRQHRLREVMFYLN----LSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDK 336
Cdd:cd05919 181 FRPTVLYGVPTFYANLL---DSCAGSPDALRSLRLCVSageaLPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAW 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 337 RrWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYF 416
Cdd:cd05919 258 R-LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG---PSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTH 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFRFCEQNMAKFKV 493
Cdd:cd05919 333 AGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKV 412
|
490 500
....*....|....*....|....
gi 1629467165 494 PSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05919 413 PRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
37-517 |
1.63e-56 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 199.41 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGlAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG-GEAAGIANPINPLLEPEQIAELLRAAGAKVLVTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFyP---MYQQIQQ--EDATQLRHICLID---------------VALPADDGVSSF-TQLKNQQPATLCYAPPLSTDDT 175
Cdd:PRK07529 137 GPF-PgtdIWQKVAEvlAALPELRTVVEVDlarylpgpkrlavplIRRKAHARILDFdAELARQPGDRLFSGRPIGPDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 176 AEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCA----LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLV----- 246
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNE----VANAWLGAlllgLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgy 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 247 --EKYSARaFWGQVQKYRATVTECIPMMIRTLMVQPPSANDrqhrLREVMFYLN----LSEQEKDAFCERFGVRLLTSYG 320
Cdd:PRK07529 292 rgPGVIAN-FWKIVERYRINFLSGVPTVYAALLQVPVDGHD----ISSLRYALCgaapLPVEVFRRFEAATGVRIVEGYG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETIVGIIGDRPGDKRRWPSIG-RAGFCyEAEI-----RDDHNRPLPAGEIGEICIKGvPGktIFKEYfLNPKATAKVL 394
Cdd:PRK07529 367 LTEATCVSSVNPPDGERRIGSVGlRLPYQ-RVRVvilddAGRYLRDCAVDEVGVLCIAG-PN--VFSGY-LEAAHNKGLW 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 395 EADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET 474
Cdd:PRK07529 442 LEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1629467165 475 LSEEEFFRFCEQNMA-KFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07529 522 ATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
178-513 |
1.88e-56 |
|
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: 191.71 E-value: 1.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 178 ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATfVLVEKYSARAFWGQ 257
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAN-VVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 258 VQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVmfyLNLSEQEK-DAFCERFGVRLLTSYGMTET----IVGIIGDR 332
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV---LGLDAPETiQRFEETTGATFWSLYGQTETsglvTLSPYRER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 PGdkrrwpSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEG 412
Cdd:cd17637 161 PG------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRG-P--LVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 413 FFYFVDRRC--NMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAK 490
Cdd:cd17637 231 YLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIAR 310
|
330 340
....*....|....*....|...
gi 1629467165 491 FKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:cd17637 311 YKKPRYVVFVEALPKTADGSIDR 333
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
21-517 |
3.09e-56 |
|
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: 195.83 E-value: 3.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
Cdd:TIGR02262 19 GGKTAFIDDIS-----SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 101 SAWILQNSQACLLVTSAQFYPMYQQIQQeDATQLRHICLIDVALPADDGVSSFTQLKNQQPATlcyaPPLSTDDTAEILF 180
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALG-KSPHLEHRVVVGRPEAGEVQLAELLATESEQFKP----AATQADDPAFWLY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 181 TSGTTSRPKGVVITHYNLRF-AGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLV-EKYSARAFWGQV 258
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNPYWtAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMgERPTPDAVFDRL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 QKYRATVTECIPMMIRTLMVQPPSANDRQHRLR------EVmfylnLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDR 332
Cdd:TIGR02262 249 RRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRlctsagEA-----LPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 PGDKRR----WPSIGragfcYEAEIRDDHNRPLPAGEIGEICIKGVPGKTIfkeYFLNPKATAKVLEAdGWLHTGDTGYC 408
Cdd:TIGR02262 324 PGDVRYgtsgKPVPG-----YRLRLVGDGGQDVADGEPGELLISGPSSATM---YWNNRAKSRDTFQG-EWTRSGDKYVR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNM 488
Cdd:TIGR02262 395 NDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRL 474
|
490 500
....*....|....*....|....*....
gi 1629467165 489 AKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:TIGR02262 475 APYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
8-511 |
7.42e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 195.66 E-value: 7.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 8 HLRQMWDDLADVYGH---KTALICESSG-GVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLA 83
Cdd:PRK13295 22 HDRTINDDLDACVAScpdKTAVTAVRLGtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 84 KIGAIMVPInARLLRE-ESAWILQNSQACLLVTSAQF----YP-MYQQIQqEDATQLRHICLIDvalpaDDGVSSFTQL- 156
Cdd:PRK13295 102 RIGAVLNPL-MPIFRErELSFMLKHAESKVLVVPKTFrgfdHAaMARRLR-PELPALRHVVVVG-----GDGADSFEALl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 157 ------KNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHyNLRFAGYYS-AWQCALRDDDVYLTVMPAFHidcq 229
Cdd:PRK13295 175 itpaweQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTA-NTLMANIVPyAERLGLGADDVILMASPMAH---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 230 ctaamaafsaGATFVlvekYSARafwgqvqkyratvtecIPMMIRTLMV-----QPPSAND--RQHRLREVM----FYLN 298
Cdd:PRK13295 250 ----------QTGFM----YGLM----------------MPVMLGATAVlqdiwDPARAAEliRTEGVTFTMastpFLTD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 299 LSEQEK---------DAFC---------------ERFGVRLLTSYGMTET--IVGIIGDRPGDKrrwpSIGRAGFCY--- 349
Cdd:PRK13295 300 LTRAVKesgrpvsslRTFLcagapipgalverarAALGAKIVSAWGMTENgaVTLTKLDDPDER----ASTTDGCPLpgv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 EAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKvlEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGE 429
Cdd:PRK13295 376 EVRVVDADGAPLPAGQIGRLQVRGC---SNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC-EQNMAKFKVPSYLEIRKDLPRNCS 508
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPS 530
|
...
gi 1629467165 509 GKI 511
Cdd:PRK13295 531 GKI 533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
174-513 |
1.34e-55 |
|
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: 189.25 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 174 DTAEILFTSGTTSRPKGVVITHynLRFAGYYSAW-QCA-LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSA 251
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAH--RQTLRAAAAWaDCAdLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLRevmFYLNLSEQEKDAFCERFGVRL-----LTSYGMTETIV 326
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLR---AAVTGAATVPVELVRRMRSELgfetvLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 327 GIIGdRPGDKRRWPS--IGRAGFCYEAEIRDDhnrplpageiGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGD 404
Cdd:cd17638 156 ATMC-RPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRG---YNVMQGYLDDPEATAEAIDADGWLHTGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC 484
Cdd:cd17638 222 VGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWC 301
|
330 340
....*....|....*....|....*....
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:cd17638 302 RERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
38-502 |
6.01e-55 |
|
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: 190.88 E-value: 6.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSA 117
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 qfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplsTDDTAEILFTSGTTSRPKGVVITHYN 197
Cdd:cd05907 86 ------------------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRN 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEkySARAFWGQVQKYRATVTECIPmmirtLM 277
Cdd:cd05907 112 ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAVP-----RV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 278 VQPPSANDRQH---RLREVMFYL----NLS---------EQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRwPS 341
Cdd:cd05907 185 WEKVYAAIKVKavpGLKRKLFDLavggRLRfaasggaplPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRI-GT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 342 IGRAGFCYEAEIRDDhnrplpageiGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRC 421
Cdd:cd05907 264 VGKPLPGVEVRIADD----------GEILVRG---PNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 422 NMIK-RGGENVSCVELENIIATHPKIQDIVVVGIKDSirdeAIKAFVVLNegetlsEEEFFRFCEQNMAKFKvpSYLEIR 500
Cdd:cd05907 331 DLIItSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPD------PEALEAWAEEHGIAYT--DVAELA 398
|
..
gi 1629467165 501 KD 502
Cdd:cd05907 399 AN 400
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
17-511 |
9.22e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 192.85 E-value: 9.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALIcesSGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PRK08162 28 AEVYPDRPAVI---HGDR--RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQ-IQQEDATqlrHICLIDVALPADDGVSSFTQLKNQQ------PAtlcYAPP 169
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIVDTEFAEVAREaLALLPGP---KPLVIDVDDPEYPGGRFIGALDYEAflasgdPD---FAWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 170 LSTD--DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQC---TAAMAAFsagaTFV 244
Cdd:PRK08162 177 LPADewDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWCfpwTVAARAG----TNV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 245 LVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSAND-RQHRLR-------------EVMfylnlseqekdafcER 310
Cdd:PRK08162 253 CLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAgIDHPVHamvagaappaaviAKM--------------EE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 311 FGVRLLTSYGMTETI--VGIIGDRPG-----DKRRWPSIGRAGFCYEAE----IRD-DHNRPLPA-GE-IGEICIKGvpg 376
Cdd:PRK08162 319 IGFDLTHVYGLTETYgpATVCAWQPEwdalpLDERAQLKARQGVRYPLQegvtVLDpDTMQPVPAdGEtIGEIMFRG--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 377 KTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
Cdd:PRK08162 396 NIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1629467165 457 SIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIrKDLPRNCSGKI 511
Cdd:PRK08162 475 PKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKI 528
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
24-517 |
1.20e-54 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 192.75 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 24 TALICESSGGVVNRYSYLELNQEInrTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
Cdd:PLN02574 56 TALIDSSTGFSISYSELQPLVKSM--AAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 104 ILQNSQACLLVTSAqfypmyqqiqqEDATQLRHICLIDVALPA----DDGVSSFTQLKN--QQPATLCYAPPLSTDDTAE 177
Cdd:PLN02574 134 RVVDCSVGLAFTSP-----------ENVEKLSPLGVPVIGVPEnydfDSKRIEFPKFYEliKEDFDFVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 178 ILFTSGTTSRPKGVVITHYNL--------RF-AGYYSAWQCalrdDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEK 248
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLiamvelfvRFeASQYEYPGS----DNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAFWGQVQKYRATVTECIP--MMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFG-VRLLTSYGMTE-T 324
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPpiLMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTEsT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 325 IVGIIGDRPGDKRRWPSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKGvPGktIFKEYFLNPKATAKVLEADGWLHTG 403
Cdd:PLN02574 359 AVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQG-PG--VMKGYLNNPKATQSTIDKDGWLRTG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 404 DTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRF 483
Cdd:PLN02574 436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINY 515
|
490 500 510
....*....|....*....|....*....|....
gi 1629467165 484 CEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PLN02574 516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
6-517 |
2.11e-54 |
|
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: 191.59 E-value: 2.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGhKTALICESSGgvVNrYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
Cdd:cd17642 17 GEQLHKAMKRYASVPG-TIAFTDAHTG--VN-YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATqLRHICLIDVALPADDGVSSFTQLKNQQPATL- 164
Cdd:cd17642 93 GVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKI-IKTIIILDSKEDYKGYQCLYTFITQNLPPGFn 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 165 --CYAPPLST--DDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSAWQ----CALRDDDVYLTVMPaFHIDCQCTAAMAA 236
Cdd:cd17642 172 eyDFKPPSFDrdEQVALIMNSSGSTGLPKGVQLTHKNI-VARFSHARDpifgNQIIPDTAILTVIP-FHHGFGMFTTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 237 FSAGATFVLVEKYSARAFWGQVQKYRATVTecipMMIRTLMV-QPPSANDRQHRLREVMFYLN----LSEQEKDAFCERF 311
Cdd:cd17642 250 LICGFRVVLMYKFEEELFLRSLQDYKVQSA----LLVPTLFAfFAKSTLVDKYDLSNLHEIASggapLSKEVGEAVAKRF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLL-TSYGMTETIVGII-----GDRPGdkrrwpSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKGvPGktIFKEYF 384
Cdd:cd17642 326 KLPGIrQGYGLTETTSAILitpegDDKPG------AVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKG-PM--IMKGYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 385 LNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
Cdd:cd17642 397 NNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 465 AFVVLNEGETLSEEEFFRFCEQNMAKFK-VPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd17642 477 AVVVLEAGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
65-516 |
3.34e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 188.31 E-value: 3.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 65 VALHLDNCPEFIFCWFGLAKIGAIMVPIN-----ARLLREesawiLQNSQACLLVTSAQFYPMYqqiqqeDATQLRHICL 139
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNttrrgAALAAD-----IRRADCQLLVTDAEHRPLL------DGLDLPGVRV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 140 IDVALPAddgvssFTQLKnQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLT 219
Cdd:PRK13388 124 LDVDTPA------YAELV-AAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 220 VMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLReVMFYLNL 299
Cdd:PRK13388 197 SMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLR-VAFGNEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 300 SEQEKDAFCERFGVRLLTSYGMTETIVGIIGDR---PGdkrrwpSIGRaGF-------------CYEAEIrDDHNRPLPA 363
Cdd:PRK13388 276 SPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPgtpPG------SIGR-GApgvaiynpetlteCAVARF-DAHGALLNA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 364 GE-IGEICIKGVPGKtiFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIAT 442
Cdd:PRK13388 348 DEaIGELVNTAGAGF--FEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLR 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629467165 443 HPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRF--CEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK13388 425 HPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
37-516 |
4.80e-53 |
|
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: 186.95 E-value: 4.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMyqqiqqeDATQLRHICLIDVALPADDGV-SSFTQLKNqqpatlcyAPPLSTDDTAEILFTSGTTSRPKGVVITH 195
Cdd:cd05923 108 VDAQVM-------DAIFQSGVRVLALSDLVGLGEpESAGPLIE--------DPPREPEQPAFVFYTSGTTGLPKGAVIPQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YNLRFAGYYSAWQCALR--DDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMI 273
Cdd:cd05923 173 RAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 274 RTLMVQPPSANDRQHRLREVMFylnLSEQEKDAFCERFG----VRLLTSYGMTETIVGIIGDRPgdkrRWPSIGRAGFCY 349
Cdd:cd05923 253 DALAAAAEFAGLKLSSLRHVTF---AGATMPDAVLERVNqhlpGEKVNIYGTTEAMNSLYMRDA----RTGTEMRPGFFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 EAEIRDDHNRP---LPAGEIGEICIKgVPGKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:cd05923 326 EVRIVRIGGSPdeaLANGEEGELIVA-AAADAAFTGYLNQPEATAKKLQ-DGWYRTGDVGYVDPSGDVRILGRVDDMIIS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGeTLSEEEFFRFC-EQNMAKFKVPSYLEIRKDLPR 505
Cdd:cd05923 404 GGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCrASELADFKRPRRYFFLDELPK 482
|
490
....*....|.
gi 1629467165 506 NCSGKIIRKNL 516
Cdd:cd05923 483 NAMNKVLRRQL 493
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
37-517 |
2.66e-52 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 185.29 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQ-FYPMYQQIQQ-----------EDATQLRhicLIDVALPADDGVSSFTQ-LKNQQPATlcyAPPLSTddTAEILFTSG 183
Cdd:PRK12406 91 ADlLHGLASALPAgvtvlsvptppEIAAAYR---ISPALLTPPAGAIDWEGwLAQQEPYD---GPPVPQ--PQSMIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 184 TTSRPKGVvithynLRFAGyySAWQCALRDDDVYL---------TVMP---------AFHIdcqctaamAAFSAGATFVL 245
Cdd:PRK12406 163 TTGHPKGV------RRAAP--TPEQAAAAEQMRALiyglkpgirALLTgplyhsapnAYGL--------RAGRLGGVLVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 246 VEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQ--HRLREVMFYLNLSEQE-KDAFCERFGVRLLTSYGMT 322
Cdd:PRK12406 227 QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADvKRAMIEWWGPVIYEYYGST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 323 ETivGIIG--------DRPGdkrrwpSIGRAgfCYEAEIR--DDHNRPLPAGEIGEICIKgVPGKTIFKeYFLNPKATAK 392
Cdd:PRK12406 307 ES--GAVTfatsedalSHPG------TVGKA--APGAELRfvDEDGRPLPQGEIGEIYSR-IAGNPDFT-YHNKPEKRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 393 VlEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
Cdd:PRK12406 375 I-DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1629467165 473 ETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK12406 454 ATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
39-517 |
3.98e-52 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 185.85 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINR-TANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN----ARLLREEsawiLQNSQACLL 113
Cdd:PRK08751 52 TYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNplytPRELKHQ----LIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 114 VTSAQFYPMYQQIQQEdaTQLRHI--------------CLIDVALP---------ADDGVSSFTQ-LKNQQPATLcyaPP 169
Cdd:PRK08751 128 VVIDNFGTTVQQVIAD--TPVKQVittglgdmlgfpkaALVNFVVKyvkklvpeyRINGAIRFREaLALGRKHSM---PT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 170 L--STDDTAEILFTSGTTSRPKGVVITHYNL----RFAGYYSAWQCALRD-DDVYLTVMPAFHI-DCQCTAAMAAFSAGA 241
Cdd:PRK08751 203 LqiEPDDIAFLQYTGGTTGVAKGAMLTHRNLvanmQQAHQWLAGTGKLEEgCEVVITALPLYHIfALTANGLVFMKIGGC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 242 TFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSAndrQHRLREVMFYLNLSEQEKDAFCERF----GVRLLT 317
Cdd:PRK08751 283 NHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFD---QIDFSSLKMTLGGGMAVQRSVAERWkqvtGLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 318 SYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEAD 397
Cdd:PRK08751 360 AYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG---PQVMKGYWKRPEETAKVMDAD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 398 GWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAfVVLNEGETLSE 477
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKV-VIVKKDPALTA 515
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1629467165 478 EEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08751 516 EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
22-516 |
2.18e-51 |
|
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: 181.19 E-value: 2.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:cd05930 2 DAVAVVDGDQ-----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqQPATLCYapplstddtaeILFT 181
Cdd:cd05930 77 AYILEDSGAKLVLT--------------------------------------------DPDDLAY-----------VIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYNL--RFAGYYSAWQcaLRDDDVYLTVMP-AFhiDCQCTAAMAAFSAGATFVLV---EKYSARAFW 255
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLvnLLLWMQEAYP--LTPGDRVLQFTSfSF--DVSVWEIFGALLAGATLVVLpeeVRKDPEALA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 256 GQVQKYRATVTECIPMMIRTLMVQPpsANDRQHRLREVMFyl-nLSEQEKDAFCERF-GVRLLTSYGMTETIVGI---IG 330
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLVggeaLPPDLVRRWRELLpGARLVNLYGPTEATVDAtyyRV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 331 DRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYFLNPKATAKVLEAD-----GWLH-TGD 404
Cdd:cd05930 256 PPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGG-AGLAR--GYLNRPELTAERFVPNpfgpgERMYrTGD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRGGENVscvEL---ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF 481
Cdd:cd05930 333 LVRWLPDGNLEFLGRIDDQVKIRGYRI---ELgeiEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELR 409
|
490 500 510
....*....|....*....|....*....|....*
gi 1629467165 482 RFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd05930 410 AHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-517 |
2.99e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 181.10 E-value: 2.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 48 NRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA----IMVPINArllreesawILQNSQACLLVTSAQfypmy 123
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNP---------TLKESVLRYLVADAG----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 124 QQIQQEDATQLRHICLIDVALPADDGVSSFTQLKNQQpaTLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGY 203
Cdd:cd05922 70 GRIVLADAGAADRLRDALPASPDPGTVLDADGIRAAR--ASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 204 YSAWQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLVEKYS-ARAFWGQVQKYRATVTECIPM---MIRTLMVQ 279
Cdd:cd05922 148 SIAEYLGITADDRALTVLP-LSYDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPStyaMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 280 P---PSandrqhrLRevmfYLN-----LSEQEKDAFCERF-GVRLLTSYGMTETIVGI-------IGDRPGdkrrwpSIG 343
Cdd:cd05922 227 PaklPS-------LR----YLTqaggrLPQETIARLRELLpGAQVYVMYGQTEATRRMtylpperILEKPG------SIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 344 RAGFCYEAEIRDDHNRPLPAGEIGEIcikGVPGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNM 423
Cdd:cd05922 290 LAIPGGEFEILDDDGTPTPPGEPGEI---VHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 424 IKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIrDEAIKAFVVLNEGETLSeeEFFRFCEQNMAKFKVPSYLEIRKDL 503
Cdd:cd05922 367 IKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDEL 443
|
490
....*....|....
gi 1629467165 504 PRNCSGKIIRKNLK 517
Cdd:cd05922 444 PLTASGKVDYAALR 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
57-517 |
3.47e-50 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 180.63 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQqeDATQLRH 136
Cdd:PRK08974 69 LGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVV--FKTPVKH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 137 ICLIDVA--LPADDG------VSSFTQL--KNQQPATLCY-------------APPLSTDDTAEILFTSGTTSRPKGVVI 193
Cdd:PRK08974 147 VILTRMGdqLSTAKGtlvnfvVKYIKRLvpKYHLPDAISFrsalhkgrrmqyvKPELVPEDLAFLQYTGGTTGVAKGAML 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 194 THYN-----LRFAGYYSAwqcALRD-DDVYLTVMPAFHI-----DCqctaamaafsagatFVLVEKYSAR---------- 252
Cdd:PRK08974 227 THRNmlanlEQAKAAYGP---LLHPgKELVVTALPLYHIfaltvNC--------------LLFIELGGQNllitnprdip 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 253 AFWGQVQKYRATVTECIPMMIRTLMvqppsaNDRQhrLREVMF-YLNLS----EQEKDAFCERF----GVRLLTSYGMTE 323
Cdd:PRK08974 290 GFVKELKKYPFTAITGVNTLFNALL------NNEE--FQELDFsSLKLSvgggMAVQQAVAERWvkltGQYLLEGYGLTE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTG 403
Cdd:PRK08974 362 CSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKG---PQVMLGYWQRPEATDEVIK-DGWLATG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 404 DTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFRF 483
Cdd:PRK08974 438 DIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITH 516
|
490 500 510
....*....|....*....|....*....|....
gi 1629467165 484 CEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08974 517 CRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
57-517 |
6.00e-50 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 179.99 E-value: 6.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLR- 135
Cdd:PLN02860 52 LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPSLMw 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 136 HICLIDVALPADDGVSSF-------TQLKNQQPATLCYAPplstDDTAEILFTSGTTSRPKGVVITHYNL--------RF 200
Cdd:PLN02860 132 QVFLESPSSSVFIFLNSFlttemlkQRALGTTELDYAWAP----DDAVLICFTSGTTGRPKGVTISHSALivqslakiAI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 201 AGYYSawqcalrdDDVYLTVMPAFHI-------------DCQctaamaafsagatfVLVEKYSARAFWGQVQKYRATVTE 267
Cdd:PLN02860 208 VGYGE--------DDVYLHTAPLCHIgglssalamlmvgACH--------------VLLPKFDAKAALQAIKQHNVTSMI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 268 CIPMMIRTLmVQPPSANDRQHRLREVMFYLN----LSEQEKDAFCERF-GVRLLTSYGMTETIVGIIGDRPGDKRRWPSi 342
Cdd:PLN02860 266 TVPAMMADL-ISLTRKSMTWKVFPSVRKILNgggsLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTLHDPTLESP- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 343 gRAGFCYEAEIRDDHN---------RPLPAGEIGeICIKGVP--------GKTIFKEYFLNPKATAKVLEADGWLHTGDT 405
Cdd:PLN02860 344 -KQTLQTVNQTKSSSVhqpqgvcvgKPAPHVELK-IGLDESSrvgriltrGPHVMLGYWGQNSETASVLSNDGWLDTGDI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 406 GYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG------------- 472
Cdd:PLN02860 422 GWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakk 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1629467165 473 -ETLSEEEFFRFC-EQNMAKFKVP-SYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PLN02860 502 nLTLSSETLRHHCrEKNLSRFKIPkLFVQWRKPFPLTTTGKIRRDEVR 549
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
24-517 |
9.47e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 179.17 E-value: 9.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 24 TALICEssGGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
Cdd:PRK06164 27 VALIDE--DRPL---SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 104 ILQNSQACLLVTSAQF-----YPMYQQIQQEDATQLRHICLIDV---ALPADDGVSSFTQLKNQQPATL-CYAPPLSTDD 174
Cdd:PRK06164 102 ILGRGRARWLVVWPGFkgidfAAILAAVPPDALPPLRAIAVVDDaadATPAPAPGARVQLFALPDPAPPaAAGERAADPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 175 TAEILF-TSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMP---AFHIdcqcTAAMAAFSAGATFVLVEKYS 250
Cdd:PRK06164 182 AGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPfcgVFGF----STLLGALAGGAPLVCEPVFD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 251 ARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHrLREVMF---------YLNLSEQEkdafcerfGVRLLTSYGM 321
Cdd:PRK06164 258 AARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPS-ARLFGFasfapalgeLAALARAR--------GVPLTGLYGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 322 TETIVGI-IGDRPGDKR-RWPSIGRAGFCyEAEIR---DDHNRPLPAGEIGEICIKGvPGktIFKEYFLNPKATAKVLEA 396
Cdd:PRK06164 329 SEVQALVaLQPATDPVSvRIEGGGRPASP-EARVRardPQDGALLPDGESGEIEIRA-PS--LMRGYLDNPDATARALTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 397 DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIkAFVVLNEGETLS 476
Cdd:PRK06164 405 DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPD 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1629467165 477 EEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSG---KIIRKNLK 517
Cdd:PRK06164 484 EAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
21-512 |
1.67e-49 |
|
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: 179.31 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICESSGGVVNR-YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:cd17634 67 GDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSAQFY---------PMYQQIQQEDATQLRHICLID---VALPADDGVSSF--TQLKNQQPAtlc 165
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVragrsvplkKNVDDALNPNVTSVEHVIVLKrtgSDIDWQEGRDLWwrDLIAKASPE--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 YAP-PLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLTVMPAFHIDCQCTAAMAAFS 238
Cdd:cd17634 224 HQPeAMNAEDPLFILYTSGTTGKPKGVLHTT-----GGYlvYAATTMKYVFDygpgDIYWCTADVGWVTGHSYLLYGPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 239 AGATFVLVEKY----SARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHR--LReVMFYLN--LSEQEKDAFCER 310
Cdd:cd17634 299 CGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRssLR-ILGSVGepINPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 311 FGVR---LLTSYGMTETIVGIIGDRPG-DKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKG-VPGKTifKEYFL 385
Cdd:cd17634 378 IGKEkcpVVDTWWQTETGGFMITPLPGaIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpWPGQT--RTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 386 NPKATAKVLEA--DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463
Cdd:cd17634 456 DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAP 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1629467165 464 KAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
Cdd:cd17634 536 YAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
6-516 |
3.34e-49 |
|
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: 176.36 E-value: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGHKTALICessGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVD---GDR--RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAimVPINA----RLlREESAWIlQNSQACLLVTSAQFYPMYQQiqqEDATQLRHiclidvalpaddgvssftqlknqqp 161
Cdd:cd05920 89 GA--VPVLAlpshRR-SELSAFC-AHAEAVAYIVPDRHAGFDHR---ALARELAE------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 162 atlcyapplSTDDTAEILFTSGTTSRPKGVVITH----YNLRfagyYSAWQCALRDDDVYLTVMPAFH-IDCQCTAAMAA 236
Cdd:cd05920 137 ---------SIPEVALFLLSGGTTGTPKLIPRTHndyaYNVR----ASAEVCGLDQDTVYLAVLPAAHnFPLACPGVLGT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 237 FSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLM--VQPPSANDRQHRLREV---MFYLNLSEQEKDAFcerf 311
Cdd:cd05920 204 LLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLdaAASRRADLSSLRLLQVggaRLSPALARRVPPVL---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLLTSYGMTEtivGIIG----DRPGDkRRWPSIGRAgFCYEAEIR--DDHNRPLPAGEIGEICIKGvPgkTIFKEYFL 385
Cdd:cd05920 280 GCTLQQVFGMAE---GLLNytrlDDPDE-VIIHTQGRP-MSPDDEIRvvDEEGNPVPPGEEGELLTRG-P--YTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 386 NPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1629467165 466 FVVLNeGETLSEEEFFRFC-EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd05920 432 FVVLR-DPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
65-517 |
5.87e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 176.80 E-value: 5.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 65 VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQqiqqEDATQLRHIcliDVAL 144
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLD----GLDPGVRVI---NVDS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 145 PAddgvssFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAF 224
Cdd:PRK07867 130 PA------WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 225 HIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLReVMFYLNLSEQEK 304
Cdd:PRK07867 204 HSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLR-IVYGNEGAPGDI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 305 DAFCERFGVRLLTSYGMTETIVGII---GDRPGdkrrwpSIGRAGF------------CYEAEIrDDHNRPLPAGEIGEI 369
Cdd:PRK07867 283 ARFARRFGCVVVDGFGSTEGGVAITrtpDTPPG------ALGPLPPgvaivdpdtgteCPPAED-ADGRLLNADEAIGEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 370 CIKGVPGKtiFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI 449
Cdd:PRK07867 356 VNTAGPGG--FEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 450 VVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRF-CEQ-NMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07867 433 AVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFlAAQpDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
37-496 |
9.08e-49 |
|
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: 176.33 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTAN-LFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVT 115
Cdd:cd05938 5 TYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 SAQFYPMYQQIQQEDATQLRHICLIDVALPADdGVSSFTQLKNQQPATlcyAPP------LSTDDTAEILFTSGTTSRPK 189
Cdd:cd05938 85 APELQEAVEEVLPALRADGVSVWYLSHTSNTE-GVISLLDKVDAASDE---PVPaslrahVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 190 GVVITHYN-LRFAGYYSAwqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTEC 268
Cdd:cd05938 161 AARISHLRvLQCSGFLSL--CGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 269 IPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDaFCERFG-VRLLTSYGMTETIVGIIG--DRPGdkrrwpSIGRA 345
Cdd:cd05938 239 IGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWRE-FLRRFGpIRIREFYGSTEGNIGFFNytGKIG------AVGRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 346 GFCY---------------EAEIRDDHNR--PLPAGEIGeICIKGVPGKTIFKEYFLNPKATAKVL------EADGWLHT 402
Cdd:cd05938 312 SYLYkllfpfelikfdvekEEPVRDAQGFciPVAKGEPG-LLVAKITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 403 GDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI-KAFVVLNEGETLSEEEFF 481
Cdd:cd05938 391 GDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIgMAAVKLKPGHEFDGKKLY 470
|
490
....*....|....*
gi 1629467165 482 rfceQNMAKFkVPSY 496
Cdd:cd05938 471 ----QHVREY-LPAY 480
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
17-517 |
1.19e-48 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 176.32 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSGgvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PLN02330 38 AELYADKVAFVEAVTG---KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFY--------PMYQQIQQEDATQLRHICLIDVALPADDgvssftqlknqqpaTLCYAP 168
Cdd:PLN02330 115 LESEIKKQAEAAGAKLIVTNDTNYgkvkglglPVIVLGEEKIEGAVNWKELLEAADRAGD--------------TSDNEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 PLSTDDTAeILFTSGTTSRPKGVVITHYNLrFAGYYSAW---QCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL 245
Cdd:PLN02330 181 ILQTDLCA-LPFSSGTTGISKGVMLTHRNL-VANLCSSLfsvGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 246 VEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQP--PSANDRQHRLREVMFYLN-LSEQEKDAFCERF-GVRLLTSYGM 321
Cdd:PLN02330 259 MSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPivEEFDLSKLKLQAIMTAAApLAPELLTAFEAKFpGVQVQEAYGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 322 TETivGIIGDRPGDKRRWPSIGR---AGFCY---EAE-IRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVL 394
Cdd:PLN02330 339 TEH--SCITLTHGDPEKGHGIAKknsVGFILpnlEVKfIDPDTGRSLPKNTPGELCVRS---QCVMQGYYNNKEETDRTI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 395 EADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET 474
Cdd:PLN02330 414 DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK 493
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1629467165 475 LSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PLN02330 494 ESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
25-516 |
3.70e-48 |
|
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: 173.68 E-value: 3.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICEssGGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
Cdd:cd17651 13 ALVAE--GRRL---TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 LQNSQACLLVTsaqfypmyqqiQQEDAtqlrhicliDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGT 184
Cdd:cd17651 88 LADAGPVLVLT-----------HPALA---------GELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 185 TSRPKGVVITHYNLrfaGYYSAWQCAL----RDDDVYLTVMPAFHIDCQ------CTaamaafsaGATFVLV---EKYSA 251
Cdd:cd17651 148 TGRPKGVVMPHRSL---ANLVAWQARAsslgPGARTLQFAGLGFDVSVQeifstlCA--------GATLVLPpeeVRTDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMF---YLNLSEQEKDAFCERFGVRLLTSYGMTETIVGI 328
Cdd:cd17651 217 PALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTggeQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 329 IGDRPGDKRRW---PSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGWL----- 400
Cdd:cd17651 297 ALSLPGDPAAWpapPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA---GLARGYLNRPELTAERFVPDPFVpgarm 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 -HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEE 479
Cdd:cd17651 374 yRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAE 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 1629467165 480 FFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17651 454 LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
37-516 |
1.88e-47 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 171.98 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQQIQQEDATqlRHICLIDvalpaDDGVSSFTQLKNQQPATLCYAPpLSTDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:PRK07514 108 PANFAWLSKIAAAAGA--PHVETLD-----ADGTGSLLEAAAAAPDDFETVP-RGADDLAAILYTSGTTGRSKGAMLSHG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLrfagyYS-------AWqcALRDDDVYLTVMPAFH-----IDCQCTAAMaafsagatfvlvekySARAFW------GQV 258
Cdd:PRK07514 180 NL-----LSnaltlvdYW--RFTPDDVLIHALPIFHthglfVATNVALLA---------------GASMIFlpkfdpDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 QKY--RATVtecipMM----IRTLMVQPPsandrqhRL-REVMFYLNL--------SEQEKDAFCERFGVRLLTSYGMTE 323
Cdd:PRK07514 238 LALmpRATV-----MMgvptFYTRLLQEP-------RLtREAAAHMRLfisgsaplLAETHREFQERTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TivGIIGDRPGD-KRRWPSIGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAKVLEADGWLH 401
Cdd:PRK07514 306 T--NMNTSNPYDgERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG-P--NVFKGYWRMPEKTAEEFRADGFFI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 402 TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF 481
Cdd:PRK07514 381 TGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAIL 460
|
490 500 510
....*....|....*....|....*....|....*
gi 1629467165 482 RFCEQNMAKFKVPSYLEIRKDLPRNCSGKiIRKNL 516
Cdd:PRK07514 461 AALKGRLARFKQPKRVFFVDELPRNTMGK-VQKNL 494
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
37-517 |
2.35e-46 |
|
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: 168.37 E-value: 2.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQfYPMYQQIQQEdatqlrhiclidvaLPADDGVSsFTqlknqqpATLCYapplstddtaeiLFTSGTTSRPKGVVITHY 196
Cdd:cd05939 83 LL-DPLLTQSSTE--------------PPSQDDVN-FR-------DKLFY------------IYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:cd05939 128 RYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDRQHRLReVMFYLNLSEQEKDAFCERFGV-RLLTSYGMTE---------TIVGIIGDRPgdkrRWPSigrag 346
Cdd:cd05939 208 LAQPPSEEEQKHNVR-LAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEgnsslvnidNHVGACGFNS----RILP----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 347 FCYEAEI--RDDHNRPLPAGEIGeICIKGVPGKT------IFK-------EYFLNPKATAKVLEADGWLH------TGDT 405
Cdd:cd05939 278 SVYPIRLikVDEDTGELIRDSDG-LCIPCQPGEPgllvgkIIQndplrrfDGYVNEGATNKKIARDVFKKgdsaflSGDV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 406 GYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK-DSIRDEAIKAFVVLNEGETlSEEEFFRFC 484
Cdd:cd05939 357 LVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvPGVEGRAGMAAIVDPERKV-DLDRFSAVL 435
|
490 500 510
....*....|....*....|....*....|...
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05939 436 AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
23-517 |
2.38e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 169.03 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESSGGVVnrySYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:PRK13390 13 RPAVIVAETGEQV---SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDvalpaddGVSSFTqlknqqpATLCYA-PPLSTDDT-AEILF 180
Cdd:PRK13390 90 YIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEID-------GFGSFE-------AALAGAgPRLTEQPCgAVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 181 TSGTTSRPKG-----------------VVIThynlrfAGYYSawqcaLRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATF 243
Cdd:PRK13390 156 SSGTTGFPKGiqpdlpgrdvdapgdpiVAIA------RAFYD-----ISESDIYYSSAPIYHA-APLRWCSMVHALGGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 244 VLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQH--RLREVMFYLNLSEQE-KDAFCERFGVRLLTSYG 320
Cdd:PRK13390 224 VLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDvsSLRAVIHAAAPCPVDvKHAMIDWLGPIVYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETIVGIIGDRPGDKRRWPSIGRAgFCYEAEIRDDHNRPLPAGEIGEICIK--GVPGKtifkeYFLNPKATAKVLEADG 398
Cdd:PRK13390 304 STEAHGMTFIDSPDWLAHPGSVGRS-VLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-----YLNDPEKTAAAQHPAH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 399 --WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS 476
Cdd:PRK13390 378 pfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGS 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1629467165 477 EE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK13390 458 DElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
16-517 |
3.29e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 169.30 E-value: 3.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 16 LADVYGHKTALICESSGGVV--NR--YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVtaDRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 92 INARLLREEsawilQNSQACLLVTSAQFYPMYQQIQQEDATqlrHICL-IDVALPADDGVSSFTqLKNQQPATLCYAPPL 170
Cdd:PRK05852 98 LDPALPIAE-----QRVRSQAAGARVVLIDADGPHDRAEPT---TRWWpLTVNVGGDSGPSGGT-LSVHLDAATEPTPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 171 STD-----DTAEILFTSGTTSRPKGVVITHYNLR------FAGYysawqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
Cdd:PRK05852 169 STPeglrpDDAMIMFTGGTTGLPKMVPWTHANIAssvraiITGY------RLSPRDATVAVMPLYHGHGLIAALLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 240 GATFVLVE--KYSARAFWGQVQKYRATVTECIPMMIRTLMVQPpsANDRQHRLREVMFYLN-----LSEQEKDAFCERFG 312
Cdd:PRK05852 243 GGAVLLPArgRFSAHTFWDDIKAVGATWYTAVPTIHQILLERA--ATEPSGRKPAALRFIRscsapLTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 313 VRLLTSYGMTE-----TIVGIIGDRPGDKRRwPSIGRAGFCYEAEIR----DDHnrPLPAGEIGEICIKGvpgKTIFKEY 383
Cdd:PRK05852 321 APVVCAFGMTEathqvTTTQIEGIGQTENPV-VSTGLVGRSTGAQIRivgsDGL--PLPAGAVGEVWLRG---TTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 384 FLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463
Cdd:PRK05852 395 LGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAV 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 464 KAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK05852 474 AAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
22-516 |
3.47e-46 |
|
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: 167.42 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARllrees 101
Cdd:cd05945 6 DRPAVVEGG-----RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 awilqnsqacllvtsaqfYPmyqqiqqedATQLRHIclIDVAlpaddgvssftqlknqQPATLCYAPplstDDTAEILFT 181
Cdd:cd05945 75 ------------------SP---------AERIREI--LDAA----------------KPALLIADG----DDNAYIIFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYNLRFagyYSAWQCA---LRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLV---EKYSARAFW 255
Cdd:cd05945 106 SGSTGRPKGVQISHDNLVS---FTNWMLSdfpLGPGDVFLNQAP-FSFDLSVMDLYPALASGATLVPVprdATADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 256 GQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFYLN-LSEQEKDAFCERF-GVRLLTSYGMTETIVGIIGDR- 332
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEvLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEv 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 ----PGDKRRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEAD---GWLHTGDT 405
Cdd:cd05945 262 tpevLDGYDRLP-IGYAKPGAKLVILDEDGRPVPPGEKGELVISG---PSVSKGYLNNPEKTAAAFFPDegqRAYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 406 GYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-ETLSEEEFFRFC 484
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaEAGLTKAIKAEL 417
|
490 500 510
....*....|....*....|....*....|..
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd05945 418 AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
14-517 |
5.26e-46 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 168.78 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 14 DDLADVYGHKTaLICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:PRK06018 17 DHAARIHGNRE-VVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLIDVA-LPAddgvssfTQLKNqqpaTLCYAPPLST 172
Cdd:PRK06018 96 PRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAhMPQ-------TTLKN----AVAYEEWIAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DD------------TAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCAL--RDDDVYLTVMPAFHIDCQCTAAMAAFS 238
Cdd:PRK06018 165 ADgdfawktfdentAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALgtSAADTMLPVVPLFHANSWGIAFSAPSM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 239 AGATFVLVEKYSARAFWGQVQKYRATVTECIP---MMIRTLMvqppsandRQHRLRevMFYLN--------LSEQEKDAF 307
Cdd:PRK06018 245 GTKLVMPGAKLDGASVYELLDTEKVTFTAGVPtvwLMLLQYM--------EKEGLK--LPHLKmvvcggsaMPRSMIKAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 308 cERFGVRLLTSYGMTETI-VGIIG-------DRPGDKR--RWPSIGRAGFCYEAEIRDDHNRPLP--AGEIGEICIKGvp 375
Cdd:PRK06018 315 -EDMGVEVRHAWGMTEMSpLGTLAalkppfsKLPGDARldVLQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRG-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 376 gKTIFKEYFlnpKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
Cdd:PRK06018 392 -PAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1629467165 456 DSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK06018 468 HPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
39-517 |
6.10e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 168.40 E-value: 6.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQE--DATQLrhiclidVALPADDGVSSFTQLKNqqpATLCYAPPLSTDDTAEILFTSGTTSRPKGVviTHY 196
Cdd:PRK13382 150 FSATVDRALADcpQATRI-------VAWTDEDHDLTVEVLIA---AHAGQRPEPTGRKGRVILLTSGTTGTPKGA--RRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAW--QCALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIR 274
Cdd:PRK13382 218 GPGGIGTLKAIldRTPWRAEEPTVIVAPMFHA-WGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 275 TLMVQPPSANDRqHRLREVMFYLNLSEQEK----DAFCERFGVRLLTSYGMTEtiVGIIGD-RPGDKRRWP-SIGRAGFC 348
Cdd:PRK13382 297 RIMDLPAEVRNR-YSGRSLRFAAASGSRMRpdvvIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAAPdTAGRPAEG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 349 YEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYflNPKATAKVLeaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGG 428
Cdd:PRK13382 374 TEIRILDQDFREVPTGEVGTIFVRN---DTQFDGY--TSGSTKDFH--DGFMASGDVGYLDENGRLFVVGRDDEMIVSGG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 429 ENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCS 508
Cdd:PRK13382 447 ENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGAT 526
|
....*....
gi 1629467165 509 GKIIRKNLK 517
Cdd:PRK13382 527 GKILRRELQ 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
41-517 |
7.37e-46 |
|
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: 166.78 E-value: 7.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 41 LELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIF-CWFGLakiGAIMVPINARLLREESAWILQNSQACLLVTSAQF 119
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEgVWIAD---GVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 120 YPMYQqiqqeDATQLRHICLIDVALPADDGVSSFTQLknqqPATLCYAPPLSTDDTAE---ILFTSGTTSRPKGV----- 191
Cdd:cd05929 78 RAEAC-----AIIEIKAAALVCGLFTGGGALDGLEDY----EAAEGGSPETPIEDEAAgwkMLYSGGTTGRPKGIkrglp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 192 -VITHYNLRFAgyySAWQCALRDDDVYLTVMPAFHIDCQcTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIP 270
Cdd:cd05929 149 gGPPDNDTLMA---AALGFGPGADSVYLSPAPLYHAAPF-RWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 271 -MMIRTLMVQppsandrqhrlREVMFYLNLSEQE-------------KDAFCERFGVRLLTSYGMTE----TIvgIIGDR 332
Cdd:cd05929 225 tMFVRLLKLP-----------EAVRNAYDLSSLKrvihaaapcppwvKEQWIDWGGPIIWEYYGGTEgqglTI--INGEE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 ----PGdkrrwpSIGRAGFCyEAEIRDDHNRPLPAGEIGEICIKGVPGKtifkEYFLNPKATAKVLEADGWLHTGDTGYC 408
Cdd:cd05929 292 wlthPG------SVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGF----EYTNDPEKTAAARNEGGWSTLGDVGYL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE---TLSEEEFFRFCE 485
Cdd:cd05929 361 DEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLR 440
|
490 500 510
....*....|....*....|....*....|..
gi 1629467165 486 QNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05929 441 DRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
17-517 |
8.65e-45 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 165.96 E-value: 8.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PLN03102 24 SECYPNRTSIIYGKT-----RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQ------------------IQQEDAT------QLRHICLIDVALPADDGVSS 152
Cdd:PLN03102 99 DATSIAAILRHAKPKILFVDRSFEPLAREvlhllssedsnlnlpvifIHEIDFPkrpsseELDYECLIQRGEPTPSLVAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 153 FTQLKNQQPatlcyapPLSTDdtaeilFTSGTTSRPKGVVITHYnlrfAGYYSA------WQCALRDddVYLTVMPAFHI 226
Cdd:PLN03102 179 MFRIQDEHD-------PISLN------YTSGTTADPKGVVISHR----GAYLSTlsaiigWEMGTCP--VYLWTLPMFHC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 227 DcQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMvqPPSANDRQHRLREVMFYLNLSEQEKDA 306
Cdd:PLN03102 240 N-GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL--KGNSLDLSPRSGPVHVLTGGSPPPAAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 307 F--CERFGVRLLTSYGMTETIVGII-------GDRPGDKRRWPSIGRAGFCY----EAEIRDDHNR---PLPAGEIGEIC 370
Cdd:PLN03102 317 VkkVQRLGFQVMHAYGLTEATGPVLfcewqdeWNRLPENQQMELKARQGVSIlglaDVDVKNKETQesvPRDGKTMGEIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 371 IKGvpgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
Cdd:PLN03102 397 IKG---SSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETA 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1629467165 451 VVGIKDSIRDEAIKAFVVLNEGET----------LSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PLN03102 473 VVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
62-517 |
1.13e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 165.38 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 62 GDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN----ARLLREEsawiLQNSQACLLVTSAQFYPMYQQIQQEdaTQLRHi 137
Cdd:PRK12492 75 GDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNplytAREMRHQ----FKDSGARALVYLNMFGKLVQEVLPD--TGIEY- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 138 cLIDVA----LPADDG---------------------VSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVV 192
Cdd:PRK12492 148 -LIEAKmgdlLPAAKGwlvntvvdkvkkmvpayhlpqAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 193 ITHYNLrFAGYYSAWQC--ALRDD---------DVYLTVMPAFHI-----DCQCTAAMAAFSAGATfvlvEKYSARAFWG 256
Cdd:PRK12492 227 LTHGNL-VANMLQVRAClsQLGPDgqplmkegqEVMIAPLPLYHIyaftaNCMCMMVSGNHNVLIT----NPRDIPGFIK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 257 QVQKYRATVTECIPMMIRTLMVQPpsandrqhRLREVMF-YLNLSEQEKDAF----CERF----GVRLLTSYGMTETIVG 327
Cdd:PRK12492 302 ELGKWRFSALLGLNTLFVALMDHP--------GFKDLDFsALKLTNSGGTALvkatAERWeqltGCTIVEGYGLTETSPV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 328 IIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGY 407
Cdd:PRK12492 374 ASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKG---PQVMKGYWQQPEATAEALDAEGWFKTGDIAV 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 408 CDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGeTLSEEEFFRFCEQN 487
Cdd:PRK12492 451 IDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKEN 529
|
490 500 510
....*....|....*....|....*....|
gi 1629467165 488 MAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK12492 530 FTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
20-517 |
1.50e-44 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 165.19 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 20 YGHKTALICESSGgvvnrYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:PRK07059 36 YADRPAFICMGKA-----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSAQFYPMYQQIQqeDATQLRHIClidVA-----------------------LPADD--GVSSFT 154
Cdd:PRK07059 111 ELEHQLKDSGAEAIVVLENFATTVQQVL--AKTAVKHVV---VAsmgdllgfkghivnfvvrrvkkmVPAWSlpGHVRFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 155 QLKnQQPATLCYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYNLrFAGYY--SAW-QCALR---DDDVYLTV--MPAFH 225
Cdd:PRK07059 186 DAL-AEGARQTFKPVkLGPDDVAFLQYTGGTTGVSKGATLLHRNI-VANVLqmEAWlQPAFEkkpRPDQLNFVcaLPLYH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 226 IDCQCTAAMAAFSAGATFVLVEkySAR---AFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLReVMFYLNLSEQ 302
Cdd:PRK07059 264 IFALTVCGLLGMRTGGRNILIP--NPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLI-VANGGGMAVQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 303 EKDA--FCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIF 380
Cdd:PRK07059 341 RPVAerWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRG---PQVM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 381 KEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD 460
Cdd:PRK07059 418 AGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSG 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1629467165 461 EAIKAFVVlNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07059 498 EAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
38-496 |
1.68e-44 |
|
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: 162.99 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFY-TLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLlreESAWILQnsqaCLLVTS 116
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNL---SGDPLIH----CLKLSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFypmyqqiqqedatqlrhiclidvaLPADDgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVIT-H 195
Cdd:cd05937 79 SRF------------------------VIVDP------------------------DDPAILIYTSGTTGLPKAAAISwR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YNLRFAGYYSAWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRT 275
Cdd:cd05937 111 RTLVTSNLLSHD-LNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 276 LMVQPPSANDRQHRLReVMFYLNLSEQEKDAFCERFGVRLLTS-YGMTETI------------VGIIGDRpGDKRRW--- 339
Cdd:cd05937 190 LLSTPPSPYDRDHKVR-VAWGNGLRPDIWERFRERFNVPEIGEfYAATEGVfaltnhnvgdfgAGAIGHH-GLIRRWkfe 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 340 ---------PSIG------RAGFCYEAeirddhnrplPAGEIGEIcIKGVPGKTI--FKEYFLNPKATAK-----VLE-A 396
Cdd:cd05937 268 nqvvlvkmdPETDdpirdpKTGFCVRA----------PVGEPGEM-LGRVPFKNReaFQGYLHNEDATESklvrdVFRkG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 397 DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS 476
Cdd:cd05937 337 DIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAV 416
|
490 500
....*....|....*....|
gi 1629467165 477 EEEFFRFCEQNMAKFKVPSY 496
Cdd:cd05937 417 PTEFTKSLLASLARKNLPSY 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
58-517 |
3.57e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 164.17 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEdaTQLRHI 137
Cdd:PRK05677 71 DLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPK--TGVKHV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 138 CLIDVA--LPADDGV---SSFTQLKNQQPA-TLCYAPPLST-----------------DDTAEILFTSGTTSRPKGVVIT 194
Cdd:PRK05677 149 IVTEVAdmLPPLKRLlinAVVKHVKKMVPAyHLPQAVKFNDalakgagqpvteanpqaDDVAVLQYTGGTTGVAKGAMLT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 195 HYNLrfagYYSAWQC-ALRDD------DVYLTVMPAFHI-----DCQCTAAMAAFsagaTFVLVEKYSARAFWGQVQKYR 262
Cdd:PRK05677 229 HRNL----VANMLQCrALMGSnlnegcEILIAPLPLYHIyaftfHCMAMMLIGNH----NILISNPRDLPAMVKELGKWK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 263 ATVTecipMMIRTLMVqppsANDRQHRLREVMFY---LNLS--EQEKDAFCERF----GVRLLTSYGMTET--IVGIigd 331
Cdd:PRK05677 301 FSGF----VGLNTLFV----ALCNNEAFRKLDFSalkLTLSggMALQLATAERWkevtGCAICEGYGMTETspVVSV--- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 332 RPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEE 411
Cdd:PRK05677 370 NPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKG---PQVMKGYWQRPEATDEILDSDGWLKTGDIALIQED 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKF 491
Cdd:PRK05677 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGY 526
|
490 500
....*....|....*....|....*.
gi 1629467165 492 KVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK05677 527 KVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
37-517 |
1.61e-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: 161.86 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFY-TLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVT 115
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 SAQFYPMYQQIQQEdATQLRHICLidVALPADDGVSSFTQL-KNQQPATLCYAPplSTDDTAEILFTSGTTSRPKGVVIT 194
Cdd:cd05928 121 SDELAPEVDSVASE-CPSLKTKLL--VSEKSRDGWLNFKELlNEASTEHHCVET--GSQEPMAIYFTSGTTGSPKMAEHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 195 H--YNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFV-LVEKYSARAFWGQVQKYRATVTECIPM 271
Cdd:cd05928 196 HssLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhHLPRFDPLVILKTLSSYPITTFCGAPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 272 MIRtLMVQPPSANDRQHRLREVMFY---LNLSEQEKdaFCERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRAGFC 348
Cdd:cd05928 276 VYR-MLVQQDLSSYKFPSLQHCVTGgepLNPEVLEK--WKAQTGLDIYEGYGQTETGL-ICANFKGMKIKPGSMGKASPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 349 YEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYFLNPKATAKVLEADGWLhTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:cd05928 352 YDVQIIDDNGNVLPPGTEGDIGIRVKPIRpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-ETLSEEEFFRFCEQNM----AKFKVPSYLEIRK 501
Cdd:cd05928 431 SGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKELQQHVksvtAPYKYPRKVEFVQ 510
|
490
....*....|....*.
gi 1629467165 502 DLPRNCSGKIIRKNLK 517
Cdd:cd05928 511 ELPKTVTGKIQRNELR 526
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
17-517 |
2.81e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 161.25 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PRK07788 59 ARRAPDRAALIDERG-----TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQIQqEDATQLRHICL-IDVALPADDGVSSFTQLKNQQPATlcyAPPLSTDDT 175
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALP-PDLGRLRAWGGnPDDDEPSGSTDETLDDLIAGSSTA---PLPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 176 AEILFTSGTTSRPKGVVITHYNL--RFAGYYSawQCALRDDDVYLTVMPAFHID--CQCTAAMAAFSagaTFVLVEKYSA 251
Cdd:PRK07788 210 GIVILTSGTTGTPKGAPRPEPSPlaPLAGLLS--RVPFRAGETTLLPAPMFHATgwAHLTLAMALGS---TVVLRRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQ--HRLReVMFYLN--LSEQEKDAFCERFGVRLLTSYGMTETIVG 327
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYdtSSLK-IIFVSGsaLSPELATRALEAFGPVLYNLYGSTEVAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 328 IIGDrPGDKRRWPSI-GRAGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYfLNPKATAKVleaDGWLHTGDTG 406
Cdd:PRK07788 364 TIAT-PEDLAEAPGTvGRPPKGVTVKILDENGNEVPRGVVGRIF---VGNGFPFEGY-TDGRDKQII---DGLLSSGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 407 YCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQ 486
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRD 515
|
490 500 510
....*....|....*....|....*....|.
gi 1629467165 487 NMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07788 516 NLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
21-517 |
3.86e-42 |
|
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: 158.88 E-value: 3.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICES-SGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI----NAR 95
Cdd:cd05966 67 GDKVAIIWEGdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfagfSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 96 LLREEsawiLQNSQACLLVTSAQFY------PMYQQIQQ--EDATQLRHiCLidVALPADDGVSS-------FTQLKNQQ 160
Cdd:cd05966 147 SLADR----INDAQCKLVITADGGYrggkviPLKEIVDEalEKCPSVEK-VL--VVKRTGGEVPMtegrdlwWHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 161 PATlCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSA----WQCALRDDDV--------------YLTV 220
Cdd:cd05966 220 SPE-CEPEWMDSEDPLFILYTSGSTGKPKGVVHTT-----GGYllYAAttfkYVFDYHPDDIywctadigwitghsYIVY 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 221 MPAfhidCQCTaamaafsagaTFVLVE---KYSARA-FWGQVQKYRATVTECIPMMIRTLMVQ---PPSANDRQHrLR-- 291
Cdd:cd05966 294 GPL----ANGA----------TTVMFEgtpTYPDPGrYWDIVEKHKVTIFYTAPTAIRALMKFgdeWVKKHDLSS-LRvl 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 292 ---------EV-MFYLNLSEQEKDAFCErfgvrlltSYGMTET-------IVGIIGDRPGdkrrwpSIGRAGFCYEAEIR 354
Cdd:cd05966 359 gsvgepinpEAwMWYYEVIGKERCPIVD--------TWWQTETggimitpLPGATPLKPG------SATRPFFGIEPAIL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 355 DDHNRPLPAGEIGEICIKGV-PG--KTIF-------KEYFlnpkataKVLEadGWLHTGDTGYCDEEGFFYFVDRRCNMI 424
Cdd:cd05966 425 DEEGNEVEGEVEGYLVIKRPwPGmaRTIYgdheryeDTYF-------SKFP--GYYFTGDGARRDEDGYYWITGRVDDVI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 425 KRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRK 501
Cdd:cd05966 496 NVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVP 575
|
570
....*....|....*.
gi 1629467165 502 DLPRNCSGKIIRKNLK 517
Cdd:cd05966 576 GLPKTRSGKIMRRILR 591
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
174-517 |
4.99e-42 |
|
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: 152.87 E-value: 4.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 174 DTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWQCALRDddVYLTVMPAFHIDCQcTAAMAAFSAGATFVLVEKysA 251
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLlaSAAGLHSRLGFGGGD--SWLLSLPLYHVGGL-AILVRSLLAGAELVLLER--N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMvQPPSANDRQHRLREVMfyLN---LSEQEKDAFCERfGVRLLTSYGMTETIVGI 328
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVL--LGgapIPPELLERAADR-GIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 329 IGDRPGDKRRwpsiGRAGfcyeaeirddhnRPLPAGEI-----GEICIKGVpgkTIFKEYFLNPkaTAKVLEADGWLHTG 403
Cdd:cd17630 152 ATKRPDGFGR----GGVG------------VLLPGRELrivedGEIWVGGA---SLAMGYLRGQ--LVPEFNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 404 DTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGetLSEEEFFRF 483
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAW 288
|
330 340 350
....*....|....*....|....*....|....
gi 1629467165 484 CEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd17630 289 LKDKLARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-517 |
1.42e-41 |
|
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: 157.65 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:cd05968 76 TRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTSAQFY--------------PMYQQIQQEDATQLRHICLIDVALPADDgvSSFTQLKNQQPAtlcYA 167
Cdd:cd05968 156 ATRLQDAEAKALITADGFTrrgrevnlkeeadkACAQCPTVEKVVVVRHLGNDFTPAKGRD--LSYDEEKETAGD---GA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 168 PPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCA-LRDDDVYLTV------MPAFHIdcqctaaMAAFSAG 240
Cdd:cd05968 231 ERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFdLKPGDLLTWFtdlgwmMGPWLI-------FGGLILG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 241 ATFVLVEKY----SARAFWGQVQKYRATVTECIPMMIRTLMVQpPSANDRQHRLREVMFYLNLSEQ-EKDAFCERFGVRL 315
Cdd:cd05968 304 ATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPR-GDAPVNAHDLSSLRVLGSTGEPwNPEPWNWLFETVG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 316 -----LTSY-GMTETIVGIIGD---RPgdkrrwpsIGRAGFC-----YEAEIRDDHNRPLPaGEIGEICIKGV-PGKTif 380
Cdd:cd05968 383 kgrnpIINYsGGTEISGGILGNvliKP--------IKPSSFNgpvpgMKADVLDESGKPAR-PEVGELVLLAPwPGMT-- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 381 KEYFLNPKataKVLEA------DGWLHtGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
Cdd:cd05968 452 RGFWRDED---RYLETywsrfdNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629467165 455 KDSIRDEAIKAFVVLNEGETLSE---EEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05968 528 PHPVKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
21-517 |
3.77e-41 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 156.32 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICESS-GGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:cd05967 65 GDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSA---------QFYPMYQQIQQEDATQLRHiCLI----DVALPADDGVSSF---TQLKNQQPAT 163
Cdd:cd05967 145 ELASRIDDAKPKLIVTAScgiepgkvvPYKPLLDKALELSGHKPHH-VLVlnrpQVPADLTKPGRDLdwsELLAKAEPVD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 164 lcYAPPLSTDdTAEILFTSGTTSRPKGV--------VITHYNLRF-----AGyySAWQCAlrdDDV-------YLTVMPA 223
Cdd:cd05967 224 --CVPVAATD-PLYILYTSGTTGKPKGVvrdngghaVALNWSMRNiygikPG--DVWWAA---SDVgwvvghsYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 224 FHidcqctaamaafsaGATFVLVEKYSAR-----AFWGQVQKYRATVTECIPMMIRTLMVQPPSAND-RQHRLR--EVMF 295
Cdd:cd05967 296 LH--------------GATTVLYEGKPVGtpdpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYiKKYDLSslRTLF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 296 Y----LNLSEQEkdaFCER-FGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAG---FCYEAEIRDDHNRPLPAGEIG 367
Cdd:cd05967 362 LagerLDPPTLE---WAENtLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGkpvPGYQVQVLDEDGEPVGPNELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 368 EICIKG-VPGKTI---------FKEYFLNpkatakvlEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
Cdd:cd05967 439 NIVIKLpLPPGCLltlwknderFKKLYLS--------KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEME 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC-----EQ--NMAKFKVPSYLeirKDLPRNCSGK 510
Cdd:cd05967 511 ESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELvalvrEQigPVAAFRLVIFV---KRLPKTRSGK 587
|
....*..
gi 1629467165 511 IIRKNLK 517
Cdd:cd05967 588 ILRRTLR 594
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
17-517 |
5.88e-41 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 155.00 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:PLN02479 30 AVVHPTRKSVVHGSV-----RYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFYPMYQQ----IQQEDATQLRHICLIDVALPADD----------GVSSFTQ-LKNQQP 161
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEalkiLAEKKKSSFKPPLLIVIGDPTCDpkslqyalgkGAIEYEKfLETGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 162 AtLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlRFAgYYSAWQCAL----RDDDVYLTVMPAFHIDCQCtAAMAAF 237
Cdd:PLN02479 185 E-FAWKPPADEWQSIALGYTSGTTASPKGVVLHH---RGA-YLMALSNALiwgmNEGAVYLWTLPMFHCNGWC-FTWTLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 238 SAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQ-HRLREVM---------FYLNLSEQekdaf 307
Cdd:PLN02479 259 ALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPlPRVVHVMtagaapppsVLFAMSEK----- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 308 cerfGVRLLTSYGMTETIvgiigdRPGD----KRRWPSI---------GRAGFCYEAEIRDD-----HNRPLPA--GEIG 367
Cdd:PLN02479 334 ----GFRVTHTYGLSETY------GPSTvcawKPEWDSLppeeqarlnARQGVRYIGLEGLDvvdtkTMKPVPAdgKTMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 368 EICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQ 447
Cdd:PLN02479 404 EIVMRG---NMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVL 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1629467165 448 DIVVVGIKDSIRDEAIKAFVVLNEGETLSEE-----EFFRFCEQNMAKFKVPSYLeIRKDLPRNCSGKIIRKNLK 517
Cdd:PLN02479 480 EASVVARPDERWGESPCAFVTLKPGVDKSDEaalaeDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
36-513 |
1.14e-40 |
|
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: 152.60 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 36 NRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVT 115
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 SAQfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITH 195
Cdd:cd05914 86 SDE------------------------------------------------------DDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKY-SARAFwgQVQKYRATVTECIP---- 270
Cdd:cd05914 112 RNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIpSAKII--ALAFAQVTPTLGVPvplv 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 271 MMIRTLMVQPPSANDR--QHRLREVMFYLNLSEQEKDAFCERFG--VRLLTS-----------------------YGMTE 323
Cdd:cd05914 190 IEKIFKMDIIPKLTLKkfKFKLAKKINNRKIRKLAFKKVHEAFGgnIKEFVIggakinpdveeflrtigfpytigYGMTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TIVGIIGDRPGDKRrwpsIGRAGFCYE-AEIRDDhnRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHT 402
Cdd:cd05914 270 TAPIISYSPPNRIR----LGSAGKVIDgVEVRID--SPDPATGEGEIIVRG---PNVMKGYYKNPEATAEAFDKDGWFHT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 403 GDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKI-QDIVVVGIKDSI-------RDEAIKAFVVLNEGE 473
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVlESLVVVQEKKLValayidpDFLDVKALKQRNIID 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1629467165 474 TLSEEeffrfceqNMAKF--KVPSYLEIRK------DLPRNCSGKIIR 513
Cdd:cd05914 421 AIKWE--------VRDKVnqKVPNYKKISKvkivkeEFEKTPKGKIKR 460
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
37-453 |
4.77e-40 |
|
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: 150.97 E-value: 4.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVts 116
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 aqfypmyqqiqqedatqlrhiclidvalpaddgvssftqLKNqqpatlcyapplSTDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd17640 83 ---------------------------------------VEN------------DSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFaGYYSAWQCA-LRDDDVYLTVMPAFHIdcqctaamaAFSAGATFVL----VEKYSA-RAFWGQVQKYRATVTECIP 270
Cdd:cd17640 112 NLLH-QIRSLSDIVpPQPGDRFLSILPIWHS---------YERSAEYFIFacgcSQAYTSiRTLKDDLKRVKPHYIVSVP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 271 MMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEK--------------DAFCERFGVRLLTSYGMTETIVGIIGDRPGDK 336
Cdd:cd17640 182 RLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIFkfgisgggalpphvDTFFEAIGIEVLNGYGLTETSPVVSARRLKCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 337 RRwPSIGRAGFCYEAEIRDDHNR-PLPAGEIGEICIKGVPgktIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFY 415
Cdd:cd17640 262 VR-GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQ---VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELV 337
|
410 420 430
....*....|....*....|....*....|....*....
gi 1629467165 416 FVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVG 453
Cdd:cd17640 338 LTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
14-510 |
9.42e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 151.19 E-value: 9.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 14 DDLADVYGHKTALICessGGVvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:PRK07798 10 EAVADAVPDRVALVC---GDR--RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAWILQNSQACLLVTSAQFYPMYQQIqQEDATQLRHICLID--VALPADDGVSSFTQLKNQQPATLCYAPPlS 171
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVYEREFAPRVAEV-LPRLPKLRTLVVVEdgSGNDLLPGAVDYEDALAAGSPERDFGER-S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 172 TDDTAeILFTSGTTSRPKGVVITHYNLRFAG---------------YYSAWQCALRDDDVYLTVMPAFHIDCQCTaAMAA 236
Cdd:PRK07798 163 PDDLY-LLYTGGTTGMPKGVMWRQEDIFRVLlggrdfatgepiedeEELAKRAAAGPGMRRFPAPPLMHGAGQWA-AFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 237 FSAGATFVL--VEKYSARAFWGQVQKYRATVtecIPM--------MIRTLmvqppsANDRQHRLREV--------MFyln 298
Cdd:PRK07798 241 LFSGQTVVLlpDVRFDADEVWRTIEREKVNV---ITIvgdamarpLLDAL------EARGPYDLSSLfaiasggaLF--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 299 lSEQEKDAFCERFGVRLLT-SYGMTETIVGIIG--DRPGDKRRWPSIGRAGFCyeAEIRDDHNRPLP-AGEIGEICIKG- 373
Cdd:PRK07798 309 -SPSVKEALLELLPNVVLTdSIGSSETGFGGSGtvAKGAVHTGGPRFTIGPRT--VVLDEDGNPVEPgSGEIGWIARRGh 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 374 VP-GktifkeYFLNPKATAKVL-EADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI 449
Cdd:PRK07798 386 IPlG------YYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 450 VVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
39-451 |
2.50e-39 |
|
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: 147.80 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTAN-LFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSA 117
Cdd:TIGR01733 1 TYRELDERANRLARhLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 QFYPmyqqiQQEDATQLRHICLIDVALPADDGVSSFTQlknqqpatlcyAPPLSTDDTAEILFTSGTTSRPKGVVITHYN 197
Cdd:TIGR01733 81 ALAS-----RLAGLVLPVILLDPLELAALDDAPAPPPP-----------DAPSGPDDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 L-----RFAGYYsawqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLVEK---YSARAFWGQV-QKYRATVTEC 268
Cdd:TIGR01733 145 LvnllaWLARRY-----GLDPDDRVLQFAS-LSFDASVEEIFGALLAGATLVVPPEdeeRDDAALLAALiAEHPVTVLNL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 269 IPMMIRTLMVQPPSANDrqhRLREVMF---YLNLSEQEKdaFCERFG-VRLLTSYGMTETIVGIIG---DRPGDKR-RWP 340
Cdd:TIGR01733 219 TPSLLALLAAALPPALA---SLRLVILggeALTPALVDR--WRARGPgARLINLYGPTETTVWSTAtlvDPDDAPReSPV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 341 SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADG--------WLHTGDTGYCDEEG 412
Cdd:TIGR01733 294 PIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGP---GVARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDG 370
|
410 420 430
....*....|....*....|....*....|....*....
gi 1629467165 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
Cdd:TIGR01733 371 NLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-483 |
4.61e-39 |
|
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: 152.32 E-value: 4.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 11 QMWDDLADVYGHKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMV 90
Cdd:COG1020 480 ELFEAQAARTPDAVAVVFGD-----QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 91 PIN-----ARLlreesAWILQNSQACLLVTSAQFypmyqqIQQEDATQLRHICLIDVALPaddgvssftqlknQQPATLc 165
Cdd:COG1020 555 PLDpaypaERL-----AYMLEDAGARLVLTQSAL------AARLPELGVPVLALDALALA-------------AEPATN- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLrfAGYYSAWQ--CALRDDDVYLTVMPafhidcqctaamaafsagATF 243
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL--VNLLAWMQrrYGLGPGDRVLQFAS------------------LSF 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 244 -----------------VLVEKYSAR---AFWGQVQKYRATVTECIPMMIRTLMVQPPSAndrQHRLREVMFyl-nLSEQ 302
Cdd:COG1020 670 dasvweifgallsgatlVLAPPEARRdpaALAELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVggeaLPPE 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 303 EKDAFCERF-GVRLLTSYGMTETIVGIIG---DRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGV---- 374
Cdd:COG1020 747 LVRRWRARLpGARLVNLYGPTETTVDSTYyevTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAglar 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 375 -----PGKTifKEYFL-NPkatakvLEADG--WLHTGDTGYCDEEGFFYFVDRRCNMIK-RG-----GenvscvELENII 440
Cdd:COG1020 827 gylnrPELT--AERFVaDP------FGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKiRGfrielG------EIEAAL 892
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1629467165 441 ATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRF 483
Cdd:COG1020 893 LQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA 935
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
22-517 |
4.25e-38 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 146.67 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGaiMVPINA-----RL 96
Cdd:PRK10946 38 DAIAVICGE-----RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNAlfshqRS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 lrEESAWILQNSQAcLLVTSAQfYPMYQQIQQEDATQLRHICLIDVALPADDGVSSFTQLKnQQPATLCYAPPLSTDDTA 176
Cdd:PRK10946 111 --ELNAYASQIEPA-LLIADRQ-HALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAI-NHPAEDFTATPSPADEVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITH----YNLRfagyYSAWQCALRDDDVYLTVMPA--------------FHidcqctaamaafs 238
Cdd:PRK10946 186 FFQLSGGSTGTPKLIPRTHndyyYSVR----RSVEICGFTPQTRYLCALPAahnypmsspgalgvFL------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 239 AGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIrTLMVQPPSANDRQHRLREVMFYL----NLSEQEKDAFCERFGVR 314
Cdd:PRK10946 249 AGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAV-SLWLQAIAEGGSRAQLASLKLLQvggaRLSETLARRIPAELGCQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 315 LLTSYGMTETIVGIIGDRPGDKRRWPSIGRAgFCYEAEIR--DDHNRPLPAGEIGEICIKGvPgkTIFKEYFLNPKATAK 392
Cdd:PRK10946 328 LQQVFGMAEGLVNYTRLDDSDERIFTTQGRP-MSPDDEVWvaDADGNPLPQGEVGRLMTRG-P--YTFRGYYKSPQHNAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 393 VLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
Cdd:PRK10946 404 AFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1629467165 473 etLSEEEFFRFC-EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK10946 484 --LKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
33-517 |
1.04e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 142.54 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 33 GVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACL 112
Cdd:PRK07008 35 GDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 113 LVTSAQFYPMYQQIQQEDATQLRHICLIDVA-LPADDG-VSSFTQLKNQQPATlcYAPPLSTDDTAEIL-FTSGTTSRPK 189
Cdd:PRK07008 115 VLFDLTFLPLVDALAPQCPNVKGWVAMTDAAhLPAGSTpLLCYETLVGAQDGD--YDWPRFDENQASSLcYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 190 GVVITHYNLRFAGYYSAWQCA--LRDDDVYLTVMPAFHID------------CQCTAAMAAFSAGATFVLVEK----YSA 251
Cdd:PRK07008 193 GALYSHRSTVLHAYGAALPDAmgLSARDAVLPVVPMFHVNawglpysapltgAKLVLPGPDLDGKSLYELIEAervtFSA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 --RAFW----GQVQ-------KYRATV---TECIPMMIRTlmvqppsandrqhrlrevmfylnlseqekdaFCERFGVRL 315
Cdd:PRK07008 273 gvPTVWlgllNHMReaglrfsTLRRTViggSACPPAMIRT-------------------------------FEDEYGVEV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 316 LTSYGMTE--------TIVGIIGDRPGDKRR--WPSIGRAGFCYEAEIRDDHNRPLP--AGEIGEICIKGvpgKTIFKEY 383
Cdd:PRK07008 322 IHAWGMTEmsplgtlcKLKWKHSQLPLDEQRklLEKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVRG---PWVIDRY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 384 FlnpKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463
Cdd:PRK07008 399 F---RGDASPL-VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERP 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 464 KAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07008 475 LLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
39-516 |
1.48e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 142.06 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYpmyQQIQQEDATqlrhICLIDvalPADDGvssftqlknqqpATLCYAPPLSTDDTAEILFTSGTTSRPKGVvitHYNL 198
Cdd:PRK13383 142 FA---ERIAGADDA----VAVID---PATAG------------AEESGGRPAVAAPGRIVLLTSGTTGKPKGV---PRAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 RFAGYYSAW-----QCALRDDDVYLTVMPAFHiDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMI 273
Cdd:PRK13383 197 QLRSAVGVWvtildRTRLRTGSRISVAMPMFH-GLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 274 RTLMVQPPSANDRQH--RLREVMFYLN-LSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDrPGDKRRWP-SIGRAGFCY 349
Cdd:PRK13383 276 ARILELPPRVRARNPlpQLRVVMSSGDrLDPTLGQRFMDTYGDILYNGYGSTEVGIGALAT-PADLRDAPeTVGKPVAGC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 EAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEyflnpkATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGE 429
Cdd:PRK13383 355 PVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD------GGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
Cdd:PRK13383 428 NVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTG 507
|
....*..
gi 1629467165 510 KIIRKNL 516
Cdd:PRK13383 508 KVLRKEL 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
37-440 |
4.35e-36 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 140.88 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIfCWFG---LAKIGAIMVPI-------NARLLREESAWILQ 106
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFI-PAFWacvLAGFVPAPLTVpptydepNARLRKLRHIWQLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 107 NSQACLlvTSAQfypMYQQIqqEDATQLRHIClidvalpaDDGVSSFTQLKNQQPATLcyAPPLSTDDTAEILFTSGTTS 186
Cdd:cd05906 118 GSPVVL--TDAE---LVAEF--AGLETLSGLP--------GIRVLSIEELLDTAADHD--LPQSRPDDLALLMLTSGSTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 187 RPKGVVITHYNL--RFAGyySAWQCALRDDDVYLTVMPAFHIDcqctaamaafsagatfVLVEkYSARA----------- 253
Cdd:cd05906 181 FPKAVPLTHRNIlaRSAG--KIQHNGLTPQDVFLNWVPLDHVG----------------GLVE-LHLRAvylgcqqvhvp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 ----------FWGQVQKYRATVTeCIPMMIRTLMVQPPSANDRQH-RLREVMFYLNLSEQEKDAFCERFgVRLLT----- 317
Cdd:cd05906 242 teeiladplrWLDLIDRYRVTIT-WAPNFAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAKTIRRL-LRLLEpyglp 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 318 ------SYGMTETIVGIIGDRP------GDKRRWPSIGR--AGFcyeaEIR--DDHNRPLPAGEIGEICIKGvpgKTIFK 381
Cdd:cd05906 320 pdairpAFGMTETCSGVIYSRSfptydhSQALEFVSLGRpiPGV----SMRivDDEGQLLPEGEVGRLQVRG---PVVTK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 382 EYFLNPKATAKVLEADGWLHTGDTGYCDeEGFFYFVDRRCNMIKRGGENVSCVELENII 440
Cdd:cd05906 393 GYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
86-517 |
6.03e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 139.35 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAIMVPINARLLREESAWILQNSQACLLVTSAQfypmyqqiqqEDATQLRHIcliDVALPADDGVSsftqlknqqpatlc 165
Cdd:PRK07787 69 GVPVVPVPPDSGVAERRHILADSGAQAWLGPAP----------DDPAGLPHV---PVRLHARSWHR-------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 YAPPlSTDDTAEILFTSGTTSRPKGVVIThynlRFA------GYYSAWQCAlrDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
Cdd:PRK07787 122 YPEP-DPDAPALIVYTSGTTGPPKGVVLS----RRAiaadldALAEAWQWT--ADDVLVHGLPLFHVHGLVLGVLGPLRI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 240 GATFVLVEKYSARAFwGQVQKYRATVTECIPMMIRTLMVQPPSAND-RQHRLReVMFYLNLSEQEKDAFCERFGVRLLTS 318
Cdd:PRK07787 195 GNRFVHTGRPTPEAY-AQALSEGGTLYFGVPTVWSRIAADPEAARAlRGARLL-VSGSAALPVPVFDRLAALTGHRPVER 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTETIVgIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPA-GE-IGEIcikGVPGKTIFKEYFLNPKATAKVLEA 396
Cdd:PRK07787 273 YGMTETLI-TLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHdGEtVGEL---QVRGPTLFDGYLNRPDATAAAFTA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 397 DGWLHTGDTGYCDEEGFFYFVDRRC-NMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGetL 475
Cdd:PRK07787 349 DGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--V 426
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1629467165 476 SEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07787 427 AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
38-517 |
1.76e-35 |
|
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: 137.31 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPinarllreesawilqnsqACLLVTSA 117
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 QfypMYQQIQQEDATqlrhICLIDVALPADDgvssftqlknqqpatlcyaPPLstddtaeILFTSGTTSRPKGVVITHYN 197
Cdd:cd05974 63 D---LRDRVDRGGAV----YAAVDENTHADD-------------------PML-------LYFTSGTTSKPKLVEHTHRS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LRFAGYYSAWQCALRDDDVYLTVM-PAFHIDCQCTAAMAAFSAGATFVLVE-KYSARAFWGQVQKYRATvTECIPMMIRT 275
Cdd:cd05974 110 YPVGHLSTMYWIGLKPGDVHWNISsPGWAKHAWSCFFAPWNAGATVFLFNYaRFDAKRVLAALVRYGVT-TLCAPPTVWR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 276 LMVQPPSANDRQhRLREVMFY---LN--LSEQEKDAFcerfGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRAGFCYE 350
Cdd:cd05974 189 MLIQQDLASFDV-KLREVVGAgepLNpeVIEQVRRAW----GLTIRDGYGQTETTA-LVGNSPGQPVKAGSMGRPLPGYR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 351 AEIRDDHNRPLPAGEIGEICIKGVPgKTIFKEYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGEN 430
Cdd:cd05974 263 VALLDPDGAPATEGEVALDLGDTRP-VGLMKGYAGDPDKTAHAMR-GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 431 VSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRkDLPRNC 507
Cdd:cd05974 341 ISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFA-ELPKTI 419
|
490
....*....|
gi 1629467165 508 SGKIIRKNLK 517
Cdd:cd05974 420 SGKIRRVELR 429
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
23-516 |
2.10e-35 |
|
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: 137.81 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd12116 3 ATAVRDDD-----RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTsaqfypmyqqiQQEDATQLRHICLIdVALPADDGVSSFTQLknqqpatlcyAPPLSTDDTAEILFTS 182
Cdd:cd12116 78 YILEDAEPALVLT-----------DDALPDRLPAGLPV-LLLALAAAAAAPAAP----------RTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 183 GTTSRPKGVVITHYNL---------RFagyysawqcALRDDDVYLTVM-PAFHID--------CQctaamaafsaGATFV 244
Cdd:cd12116 136 GSTGRPKGVVVSHRNLvnflhsmreRL---------GLGPGDRLLAVTtYAFDISllelllplLA----------GARVV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 245 LVEK---YSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRL--REVmfylnLSEQEKDAFCERFGvRLLTSY 319
Cdd:cd12116 197 IAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTALcgGEA-----LPPDLAARLLSRVG-SLWNLY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 320 GMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTifKEYFLNPKATAKVLEADGW 399
Cdd:cd12116 271 GPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGG-DGVA--QGYLGRPALTAERFVPDPF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 400 LH-------TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgIKDSIRDEAIKAFVVLNEG 472
Cdd:cd12116 348 AGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAG 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1629467165 473 ETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd12116 427 AAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
23-516 |
3.47e-35 |
|
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: 137.40 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICesSGGvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd12114 3 ATAVIC--GDG---TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTsaqfypmyqqiqQEDATQLRHICLIDVALPADDGVSSFTQLKnqqpatlcyaPPLSTDDTAEILFTS 182
Cdd:cd12114 78 AILADAGARLVLT------------DGPDAQLDVAVFDVLILDLDALAAPAPPPP----------VDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 183 GTTSRPKGVVITH---------YNLRFagyysawqcALRDDDVYLTVmPAFHIDCQCTAAMAAFSAGATFVLVEKYSAR- 252
Cdd:cd12114 136 GSTGTPKGVMISHraalntildINRRF---------AVGPDDRVLAL-SSLSFDLSVYDIFGALSAGATLVLPDEARRRd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 253 -AFWGQ-VQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFY-----LNLSEQEKDAFCerfGVRLLTSYGMTET- 324
Cdd:cd12114 206 pAHWAElIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSgdwipLDLPARLRALAP---DARLISLGGATEAs 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 325 ---IVGIIGDRPGDkrrWPSI--GRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAK--VLEAD 397
Cdd:cd12114 283 iwsIYHPIDEVPPD---WRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGR---GVALGYLGDPELTAArfVTHPD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 398 G--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIRDEAIKAFVVL-NEGET 474
Cdd:cd12114 357 GerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPdNDGTP 435
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1629467165 475 LSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd12114 436 IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-516 |
9.75e-35 |
|
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: 136.25 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 12 MWDDLADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGR-----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 92 INARLLREESAWILQNSQACLLVTSAqfypmyqqiqqedATQLRHICLIDVALPADDGVSSFtqlknqqPATLCYAPPLS 171
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTA-------------DLAARLPAGGDVALLGDEALAAP-------PATPPLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 172 tDDTAEILFTSGTTSRPKGVVITHYNL--RFagyysAWQCA---LRDDDVYLTVMP-AFhiDCQCTAAMAAFSAGATFVL 245
Cdd:cd17646 138 -DNLAYVIYTSGSTGRPKGVMVTHAGIvnRL-----LWMQDeypLGPGDRVLQKTPlSF--DVSVWELFWPLVAGARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 246 VE-------KYSARAfwgqVQKYRATVTECIPMMIRTLMVQPpsANDRQHRLREVMfylnLSEQEKDA-----FCERFGV 313
Cdd:cd17646 210 ARpgghrdpAYLAAL----IREHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVF----CSGEALPPelaarFLALPGA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 314 RLLTSYGMTETIVGIIGD--RPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVPgktIFKEYFLNPKATA 391
Cdd:cd17646 280 ELHNLYGPTEAAIDVTHWpvRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQ---LARGYLGRPALTA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 392 KVLEADGWLH------TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
Cdd:cd17646 357 ERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1629467165 466 FVVLNEGET-LSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17646 437 YVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
38-513 |
1.85e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 134.57 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPinarllreesawilqnsqaclLVTSa 117
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQP---------------------LFTA- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 118 qFYPmyQQIQQEDATQLRHICLIDVAlpaddgvssftqlknqQPATLcyapplsTDDTAEILFTSGTTSRPKGVVITHYN 197
Cdd:cd05973 59 -FGP--KAIEHRLRTSGARLVVTDAA----------------NRHKL-------DSDPFVMMFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LRFAGYYSAWQCALRDDDVYLTVM-PAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTL 276
Cdd:cd05973 113 LAAFGAYLRDAVDLRPEDSFWNAAdPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MVQPPSANDR-QHRLREVMFYLN-LSEQEKDAFCERFGVRLLTSYGMTEtiVGII---GDRPGDKRRWPSIGRAGFCYEA 351
Cdd:cd05973 193 MAAGAEVPARpKGRLRRVSSAGEpLTPEVIRWFDAALGVPIHDHYGQTE--LGMVlanHHALEHPVHAGSAGRAMPGWRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EIRDDHNRPLPAGEIGEICIKGVPGKTI-FKEYFLNPKATAkvleADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGEN 430
Cdd:cd05973 271 AVLDDDGDELGPGEPGRLAIDIANSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 431 VSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNC 507
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
....*.
gi 1629467165 508 SGKIIR 513
Cdd:cd05973 427 SGKIQR 432
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
17-516 |
4.85e-34 |
|
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: 134.25 E-value: 4.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 17 ADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
Cdd:cd12117 7 AARTPDAVAVVYGDR-----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 97 LREESAWILQNSQACLLVTSAQFypmyqqiqQEDATQLRHICLIDVALPADDGVSSftqlknqqpatlcyAPPLSTDDTA 176
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSL--------AGRAGGLEVAVVIDEALDAGPAGNP--------------AVPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYN-LRFAgyYSAWQCALRDDDVYLTVMP-AFhiDcqctaamaafsaGATF----------- 243
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGvVRLV--KNTNYVTLGPDDRVLQTSPlAF--D------------ASTFeiwgallngar 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 244 -VLVEKY---SARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDrqhRLREVMFYlnlSEQEKDAFCERF-----GVR 314
Cdd:cd12117 204 lVLAPKGtllDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFA---GLRELLTG---GEVVSPPHVRRVlaacpGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 315 LLTSYGMTETIV----GIIGDRPGDKRRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYFLNPKAT 390
Cdd:cd12117 278 LVNGYGPTENTTfttsHVVTELDEVAGSIP-IGRPIANTRVYVLDEDGRPVPPGVPGELYVGG-DG--LALGYLNRPALT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 391 AKVLEADGWL------HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
Cdd:cd12117 354 AERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLV 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1629467165 465 AFVVLneGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd12117 434 AYVVA--EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
178-509 |
4.95e-34 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 131.27 E-value: 4.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 178 ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQctaamaaFSAGATF------VLVEKYSA 251
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTL-------MFTLATFhaggtnVFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAFWGQVQKYRATVTECIPMMIRTLMvqppSAN-DRQHRLREVMFYLNLSEQEKDA------FCERFGvrlltSYGMTE- 323
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIV----ELNaDGLYDLSSLRSSPAAPEWNDMAtvdtspWGRKPG-----GYGQTEv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 ----TIVGIIGDRPGdkrrwpSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGW 399
Cdd:cd17636 149 mglaTFAALGGGAIG------GAGRPSPLVQVRILDEDGREVPDGEVGEIVARG---PTVMAGYWNRPEVNARRT-RGGW 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 400 LHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEE 479
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAE 298
|
330 340 350
....*....|....*....|....*....|
gi 1629467165 480 FFRFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
Cdd:cd17636 299 LIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
32-482 |
3.52e-33 |
|
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: 132.21 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 32 GGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAC 111
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 112 LLVTSaqfypmyqqiQQEDATQLRHIC---LIDVALPADDGVS---SFTQLKNQQPAtLCYAPPLSTDDTAEILFTSGTT 185
Cdd:cd05932 81 ALFVG----------KLDDWKAMAPGVpegLISISLPPPSAANcqyQWDDLIAQHPP-LEERPTRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 186 SRPKGVVIThynlrFAGYysAWQCA-------LRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEkySARAFWGQV 258
Cdd:cd05932 150 GQPKGVMLT-----FGSF--AWAAQagiehigTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 QKYRATVTECIPMmIRTLMVQ------PPSANDRQHRL--------REVMFYLNLsEQEKDAFC-------------ERF 311
Cdd:cd05932 221 QRARPTLFFSVPR-LWTKFQQgvqdkiPQQKLNLLLKIpvvnslvkRKVLKGLGL-DQCRLAGCgsapvppallewyRSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLLTSYGMTETIVGIIGDRPGDkRRWPSIGRAGFCYEAEIRDDhnrplpageiGEICIKGvpgKTIFKEYFLNPKATA 391
Cdd:cd05932 299 GLNILEAYGMTENFAYSHLNYPGR-DKIGTVGNAGPGVEVRISED----------GEILVRS---PALMMGYYKDPEATA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 392 KVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGIKDSirdeAIKAFVVLN 470
Cdd:cd05932 365 EAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLP----APLALVVLS 440
|
490
....*....|..
gi 1629467165 471 EGETLSEEEFFR 482
Cdd:cd05932 441 EEARLRADAFAR 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-517 |
8.29e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 128.37 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCAL----RDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEK 248
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNE----VYNAWMLALnslfDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARA------FWGQVQKYRATVTECIPMMIRTLMVQPPSANdrqhrLREVMFYLN----LSEQEKDAFCERFGVRLLTS 318
Cdd:cd05944 78 AGYRNpglfdnFWKLVERYRITSLSTVPTVYAALLQVPVNAD-----ISSLRFAMSgaapLPVELRARFEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTETIVGIIGDRPGDKRRWPSIG-RAGFCYEAEIRDD----HNRPLPAGEIGEICIKGvPGktIFKEYfLNPKATAKV 393
Cdd:cd05944 153 YGLTEATCLVAVNPPDGPKRPGSVGlRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAG-PG--VFGGY-LYTEGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 394 LEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE 473
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1629467165 474 TLSEEEFFRFCEQNMA-KFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd05944 309 VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
23-516 |
1.57e-32 |
|
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: 130.14 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd17655 13 HTAVVFED-----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTSAQFYP--MYQQ-IQQEDATQLRHiclidvalpadDGVSSFtqlknqqpatlcyAPPLSTDDTAEIL 179
Cdd:cd17655 88 YILEDSGADILLTQSHLQPpiAFIGlIDLLDEDTIYH-----------EESENL-------------EPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 180 FTSGTTSRPKGVVITHYNL----RFAG--YYSAWQcalrdDDVYLTVmpAFHIDCQCTAAMAAFSAGATFVLV---EKYS 250
Cdd:cd17655 144 YTSGSTGKPKGVMIEHRGVvnlvEWANkvIYQGEH-----LRVALFA--SISFDASVTEIFASLLSGNTLYIVrkeTVLD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 251 ARAFWGQVQKYRATVTECIPMMIRTLmvqPPSANDRQHRLREVMFY-LNLSEQEKDAFCERFG--VRLLTSYGMTETIVG 327
Cdd:cd17655 217 GQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGgEALSTELAKKIIELFGtnPTITNAYGPTETTVD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 328 -IIGDRPGDKRRWPS--IGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKVLEADGWL---- 400
Cdd:cd17655 294 aSIYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIG---GEGVARGYLNRPELTAEKFVDDPFVpger 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 --HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEE 478
Cdd:cd17655 371 myRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KELPVA 448
|
490 500 510
....*....|....*....|....*....|....*....
gi 1629467165 479 EFFRFCEQNMAKFKVPSYLeIRKD-LPRNCSGKIIRKNL 516
Cdd:cd17655 449 QLREFLARELPDYMIPSYF-IKLDeIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
24-516 |
4.76e-32 |
|
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: 128.19 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 24 TALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
Cdd:cd17643 4 VAVVDEDR-----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 104 ILQNSQACLLVTSAqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSG 183
Cdd:cd17643 79 ILADSGPSLLLTDP-------------------------------------------------------DDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 184 TTSRPKGVVITHYNLrfAGYYSAWQCALR--DDDVYLTvmpaFH---IDCQCTAAMAAFSAGATFVLVEKYSAR---AFW 255
Cdd:cd17643 104 STGRPKGVVVSHANV--LALFAATQRWFGfnEDDVWTL----FHsyaFDFSVWEIWGALLHGGRLVVVPYEVARspeDFA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 256 GQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMF---YLNLSEQEKdaFCERFGV---RLLTSYGMTETIVGII 329
Cdd:cd17643 178 RLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFggeALEAAMLRP--WAGRFGLdrpQLVNMYGITETTVHVT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 330 ------GDRPGDKRRwpSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTifKEYFLNPKATAKV-------LEA 396
Cdd:cd17643 256 frpldaADLPAAAAS--PIGRPLPGLRVYVLDADGRPVPPGVVGELYVSG-AGVA--RGYLGRPELTAERfvanpfgGPG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 397 DGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS 476
Cdd:cd17643 331 SRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAD 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1629467165 477 EEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17643 411 IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
180-513 |
5.96e-31 |
|
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: 122.13 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 180 FTSGTTSRPKGvvithynlrfagYYsawqcalRDDDVYLTVMPA----FHIDCQCTAAM--------------AAFSAGA 241
Cdd:cd17633 7 FTSGTTGLPKA------------YY-------RSERSWIESFVCnedlFNISGEDAILApgplshslflygaiSALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 242 TFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLM-VQPP-----SANDRQHRLREVMFYlNLSEQEKDAfcerfgvRL 315
Cdd:cd17633 68 TFIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALArTLEPeskikSIFSSGQKLFESTKK-KLKNIFPKA-------NL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 316 LTSYGMTETIVgIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNrplpaGEIGEICIKgvpgktifKEYFLNPKATAKVLE 395
Cdd:cd17633 140 IEFYGTSELSF-ITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK--------SEMVFSGYVRGGFSN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 396 ADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEaIKAFVVlnEGETL 475
Cdd:cd17633 206 PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALY--SGDKL 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 1629467165 476 SEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:cd17633 283 TYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
174-513 |
2.50e-30 |
|
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: 121.21 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 174 DTAEILFTSGTTSRPKGVVITHYNLRFA-GYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSAR 252
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVpDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 253 AFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFG-VRLLTSYGMTETIVGIIGD 331
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGlTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 332 RPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEE 411
Cdd:cd17635 162 TDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS---PANMLGYWNNPERTAEVL-IDGWVNTGDLGERRED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVV----LNEGETLSEEEFFRfceQN 487
Cdd:cd17635 238 GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeLDENAIRALKHTIR---RE 314
|
330 340
....*....|....*....|....*.
gi 1629467165 488 MAKFKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:cd17635 315 LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
22-517 |
3.13e-30 |
|
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: 122.42 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESSGGvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:cd17653 10 HPDAVAVESLGG---SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTSAqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplSTDDTAEILFT 181
Cdd:cd17653 87 QAILRTSGATLLLTTD-----------------------------------------------------SPDDLAYIIFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYNLrfAGYYSAWQCALR---DDDVYLTVMPAFhiDCQCTAAMAAFSAGATFVLVEkysARAFWGQV 258
Cdd:cd17653 114 SGSTGIPKGVMVPHRGV--LNYVSQPPARLDvgpGSRVAQVLSIAF--DACIGEIFSTLCNGGTLVLAD---PSDPFAHV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 QKyRATVTECIPMMIRTLMVQ---------------PPSANDRQhrlrevmfylnlseqekdafceRFGVRLLTSYGMTE 323
Cdd:cd17653 187 AR-TVDALMSTPSILSTLSPQdfpnlktiflggeavPPSLLDRW----------------------SPGRRLYNAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 TIVGIIGD--RPGDKRrwpSIGRA---GFCYeaeIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATA-KVLEA- 396
Cdd:cd17653 244 CTISSTMTelLPGQPV---TIGKPipnSTCY---ILDADLQPVPEGVVGEICISGV---QVARGYLGNPALTAsKFVPDp 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 397 --DGWLH--TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELEN-IIATHPKIQDIVVVGIKDSirdeaIKAFVVlne 471
Cdd:cd17653 315 fwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR-----LVAFVT--- 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1629467165 472 GETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd17653 387 PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
23-516 |
3.91e-30 |
|
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: 122.43 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 23 KTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd12115 15 AIALVCGDE-----SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTSAqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTS 182
Cdd:cd12115 90 FILEDAQARLVLTDP-------------------------------------------------------DDLAYVIYTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 183 GTTSRPKGVVITHYN----LRFAG-YYSAWQCAlrdddvylTVMPA---------FHIDCQCTAAMAAFSAGATFVLVEk 248
Cdd:cd12115 115 GSTGRPKGVAIEHRNaaafLQWAAaAFSAEELA--------GVLAStsicfdlsvFELFGPLATGGKVVLADNVLALPD- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAfwgqvqkyRATVTECIPMMIRTLMVQ---PPSA---NDRQHRLREVMfYLNLSEQEKdafcerfGVRLLTSYGMT 322
Cdd:cd12115 186 LPAAA--------EVTLINTVPSAAAELLRHdalPASVrvvNLAGEPLPRDL-VQRLYARLQ-------VERVVNLYGPS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 323 E-TIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWL- 400
Cdd:cd12115 250 EdTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGG---AGVARGYLGRPGLTAERFLPDPFGp 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 -----HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETL 475
Cdd:cd12115 327 garlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1629467165 476 SEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd12115 407 LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
164-517 |
8.68e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 124.27 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 164 LCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYN-----------LRFagyysawqcalRDDDVYLTVMPAFHidcqcta 232
Cdd:PRK08633 773 RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNilsnieqisdvFNL-----------RNDDVILSSLPFFH------- 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 233 aMAAFSAGATFVLVEKYS---------ARAFWGQVQKYRATVTECIPMMIRTLMvqppsandRQHRLREVMF---YLNLS 300
Cdd:PRK08633 835 -SFGLTVTLWLPLLEGIKvvyhpdptdALGIAKLVAKHRATILLGTPTFLRLYL--------RNKKLHPLMFaslRLVVA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 301 EQEK------DAFCERFGVRLLTSYGMTET------------IVGI---IGDRPGdkrrwpSIGRA--GFCyeAEIRD-D 356
Cdd:PRK08633 906 GAEKlkpevaDAFEEKFGIRILEGYGATETspvasvnlpdvlAADFkrqTGSKEG------SVGMPlpGVA--VRIVDpE 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 357 HNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVL-EADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSC 433
Cdd:PRK08633 978 TFEELPPGEDGLILIGGP---QVMKGYLGDPEKTAEVIkDIDGigWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPL 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 434 VELENIIAT--HPKIQDIVVVGIKDSIRDEAIkafVVLNEGETLSEEEFFRFC-EQNMAKFKVPSYLEIRKDLPRNCSGK 510
Cdd:PRK08633 1055 GAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVLHTCGAEDVEELKRAIkESGLPNLWKPSRYFKVEALPLLGSGK 1131
|
....*..
gi 1629467165 511 IIRKNLK 517
Cdd:PRK08633 1132 LDLKGLK 1138
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
39-516 |
2.01e-29 |
|
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: 120.44 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAq 118
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 fypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:cd17652 93 ------------------------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 -RFAGYYSAwQCALRDDDVYLT-VMPAFhiDCQCTAAMAAFSAGATFVLVEKYSARA---FWGQVQKYRATV-------- 265
Cdd:cd17652 119 aNLAAAQIA-AFDVGPGSRVLQfASPSF--DASVWELLMALLAGATLVLAPAEELLPgepLADLLREHRITHvtlppaal 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 266 ----TECIPMmIRTLMVQ----PPSANDRQHRLRevmfylnlseqekdafcerfgvRLLTSYGMTETIVGIIGDRPGDKR 337
Cdd:cd17652 196 aalpPDDLPD-LRTLVVAgeacPAELVDRWAPGR----------------------RMINAYGPTETTVCATMAGPLPGG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 338 RWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYFLNPKATAKVLEAD------GWLH-TGDTGYCDE 410
Cdd:cd17652 253 GVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAG-AG--LARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAK 490
Cdd:cd17652 330 DGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPG 409
|
490 500
....*....|....*....|....*.
gi 1629467165 491 FKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
38-471 |
3.68e-29 |
|
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: 120.78 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANLFYTLGIR--KGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLvt 115
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 116 saqfypmyqqiqqedatqlrhIClidvalpaDDGVS--SFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVI 193
Cdd:cd05927 84 ---------------------FC--------DAGVKvySLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVML 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 194 THYNL--RFAGYYSAWQ--CALRDDDVYLTVMPAFHIdcqctaamaafsagatFVLVEKYSARAFWGQVQKYR---ATVT 266
Cdd:cd05927 135 THGNIvsNVAGVFKILEilNKINPTDVYISYLPLAHI----------------FERVVEALFLYHGAKIGFYSgdiRLLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 267 ECIPMMIRTLMVQPPSANDRQH-----------RLREVMF---------YLNLSEQEKDAFCER---------------- 310
Cdd:cd05927 199 DDIKALKPTVFPGVPRVLNRIYdkifnkvqakgPLKRKLFnfalnyklaELRSGVVRASPFWDKlvfnkikqalggnvrl 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 311 -------------------FGVRLLTSYGMTETIVGIIGDRPGDKrrwpSIGRAGF---CYEAEIRD------DHNRPLP 362
Cdd:cd05927 279 mltgsaplspevleflrvaLGCPVLEGYGQTECTAGATLTLPGDT----SVGHVGGplpCAEVKLVDvpemnyDAKDPNP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 363 AGEIgeiCIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIA 441
Cdd:cd05927 355 RGEV---CIRG---PNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIENIYA 428
|
490 500 510
....*....|....*....|....*....|
gi 1629467165 442 THPKIQDIVVVGikDSIRDEAIkAFVVLNE 471
Cdd:cd05927 429 RSPFVAQIFVYG--DSLKSFLV-AIVVPDP 455
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
169-511 |
4.55e-29 |
|
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: 120.13 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLrfagYYSAWQCA----LRDDDVYLTVMPAFHidcqctaamaafsagaTFV 244
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNL----LANVEQITaifdPNPEDVVFGALPFFH----------------SFG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 245 LVEkysarAFW-------GQVQKYRATVTECIPMMIR----TLMVQPP--------SANDRQ-HRLREVMFYLN-LSEQE 303
Cdd:cd05909 203 LTG-----CLWlpllsgiKVVFHPNPLDYKKIPELIYdkkaTILLGTPtflrgyarAAHPEDfSSLRLVVAGAEkLKDTL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 304 KDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGR--AGFCYEAEIRDDHNrPLPAGEIGEICIKGVpgkTIFK 381
Cdd:cd05909 278 RQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRplPGMEVKIVSVETHE-EVPIGEGGLLLVRGP---NVML 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 382 EYFLNPKATAKVLEaDGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV-VVGIKDSIRD 460
Cdd:cd05909 354 GYLNEPELTSFAFG-DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 461 EAIKAFVVLNEGETLSEEEFFRfcEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
Cdd:cd05909 433 EKIVLLTTTTDTDPSSLNDILK--NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-516 |
5.65e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 122.19 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGHKTALICESsggvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
Cdd:PRK12467 511 PDCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKA 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAIMVPINARLLREESAWILQNSQACLLVTSAQfypmyQQIQQEDATQLRHICLIDVALPADDGVSSFTQLkNQQPATLC 165
Cdd:PRK12467 586 GGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH-----LLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEV-ALDPDNLA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 YapplstddtaeILFTSGTTSRPKGVVITHYNL-RFAGYYSAWQCALRDDDVYLTVMPAFhiDCQCTAAMAAFSAGATFV 244
Cdd:PRK12467 660 Y-----------VIYTSGSTGQPKGVAISHGALaNYVCVIAERLQLAADDSMLMVSTFAF--DLGVTELFGALASGATLH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 245 LVEK---YSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRqhRLREVMF---YLNLSEQEKdAFCERFGVRLLTS 318
Cdd:PRK12467 727 LLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRALVCggeALQVDLLAR-VRALGPGARLINH 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTETIVGI----IGDRPGDKRRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKVL 394
Cdd:PRK12467 804 YGPTETTVGVstyeLSDEERDFGNVP-IGQPLANLGLYILDHYLNPVPVGVVGELYIG---GAGLARGYHRRPALTAERF 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 395 EAD------GWLH-TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIRDEAIKAFV 467
Cdd:PRK12467 880 VPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYL 958
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 468 VLNEGETLSE-----EEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12467 959 VPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
22-517 |
9.57e-29 |
|
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: 118.80 E-value: 9.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTAlICESSGgvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL----L 97
Cdd:cd05918 14 DAPA-VCAWDG----SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHplqrL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 98 REesawILQNSQACLLVTSaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplSTDDTAE 177
Cdd:cd05918 89 QE----ILQDTGAKVVLTS------------------------------------------------------SPSDAAY 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 178 ILFTSGTTSRPKGVVITHynlrfagyySAWQCALRdddvylTVMPAFHIDCQctaamaafsagaTFVLveKYSARAF--- 254
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEH---------RALSTSAL------AHGRALGLTSE------------SRVL--QFASYTFdvs 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 255 -------W-------------------GQVQKYRATVTECIPMMIRTLM-VQPPSandrqhrLR------EVMfylnlSE 301
Cdd:cd05918 162 ileifttLaaggclcipseedrlndlaGFINRLRVTWAFLTPSVARLLDpEDVPS-------LRtlvlggEAL-----TQ 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 302 QEKDAFCERfgVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRA--GFCYEAEiRDDHNRPLPAGEIGEICIKGvPgkTI 379
Cdd:cd05918 230 SDVDTWADR--VRLINAYGPAECTIAATVSPVVPSTDPRNIGRPlgATCWVVD-PDNHDRLVPIGAVGELLIEG-P--IL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 380 FKEYFLNPKATAKV-LEADGWLH------------TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
Cdd:cd05918 304 ARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 447 QDIVVVGI---KDSIRDEAIKAFVVLNEGETLSEEEFFRF-----------------CEQNMAKFKVPS-YLEIrKDLPR 505
Cdd:cd05918 384 AKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGDGDSLFlepsdefralvaelrskLRQRLPSYMVPSvFLPL-SHLPL 462
|
570
....*....|..
gi 1629467165 506 NCSGKIIRKNLK 517
Cdd:cd05918 463 TASGKIDRRALR 474
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
33-453 |
1.01e-28 |
|
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: 119.84 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 33 GVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACL 112
Cdd:cd17641 7 GIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 113 LVTSAQfypmyQQIQQ--EDATQLRHICLIDVALPA------DDGVSSFTQLKNQQPATLCYAPPL--------STDDTA 176
Cdd:cd17641 87 VIAEDE-----EQVDKllEIADRIPSVRYVIYCDPRgmrkydDPRLISFEDVVALGRALDRRDPGLyerevaagKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 177 EILFTSGTTSRPKGVVITHYNlrFAGYYSAWQCA--LRDDDVYLTVMP-----------------AFHIDC---QCTAAM 234
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGN--FLGHCAAYLAAdpLGPGDEYVSVLPlpwigeqmysvgqalvcGFIVNFpeePETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 235 AAFSAGATFVLVekySARAFWGQVQKYRATVTECIPM---MIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDA----- 306
Cdd:cd17641 240 DLREIGPTFVLL---PPRVWEGIAADVRARMMDATPFkrfMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADAllfrp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 307 --------------------------FCERFGVRLLTSYGMTETIVGIIGDRPGDKRrWPSIGRAgfCYEAEIRDDhnrp 360
Cdd:cd17641 317 lrdrlgfsrlrsaatggaalgpdtfrFFHAIGVPLKQLYGQTELAGAYTVHRDGDVD-PDTVGVP--FPGTEVRID---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 361 lpagEIGEICIKGvPGktIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENI 439
Cdd:cd17641 390 ----EVGEILVRS-PG--VFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENK 462
|
490
....*....|....
gi 1629467165 440 IATHPKIQDIVVVG 453
Cdd:cd17641 463 LKFSPYIAEAVVLG 476
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
37-516 |
1.88e-28 |
|
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: 117.57 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTs 116
Cdd:cd17650 12 QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 aqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqQPatlcyapplstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd17650 91 -------------------------------------------QP-----------EDLAYVIYTSGTTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NlrFAGYYSAWQ--CALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVE---KYSARAFWGQVQKYRATVTECIPM 271
Cdd:cd17650 117 N--VAHAAHAWRreYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 272 MIRTLMVQPPSANDRQHRLREVMFYLNLSEQE--KDAFcERFG--VRLLTSYGMTETIVG-----IIGDRPGDKRRWPsI 342
Cdd:cd17650 195 LIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQdfKTLA-ARFGqgMRIINSYGVTEATIDstyyeEGRDPLGDSANVP-I 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 343 GRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAK-----VLEADGWLH-TGDTGYCDEEGFFYF 416
Cdd:cd17650 273 GRPLPNTAMYVLDERLQPQPVGVAGELYIG---GAGVARGYLNRPELTAErfvenPFAPGERMYrTGDLARWRADGNVEL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVlnEGETLSEEEFFRFCEQNMAKFKVPSY 496
Cdd:cd17650 350 LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPSYMIPSY 427
|
490 500
....*....|....*....|
gi 1629467165 497 LEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17650 428 YVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
56-517 |
1.23e-27 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 116.42 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 56 TLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATqLR 135
Cdd:PRK05620 58 ELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPC-VR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 136 HICLI--------DVALPADDGVSSFTQLKNQQPATLCYaPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFA--GYYS 205
Cdd:PRK05620 137 AVVFIgpsdadsaAAHMPEGIKVYSYEALLDGRSTVYDW-PELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQslSLRT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 206 AWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMVQ----PP 281
Cdd:PRK05620 216 TDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHylknPP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 282 sandRQHRLREVmfYLNLSE---QEKDAFCERFGVRLLTSYGMTETI-VGIIGDRPGD---KRRWP---SIGRAGFCYEA 351
Cdd:PRK05620 296 ----ERMSLQEI--YVGGSAvppILIKAWEERYGVDVVHVWGMTETSpVGTVARPPSGvsgEARWAyrvSQGRFPASLEY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EIRDD------HNRPlpAGEIGeicikgVPGKTIFKEYFLNPKAT----------------AKVLEADGWLHTGDTGYCD 409
Cdd:PRK05620 370 RIVNDgqvmesTDRN--EGEIQ------VRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVT 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 410 EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMA 489
Cdd:PRK05620 442 RDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRD 521
|
490 500 510
....*....|....*....|....*....|.
gi 1629467165 490 KFK---VPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK05620 522 RLPnwmLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
37-516 |
2.39e-27 |
|
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: 115.22 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYpmyqQIQQEDATQLRHICLIDVALPADDGVSSFTQLKNQQpatlcYAP--PLSTDDTAEILFTSGTTSRPKGVVIT 194
Cdd:cd05915 104 PNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGE-----EADpvRVPERAACGMAYTTGTTGLPKGVVYS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 195 HYnlrfAGYYSAWQCALRDD------DVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTEC 268
Cdd:cd05915 175 HR----ALVLHSLAASLVDGtalsekDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 269 IPMMIRTLmvqppsANDRQHRLREVMFYLNL-----SEQEKDAFCERFGV-RLLTSYGMTEtiVGIIGDRPGDKRRWPSI 342
Cdd:cd05915 251 VPTVWLAL------ADYLESTGHRLKTLRRLvvggsAAPRSLIARFERMGvEVRQGYGLTE--TSPVVVQNFVKSHLESL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 343 ---------GRAGFCYEAE---IRDDHNRPLPAgEIGEICIKGVPGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDE 410
Cdd:cd05915 323 seeekltlkAKTGLPIPLVrlrVADEEGRPVPK-DGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETlSEEEFFRFCEQNMAK 490
Cdd:cd05915 402 EGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKP-TPEELNEHLLKAGFA 480
|
490 500
....*....|....*....|....*..
gi 1629467165 491 FK-VPSYLEIRKDLPRNCSGKiIRKNL 516
Cdd:cd05915 481 KWqLPDAYVFAEEIPRTSAGK-FLKRA 506
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
22-517 |
2.95e-26 |
|
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: 111.31 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:cd17649 2 DAVALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTsaqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknQQPATLCYapplstddtaeILFT 181
Cdd:cd17649 77 RYMLEDSGAGLLLT-------------------------------------------HHPRQLAY-----------VIYT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYNL-----RFAGYYsawqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLVEK---YSARA 253
Cdd:cd17649 103 SGSTGTPKGVAVSHGPLaahcqATAERY-----GLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDelwASADE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 FWGQVQKYRATVTECIPMMIRTL---MVQPPSanDRQHRLR------EVMFYLNLSEQEKDAfcerfgVRLLTSYGMTET 324
Cdd:cd17649 177 LAEMVRELGVTVLDLPPAYLQQLaeeADRTGD--GRPPSLRlyifggEALSPELLRRWLKAP------VRLFNAYGPTEA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 325 IVG--IIGDRPGDKRRWPS--IGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAK--VLEADG 398
Cdd:cd17649 249 TVTplVWKCEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGE---GLARGYLGRPELTAErfVPDPFG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 399 -----WLHTGD-TGYCDeEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGiKDSIRDEAIKAFVVLNEG 472
Cdd:cd17649 326 apgsrLYRTGDlARWRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1629467165 473 ETLSE--EEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:cd17649 404 AAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
21-517 |
3.98e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 112.16 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICES-SGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI----NAR 95
Cdd:PRK00174 81 GDKVAIIWEGdDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 96 LLREEsawiLQNSQACLLVTSAQFY------PMYQQIqqedatqlrhicliDVALPADDGVSS----------------- 152
Cdd:PRK00174 161 ALADR----IIDAGAKLVITADEGVrggkpiPLKANV--------------DEALANCPSVEKvivvrrtggdvdwvegr 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 153 ---FTQLKNQQPATlCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSA----WQCALRDDDVY------ 217
Cdd:PRK00174 223 dlwWHELVAGASDE-CEPEPMDAEDPLFILYTSGSTGKPKGVLHTT-----GGYlvYAAmtmkYVFDYKDGDVYwctadv 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 218 ------------------LTVMpafhidcqctaamaafsagatFVLVEKYSARA-FWGQVQKYRATVTECIPMMIRTLMV 278
Cdd:PRK00174 297 gwvtghsyivygplangaTTLM---------------------FEGVPNYPDPGrFWEVIDKHKVTIFYTAPTAIRALMK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 279 ---QPPSANDRQhrlrevmfylnlseqekdafcerfGVRLLTSYG---------------------------MTET---- 324
Cdd:PRK00174 356 egdEHPKKYDLS------------------------SLRLLGSVGepinpeawewyykvvggercpivdtwwQTETggim 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 325 ---IVGIIGDRPGdkrrwpSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIK--------GVPG------KTIFKEYFlnp 387
Cdd:PRK00174 412 itpLPGATPLKPG------SATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKdpwpgmmrTIYGdherfvKTYFSTFK--- 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 388 katakvleadGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFV 467
Cdd:PRK00174 483 ----------GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFV 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1629467165 468 VLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK00174 553 TLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
7-455 |
4.34e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 111.91 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 7 QHLRQMwddlADVYGHKTALICESSGGVVNRY-----SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFG 81
Cdd:PRK09274 10 RHLPRA----AQERPDQLAVAVPGGRGADGKLaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 82 LAKIGAIMVPIN-----ARLLReesawILQNSQAcllvtSAqFypmyqqIQQEDATQLRHIC---------LIDVALPAD 147
Cdd:PRK09274 86 LFKAGAVPVLVDpgmgiKNLKQ-----CLAEAQP-----DA-F------IGIPKAHLARRLFgwgkpsvrrLVTVGGRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 148 DGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNlrFAGYYSAWQC--ALRDDDVYLTVMPAF- 224
Cdd:PRK09274 149 WGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGM--FEAQIEALREdyGIEPGEIDLPTFPLFa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 225 --------------------------HI-----DCQCTAamaafsagaTFVlvekysARAFWGQVQKYRATVTECIPMMI 273
Cdd:PRK09274 227 lfgpalgmtsvipdmdptrpatvdpaKLfaaieRYGVTN---------LFG------SPALLERLGRYGEANGIKLPSLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 274 RTLM----VQPPSANdrqhRLREVmfylnLSEqekdafcerfGVRLLTSYGMTETI-VGIIGDR---PGDKRRWPS---- 341
Cdd:PRK09274 292 RVISagapVPIAVIE----RFRAM-----LPP----------DAEILTPYGATEALpISSIESReilFATRAATDNgagi 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 342 -IGRAGFCYEAEIRD---------DHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKAT--AKVLEADG--WLHTGDTGY 407
Cdd:PRK09274 353 cVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA---GPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGY 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1629467165 408 CDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
Cdd:PRK09274 430 LDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
173-485 |
5.83e-26 |
|
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: 111.15 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSAWQC---ALRDDDVYLTVMPAFHIdcqctaamaafsAGATFVLVEKY 249
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNL-VAGIAGLGDRvpeLLGPDDRYLAYLPLAHI------------FELAAENVCLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 250 ----------------SARAFWGQVQKYRATVTECIPMMIRTL------MVQPPSANDRQ-------------------- 287
Cdd:cd17639 155 rggtigygsprtltdkSKRGCKGDLTEFKPTLMVGVPAIWDTIrkgvlaKLNPMGGLKRTlfwtayqsklkalkegpgtp 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 288 -------HRLREVM-----FYLN----LSEQEKdAFCERFGVRLLTSYGMTETIVGIIGDRPGDkrrwPSIGRAGF---C 348
Cdd:cd17639 235 lldelvfKKVRAALggrlrYMLSggapLSADTQ-EFLNIVLCPVIQGYGLTETCAGGTVQDPGD----LETGRVGPplpC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 349 YEAEIRD------DHNRPLPAGEIgeiCIKGVPgktIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCN 422
Cdd:cd17639 310 CEIKLVDweeggySTDKPPPRGEI---LIRGPN---VFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629467165 423 MIK-RGGENVSCVELENIIATHPKIQDIVVVGikDSIRDEAIkAFVVLNEG--ETLSEEEFFRFCE 485
Cdd:cd17639 384 LVKlQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPNEKhlTKLAEKHGVINSE 446
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
22-517 |
1.43e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 109.48 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 22 HKTALICESsggvvNRYSYLELNQEINRTANLFYTLGiRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
Cdd:PRK07638 16 NKIAIKEND-----RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 102 AWILQNSQACLLVTSAQFYpmyQQIQQEDAT--QLRHIC-LIDVALPAddgvssFTQLKNQQPAtlcyapPLSTDdtaei 178
Cdd:PRK07638 90 KERLAISNADMIVTERYKL---NDLPDEEGRviEIDEWKrMIEKYLPT------YAPIENVQNA------PFYMG----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 179 lFTSGTTSRPKGVVITHYNlrfagYYSAWQCALRD-----DDVYL---TVM---------PAFHIDcqctaamaafsagA 241
Cdd:PRK07638 150 -FTSGSTGKPKAFLRAQQS-----WLHSFDCNVHDfhmkrEDSVLiagTLVhslflygaiSTLYVG-------------Q 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 242 TFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLMvqppSAND-RQHRLREVMFYLNLSEQEKDAFCERF-GVRLLTSY 319
Cdd:PRK07638 211 TVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLY----KENRvIENKMKIISSGAKWEAEAKEKIKNIFpYAKLYEFY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 320 GMTE-TIVGIIGDRPGdKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYfLNPKATAKVLEADG 398
Cdd:PRK07638 287 GASElSFVTALVDEES-ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKS---PQFFMGY-IIGGVLARELNADG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 399 WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVvlnEGETlSEE 478
Cdd:PRK07638 362 WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQ 437
|
490 500 510
....*....|....*....|....*....|....*....
gi 1629467165 479 EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
32-513 |
2.92e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.32 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 32 GGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP--INARLLREESaWI----- 104
Cdd:PRK09192 44 GQLEEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGGRES-YIaqlrg 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 -LQNSQACLLVTSAQFYPMYQQIQqeDATQLRHiclidvalpaddgVSSFTQLkNQQPATLCYAPPLSTDDTAEILFTSG 183
Cdd:PRK09192 123 mLASAQPAAIITPDELLPWVNEAT--HGNPLLH-------------VLSHAWF-KALPEADVALPRPTPDDIAYLQYSSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 184 TTSRPKGVVITHY----NLRfagYYSAWQCALRDDDVYLTVMPAFH-----------IDCQCTaamaafsagatfvlVEK 248
Cdd:PRK09192 187 STRFPRGVIITHRalmaNLR---AISHDGLKVRPGDRCVSWLPFYHdmglvgflltpVATQLS--------------VDY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAF------WGQ-VQKYRATVTecipmmirtlmVQPPSANDR-QHRLREV-MFYLNLSE-------------QEKDA 306
Cdd:PRK09192 250 LPTRDFarrplqWLDlISRNRGTIS-----------YSPPFGYELcARRVNSKdLAELDLSCwrvagigadmirpDVLHQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 307 FCERFGVR------LLTSYGMTETIV---------GIIGDR---------------PGDKRRWPSI---GRAGFCYEAEI 353
Cdd:PRK09192 319 FAEAFAPAgfddkaFMPSYGLAEATLavsfsplgsGIVVEEvdrdrleyqgkavapGAETRRVRTFvncGKALPGHEIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 354 RDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPkATAKVLEADGWLHTGDTGYCdEEGFFYFVDRRCNMIKRGGENVSC 433
Cdd:PRK09192 399 RNEAGMPLPERVVGHICVRG---PSLMSGYFRDE-ESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 434 VELENIIATHPKIQ--DIVVVgikdSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFK-----------VPSYleir 500
Cdd:PRK09192 474 QDIEWIAEQEPELRsgDAAAF----SIAQENGEKIVLLVQCRISDEERRGQLIHALAALVRsefgveaavelVPPH---- 545
|
570
....*....|...
gi 1629467165 501 kDLPRNCSGKIIR 513
Cdd:PRK09192 546 -SLPRTSSGKLSR 557
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
57-475 |
1.53e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 107.49 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQ-ACLLVTSAQFYPMYQQIqqedaTQLR 135
Cdd:PLN02736 98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvAAIFCVPQTLNTLLSCL-----SEIP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 136 HICLIDV---------ALPADDGVS--SFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNL--RFAG 202
Cdd:PLN02736 173 SVRLIVVvggadeplpSLPSGTGVEivTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLiaNVAG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 203 YysAWQCALRDDDVYLTVMPAFHIDCQCTAamaafsagatFVLVEKYSARAFW-GQVQKY-------RATVTECIPMMIR 274
Cdd:PLN02736 253 S--SLSTKFYPSDVHISYLPLAHIYERVNQ----------IVMLHYGVAVGFYqGDNLKLmddlaalRPTIFCSVPRLYN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 275 ------TLMVQ-------------------------PPSAN-DR----------QHRLR-----------EVMFYLNLse 301
Cdd:PLN02736 321 riydgiTNAVKesgglkerlfnaaynakkqalengkNPSPMwDRlvfnkikaklGGRVRfmssgasplspDVMEFLRI-- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 302 qekdafCerFGVRLLTSYGMTETIVGIIGDRPGDKrrwpSIGRAGF---CYEAEIRD-------DHNRPLPAGEIgeiCI 371
Cdd:PLN02736 399 ------C--FGGRVLEGYGMTETSCVISGMDEGDN----LSGHVGSpnpACEVKLVDvpemnytSEDQPYPRGEI---CV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 372 KGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIV 450
Cdd:PLN02736 464 RG---PIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCKFVAQCF 540
|
490 500
....*....|....*....|....*
gi 1629467165 451 VVGikDSIRDEAIkAFVVLNEgETL 475
Cdd:PLN02736 541 VYG--DSLNSSLV-AVVVVDP-EVL 561
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-473 |
2.21e-24 |
|
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: 106.55 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 15 DLADVYGHKTALI-CESSGGVVNRYSYLELNQEINRTANLFYTLGiRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
Cdd:cd05931 1 RRAAARPDRPAYTfLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 94 ARLLREESAW---ILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHIcLIDVALPADDGVSSFTqlknqqpatlcyAPPL 170
Cdd:cd05931 80 PPTPGRHAERlaaILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR-LLVVDLLPDTSAADWP------------PPSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 171 STDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQcaLRDDDVYLTVMPAFH-----------IDCQCtaamaaf 237
Cdd:cd05931 147 DPDDIAYLQYTSGSTGTPKGVVVTHRNLLanVRQIRRAYG--LDPGDVVVSWLPLYHdmgligglltpLYSGG------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 238 sagaTFVLVekySARAF------WGQ-VQKYRATVT--------ECIPMmirtlmvqppsANDRQ------HRLRevmFY 296
Cdd:cd05931 218 ----PSVLM---SPAAFlrrplrWLRlISRYRATISaapnfaydLCVRR-----------VRDEDlegldlSSWR---VA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 297 LNLSE--QEK--DAFCERF---GVR---LLTSYGMTETIVGIIGDRPG-------------------------DKRRWPS 341
Cdd:cd05931 277 LNGAEpvRPAtlRRFAEAFapfGFRpeaFRPSYGLAEATLFVSGGPPGtgpvvlrvdrdalagravavaaddpAARELVS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 342 IGRAGFCYEAEIRD-DHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKV------LEADGWLHTGDTGYCDeEGFF 414
Cdd:cd05931 357 CGRPLPDQEVRIVDpETGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH-DGEL 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 415 YFVDRRCNMIKRGGENVscveleniiatHPkiQDI--VVVGIKDSIRDEAIKAFVVLNEGE 473
Cdd:cd05931 433 YITGRLKDLIIVRGRNH-----------YP--QDIeaTAEEAHPALRPGCVAAFSVPDDGE 480
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-516 |
2.87e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.74 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTs 116
Cdd:PRK12316 2028 HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT- 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 aqfypmyQQIQQEDatqlrhiclidvaLPADDGVSSF---TQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVI 193
Cdd:PRK12316 2107 -------QRHLLER-------------LPLPAGVARLpldRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAV 2166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 194 THYNL----RFAGYYSawqcALRDDDVYLTVMP----AFHIDCqctaamAAFSAGATFVLV---EKYSARAFWGQVQKYR 262
Cdd:PRK12316 2167 SHGALvahcQAAGERY----ELSPADCELQFMSfsfdGAHEQW------FHPLLNGARVLIrddELWDPEQLYDEMERHG 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 263 ATVTECIPMMIRTLmVQPPSANDRQHRLREVMFYLNLSEQEK-DAFCERF-GVRLLTSYGMTETIVGII-----GDRPGD 335
Cdd:PRK12316 2237 VTILDFPPVYLQQL-AEHAERDGRPPAVRVYCFGGEAVPAASlRLAWEALrPVYLFNGYGPTEAVVTPLlwkcrPQDPCG 2315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 336 KRRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGWLH-------TGDTGYC 408
Cdd:PRK12316 2316 AAYVP-IGRALGNRRAYILDADLNLLAPGMAGELYLGGE---GLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARY 2391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNM 488
Cdd:PRK12316 2392 RADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARL 2470
|
490 500
....*....|....*....|....*...
gi 1629467165 489 AKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12316 2471 PAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
37-454 |
3.40e-24 |
|
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: 105.24 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREEsawilqnsqaclLVTs 116
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKN------------LKQ- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 aqfypmyqqiqqedatqlrhiCLIDVALPADDGVssftqlknqqpatlcyapPLStDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd05910 69 ---------------------CLQEAEPDAFIGI------------------PKA-DEPAAILFTSGSTGTPKGVVYRHG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NlrFAGYYSAwqcaLRDD------DVYLTVMPAF--------------HIDCQCTAAMAAFSAGATfvlVEKYSAR---- 252
Cdd:cd05910 109 T--FAAQIDA----LRQLygirpgEVDLATFPLFalfgpalgltsvipDMDPTRPARADPQKLVGA---IRQYGVSivfg 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 253 --AFWGQVQKYRATVTECIPMMIRTLMVQ---PPSANDRQHRLrevmfylnLSEqekdafcerfGVRLLTSYGMTETI-V 326
Cdd:cd05910 180 spALLERVARYCAQHGITLPSLRRVLSAGapvPIALAARLRKM--------LSD----------EAEILTPYGATEALpV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 327 GIIGDRP-GDKRRWPSIGRAGFCY---------------EAEIRD-DHNRPLPAGEIGEICikgVPGKTIFKEYFLNPKA 389
Cdd:cd05910 242 SSIGSRElLATTTAATSGGAGTCVgrpipgvrvriieidDEPIAEwDDTLELPRGEIGEIT---VTGPTVTPTYVNRPVA 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 390 TA--KVLEADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
Cdd:cd05910 319 TAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
32-474 |
1.52e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 104.51 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 32 GGVVNRY---SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNS 108
Cdd:PLN02430 68 DGKVGPYmwkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 109 QACLLVTSAQFYPMYQQIQQEDATQLRHI-CLIDVA-----LPADDGVSS-----FTQLKNQQPATLCYAPPLstdDTAE 177
Cdd:PLN02430 148 EIDFVFVQDKKIKELLEPDCKSAKRLKAIvSFTSVTeeesdKASQIGVKTyswidFLHMGKENPSETNPPKPL---DICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 178 ILFTSGTTSRPKGVVITHYNLR--FAG---YYSAWQCALRDDDVYLTVMPAFHIDCQctaamaafsagatfvLVEKY--- 249
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVAtfVRGvdlFMEQFEDKMTHDDVYLSFLPLAHILDR---------------MIEEYffr 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 250 ---SARAFWGQVQKYRATVTECIPmmirTLMVQPPSANDRQHR-----------LREVMFY---------LNLSEQEKDA 306
Cdd:PLN02430 290 kgaSVGYYHGDLNALRDDLMELKP----TLLAGVPRVFERIHEgiqkalqelnpRRRLIFNalykyklawMNRGYSHKKA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 307 -----------FCERFG--VRLLTS------------------------YGMTETIVGIIGDRPGDKRRWPSIGRAGFCY 349
Cdd:PLN02430 366 spmadflafrkVKAKLGgrLRLLISggaplsteieeflrvtscafvvqgYGLTETLGPTTLGFPDEMCMLGTVGAPAVYN 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 E---AEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKR 426
Cdd:PLN02430 446 ElrlEEVPEMGYDPLGEPPRGEICVRG---KCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKL 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1629467165 427 G-GENVSCVELENIIATHPKIQDIVVVGikDSIRDEAIkAFVVLNEGET 474
Cdd:PLN02430 522 SqGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEENT 567
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
39-516 |
1.96e-23 |
|
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: 103.32 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQedatqlrhiclidVALPADDGVSSftqlKNQQPATLCYApplsTDDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:cd17656 95 LKSKLSFNKS-------------TILLEDPSISQ----EDTSNIDYINN----SDDLLYIIYTSGTTGKPKGVQLEHKNM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 -RFAGYYSAWQCALRDDDVYLTVMPAFHIDCQ------CTAAMAAFSAGAT-------FVLVEKYSAR------AFWGQV 258
Cdd:cd17656 154 vNLLHFEREKTNINFSDKVLQFATCSFDVCYQeifstlLSGGTLYIIREETkrdveqlFDLVKRHNIEvvflpvAFLKFI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 ---QKYRATVTECIPMMI---RTLMVQPPsandrqhrLREVMfylnlseqekdafcERFGVRLLTSYGMTET-IVGIIGD 331
Cdd:cd17656 234 fseREFINRFPTCVKHIItagEQLVITNE--------FKEML--------------HEHNVHLHNHYGPSEThVVTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 332 RPGDK-RRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGW------LHTGD 404
Cdd:cd17656 292 NPEAEiPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGA---SVARGYLNRQELTAEKFFPDPFdpnermYRTGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 405 TGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEEFFRFC 484
Cdd:cd17656 369 LARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELNISQLREYL 446
|
490 500 510
....*....|....*....|....*....|..
gi 1629467165 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17656 447 AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
173-516 |
6.95e-23 |
|
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: 101.80 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMP--------AFHIDCQCTAAMAAFSAGATFV 244
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPlthdmgliAFHLAPLIAGMNQYLMPTRLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 245 LvekysARAFW-GQVQKYRATVTEC----IPMMIRTLmvQPPSANDRQhrLREVMFYLNLSEQEKDAFCERFGVRL---- 315
Cdd:cd05908 186 R-----RPILWlKKASEHKATIVSSpnfgYKYFLKTL--KPEKANDWD--LSSIRMILNGAEPIDYELCHEFLDHMskyg 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 316 ------LTSYGMTETIVGIIGDRPGDKRRWPSIGRAGF---------------CY----------EAEIR--DDHNRPLP 362
Cdd:cd05908 257 lkrnaiLPVYGLAEASVGASLPKAQSPFKTITLGRRHVthgepepevdkkdseCLtfvevgkpidETDIRicDEDNKILP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 363 AGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCdEEGFFYFVDRRCNMIKRGGENVSCVELENIIAT 442
Cdd:cd05908 337 DGYIGHIQIRG---KNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 443 HPKIQ--DIVVVGIKDS-IRDEAIKAFVVLNEgetlSEEEFFRFCEQ------NMAKFKVPSYLEIRKdLPRNCSGKIIR 513
Cdd:cd05908 413 LEGVElgRVVACGVNNSnTRNEEIFCFIEHRK----SEDDFYPLGKKikkhlnKRGGWQINEVLPIRR-IPKTTSGKVKR 487
|
...
gi 1629467165 514 KNL 516
Cdd:cd05908 488 YEL 490
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
25-516 |
1.30e-22 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 101.56 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESS-GGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI---------MVPINA 94
Cdd:PRK10524 71 ALIAVSTeTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggfaSHSLAA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 95 RLlreesawilQNSQACLLVTS---------AQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSS----FTQLKNQQ- 160
Cdd:PRK10524 151 RI---------DDAKPVLIVSAdagsrggkvVPYKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGrdvdYATLRAQHl 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 161 ----PATLcyappLSTDDTAEILFTSGTTSRPKGVVithynlRFAGYYSAwqcALRdddvylTVMPafHIDCQ------- 229
Cdd:PRK10524 222 garvPVEW-----LESNEPSYILYTSGTTGKPKGVQ------RDTGGYAV---ALA------TSMD--TIFGGkagetff 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 230 CT-----------AAMAAFSAGATFVLVEKYSARA----FWGQVQKYRATVTECIPMMIRTLMVQPPsANDRQHRLREV- 293
Cdd:PRK10524 280 CAsdigwvvghsyIVYAPLLAGMATIMYEGLPTRPdagiWWRIVEKYKVNRMFSAPTAIRVLKKQDP-ALLRKHDLSSLr 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 294 MFYLN---LSEQEKDAFCERFGVRLLTSYGMTET---IVGI---IGDRPgdkRRWPSIGRAGFCYEAEIRDDHN-RPLPA 363
Cdd:PRK10524 359 ALFLAgepLDEPTASWISEALGVPVIDNYWQTETgwpILAIargVEDRP---TRLGSPGVPMYGYNVKLLNEVTgEPCGP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 364 GEIGEICIKGV--PG--KTIFK--EYFLNP--KATAKVLEAdgwlhTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVE 435
Cdd:PRK10524 436 NEKGVLVIEGPlpPGcmQTVWGddDRFVKTywSLFGRQVYS-----TFDWGIRDADGYYFILGRTDDVINVAGHRLGTRE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAK--------FKVPSYLEIRKDLPRNC 507
Cdd:PRK10524 511 IEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEIMAlvdsqlgaVARPARVWFVSALPKTR 590
|
....*....
gi 1629467165 508 SGKIIRKNL 516
Cdd:PRK10524 591 SGKLLRRAI 599
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-510 |
1.35e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 99.38 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 171 STDDTAeILFTSGTTSRPKGVVITH---YNLRFAGYYSAWQCALRDDDVY--------LTVMPA---FHIDCQCTAAMAA 236
Cdd:cd05924 2 SADDLY-ILYTGGTTGMPKGVMWRQediFRMLMGGADFGTGEFTPSEDAHkaaaaaagTVMFPApplMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 237 FSAGATFVLVEKYSARAFWGQVQKYRATVTecipMMIRTLMVQPPSANDRQHRLREV--MFYLN-----LSEQEKDAFCE 309
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDAMARPLIDALRDAGPYDLssLFAISsggalLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 310 RFGVRLLT-SYGMTETIVGIIG-DRPGDKRRWPSIGRAGfcyEAEIRDDHNRPLPAGE--IGEICIKGVpgktIFKEYFL 385
Cdd:cd05924 157 LVPNITLVdAFGSSETGFTGSGhSAGSGPETGPFTRANP---DTVVLDDDGRVVPPGSggVGWIARRGH----IPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 386 NPKATAKVL-EADG--WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEA 462
Cdd:cd05924 230 DEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1629467165 463 IKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
Cdd:cd05924 310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-516 |
2.11e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.78 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
Cdd:PRK12467 3113 ALVFGDQ-----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYM 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 LQNSQACLLVTSAQFYpmyqqiqqEDATQLRHicliDVALPADDGVssftqLKNQQPAtlCYAPPLSTDDTAEILFTSGT 184
Cdd:PRK12467 3188 IEDSGVKLLLTQAHLL--------EQLPAPAG----DTALTLDRLD-----LNGYSEN--NPSTRVMGENLAYVIYTSGS 3248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 185 TSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLV--EKYSARAFWGQVQKYR 262
Cdd:PRK12467 3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHR 3327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 263 ATVTECIPMMIRTLMvqppSANDRQ--HRLREVMFylNLSEQEKDAFCERFG----VRLLTSYGMTETIVGIIG-DRPGD 335
Cdd:PRK12467 3328 ISIACFPPAYLQQFA----EDAGGAdcASLDIYVF--GGEAVPPAAFEQVKRklkpRGLTNGYGPTEAVVTVTLwKCGGD 3401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 336 KRRWPS---IGR--AGF-CYeaeIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEAD------GWLH-T 402
Cdd:PRK12467 3402 AVCEAPyapIGRpvAGRsIY---VLDGQLNPVPVGVAGELYIGGV---GLARGYHQRPSLTAERFVADpfsgsgGRLYrT 3475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 403 GDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIRDEAIKAFVVLNEGETLSEEEFFR 482
Cdd:PRK12467 3476 GDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRD 3554
|
490 500 510
....*....|....*....|....*....|....
gi 1629467165 483 FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12467 3555 HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-516 |
3.84e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.19 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQF-YPMYQQIQQEDATqlrhiclidvalPADDGVSSFTQLKNQQPATLCYapplstddtaeILFTSGTTSRPKGVVITH 195
Cdd:PRK12316 3162 SHLrLPLAQGVQVLDLD------------RGDENYAEANPAIRTMPENLAY-----------VIYTSGSTGKPKGVGIRH 3218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YNLRFAGYYSAWQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVL--VEKYSA-RAFWGQVQKYRATVTECIPMM 272
Cdd:PRK12316 3219 SALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLagPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 273 IRTLMVQPpsandRQHRLREVMFYLNLSEQEKDAFCERF--GVRLLTSYGMTETIVGIIGDRPGDKRR-WPSIGRAGFCY 349
Cdd:PRK12316 3298 LQAFLEEE-----DAHRCTSLKRIVCGGEALPADLQQQVfaGLPLYNLYGPTEATITVTHWQCVEEGKdAVPIGRPIANR 3372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 350 EAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGW------LHTGDTGYCDEEGFFYFVDRRCNM 423
Cdd:PRK12316 3373 ACYILDGSLEPVPVGALGELYLGGE---GLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 424 IKRGGENVSCVELENIIATHPKIQDIVVVgikdSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDL 503
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERM 3525
|
490
....*....|...
gi 1629467165 504 PRNCSGKIIRKNL 516
Cdd:PRK12316 3526 PLTPNGKLDRKAL 3538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-516 |
2.70e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPmyqqiqqedatqlrhiclidvALPADDGVSSFTQLKNQQ----PATlcyAP--PLSTDDTAEILFTSGTTSRPKG 190
Cdd:PRK12316 4656 SHLLQ---------------------RLPIPDGLASLALDRDEDwegfPAH---DPavRLHPDNLAYVIYTSGSTGRPKG 4711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 191 VVITHYNLRFAGYYSAWQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVL--VEKYSARAFWGQVQKYRATVTEC 268
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIrdDSLWDPERLYAEIHEHRVTVLVF 4790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 269 IPMMIRTLMVQPPSANDRQhRLREVMFYLNLSEQE--KDAFCERFGVRLLTSYGMTETIVGII------GDRPGdkRRWP 340
Cdd:PRK12316 4791 PPVYLQQLAEHAERDGEPP-SLRVYCFGGEAVAQAsyDLAWRALKPVYLFNGYGPTETTVTVLlwkardGDACG--AAYM 4867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 341 SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKVLEAD------GWLH-TGDTGYCDEEGF 413
Cdd:PRK12316 4868 PIGTPLGNRSGYVLDGQLNPLPVGVAGELYLG---GEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 414 FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIkAFVVLNEGETLSEEEFFRFCEQ------- 486
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEAQAELRDelkaalr 5023
|
490 500 510
....*....|....*....|....*....|.
gi 1629467165 487 -NMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12316 5024 eRLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
39-516 |
1.18e-20 |
|
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: 94.81 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTsaq 118
Cdd:cd17644 27 TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 fypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqQPATLCYapplstddtaeILFTSGTTSRPKGVVITHYNL 198
Cdd:cd17644 104 -----------------------------------------QPENLAY-----------VIYTSGSTGKPKGVMIEHQSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 -RFAGYYSAWQCALRDDDVYLTVMPAFhiDCQCTAAMAAFSAGATFVLVEK---YSARAFWGQVQKYRATVTECIPMMIR 274
Cdd:cd17644 132 vNLSHGLIKEYGITSSDRVLQFASIAF--DVAAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWH 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 275 TLM-VQPPSANDRQHRLREVM-----FYLNLSEQEKDAFCERfgVRLLTSYGMTE----TIVGIIGDRPGDKRRWPSIGR 344
Cdd:cd17644 210 LLVlELLLSTIDLPSSLRLVIvggeaVQPELVRQWQKNVGNF--IQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 345 AGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGWLH--------TGDTGYCDEEGFFYF 416
Cdd:cd17644 288 PIANTQVYILDENLQPVPVGVPGELHIGGV---GLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSY 496
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSA 444
|
490 500
....*....|....*....|
gi 1629467165 497 LEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17644 445 FVVLEELPLTPNGKIDRRAL 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
435-510 |
1.42e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 85.67 E-value: 1.42e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629467165 435 ELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
21-517 |
1.78e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 94.96 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 21 GHKTALICESSG-GVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
Cdd:PLN02654 103 GDKIAIYWEGNEpGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 100 ESAWILQNSQACLLVTSAQFYPMYQQIQQEDatqlrhicLIDVAL--PADDGVSSFTQL--KNQ---------------- 159
Cdd:PLN02654 183 SLAQRIVDCKPKVVITCNAVKRGPKTINLKD--------IVDAALdeSAKNGVSVGICLtyENQlamkredtkwqegrdv 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 160 -------QPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSA----WQCALRDDDVYLTVMPAFHI 226
Cdd:PLN02654 255 wwqdvvpNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTT-----GGYmvYTAttfkYAFDYKPTDVYWCTADCGWI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 227 DCQCTAAMAAFSAGATFVLVE---KY--SARAfWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHR-----LREVMFY 296
Cdd:PLN02654 330 TGHSYVTYGPMLNGATVLVFEgapNYpdSGRC-WDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRkslrvLGSVGEP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 297 LNLS------EQEKDAFCErfgvrLLTSYGMTETIVGIIGDRPGdkrRWP-SIGRAGFCY---EAEIRDDHNRPLPAGEI 366
Cdd:PLN02654 409 INPSawrwffNVVGDSRCP-----ISDTWWQTETGGFMITPLPG---AWPqKPGSATFPFfgvQPVIVDEKGKEIEGECS 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 367 GEICIKGV-PG--KTIFKEY------FLNPKAtakvleadGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
Cdd:PLN02654 481 GYLCVKKSwPGafRTLYGDHeryettYFKPFA--------GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRK 514
Cdd:PLN02654 553 SALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRR 632
|
...
gi 1629467165 515 NLK 517
Cdd:PLN02654 633 ILR 635
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
37-516 |
2.72e-20 |
|
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: 93.39 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AqfypmyqqiqqedatqlrhiclidvalpaddgvssftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:cd17645 103 P-------------------------------------------------------DDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NL-RFAGYYSAwqcalrdddvYLTVMPAFHidcqctaamaafsagatfvlVEKYSARAFWGQVQKYRATVT-----ECIP 270
Cdd:cd17645 128 NLvNLCEWHRP----------YFGVTPADK--------------------SLVYASFSFDASAWEIFPHLTagaalHVVP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 271 MMIR---------------TLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVgIIGDRPGD 335
Cdd:cd17645 178 SERRldldalndyfnqegiTISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPTENTV-VATSFEID 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 336 KRRWP-SIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWL------HTGDTGYC 408
Cdd:cd17645 257 KPYANiPIGKPIDNTRVYILDEALQLQPIGVAGELCIAG---EGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 409 DEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEEFFRFCEQNM 488
Cdd:cd17645 334 LPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 1629467165 489 AKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
39-516 |
3.59e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 93.53 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLlreESAWILQNSQACllvtsaq 118
Cdd:PRK05857 43 RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNL---PIAAIERFCQIT------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 fYPMYQQIQQE---DATQLRHICLIDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITH 195
Cdd:PRK05857 113 -DPAAALVAPGskmASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 196 YN-------LRFAGYysAWQCALRDDDVYlTVMPAFHI-------DCQCTAAMAAFSAGATFVLVEKYSARAfwgqvqky 261
Cdd:PRK05857 192 RTffavpdiLQKEGL--NWVTWVVGETTY-SPLPATHIgglwwilTCLMHGGLCVTGGENTTSLLEILTTNA-------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 262 raTVTEC-IPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTETIVGIIGdRPGDKRRWP 340
Cdd:PRK05857 261 --VATTClVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPTDDGSIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 341 SI--GRAGFCY-------EAEIRDDHNRPL--PAGEIGEICIKGvPGKTIfkEYFLNPKATAKVLeADGWLHTGDTGYCD 409
Cdd:PRK05857 338 KIeaGAVGRPYpgvdvylAATDGIGPTAPGagPSASFGTLWIKS-PANML--GYWNNPERTAEVL-IDGWVNTGDLLERR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 410 EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD----SIRDEAIKAFVVLNEGETLSEEE----FF 481
Cdd:PRK05857 414 EDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDeefgALVGLAVVASAELDESAARALKHtiaaRF 493
|
490 500 510
....*....|....*....|....*....|....*
gi 1629467165 482 RFCEQNMAKfkvPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK05857 494 RRESEPMAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
36-511 |
4.31e-20 |
|
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: 92.85 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 36 NRYSYLELNQEINRTANLFYTLG-IRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLV 114
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 115 TsaqfypmyqqiqqeDATQLrhiclidvalpaddgvssftqlknqqpatlcyapplstddtAEILFTSGTTSRPKGVVIT 194
Cdd:cd17648 91 T--------------NSTDL-----------------------------------------AYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 195 HY---NLR--FAGYYSAwqcALRDDDVYLtVMPAFHIDCQCTAAMAAFSAGATFVLVE---KYSARAFWGQVQKYRATVT 266
Cdd:cd17648 116 HGsvvNLRtsLSERYFG---RDNGDEAVL-FFSNYVFDFFVEQMTLALLNGQKLVVPPdemRFDPDRFYAYINREKVTYL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 267 ECIPMMIrtlmvQPPSANDRQHRLREVMFYLNLSEQEKDAFCERFGVRLLTSYGMTE-TIVGIIGDRPGDKRRWPSIGRA 345
Cdd:cd17648 192 SGTPSVL-----QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTEtTVTNHKRFFPGDQRFDKSLGRP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 346 ---GFCYeaeIRDDHNRPLPAGEIGEICIKGV---PG----KTIFKEYFL-NPKATAKVlEADG----WLHTGDTGYCDE 410
Cdd:cd17648 267 vrnTKCY---VLNDAMKRVPVGAVGELYLGGDgvaRGylnrPELTAERFLpNPFQTEQE-RARGrnarLYKTGDLVRWLP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV-----GIKDSIRDEAIKAFVVLNEGeTLSEEEFFRFCE 485
Cdd:cd17648 343 SGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedaSQAQSRIQKYLVGYYLPEPG-HVPESDLLSFLR 421
|
490 500
....*....|....*....|....*.
gi 1629467165 486 QNMAKFKVPSYLEIRKDLPRNCSGKI 511
Cdd:cd17648 422 AKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
312-517 |
2.58e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 90.44 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLLTSYGMTETIVGIIGDRPGD----KRrwpSIGRagfcyeaeirddhnrPLP-------AGEIGEICIKGvpgKTIF 380
Cdd:PRK07445 254 QLRLAPTYGMTETASQIATLKPDDflagNN---SSGQ---------------VLPhaqitipANQTGNITIQA---QSLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 381 KEYFLNPKATAKVLEadgwlhTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD 460
Cdd:PRK07445 313 LGYYPQILDSQGIFE------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWG 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1629467165 461 EAIKAFVVLNEGETlSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK07445 387 EVVTAIYVPKDPSI-SLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
168-437 |
4.93e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.06 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 168 PPLSTDDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSAWQCALRD--DDVYLTVMPAFH-----------IDCQCTAam 234
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNL-YANAEAMFVAAEFDveTDVMVSWLPLFHdmgmvgfltvpMYFGAEL-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 235 aafsagaTFVLVEKYSAR-AFWGQ-VQKYRATVTeCIP-----MMIRTLMVQPPsanDRQHRLREVMFYLNLSEQ----E 303
Cdd:PRK07768 224 -------VKVTPMDFLRDpLLWAElISKYRGTMT-AAPnfayaLLARRLRRQAK---PGAFDLSSLRFALNGAEPidpaD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 304 KDAFCE---RFGVR---LLTSYGMTETIV---------GIIGDRP----------------GDKRRWPSIGRAGFCYEAE 352
Cdd:PRK07768 293 VEDLLDagaRFGLRpeaILPAYGMAEATLavsfspcgaGLVVDEVdadllaalrravpatkGNTRRLATLGPPLPGLEVR 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 353 IRDDHNRPLPAGEIGEICIKGvpgKTIFKEYfLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVS 432
Cdd:PRK07768 373 VVDEDGQVLPPRGVGVIELRG---ESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
....*
gi 1629467165 433 CVELE 437
Cdd:PRK07768 449 PTDIE 453
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
13-517 |
4.96e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 89.55 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 13 WDDLADVYGHKTALIcesSGGvvNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
Cdd:PRK09029 9 WRHWAQVRPQAIALR---LND--EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 93 NARLLREESAWILQNSQacllvtsaqfypmyqqiqqedatqlrhiclIDVALPADDGVS-SFTQLKNQQPATLCYAPPLS 171
Cdd:PRK09029 84 NPQLPQPLLEELLPSLT------------------------------LDFALVLEGENTfSALTSLHLQLVEGAHAVAWQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 172 TDDTAEILFTSGTTSRPKGVVITHYNlRFAgyySAwQ--CALRD---DDVYLTVMPAFHIdcqctaamaafsagatfvlv 246
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQA-HLA---SA-EgvLSLMPftaQDSWLLSLPLFHV-------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 247 ekySARA-FW-----------GQVQKYRATVTEC-----IPMMIRTLMVQPPSANdrqhRLREV-----MFYLNLSEQek 304
Cdd:PRK09029 189 ---SGQGiVWrwlyagatlvvRDKQPLEQALAGCthaslVPTQLWRLLDNRSEPL----SLKAVllggaAIPVELTEQ-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 305 dafCERFGVRLLTSYGMTE---TIvgiigdrpgdkrrwpsigragFCYEAEIRDDHNRPLPAGEI----GEICIKgvpGK 377
Cdd:PRK09029 260 ---AEQQGIRCWCGYGLTEmasTV---------------------CAKRADGLAGVGSPLPGREVklvdGEIWLR---GA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 378 TIFKEYFLNPKATAkVLEADGWLHTGDTGyCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
Cdd:PRK09029 313 SLALGYWRQGQLVP-LVNDEGWFATRDRG-EWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1629467165 458 ---IRDEAIkafVVLNEGETLseEEFFRFCEQNMAKFKVP-SYLEIRKDLPRncSG-KIIRKNLK 517
Cdd:PRK09029 391 efgQRPVAV---VESDSEAAV--VNLAEWLQDKLARFQQPvAYYLLPPELKN--GGiKISRQALK 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-516 |
1.61e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.63 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 9 LRQMWDDLADVYGHKTALICESSggvvnRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEE-----TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGA 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 89 MVPINARLLREESAWILQNSQACLLVTS---AQFYPMYQQIQQedatqlrhICLidvalpaDDGVSSFTQLKNQQPATlc 165
Cdd:PRK12316 588 YVPLDPEYPAERLAYMLEDSGVQLLLSQshlGRKLPLAAGVQV--------LDL-------DRPAAWLEGYSEENPGT-- 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 166 yapPLSTDDTAEILFTSGTTSRPKGVVITHYNLrfAGYYSAWQCA--LRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATF 243
Cdd:PRK12316 651 ---ELNPENLAYVIYTSGSTGKPKGAGNRHRAL--SNRLCWMQQAygLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 244 VLVEKYSAR---AFWGQVQKYRATVTECIPMMIRTLMVQP-PSANDRQHRLREVMFYLNLSEQEKdAFCERFGVRLLTSY 319
Cdd:PRK12316 725 VVAAPGDHRdpaKLVELINREGVDTLHFVPSMLQAFLQDEdVASCTSLRRIVCSGEALPADAQEQ-VFAKLPQAGLYNLY 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 320 GMTETIVGIIG----DRPGDKrrwPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKVLE 395
Cdd:PRK12316 804 GPTEAAIDVTHwtcvEEGGDS---VPIGRPIANLACYILDANLEPVPVGVLGELYLA---GRGLARGYHGRPGLTAERFV 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 396 ADGWL------HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgikdSIRDEAIKAFVVL 469
Cdd:PRK12316 878 PSPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVL 953
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1629467165 470 NEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12316 954 ESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
37-516 |
1.97e-18 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 88.03 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK04813 27 KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIAT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSSftqlknqqpatlcyapplstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:PRK04813 107 EELPLEILGIPVITLDELKDIFATGNPYDFDHAVKG--------------------DDNYYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NL-RFAGyysaWqcALRDDDV-----------Y---LTVM---PAFhidcqctaamaafSAGATFVLVEKysarafwgqv 258
Cdd:PRK04813 167 NLvSFTN----W--MLEDFALpegpqflnqapYsfdLSVMdlyPTL-------------ASGGTLVALPK---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 259 qkyraTVTECIPMMIRTLMVQP-----------------PSANDRQH-RLREVMFY-LNLSEQEKDAFCERF-GVRLLTS 318
Cdd:PRK04813 218 -----DMTANFKQLFETLPQLPinvwvstpsfadmclldPSFNEEHLpNLTHFLFCgEELPHKTAKKLLERFpSATIYNT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 YGMTETIVGI----IGDRPGDK-RRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKV 393
Cdd:PRK04813 293 YGPTEATVAVtsieITDEMLDQyKRLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISG---PSVSKGYLNNPEKTAEA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 394 L-EADGW--LHTGDTGYCDEEGFFY-----FvdrrcnMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
Cdd:PRK04813 369 FfTFDGQpaYHTGDAGYLEDGLLFYqgridF------QIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1629467165 466 FVVLNEGETLSEEEFFRFCEQNMAKFkVPSYL-----EIRKDLPRNCSGKIIRKNL 516
Cdd:PRK04813 443 YVVPKEEDFEREFELTKAIKKELKER-LMEYMiprkfIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-516 |
5.97e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.92 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGHKTALICEssGGVVNrysYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
Cdd:PRK05691 1130 QAWLPELLNEQARQTPERIALVWD--GGSLD---YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKA 1204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 86 GAIMVPINARLLREESAWILQNSQACLLVTSAQfypmyqqiqqedatqlrhicLIDvALPADDGVSSFT--QLK-NQQPA 162
Cdd:PRK05691 1205 GGAYVPLDPDYPAERLAYMLADSGVELLLTQSH--------------------LLE-RLPQAEGVSAIAldSLHlDSWPS 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 163 TlcyaPP---LSTDDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAF 237
Cdd:PRK05691 1264 Q----APglhLHGDNLAYVIYTSGSTGQPKGVGNTHAALaeRLQWMQATY--ALDDSDVLMQKAP-ISFDVSVWECFWPL 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 238 SAGATFVLV---EKYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANdrQHRLREVmFYLN--LSEQEKDAFCERF- 311
Cdd:PRK05691 1337 ITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAA--CTSLRRL-FSGGeaLPAELRNRVLQRLp 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 GVRLLTSYGMTETIVGII--GDRPGDKRRWPsIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNPKA 389
Cdd:PRK05691 1414 QVQLHNRYGPTETAINVThwQCQAEDGERSP-IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA---GLARGYLGRPAL 1489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 390 TAK--VLEADG-----WLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgIKDSIRDEA 462
Cdd:PRK05691 1490 TAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQ 1568
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1629467165 463 IKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLeIRKD-LPRNCSGKIIRKNL 516
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQL-IRLDqMPLGPSGKLDRRAL 1622
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
39-453 |
2.08e-17 |
|
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: 85.10 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTsaq 118
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 fypmyqqiqqEDATQLRHICLIDVALP--------------ADDGVSSF------------TQL----KNQQPATLCYap 168
Cdd:cd05933 87 ----------ENQKQLQKILQIQDKLPhlkaiiqykeplkeKEPNLYSWdefmelgrsipdEQLdaiiSSQKPNQCCT-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 169 plstddtaeILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDV-------YLtvmPAFHIDCQctaamaafsaga 241
Cdd:cd05933 155 ---------LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYL---PLSHIAAQ------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 242 tfvLVEKYSARAFWGQV----------------QKYRATVTECIP-----MMIRTLMVQPPSANDRQ---HRLREVMFYL 297
Cdd:cd05933 211 ---ILDIWLPIKVGGQVyfaqpdalkgtlvktlREVRPTAFMGVPrvwekIQEKMKAVGAKSGTLKRkiaSWAKGVGLET 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 298 NLSEQEKD------------------------AFCERF------------------GVRLLTSYGMTETIVGIIGDRPgD 335
Cdd:cd05933 288 NLKLMGGEspsplfyrlakklvfkkvrkalglDRCQKFftgaapisretlefflslNIPIMELYGMSETSGPHTISNP-Q 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 336 KRRWPSIGRA--GfCYEAEIRDDHNRplpageIGEICIKGvpgKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGF 413
Cdd:cd05933 367 AYRLLSCGKAlpG-CKTKIHNPDADG------IGEICFWG---RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGF 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1629467165 414 FYFVDRRCNMIKR-GGENVSCVELENIIATH-PKIQDIVVVG 453
Cdd:cd05933 437 LYITGRIKELIITaGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
37-516 |
2.52e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.98 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 aqfypmyqqiqqedatqlRHIClidVALPADDGVSSF------TQLKNQQPATLCYAPplSTDDTAEILFTSGTTSRPKG 190
Cdd:PRK12467 1679 ------------------SHLQ---ARLPLPDGLRSLvldqedDWLEGYSDSNPAVNL--APQNLAYVIYTSGSTGRPKG 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 191 VVITHYNL--RFAGYYSAWQcaLRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLVEKYSARA---FWGQVQKYRATV 265
Cdd:PRK12467 1736 AGNRHGALvnRLCATQEAYQ--LSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAPPGAHRDpeqLIQLIERQQVTT 1812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 266 TECIPMMIRTLMvQPPSANDRQHRLREVMFYLNLSEQE-KDAFCERFG-VRLLTSYGMTETIVGII---GDRPGDKRRWP 340
Cdd:PRK12467 1813 LHFVPSMLQQLL-QMDEQVEHPLSLRRVVCGGEALEVEaLRPWLERLPdTGLFNLYGPTETAVDVThwtCRRKDLEGRDS 1891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 341 S-IG-----RAGFCYEAEIrddhnRPLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEAD------GWLH-TGDTGY 407
Cdd:PRK12467 1892 VpIGqpianLSTYILDASL-----NPVPIGVAGELYLGGV---GLARGYLNRPALTAERFVADpfgtvgSRLYrTGDLAR 1963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 408 CDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgIKDSIRDEAIKAFVVLNEGETLSEEEFFRFC--- 484
Cdd:PRK12467 1964 YRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI-AQDGANGKQLVAYVVPTDPGLVDDDEAQVALrai 2042
|
490 500 510
....*....|....*....|....*....|....*..
gi 1629467165 485 -----EQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK12467 2043 lknhlKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
57-444 |
4.14e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 84.64 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 57 LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRH 136
Cdd:PTZ00216 141 LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGMPNTT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 137 ICLIDvALPA--DDG---VSSFTQ---LKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSawq 208
Cdd:PTZ00216 221 IIYLD-SLPAsvDTEgcrLVAWTDvvaKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSL-TAGILA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 209 CALR---------DDDVYLTVMPAFHIdcqctaamaafsagATFVLVEKYSARAFW-----------------GQVQKYR 262
Cdd:PTZ00216 296 LEDRlndligppeEDETYCSYLPLAHI--------------MEFGVTNIFLARGALigfgsprtltdtfarphGDLTEFR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 263 ATVTECIPMMIRTL------MVQPPSANDR-------QHRLREVMF-----YLNlseqEK--DAFCERFG--VRLLTS-- 318
Cdd:PTZ00216 362 PVFLIGVPRIFDTIkkaveaKLPPVGSLKRrvfdhayQSRLRALKEgkdtpYWN----EKvfSAPRAVLGgrVRAMLSgg 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 319 ---------------------YGMTETI-VGIIgDRPGDkRRWPSIGRAGFCYEAEIRD-DH----NRPLPAgeiGEICI 371
Cdd:PTZ00216 438 gplsaatqefvnvvfgmviqgWGLTETVcCGGI-QRTGD-LEPNAVGQLLKGVEMKLLDtEEykhtDTPEPR---GEILL 512
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1629467165 372 KgvpGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHP 444
Cdd:PTZ00216 513 R---GPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEALYGQNE 583
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
58-517 |
7.08e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 83.93 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLrhi 137
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAEL--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 138 clidvalpaddgvssFTQLKNQQPATLcyaPPLSTDDTAEILFTSGTTSRPKGVVITHYNLrFAgYYSAWQC-ALR--DD 214
Cdd:PRK06060 128 ---------------MSEAARVAPGGY---EPMGGDALAYATYTSGTTGPPKAAIHRHADP-LT-FVDAMCRkALRltPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 215 DVYL-------------TVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATVTECIPMMIRTLmvqpp 281
Cdd:PRK06060 188 DTGLcsarmyfayglgnSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSL----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 282 sandrqhrlREVmfyLNLSEQEKDAFCERF-----GVRLLTSYGMTE---TIVGIIGD--RPGdkrrwpSIGRAGFCYEA 351
Cdd:PRK06060 263 ---------RCV---VSAGEALELGLAERLmeffgGIPILDGIGSTEvgqTFVSNRVDewRLG------TLGRVLPPYEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 352 EI-RDDHNRPLPAGEiGEICIKGvpgKTIFKEYFLNPKAtakVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGEN 430
Cdd:PRK06060 325 RVvAPDGTTAGPGVE-GDLWVRG---PAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 431 VSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFRFCEQNMAKFKVPSYLEIRKDLPRNC 507
Cdd:PRK06060 398 VDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmRDLHRGLLNRLSAFKVPHRFAVVDRLPRTP 477
|
490
....*....|
gi 1629467165 508 SGKIIRKNLK 517
Cdd:PRK06060 478 NGKLVRGALR 487
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
400-517 |
2.75e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 80.85 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 400 LHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEE 479
Cdd:PRK08308 293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQ 370
|
90 100 110
....*....|....*....|....*....|....*...
gi 1629467165 480 FFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK 517
Cdd:PRK08308 371 LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
39-453 |
8.08e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 80.27 E-value: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQEDATQLRHICLI-DVA----LPADD-GVSSFTQLKNQQPATL-CYAPPLSTDDTAEILFTSGTTSRPKGV 191
Cdd:PLN02861 159 KISSILSCLPKCSSNLKTIVSFgDVSseqkEEAEElGVSCFSWEEFSLMGSLdCELPPKQKTDICTIMYTSGTTGEPKGV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 192 VITHYNLrFAGYYSAWQC------ALRDDDVYLTVMPAFHIDCQCTAAMaafsagatfvLVEKYSARAFWGQVQKYratV 265
Cdd:PLN02861 239 ILTNRAI-IAEVLSTDHLlkvtdrVATEEDSYFSYLPLAHVYDQVIETY----------CISKGASIGFWQGDIRY---L 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 266 TECIPMMIRTLMVQPPSANDRQHR-----------LREVMFYL-----------NLSEQEKDAFCER---------FG-- 312
Cdd:PLN02861 305 MEDVQALKPTIFCGVPRVYDRIYTgimqkissggmLRKKLFDFaynyklgnlrkGLKQEEASPRLDRlvfdkikegLGgr 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 313 VRLLTS------------------------YGMTETIVGI---IGDRpgdkrrWPSIGRAGFCY---EA------EIRDD 356
Cdd:PLN02861 385 VRLLLSgaaplprhveeflrvtscsvlsqgYGLTESCGGCftsIANV------FSMVGTVGVPMttiEArlesvpEMGYD 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 357 HNRPLPAGEIgeiCIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVE 435
Cdd:PLN02861 459 ALSDVPRGEI---CLRG---NTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVEN 531
|
490
....*....|....*...
gi 1629467165 436 LENIIATHPKIQDIVVVG 453
Cdd:PLN02861 532 LENTYSRCPLIASIWVYG 549
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
6-453 |
1.59e-15 |
|
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: 79.42 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 6 GQHLRQMWDDLADVYGHKTALICESSGGVVNRY---------------SYLELNQEINRTANLFYTLG-IRKGDKVALHL 69
Cdd:cd17632 21 GLRLAQIIATVMTGYADRPALGQRATELVTDPAtgrttlrllprfetiTYAELWERVGAVAAAHDPEQpVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 70 DNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATqLRHICLIDVALPADD- 148
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGT-PPRLVVFDHRPEVDAh 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 149 ----------------GVSSFTQLKNQQ----PATLCYAPPlSTDDTAEILFTSGTTSRPKGVVITHYNLRFAG-YYSAW 207
Cdd:cd17632 180 raalesarerlaavgiPVTTLTLIAVRGrdlpPAPLFRPEP-DDDPLALLIYTSGSTGTPKGAMYTERLVATFWlKVSSI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 208 QCALRDDDVYLTVMPAFHI----------------------DCQCTAAMAAFSAGATFVLVEKYSARAFwgqvQKYRATV 265
Cdd:cd17632 259 QDIRPPASITLNFMPMSHIagrislygtlarggtayfaaasDMSTLFDDLALVRPTELFLVPRVCDMLF----QRYQAEL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 266 TEcipmmiRTLMVQPPSANDRQHR--LREVMF---YLN-------LSEQEKdAFCER-FGVRLLTSYGMTETIVGIIGDR 332
Cdd:cd17632 335 DR------RSVAGADAETLAERVKaeLRERVLggrLLAavcgsapLSAEMK-AFMESlLDLDLHDGYGSTEAGAVILDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 333 pgdKRRWPSIGragfcYE----AEI---RDDhnRPLPAGEIGeicikgVPGKTIFKEYFLNPKATAKVLEADGWLHTGD- 404
Cdd:cd17632 408 ---IVRPPVLD-----YKlvdvPELgyfRTD--RPHPRGELL------VKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDv 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1629467165 405 ---TGYcDEegfFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
Cdd:cd17632 472 maeLGP-DR---LVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLVRQIFVYG 520
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
29-453 |
2.60e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 78.91 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 29 ESSGGVVNRY---SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWIL 105
Cdd:PLN02614 68 EIVDGKPGKYvwqTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 106 QNSQACLLVTSAQFYPMYQQIQQEDATQLRHIClidvalpADDGVSSFTQLKNQQPATLCYA---------------PPL 170
Cdd:PLN02614 148 SHSEVSIVFVEEKKISELFKTCPNSTEYMKTVV-------SFGGVSREQKEEAETFGLVIYAwdeflklgegkqydlPIK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 171 STDDTAEILFTSGTTSRPKGVVITHYN--------LRFAGYYSAwqcALRDDDVYLTVMPAFHI------DCqctaamaa 236
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESivtliagvIRLLKSANA---ALTVKDVYLSYLPLAHIfdrvieEC-------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 237 fsagatfvLVEKYSARAFW-GQVQKYRATVTECIPmmirTLMVQPPSANDR-----QHRLREVMFYLNL----------- 299
Cdd:PLN02614 290 --------FIQHGAAIGFWrGDVKLLIEDLGELKP----TIFCAVPRVLDRvysglQKKLSDGGFLKKFvfdsafsykfg 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 300 ------SEQEKDAFCERF-----------GVRLLTS------------------------YGMTETIVGIIGDRPGDKRR 338
Cdd:PLN02614 358 nmkkgqSHVEASPLCDKLvfnkvkqglggNVRIILSgaaplashvesflrvvacchvlqgYGLTESCAGTFVSLPDELDM 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 339 WPSIGRAgfCYEAEIR-----DDHNRPLPAGEIGEICIKGvpgKTIFKEYFLNPKATAKVLeADGWLHTGDTGYCDEEGF 413
Cdd:PLN02614 438 LGTVGPP--VPNVDIRlesvpEMEYDALASTPRGEICIRG---KTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGS 511
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1629467165 414 FYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
Cdd:PLN02614 512 MKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
158-513 |
9.13e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 77.09 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 158 NQQPATLCYAP-----PLStddtaeILFTSGTTSRPKGVVITH-YNLRFAGYYsaWQCALRDDD--VYLTVMP----AFH 225
Cdd:PTZ00237 240 NNQSPFYEYVPvesshPLY------ILYTSGTTGNSKAVVRSNgPHLVGLKYY--WRSIIEKDIptVVFSHSSigwvSFH 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 226 idcqcTAAMAAFSAGATFVLVE------KYSARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHR-----LREVM 294
Cdd:PTZ00237 312 -----GFLYGSLSLGNTFVMFEggiiknKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlsnLKEIW 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 295 FYLNLSEQEKDAFCE-RFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICIKg 373
Cdd:PTZ00237 387 CGGEVIEESIPEYIEnKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 374 VPGKTIFKEYFLNPKATAKVL--EADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
Cdd:PTZ00237 466 LPMPPSFATTFYKNDEKFKQLfsKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 452 VGIKDSIRDEAIKAFVVLNEGETLS-------EEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIR 513
Cdd:PTZ00237 546 IGIYDPDCYNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
113-511 |
2.94e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 75.77 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 113 LVTSAQF------YPMYQQIQQedatQLRHICLIDVAlpadDGVSSFTQLKN--QQPATLCYAPPLSTDDTAEILFTSGT 184
Cdd:PRK06814 733 VLTSRAFiekarlGPLIEALEF----GIRIIYLEDVR----AQIGLADKIKGllAGRFPLVYFCNRDPDDPAVILFTSGS 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 185 TSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHidcqctaamaafsagaTFVL-----------VEKYsara 253
Cdd:PRK06814 805 EGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFH----------------SFGLtgglvlpllsgVKVF---- 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 254 FWGQVQKYRaTVTECI-----PMMIRT---LMVQPPSANDRQHR-LREVmfyLNLSEQEKDA----FCERFGVRLLTSYG 320
Cdd:PRK06814 865 LYPSPLHYR-IIPELIydtnaTILFGTdtfLNGYARYAHPYDFRsLRYV---FAGAEKVKEEtrqtWMEKFGIRILEGYG 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 321 MTETIVGI-----IGDRPGdkrrwpSIGRA--GFCYEAEirddhnrPLPA-GEIGEICIKGvpgKTIFKEYFL--NPKat 390
Cdd:PRK06814 941 VTETAPVIalntpMHNKAG------TVGRLlpGIEYRLE-------PVPGiDEGGRLFVRG---PNVMLGYLRaeNPG-- 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 391 akVLE--ADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIkafVV 468
Cdd:PRK06814 1003 --VLEppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI---IL 1077
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1629467165 469 LNEGETLSEEEFFRFCEQNMA-KFKVPSYLEIRKDLPRNCSGKI 511
Cdd:PRK06814 1078 LTTASDATRAAFLAHAKAAGAsELMVPAEIITIDEIPLLGTGKI 1121
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
39-516 |
9.21e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 74.31 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQEDATQlrhiclIDVALPADDGvssfTQLKNQQPatlcyapplstDDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:PRK10252 565 QLPRFADVPDLTSLC------YNAPLAPQGA----APLQLSQP-----------HHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 199 --RFagyysAW---QCALRDDDVYLT-----------------------VM--PAFHIDCQctaamaafsagatfvlvek 248
Cdd:PRK10252 624 vnRL-----LWmqnHYPLTADDVVLQktpcsfdvsvweffwpfiagaklVMaePEAHRDPL------------------- 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YSARAFwgqvQKYRATVTECIPMMIRTLMVQPPS--ANDRQHRLREVMfylnLSEQEKDA-FCERF----GVRLLTSYGM 321
Cdd:PRK10252 680 AMQQFF----AEYGVTTTHFVPSMLAAFVASLTPegARQSCASLRQVF----CSGEALPAdLCREWqqltGAPLHNLYGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 322 TETIVgiigdrpgDKRRWPSIGRAGFCYEA--------------EIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYFLNP 387
Cdd:PRK10252 752 TEAAV--------DVSWYPAFGEELAAVRGssvpigypvwntglRILDARMRPVPPGVAGDLYLTGI---QLAQGYLGRP 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 388 KATAKVLEADGWL------HTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
Cdd:PRK10252 821 DLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAA 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 462 A------IKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK10252 901 TggdarqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
173-454 |
5.45e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.92 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSAWQC-ALRDDDVYLTVMPAFH---IDCqCTAAMAAFSAGATFVLVEK 248
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANL-LANQRACLKFfSPKEDDVMMSFLPPFHaygFNS-CTLFPLLSGVPVVFAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 249 YsARAFWGQVQKYRATVTECIPMMIRTLMVQPPSANDRQHRLREVM-----FYLNLSEQEKDAFCErfgVRLLTSYGMTE 323
Cdd:PRK06334 261 Y-PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVViggdaFKDSLYQEALKTFPH---IQLRQGYGTTE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 324 T--IVGIIGDRPGDKRRWPSIGRAGFcyEAEIRDDHNR-PLPAGEIGEICIKGVpgkTIFKEYFLNPKATAKV-LEADGW 399
Cdd:PRK06334 337 CspVITINTVNSPKHESCVGMPIRGM--DVLIVSEETKvPVSSGETGLVLTRGT---SLFSGYLGEDFGQGFVeLGGETW 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 400 LHTGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATH---PKIQD---IVVVGI 454
Cdd:PRK06334 412 YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHagpLVVCGL 472
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
25-512 |
4.36e-11 |
|
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: 65.37 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI---------------- 88
Cdd:cd05943 86 AAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwsscspdfgvpgvldr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 89 MVPINARLL---------------REESAWI---LQNSQACLLVtsaqfyPMYQQIQQEDATQL-RHICLIDVALPADDG 149
Cdd:cd05943 166 FGQIEPKVLfavdaytyngkrhdvREKVAELvkgLPSLLAVVVV------PYTVAAGQPDLSKIaKALTLEDFLATGAAG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 150 VSSFTQLKNQQPatLCyapplstddtaeILFTSGTTSRPK-------GVVITHY-NLRFagyysawQCALRDDDV---YL 218
Cdd:cd05943 240 ELEFEPLPFDHP--LY------------ILYSSGTTGLPKcivhgagGTLLQHLkEHIL-------HCDLRPGDRlfyYT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 219 TV---MPAFHIdcqctaamAAFSAGATFVLVE----KYSARAFWGQVQKYRATVTECIPMMIRTLM---VQPPSANDRQh 288
Cdd:cd05943 299 TCgwmMWNWLV--------SGLAVGATIVLYDgspfYPDTNALWDLADEEGITVFGTSAKYLDALEkagLKPAETHDLS- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 289 RLREVmfYLNLSEQEKDAF-----CERFGVRLLTSYGMTETIVGIIGDRPgDKRRWPS-IGRAGFCYEAEIRDDHNRPLP 362
Cdd:cd05943 370 SLRTI--LSTGSPLKPESFdyvydHIKPDVLLASISGGTDIISCFVGGNP-LLPVYRGeIQCRGLGMAVEAFDEEGKPVW 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 363 aGEIGE-ICIKGVPGKTIfkeYFLNPKATAKVLEA-----DG-WLHtGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVE 435
Cdd:cd05943 447 -GEKGElVCTKPFPSMPV---GFWNDPDGSRYRAAyfakyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
Cdd:cd05943 522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
39-473 |
7.56e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIrKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI-----NARLLREESAWILQNSQACLL 113
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesARRHHQERLLSIIADAEPRLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 114 VTSAQFYPMYQQIQQEDATQLRHICLIDVALPAddgvssftqlknqqPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVI 193
Cdd:PRK05691 121 LTVADLRDSLLQMEELAAANAPELLCVDTLDPA--------------LAEAWQEPALQPDDIAFLQYTSGSTALPKGVQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 194 THYNL-------RfagyySAWQCALRDDDVYLTVMPAFH---------------IDCqctaamaafsagatfVLVekySA 251
Cdd:PRK05691 187 SHGNLvaneqliR-----HGFGIDLNPDDVIVSWLPLYHdmgliggllqpifsgVPC---------------VLM---SP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 252 RAF------WGQ-VQKYRATVTecipmmirtlmvqppSANDRQHRL------REVMFYLNLS-------------EQEKD 305
Cdd:PRK05691 244 AYFlerplrWLEaISEYGGTIS---------------GGPDFAYRLcservsESALERLDLSrwrvaysgsepirQDSLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 306 AFCERFGV------RLLTSYGMTETIVGIIGDR---------------------PGDKRRWPSIGRAGFCYEAEIRD-DH 357
Cdd:PRK05691 309 RFAEKFAAcgfdpdSFFASYGLAEATLFVSGGRrgqgipaleldaealarnraePGTGSVLMSCGRSQPGHAVLIVDpQS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 358 NRPLPAGEIGEICikgVPGKTIFKEYFLNPKATAKV-LEADG--WLHTGDTGYCdEEGFFYFVDRRCNMIKRGGENVSCV 434
Cdd:PRK05691 389 LEVLGDNRVGEIW---ASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQ 464
|
490 500 510
....*....|....*....|....*....|....*....
gi 1629467165 435 ELENIIATHpkiqdivvvgiKDSIRDEAIKAFVVLNEGE 473
Cdd:PRK05691 465 DIEKTVERE-----------VEVVRKGRVAAFAVNHQGE 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-516 |
1.37e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 37 RYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTS 116
Cdd:PRK05691 3745 QWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 117 AQFYPMYQQIQQEDATQLRHICLIDVALPADDGVSsftqlknQQPATlcYAPPlstDDTAEILFTSGTTSRPKGVVITHY 196
Cdd:PRK05691 3825 AACREQARALLDELGCANRPRLLVWEEVQAGEVAS-------HNPGI--YSGP---DNLAYVIYTSGSTGLPKGVMVEQR 3892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 197 NLRFAGYYSAWQCALRDDDVYL-TVMPAFHIDCQctaamaafsagaTFVLVEKYSAR-------------AFWGQVQKYR 262
Cdd:PRK05691 3893 GMLNNQLSKVPYLALSEADVIAqTASQSFDISVW------------QFLAAPLFGARveivpnaiahdpqGLLAHVQAQG 3960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 263 ATVTECIPMMIRTLMvqppsANDRQ--HRLR------EVMFYLnLSEQekdaFCERF-GVRLLTSYGMTET---IVGIIG 330
Cdd:PRK05691 3961 ITVLESVPSLIQGML-----AEDRQalDGLRwmlptgEAMPPE-LARQ----WLQRYpQIGLVNAYGPAECsddVAFFRV 4030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 331 DRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYFLNPKATAKVL-------EADGWLHTG 403
Cdd:PRK05691 4031 DLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELC---VAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTG 4107
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 404 DTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDiVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRF 483
Cdd:PRK05691 4108 DLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERI 4186
|
490 500 510
....*....|....*....|....*....|....*.
gi 1629467165 484 CEQ---NMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK05691 4187 KQRlraELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
173-516 |
2.28e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 62.37 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGyySAWQCALRDDDVYLTVMPAFHI-DCQctaamaafsagatfVLV----- 246
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASA--DATHDRLGGPGQWLLALPAHHIaGLQ--------------VLVrsvia 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 247 ----------EKYSARAFWGQVQKYRA--TVTECIPMMIRTLMVQPPSANdrqhRLREVMFYL--------NLSEQEKDA 306
Cdd:PRK07824 99 gsepveldvsAGFDPTALPRAVAELGGgrRYTSLVPMQLAKALDDPAATA----ALAELDAVLvgggpapaPVLDAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 307 fcerfGVRLLTSYGMTETIVGIIGD-RPGDKrrwpsigragfcyeAEIRDDHNRPlpagEIGeicikgvpGKTIFKEYfL 385
Cdd:PRK07824 175 -----GINVVRTYGMSETSGGCVYDgVPLDG--------------VRVRVEDGRI----ALG--------GPTLAKGY-R 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 386 NPKATAKVLEaDGWLHTGDTGYCDEeGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
Cdd:PRK07824 223 NPVDPDPFAE-PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1629467165 466 FVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK07824 301 AVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
38-451 |
9.27e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.29 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 38 YSYLELNQEINRTANL---FYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLV 114
Cdd:PLN02387 104 YEWITYGQVFERVCNFasgLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 115 TSAQFYPMYQQIQQEDATQLRHICLIDVALPADDG--------VSSFTQL-----KNQQPATLcyapPLSTDdTAEILFT 181
Cdd:PLN02387 184 CDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSlsgssnwtVSSFSEVeklgkENPVDPDL----PSPND-IAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 182 SGTTSRPKGVVITHYNL--RFAGYYSAWQcALRDDDVYLTVMPAFHIdcqctaamaafsagatFVLVEKySARAFWGQVQ 259
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIvaTVAGVMTVVP-KLGKNDVYLAYLPLAHI----------------LELAAE-SVMAAVGAAI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 260 KYRA--TVTEC-----------IPMMIRTLMVQPPSANDR---------------QHRLREVMFYLNLSEQEKDAF---- 307
Cdd:PLN02387 321 GYGSplTLTDTsnkikkgtkgdASALKPTLMTAVPAILDRvrdgvrkkvdakgglAKKLFDIAYKRRLAAIEGSWFgawg 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 308 -----------------------------------CERF-----GVRLLTSYGMTETIVGIIGDRPGDkrrwPSIGRAG- 346
Cdd:PLN02387 401 lekllwdalvfkkiravlggrirfmlsggaplsgdTQRFiniclGAPIGQGYGLTETCAGATFSEWDD----TSVGRVGp 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 347 ---FCYEAEIRDDH------NRPLPAGEIgeicikGVPGKTIFKEYFLNPKATAKVLEADG----WLHTGDTGYCDEEGF 413
Cdd:PLN02387 477 plpCCYVKLVSWEEggylisDKPMPRGEI------VIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGC 550
|
490 500 510
....*....|....*....|....*....|....*....
gi 1629467165 414 FYFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVV 451
Cdd:PLN02387 551 LEIIDRKKDIVKlQHGEYVSLGKVEAALSVSPYVDNIMV 589
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
39-516 |
6.52e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 39 SYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQ 118
Cdd:PRK05691 2215 SYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRA 2294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 119 FYPMYQQIQQEDAtqlrHICLidvalpADDGVSsftqLKNQQPATLcyaPPLS-TDDTAEILFTSGTTSRPKGVVITHYN 197
Cdd:PRK05691 2295 LFEALGELPAGVA----RWCL------EDDAAA----LAAYSDAPL---PFLSlPQHQAYLIYTSGSTGKPKGVVVSHGE 2357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 198 LrfagyysAWQCA-------LRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATFVLvekySARAFWG-------------- 256
Cdd:PRK05691 2358 I-------AMHCQavierfgMRADDCELHFY-SINFDAASERLLVPLLCGARVVL----RAQGQWGaeeicqlireqqvs 2425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 257 ----------QVQKYRATVTECIPmmIRtLMVQPPSANDRQH--RLREvmfylnlseqekdAFCERFgvrLLTSYGMTET 324
Cdd:PRK05691 2426 ilgftpsygsQLAQWLAGQGEQLP--VR-MCITGGEALTGEHlqRIRQ-------------AFAPQL---FFNAYGPTET 2486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 325 IVGIIGDRPGDKRRWPS----IGRAGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYFLNPKATAKVLEADGWL 400
Cdd:PRK05691 2487 VVMPLACLAPEQLEEGAasvpIGRVVGARVAYILDADLALVPQGATGELYVG---GAGLAQGYHDRPGLTAERFVADPFA 2563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 401 H-------TGDTGYCDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIRDEAIKAFVVLNEGE 473
Cdd:PRK05691 2564 AdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAG 2642
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1629467165 474 TLSEEE-FFR-----FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:PRK05691 2643 QDDEAQaALRealkaHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
130-473 |
5.31e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 55.66 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 130 DATQLRHICLIDV-ALPADDGVSSFTQLKNQQPATLCYA--PPLSTDDTAEILFTSGTTSRPKGVVITHYNLrfagyySA 206
Cdd:PRK08180 163 AAVVPADVEVVAVrGAVPGRAATPFAALLATPPTAAVDAahAAVGPDTIAKFLFTSGSTGLPKAVINTHRML------CA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 207 WQCALRDddvyltVMPAFHIDCQctaamaafsagatfVLVEkysarafW-------GQVQkyratvteCIPMMIR---TL 276
Cdd:PRK08180 237 NQQMLAQ------TFPFLAEEPP--------------VLVD-------WlpwnhtfGGNH--------NLGIVLYnggTL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 277 MV---QP-PSANDRQHR-LREVM--FYLN--------LSEQEKD-AFCERF----------------------------- 311
Cdd:PRK08180 282 YIddgKPtPGGFDETLRnLREISptVYFNvpkgwemlVPALERDaALRRRFfsrlkllfyagaalsqdvwdrldrvaeat 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 312 -G--VRLLTSYGMTET-----IVGIIGDRPGDkrrwpsIGragfcyeaeirddhnRPLPAGEIG--------EICIKGVp 375
Cdd:PRK08180 362 cGerIRMMTGLGMTETapsatFTTGPLSRAGN------IG---------------LPAPGCEVKlvpvggklEVRVKGP- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 376 gkTIFKEYFLNPKATAKVLEADGWLHTGDTG-YCDEE----GFFY--------------FVdrrcnmikrggeNVSCVEL 436
Cdd:PRK08180 420 --NVTPGYWRAPELTAEAFDEEGYYRSGDAVrFVDPAdperGLMFdgriaedfklssgtWV------------SVGPLRA 485
|
410 420 430
....*....|....*....|....*....|....*..
gi 1629467165 437 ENIIATHPKIQDIVVVGIKdsiRDEaIKAFVVLNEGE 473
Cdd:PRK08180 486 RAVSAGAPLVQDVVITGHD---RDE-IGLLVFPNLDA 518
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
167-414 |
9.94e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.01 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 167 APPLSTDDTAEILFTSGTTSRPKGVVITHYNLR------FAGYYSAWQCALRDDDVYLTVMPAFH-----------IDCQ 229
Cdd:PRK05850 154 ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIanfeqlMSDYFGDTGGVPPPDTTVVSWLPFYHdmglvlgvcapILGG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 230 CTAamaafsagatfVLVekySARAF------WGQ-VQKYRATVTeCIPMMIRTLMVQPPSANDRQHR-LREVMFYLNLSE 301
Cdd:PRK05850 234 CPA-----------VLT---SPVAFlqrparWMQlLASNPHAFS-AAPNFAFELAVRKTSDDDMAGLdLGGVLGIISGSE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 302 QEKDA----FCERFG--------VRllTSYGMTETIVGIIGDRPGDKrrwP----------SIGRAGFCyEAE------- 352
Cdd:PRK05850 299 RVHPAtlkrFADRFApfnlretaIR--PSYGLAEATVYVATREPGQP---PesvrfdyeklSAGHAKRC-ETGggtplvs 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 353 ----------IRD-DHNRPLPAGEIGEICikgVPGKTIFKEYFLNPKATAKVLEA----------DG-WLHTGDTGYCDE 410
Cdd:PRK05850 373 ygsprsptvrIVDpDTCIECPAGTVGEIW---VHGDNVAAGYWQKPEETERTFGAtlvdpspgtpEGpWLRTGDLGFISE 449
|
....
gi 1629467165 411 EGFF 414
Cdd:PRK05850 450 GELF 453
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
60-195 |
1.26e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.81 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 60 RKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL---REESAWILQNSQ-ACLLVTSAQFYPMYQQIQQEDATQLR 135
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELpghAERLDTALRDAEpTVVLTTTAAAEAVEGFLRNLPRLRRP 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 136 HICLIDvALPADDGVSsFTqlknqqpatlcyAPPLSTDDTAEILFTSGTTSRPKGVVITH 195
Cdd:PRK12476 170 RVIAID-AIPDSAGES-FV------------PVELDTDDVSHLQYTSGSTRPPVGVEITH 215
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
25-195 |
6.13e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.56 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAImvpinarllreesaWi 104
Cdd:PRK03584 102 AIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI--------------W- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 105 lqnsQAC-------------------LLVTSA------QFYPMYQQIQQ--EDATQLRHICLID-----VALPADDGVSS 152
Cdd:PRK03584 167 ----SSCspdfgvqgvldrfgqiepkVLIAVDgyryggKAFDRRAKVAElrAALPSLEHVVVVPylgpaAAAAALPGALL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1629467165 153 FTQ-LKNQQPATLCYApPLSTDDTAEILFTSGTTSRPKGVVITH 195
Cdd:PRK03584 243 WEDfLAPAEAAELEFE-PVPFDHPLWILYSSGTTGLPKCIVHGH 285
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
155-516 |
9.60e-05 |
|
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: 44.77 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 155 QLKNQQPATLCYapplstddtaeILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPaFHIDCQCTAAM 234
Cdd:cd17654 111 HFNIRTDECLAY-----------VIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSP-LTFDPSVVEIF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 235 AAFSAGATFVLVEkYSARAFWGQVQK-----YRATVTECIPMMIRTLMVQppSANDRQHRLREVMFYLNL-------SEQ 302
Cdd:cd17654 179 LSLSSGATLLIVP-TSVKVLPSKLADilfkrHRITVLQATPTLFRRFGSQ--SIKSTVLSATSSLRVLALggepfpsLVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 303 EKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYEAEIRDDHNRPLPageiGEICIKGVPGKTIFKE 382
Cdd:cd17654 256 LSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGT----GQVFLGGLNRVCILDD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 383 YFLNPKATakvleadgWLHTGDtgYCD-EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKdsirDE 461
Cdd:cd17654 332 EVTVPKGT--------MRATGD--FVTvKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSD----QQ 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1629467165 462 AIKAFVVLNEGETLSEEEFFRFceqNMAKFKVPSYLEIRKDLPRNCSGKIIRKNL 516
Cdd:cd17654 398 RLIAFIVGESSSSRIHKELQLT---LLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
170-459 |
1.52e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 44.27 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 170 LSTDDTAEILFTSGTTSRPKGVVITHynlRFAGYYSAWQCALRDDD------VYLTVMPAFHIDCQCTAAMAAFSAGATF 243
Cdd:PRK12582 217 ITPDTVAKYLFTSGSTGMPKAVINTQ---RMMCANIAMQEQLRPREpdppppVSLDWMPWNHTMGGNANFNGLLWGGGTL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 244 VLVEkysARAFWGQVQKYRATVTECIPmmirTLMVQPPSAndrqhrlrevmFYLNLSEQEKD-AFCERF----------G 312
Cdd:PRK12582 294 YIDD---GKPLPGMFEETIRNLREISP----TVYGNVPAG-----------YAMLAEAMEKDdALRRSFfknlrlmaygG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 313 VRL----------------------LTSYGMTETiVGIIGDRPGDKRRwpsIGRAGFcyeaeirddhnrPL--------P 362
Cdd:PRK12582 356 ATLsddlyermqalavrttghripfYTGYGATET-APTTTGTHWDTER---VGLIGL------------PLpgvelklaP 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 363 AGEIGEICIKGVpgkTIFKEYFLNPKATAKVLEADGWLHTGDTGycdeegffYFVD-----RRCNMIKRGGEN------- 430
Cdd:PRK12582 420 VGDKYEVRVKGP---NVTPGYHKDPELTAAAFDEEGFYRLGDAA--------RFVDpddpeKGLIFDGRVAEDfklstgt 488
|
330 340 350
....*....|....*....|....*....|...
gi 1629467165 431 ---VSCVELENIIATHPKIQDIVVVGI-KDSIR 459
Cdd:PRK12582 489 wvsVGTLRPDAVAACSPVIHDAVVAGQdRAFIG 521
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
310-459 |
2.06e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 43.99 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 310 RFGVR---LLTSYGMTETIVGIIGDRPGD--------------KRRWPSIGRAGFCYEAEIR-DDHNRPLPAGEIGEICI 371
Cdd:PRK05851 298 PFGFDagaAAPSYGLAESTCAVTVPVPGIglrvdevttddgsgARRHAVLGNPIPGMEVRISpGDGAAGVAGREIGEIEI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 372 KGVPgktifkeyFLNPKATAKVLEADGWLHTGDTGYCDEEGFFyFVDRRCNMIKRGGENVSCVELENIIATHPKIQD--I 449
Cdd:PRK05851 378 RGAS--------MMSGYLGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREgaV 448
|
170
....*....|.
gi 1629467165 450 VVVGIKD-SIR 459
Cdd:PRK05851 449 VAVGTGEgSAR 459
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
35-195 |
2.10e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 43.91 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 35 VNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAC--- 111
Cdd:PLN03052 206 VNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKaif 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 112 ---LLVTSAQFYPMYQQIQQEDATQLrhiclidVALPADDGVSS------------FTQLKNQQPATLCYAP-PLSTDDT 175
Cdd:PLN03052 286 tqdVIVRGGKSIPLYSRVVEAKAPKA-------IVLPADGKSVRvklregdmswddFLARANGLRRPDEYKAvEQPVEAF 358
|
170 180
....*....|....*....|
gi 1629467165 176 AEILFTSGTTSRPKGVVITH 195
Cdd:PLN03052 359 TNILFSSGTTGEPKAIPWTQ 378
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
299-453 |
2.94e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 43.55 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 299 LSEQEKDAFCERFGVRLLTSYGMTETIVGIIGDRPGDKrRWPSIG-----------RAGFCYEAeirddhNRPLPAgeiG 367
Cdd:PTZ00342 473 LSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDN-NTESIGgpispntkykvRTWETYKA------TDTLPK---G 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 368 EICIKgvpGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYCDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKI 446
Cdd:PTZ00342 543 ELLIK---SDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYIETDMLNNLYSQISFI 619
|
....*..
gi 1629467165 447 QDIVVVG 453
Cdd:PTZ00342 620 NFCVVYG 626
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
25-482 |
8.22e-04 |
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Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 41.95 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 25 ALIC-ESSGGVVNRYSYLELNQEINRTANLFYT-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESA 102
Cdd:cd05905 1 AYTLlDSKGKEATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 103 WILQNSQACLLVTSaqfypmyqqiqqeDATQLRHICLIDVALPADDGVSS--------FTQLKNQQPATLCYA---PPLS 171
Cdd:cd05905 81 FLLGTCKVRVALTV-------------EACLKGLPKKLLKSKTAAEIAKKkgwpkildFVKIPKSKRSKLKKWgphPPTR 147
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 172 TDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMP-----AFHIDCQCTAAMAAFSAGATFVLV 246
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDfksglGLWHGCLLSVYSGHHTILIPPELM 227
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 247 EKySARAFWGQVQKYRATVTECIPMMIRTLMVQPPSAND-RQHR------LREVM--FYLNLSEQEKDAFCERFG----- 312
Cdd:cd05905 228 KT-NPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLAsLKNRdvnlssLRMCMvpCENRPRISSCDSFLKLFQtlgls 306
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 313 -VRLLTSYG----------------MTETIV-------GIIGDRPGDKRRWPSIGRAGF---CYEAEIRDDHNRPL-PAG 364
Cdd:cd05905 307 pRAVSTEFGtrvnpficwqgtsgpePSRVYLdmralrhGVVRLDERDKPNSLPLQDSGKvlpGAQVAIVNPETKGLcKDG 386
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 365 EIGEICIK---------GVPGKT--IFKEYFLNPKATakVLEADGWLHTGDTGY----------CDEEGFFYFVDRRCNM 423
Cdd:cd05905 387 EIGEIWVNspanasgyfLLDGETndTFKVFPSTRLST--GITNNSYARTGLLGFlrptkctdlnVEEHDLLFVVGSIDET 464
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490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629467165 424 IKRGGENVSCVELEN-IIATHPKIQDIVVVGIKDSIrdeaikafVVLNEGETLSEEEFFR 482
Cdd:cd05905 465 LEVRGLRHHPSDIEAtVMRVHPYRGRCAVFSITGLV--------VVVAEQPPGSEEEALD 516
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| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
143-198 |
6.02e-03 |
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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: 39.34 E-value: 6.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1629467165 143 ALPADDGVSSFTQLKnQQPATLCYAPPLST---DDTAEILFTSGTTSRPKGVVITHYNL 198
Cdd:cd05921 133 NAVAGRGAISFAELA-ATPPTAAVDAAFAAvgpDTVAKFLFTSGSTGLPKAVINTQRML 190
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